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Database: PDB
Entry: 4IUG
LinkDB: 4IUG
Original site: 4IUG 
HEADER    HYDROLASE                               21-JAN-13   4IUG              
TITLE     CRYSTAL STRUCTURE OF BETA-GALACTOSIDASE FROM ASPERGILLUS ORYZAE IN    
TITLE    2 COMPLEX WITH GALACTOSE                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BETA-GALACTOSIDASE A;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: LACTASE A;                                                  
COMPND   5 EC: 3.2.1.23;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ASPERGILLUS ORYZAE;                             
SOURCE   3 ORGANISM_COMMON: YELLOW KOJI MOLD;                                   
SOURCE   4 ORGANISM_TAXID: 5062;                                                
SOURCE   5 GENE: LACA;                                                          
SOURCE   6 EXPRESSION_SYSTEM: KLUYVEROMYCES LACTIS;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 28985                                       
KEYWDS    TIM BARREL, GLYCOSIDE HYDROLASE, HYDROLASE                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.MAKSIMAINEN,J.ROUVINEN                                              
REVDAT   1   31-JUL-13 4IUG    0                                                
JRNL        AUTH   M.M.MAKSIMAINEN,A.LAMPIO,M.MERTANEN,O.TURUNEN,J.ROUVINEN     
JRNL        TITL   THE CRYSTAL STRUCTURE OF ACIDIC BETA-GALACTOSIDASE FROM      
JRNL        TITL 2 ASPERGILLUS ORYZAE.                                          
JRNL        REF    INT.J.BIOL.MACROMOL.          V. 60C   109 2013              
JRNL        REFN                   ISSN 0141-8130                               
JRNL        PMID   23688418                                                     
JRNL        DOI    10.1016/J.IJBIOMAC.2013.05.003                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.3_928)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.91                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 52147                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.214                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2608                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 47.9222 -  6.9315    1.00     2775   146  0.2080 0.2136        
REMARK   3     2  6.9315 -  5.5043    1.00     2661   141  0.1960 0.2194        
REMARK   3     3  5.5043 -  4.8093    1.00     2659   139  0.1605 0.1975        
REMARK   3     4  4.8093 -  4.3699    1.00     2607   138  0.1334 0.1562        
REMARK   3     5  4.3699 -  4.0569    0.99     2595   136  0.1327 0.1547        
REMARK   3     6  4.0569 -  3.8178    1.00     2636   139  0.1430 0.1620        
REMARK   3     7  3.8178 -  3.6267    1.00     2585   136  0.1642 0.1980        
REMARK   3     8  3.6267 -  3.4688    1.00     2600   137  0.1702 0.2045        
REMARK   3     9  3.4688 -  3.3353    1.00     2578   136  0.1742 0.2200        
REMARK   3    10  3.3353 -  3.2203    1.00     2626   138  0.1821 0.1930        
REMARK   3    11  3.2203 -  3.1196    0.99     2564   135  0.1916 0.2494        
REMARK   3    12  3.1196 -  3.0304    1.00     2568   135  0.1932 0.2571        
REMARK   3    13  3.0304 -  2.9507    1.00     2610   137  0.2022 0.2400        
REMARK   3    14  2.9507 -  2.8787    1.00     2596   137  0.2068 0.2869        
REMARK   3    15  2.8787 -  2.8133    1.00     2571   135  0.2212 0.2658        
REMARK   3    16  2.8133 -  2.7534    1.00     2589   136  0.2333 0.2907        
REMARK   3    17  2.7534 -  2.6983    1.00     2586   137  0.2352 0.2923        
REMARK   3    18  2.6983 -  2.6474    1.00     2569   135  0.2506 0.3123        
REMARK   3    19  2.6474 -  2.6001    1.00     2564   135  0.2768 0.3268        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.38                                          
REMARK   3   B_SOL              : 34.65                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.350            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.260           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.10550                                              
REMARK   3    B22 (A**2) : 1.10550                                              
REMARK   3    B33 (A**2) : -2.21110                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           8144                                  
REMARK   3   ANGLE     :  1.328          11147                                  
REMARK   3   CHIRALITY :  0.082           1286                                  
REMARK   3   PLANARITY :  0.005           1375                                  
REMARK   3   DIHEDRAL  : 26.536           3046                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4IUG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JAN-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB077223.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-DEC-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97625                            
REMARK 200  MONOCHROMATOR                  : SI(311)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 52147                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.914                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.110                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1TG7                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.83                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M CADMIUM CHLORIDE, 0.1 M SODIUM     
REMARK 280  ACETATE, 30 % (W/V) PEG 400, PH 5.0, VAPOR DIFFUSION, HANGING       
REMARK 280  DROP, TEMPERATURE 295K                                              
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       90.88667            
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       45.44333            
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       45.44333            
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       90.88667            
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 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A3271  LIES ON A SPECIAL POSITION.                          
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     LEU A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     VAL A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     VAL 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     LEU A    25                                                      
REMARK 465     ASN A    26                                                      
REMARK 465     GLY A    27                                                      
REMARK 465     PHE A    28                                                      
REMARK 465     THR A    29                                                      
REMARK 465     ILE A    30                                                      
REMARK 465     LEU A    31                                                      
REMARK 465     GLU A    32                                                      
REMARK 465     HIS A    33                                                      
REMARK 465     PRO 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     GLY A   203                                                      
REMARK 465     GLY A   204                                                      
REMARK 465     CYS A   205                                                      
REMARK 465     CYS A   206                                                      
REMARK 465     GLY A   207                                                      
REMARK 465     VAL A   208                                                      
REMARK 465     LYS A   209                                                      
REMARK 465     TYR A   210                                                      
REMARK 465     PRO A   211                                                      
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   924              2.14            
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    LEU A 403   CA  -  CB  -  CG  ANGL. DEV. =  14.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  49     -163.04   -126.17                                   
REMARK 500    PRO A  73       43.04    -74.21                                   
REMARK 500    GLU A 103       49.81   -141.58                                   
REMARK 500    ASN A 140      -98.98     59.48                                   
REMARK 500    GLU A 198     -160.83     62.04                                   
REMARK 500    ASN A 199      115.23   -161.41                                   
REMARK 500    SER A 289       61.78   -159.86                                   
REMARK 500    ASN A 320     -158.96    -94.08                                   
REMARK 500    TYR A 359     -155.93   -107.78                                   
REMARK 500    TYR A 364       -3.55     69.43                                   
REMARK 500    LEU A 459     -154.12    -93.11                                   
REMARK 500    PHE A 497       41.35   -100.46                                   
REMARK 500    ASP A 498       85.00     56.44                                   
REMARK 500    SER A 595       44.49   -103.89                                   
REMARK 500    ALA A 601     -137.39   -135.40                                   
REMARK 500    SER A 741      -36.83   -131.47                                   
REMARK 500    ASN A 760     -111.05     38.96                                   
REMARK 500    ASP A 899       50.19   -144.38                                   
REMARK 500    VAL A 937      -51.04   -121.40                                   
REMARK 500    THR A 981      115.27    -39.18                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     M6D A 1163                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A1104  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 460   OE1                                                    
REMARK 620 2 HOH A3076   O   110.4                                              
REMARK 620 3 GLU A 460   OE2  52.5 148.4                                        
REMARK 620 4 HOH A3079   O   104.7  99.8 109.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A1105  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A3077   O                                                      
REMARK 620 2 ASP A 547   OD2 148.7                                              
REMARK 620 3 HOH A3078   O    95.8  89.3                                        
REMARK 620 4 HOH A3250   O    93.9  78.3 167.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A1108  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 804   OE1                                                    
REMARK 620 2 GLU A 142   OE2 151.0                                              
REMARK 620 3 GLU A 804   OE2  50.0 105.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A1103  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 803   OD2                                                    
REMARK 620 2 HOH A3075   O    97.9                                              
REMARK 620 3 HOH A3074   O   128.9 112.3                                        
REMARK 620 4 ASP A 803   OD1  50.2  97.4  84.6                                  
REMARK 620 5 HOH A3224   O   117.7 102.4  95.6 158.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CD A1102  CD                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 112   OE2                                                    
REMARK 620 2 HOH A3080   O   100.5                                              
REMARK 620 3 GLU A 112   OE1  50.1  89.0                                        
REMARK 620 4 BMA A1160   O6  157.0  84.1 108.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1104                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1105                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1106                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1107                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1108                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1109                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1110                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1111                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1112                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1113                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1114                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1115                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1116                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1117                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1118                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1119                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1120                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1121                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1122                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1123                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1124                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1125                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1126                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1127                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1128                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CD A 1129                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAL A 1130                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1131                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1132                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 1133                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 1134                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 1135                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1136                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1137                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1138                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 1139                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 1140                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 1141                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 1142                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 1143                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1144                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1145                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1146                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1147                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1148                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1149                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 1150                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 1151                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 1152                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 1153                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 1154                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 1155                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 1156                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN A 1157                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1158                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 1159                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 1160                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1161                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 1162                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE M6D A 1163                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1164                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 1165                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 1166                
DBREF  4IUG A    1  1005  UNP    Q2UCU3   BGALA_ASPOR      1   1005             
SEQRES   1 A 1005  MET LYS LEU LEU SER VAL ALA ALA VAL ALA LEU LEU ALA          
SEQRES   2 A 1005  ALA GLN ALA ALA GLY ALA SER ILE LYS HIS ARG LEU ASN          
SEQRES   3 A 1005  GLY PHE THR ILE LEU GLU HIS PRO ASP PRO ALA LYS ARG          
SEQRES   4 A 1005  ASP LEU LEU GLN ASP ILE VAL THR TRP ASP ASP LYS SER          
SEQRES   5 A 1005  LEU PHE ILE ASN GLY GLU ARG ILE MET LEU PHE SER GLY          
SEQRES   6 A 1005  GLU VAL HIS PRO PHE ARG LEU PRO VAL PRO SER LEU TRP          
SEQRES   7 A 1005  LEU ASP ILE PHE HIS LYS ILE ARG ALA LEU GLY PHE ASN          
SEQRES   8 A 1005  CYS VAL SER PHE TYR ILE ASP TRP ALA LEU LEU GLU GLY          
SEQRES   9 A 1005  LYS PRO GLY ASP TYR ARG ALA GLU GLY ILE PHE ALA LEU          
SEQRES  10 A 1005  GLU PRO PHE PHE ASP ALA ALA LYS GLU ALA GLY ILE TYR          
SEQRES  11 A 1005  LEU ILE ALA ARG PRO GLY SER TYR ILE ASN ALA GLU VAL          
SEQRES  12 A 1005  SER GLY GLY GLY PHE PRO GLY TRP LEU GLN ARG VAL ASN          
SEQRES  13 A 1005  GLY THR LEU ARG SER SER ASP GLU PRO PHE LEU LYS ALA          
SEQRES  14 A 1005  THR ASP ASN TYR ILE ALA ASN ALA ALA ALA ALA VAL ALA          
SEQRES  15 A 1005  LYS ALA GLN ILE THR ASN GLY GLY PRO VAL ILE LEU TYR          
SEQRES  16 A 1005  GLN PRO GLU ASN GLU TYR SER GLY GLY CYS CYS GLY VAL          
SEQRES  17 A 1005  LYS TYR PRO ASP ALA ASP TYR MET GLN TYR VAL MET ASP          
SEQRES  18 A 1005  GLN ALA ARG LYS ALA ASP ILE VAL VAL PRO PHE ILE SER          
SEQRES  19 A 1005  ASN ASP ALA SER PRO SER GLY HIS ASN ALA PRO GLY SER          
SEQRES  20 A 1005  GLY THR GLY ALA VAL ASP ILE TYR GLY HIS ASP SER TYR          
SEQRES  21 A 1005  PRO LEU GLY PHE ASP CYS ALA ASN PRO SER VAL TRP PRO          
SEQRES  22 A 1005  GLU GLY LYS LEU PRO ASP ASN PHE ARG THR LEU HIS LEU          
SEQRES  23 A 1005  GLU GLN SER PRO SER THR PRO TYR SER LEU LEU GLU PHE          
SEQRES  24 A 1005  GLN ALA GLY ALA PHE ASP PRO TRP GLY GLY PRO GLY PHE          
SEQRES  25 A 1005  GLU LYS CYS TYR ALA LEU VAL ASN HIS GLU PHE SER ARG          
SEQRES  26 A 1005  VAL PHE TYR ARG ASN ASP LEU SER PHE GLY VAL SER THR          
SEQRES  27 A 1005  PHE ASN LEU TYR MET THR PHE GLY GLY THR ASN TRP GLY          
SEQRES  28 A 1005  ASN LEU GLY HIS PRO GLY GLY TYR THR SER TYR ASP TYR          
SEQRES  29 A 1005  GLY SER PRO ILE THR GLU THR ARG ASN VAL THR ARG GLU          
SEQRES  30 A 1005  LYS TYR SER ASP ILE LYS LEU LEU ALA ASN PHE VAL LYS          
SEQRES  31 A 1005  ALA SER PRO SER TYR LEU THR ALA THR PRO ARG ASN LEU          
SEQRES  32 A 1005  THR THR GLY VAL TYR THR ASP THR SER ASP LEU ALA VAL          
SEQRES  33 A 1005  THR PRO LEU ILE GLY ASP SER PRO GLY SER PHE PHE VAL          
SEQRES  34 A 1005  VAL ARG HIS THR ASP TYR SER SER GLN GLU SER THR SER          
SEQRES  35 A 1005  TYR LYS LEU LYS LEU PRO THR SER ALA GLY ASN LEU THR          
SEQRES  36 A 1005  ILE PRO GLN LEU GLU GLY THR LEU SER LEU ASN GLY ARG          
SEQRES  37 A 1005  ASP SER LYS ILE HIS VAL VAL ASP TYR ASN VAL SER GLY          
SEQRES  38 A 1005  THR ASN ILE ILE TYR SER THR ALA GLU VAL PHE THR TRP          
SEQRES  39 A 1005  LYS LYS PHE ASP GLY ASN LYS VAL LEU VAL LEU TYR GLY          
SEQRES  40 A 1005  GLY PRO LYS GLU HIS HIS GLU LEU ALA ILE ALA SER LYS          
SEQRES  41 A 1005  SER ASN VAL THR ILE ILE GLU GLY SER ASP SER GLY ILE          
SEQRES  42 A 1005  VAL SER THR ARG LYS GLY SER SER VAL ILE ILE GLY TRP          
SEQRES  43 A 1005  ASP VAL SER SER THR ARG ARG ILE VAL GLN VAL GLY ASP          
SEQRES  44 A 1005  LEU ARG VAL PHE LEU LEU ASP ARG ASN SEP ALA TYR ASN          
SEQRES  45 A 1005  TYR TRP VAL PRO GLU LEU PRO THR GLU GLY THR SER PRO          
SEQRES  46 A 1005  GLY PHE SER THR SER LYS THR THR ALA SER SER ILE ILE          
SEQRES  47 A 1005  VAL LYS ALA GLY TYR LEU LEU ARG GLY ALA HIS LEU ASP          
SEQRES  48 A 1005  GLY ALA ASP LEU HIS LEU THR ALA ASP PHE ASN ALA THR          
SEQRES  49 A 1005  THR PRO ILE GLU VAL ILE GLY ALA PRO THR GLY ALA LYS          
SEQRES  50 A 1005  ASN LEU PHE VAL ASN GLY GLU LYS ALA SER HIS THR VAL          
SEQRES  51 A 1005  ASP LYS ASN GLY ILE TRP SER SER GLU VAL LYS TYR ALA          
SEQRES  52 A 1005  ALA PRO GLU ILE LYS LEU PRO GLY LEU LYS ASP LEU ASP          
SEQRES  53 A 1005  TRP LYS TYR LEU ASP THR LEU PRO GLU ILE LYS SER SER          
SEQRES  54 A 1005  TYR ASP ASP SER ALA TRP VAL SER ALA ASP LEU PRO LYS          
SEQRES  55 A 1005  THR LYS ASN THR HIS ARG PRO LEU ASP THR PRO THR SER          
SEQRES  56 A 1005  LEU TYR SER SER ASP TYR GLY PHE HIS THR GLY TYR LEU          
SEQRES  57 A 1005  ILE TYR ARG GLY HIS PHE VAL ALA ASN GLY LYS GLU SER          
SEQRES  58 A 1005  GLU PHE PHE ILE ARG THR GLN GLY GLY SER ALA PHE GLY          
SEQRES  59 A 1005  SER SER VAL TRP LEU ASN GLU THR TYR LEU GLY SER TRP          
SEQRES  60 A 1005  THR GLY ALA ASP TYR ALA MET ASP GLY ASN SER THR TYR          
SEQRES  61 A 1005  LYS LEU SER GLN LEU GLU SER GLY LYS ASN TYR VAL ILE          
SEQRES  62 A 1005  THR VAL VAL ILE ASP ASN LEU GLY LEU ASP GLU ASN TRP          
SEQRES  63 A 1005  THR VAL GLY GLU GLU THR MET LYS ASN PRO ARG GLY ILE          
SEQRES  64 A 1005  LEU SER TYR LYS LEU SER GLY GLN ASP ALA SER ALA ILE          
SEQRES  65 A 1005  THR TRP LYS LEU THR GLY ASN LEU GLY GLY GLU ASP TYR          
SEQRES  66 A 1005  GLN ASP LYS VAL ARG GLY PRO LEU ASN GLU GLY GLY LEU          
SEQRES  67 A 1005  TYR ALA GLU ARG GLN GLY PHE HIS GLN PRO GLN PRO PRO          
SEQRES  68 A 1005  SER GLU SER TRP GLU SER GLY SER PRO LEU GLU GLY LEU          
SEQRES  69 A 1005  SER LYS PRO GLY ILE GLY PHE TYR THR ALA GLN PHE ASP          
SEQRES  70 A 1005  LEU ASP LEU PRO LYS GLY TRP ASP VAL PRO LEU TYR PHE          
SEQRES  71 A 1005  ASN PHE GLY ASN ASN THR GLN ALA ALA ARG ALA GLN LEU          
SEQRES  72 A 1005  TYR VAL ASN GLY TYR GLN TYR GLY LYS PHE THR GLY ASN          
SEQRES  73 A 1005  VAL GLY PRO GLN THR SER PHE PRO VAL PRO GLU GLY ILE          
SEQRES  74 A 1005  LEU ASN TYR ARG GLY THR ASN TYR VAL ALA LEU SER LEU          
SEQRES  75 A 1005  TRP ALA LEU GLU SER ASP GLY ALA LYS LEU GLY SER PHE          
SEQRES  76 A 1005  GLU LEU SER TYR THR THR PRO VAL LEU THR GLY TYR GLY          
SEQRES  77 A 1005  ASN VAL GLU SER PRO GLU GLN PRO LYS TYR GLU GLN ARG          
SEQRES  78 A 1005  LYS GLY ALA TYR                                              
MODRES 4IUG ASN A  914  ASN  GLYCOSYLATION SITE                                 
MODRES 4IUG ASN A  760  ASN  GLYCOSYLATION SITE                                 
MODRES 4IUG ASN A  622  ASN  GLYCOSYLATION SITE                                 
MODRES 4IUG ASN A  777  ASN  GLYCOSYLATION SITE                                 
MODRES 4IUG ASN A  373  ASN  GLYCOSYLATION SITE                                 
MODRES 4IUG ASN A  402  ASN  GLYCOSYLATION SITE                                 
MODRES 4IUG SEP A  569  SER  PHOSPHOSERINE                                      
HET    SEP  A 569      10                                                       
HET     CD  A1101       1                                                       
HET     CD  A1102       1                                                       
HET     CD  A1103       1                                                       
HET     CD  A1104       1                                                       
HET     CD  A1105       1                                                       
HET     CD  A1106       1                                                       
HET     CD  A1107       1                                                       
HET     CD  A1108       1                                                       
HET     CD  A1109       1                                                       
HET     CD  A1110       1                                                       
HET     CD  A1111       1                                                       
HET     CD  A1112       1                                                       
HET     CD  A1113       1                                                       
HET     CD  A1114       1                                                       
HET     CD  A1115       1                                                       
HET     CD  A1116       1                                                       
HET     CD  A1117       1                                                       
HET     CD  A1118       1                                                       
HET     CD  A1119       1                                                       
HET     CD  A1120       1                                                       
HET     CD  A1121       1                                                       
HET     CD  A1122       1                                                       
HET     CD  A1123       1                                                       
HET     CD  A1124       1                                                       
HET     CD  A1125       1                                                       
HET     CD  A1126       1                                                       
HET     CD  A1127       1                                                       
HET     CD  A1128       1                                                       
HET     CD  A1129       1                                                       
HET    GAL  A1130      12                                                       
HET    NAG  A1131      14                                                       
HET    NAG  A1132      14                                                       
HET    BMA  A1133      11                                                       
HET    MAN  A1134      11                                                       
HET    MAN  A1135      11                                                       
HET    NAG  A1136      14                                                       
HET    NAG  A1137      14                                                       
HET    NAG  A1138      14                                                       
HET    BMA  A1139      11                                                       
HET    MAN  A1140      11                                                       
HET    MAN  A1141      11                                                       
HET    MAN  A1142      11                                                       
HET    MAN  A1143      11                                                       
HET    NAG  A1144      14                                                       
HET    NAG  A1145      14                                                       
HET    NAG  A1146      14                                                       
HET    NAG  A1147      14                                                       
HET    NAG  A1148      14                                                       
HET    NAG  A1149      14                                                       
HET    BMA  A1150      11                                                       
HET    MAN  A1151      11                                                       
HET    MAN  A1152      11                                                       
HET    MAN  A1153      11                                                       
HET    MAN  A1154      11                                                       
HET    MAN  A1155      11                                                       
HET    MAN  A1156      11                                                       
HET    MAN  A1157      11                                                       
HET    NAG  A1158      14                                                       
HET    BMA  A1159      11                                                       
HET    BMA  A1160      11                                                       
HET    NAG  A1161      14                                                       
HET    BMA  A1162      12                                                       
HET    M6D  A1163      15                                                       
HET    NAG  A1164      14                                                       
HET    BMA  A1165      11                                                       
HET    NAG  A1166      14                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM      CD CADMIUM ION                                                      
HETNAM     GAL BETA-D-GALACTOSE                                                 
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     M6D 6-O-PHOSPHONO-BETA-D-MANNOPYRANOSE                               
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     M6D BETA-D-MANNOSE-6-PHOSPHATE                                       
FORMUL   1  SEP    C3 H8 N O6 P                                                 
FORMUL   2   CD    29(CD 2+)                                                    
FORMUL  31  GAL    C6 H12 O6                                                    
FORMUL  32  NAG    15(C8 H15 N O6)                                              
FORMUL  32  BMA    7(C6 H12 O6)                                                 
FORMUL  32  MAN    13(C6 H12 O6)                                                
FORMUL  39  M6D    C6 H13 O9 P                                                  
FORMUL  41  HOH   *280(H2 O)                                                    
HELIX    1   1 PRO A   69  LEU A   72  5                                   4    
HELIX    2   2 VAL A   74  SER A   76  5                                   3    
HELIX    3   3 LEU A   77  LEU A   88  1                                  12    
HELIX    4   4 ASP A   98  GLU A  103  1                                   6    
HELIX    5   5 GLU A  112  ALA A  116  5                                   5    
HELIX    6   6 LEU A  117  GLY A  128  1                                  12    
HELIX    7   7 VAL A  143  PHE A  148  5                                   6    
HELIX    8   8 PRO A  149  VAL A  155  5                                   7    
HELIX    9   9 ASP A  163  THR A  170  1                                   8    
HELIX   10  10 THR A  170  ALA A  184  1                                  15    
HELIX   11  11 GLN A  185  GLY A  189  5                                   5    
HELIX   12  12 ALA A  213  LYS A  225  1                                  13    
HELIX   13  13 ASN A  280  SER A  289  1                                  10    
HELIX   14  14 GLY A  311  VAL A  319  1                                   9    
HELIX   15  15 ASN A  320  SER A  333  1                                  14    
HELIX   16  16 ASN A  349  LEU A  353  5                                   5    
HELIX   17  17 ARG A  376  ALA A  391  1                                  16    
HELIX   18  18 SER A  392  LEU A  396  5                                   5    
HELIX   19  19 ARG A  567  TYR A  571  1                                   5    
HELIX   20  20 THR A  589  SER A  595  1                                   7    
HELIX   21  21 GLY A  671  LEU A  675  5                                   5    
HELIX   22  22 LEU A  683  LYS A  687  5                                   5    
HELIX   23  23 TYR A  717  GLY A  722  5                                   6    
HELIX   24  24 GLU A  811  ASN A  815  5                                   5    
HELIX   25  25 ASP A  828  ILE A  832  5                                   5    
HELIX   26  26 LEU A  858  GLY A  864  1                                   7    
SHEET    1   A 3 VAL A  46  TRP A  48  0                                        
SHEET    2   A 3 LEU A  53  ILE A  55 -1  O  PHE A  54   N  THR A  47           
SHEET    3   A 3 GLU A  58  ILE A  60 -1  O  GLU A  58   N  ILE A  55           
SHEET    1   B 7 VAL A 192  PRO A 197  0                                        
SHEET    2   B 7 TYR A 130  GLY A 136  1  N  ALA A 133   O  GLN A 196           
SHEET    3   B 7 CYS A  92  TYR A  96  1  N  VAL A  93   O  TYR A 130           
SHEET    4   B 7 LEU A  62  VAL A  67  1  N  VAL A  67   O  SER A  94           
SHEET    5   B 7 THR A 338  PHE A 345  1  O  LEU A 341   N  SER A  64           
SHEET    6   B 7 SER A 295  GLN A 300  1  N  LEU A 296   O  THR A 338           
SHEET    7   B 7 HIS A 257  SER A 259  1  N  HIS A 257   O  SER A 295           
SHEET    1   C 7 LEU A 414  ILE A 420  0                                        
SHEET    2   C 7 SER A 426  HIS A 432 -1  O  PHE A 427   N  LEU A 419           
SHEET    3   C 7 LYS A 471  VAL A 479 -1  O  HIS A 473   N  PHE A 428           
SHEET    4   C 7 THR A 482  SER A 487 -1  O  ILE A 484   N  TYR A 477           
SHEET    5   C 7 HIS A 512  ALA A 518 -1  O  ALA A 518   N  ASN A 483           
SHEET    6   C 7 SER A 541  ASP A 547 -1  O  TRP A 546   N  HIS A 513           
SHEET    7   C 7 VAL A 534  LYS A 538 -1  N  VAL A 534   O  GLY A 545           
SHEET    1   D 2 SER A 440  TYR A 443  0                                        
SHEET    2   D 2 LEU A 463  ASN A 466 -1  O  LEU A 465   N  THR A 441           
SHEET    1   E 2 LEU A 445  THR A 449  0                                        
SHEET    2   E 2 GLY A 452  ILE A 456 -1  O  ILE A 456   N  LEU A 445           
SHEET    1   F 5 GLU A 490  PHE A 497  0                                        
SHEET    2   F 5 ASN A 500  GLY A 507 -1  O  VAL A 504   N  THR A 493           
SHEET    3   F 5 LEU A 560  ASP A 566  1  O  ARG A 561   N  LYS A 501           
SHEET    4   F 5 ARG A 553  VAL A 557 -1  N  VAL A 555   O  VAL A 562           
SHEET    5   F 5 THR A 524  GLU A 527 -1  N  THR A 524   O  GLN A 556           
SHEET    1   G 5 TYR A 573  TRP A 574  0                                        
SHEET    2   G 5 ILE A 598  LYS A 600 -1  O  VAL A 599   N  TRP A 574           
SHEET    3   G 5 THR A 625  ILE A 630 -1  O  ILE A 630   N  ILE A 598           
SHEET    4   G 5 TRP A 656  VAL A 660 -1  O  SER A 658   N  ILE A 627           
SHEET    5   G 5 THR A 649  VAL A 650 -1  N  THR A 649   O  SER A 657           
SHEET    1   H 4 LEU A 604  ASP A 611  0                                        
SHEET    2   H 4 ASP A 614  ASP A 620 -1  O  ASP A 614   N  ASP A 611           
SHEET    3   H 4 ASN A 638  VAL A 641  1  O  ASN A 638   N  LEU A 615           
SHEET    4   H 4 GLU A 644  ALA A 646 -1  O  GLU A 644   N  VAL A 641           
SHEET    1   I 6 GLU A 876  SER A 877  0                                        
SHEET    2   I 6 LYS A 678  ASP A 681 -1  N  TYR A 679   O  GLU A 876           
SHEET    3   I 6 GLY A 888  ASP A 899 -1  O  THR A 893   N  LYS A 678           
SHEET    4   I 6 ARG A 953  ALA A 964 -1  O  LEU A 960   N  TYR A 892           
SHEET    5   I 6 ALA A 919  VAL A 925 -1  N  ARG A 920   O  TRP A 963           
SHEET    6   I 6 TYR A 928  THR A 934 -1  O  PHE A 933   N  ALA A 921           
SHEET    1   J 6 VAL A 696  SER A 697  0                                        
SHEET    2   J 6 THR A 833  THR A 837 -1  O  LEU A 836   N  VAL A 696           
SHEET    3   J 6 LEU A 728  VAL A 735 -1  N  ARG A 731   O  LYS A 835           
SHEET    4   J 6 ASN A 790  ILE A 797 -1  O  ILE A 797   N  LEU A 728           
SHEET    5   J 6 SER A 755  LEU A 759 -1  N  SER A 756   O  VAL A 796           
SHEET    6   J 6 THR A 762  TRP A 767 -1  O  THR A 762   N  LEU A 759           
SHEET    1   K 3 ASP A 775  LYS A 781  0                                        
SHEET    2   K 3 GLU A 742  GLN A 748 -1  N  PHE A 743   O  TYR A 780           
SHEET    3   K 3 GLY A 818  LEU A 824 -1  O  LYS A 823   N  PHE A 744           
SHEET    1   L 2 TRP A 904  ASP A 905  0                                        
SHEET    2   L 2 VAL A 983  LEU A 984 -1  O  VAL A 983   N  ASP A 905           
SHEET    1   M 3 SER A 942  VAL A 945  0                                        
SHEET    2   M 3 LEU A 908  PHE A 912 -1  N  PHE A 910   O  PHE A 943           
SHEET    3   M 3 PHE A 975  TYR A 979 -1  O  GLU A 976   N  ASN A 911           
SSBOND   1 CYS A  266    CYS A  315                          1555   1555  2.08  
LINK         C   ASN A 568                 N   SEP A 569     1555   1555  1.34  
LINK         C   SEP A 569                 N   ALA A 570     1555   1555  1.33  
LINK         O3  BMA A1139                 C1  MAN A1142     1555   1555  1.43  
LINK         O3  MAN A1151                 C1  MAN A1156     1555   1555  1.43  
LINK         O4  NAG A1148                 C1  NAG A1149     1555   1555  1.43  
LINK         O6  MAN A1152                 C1  MAN A1153     1555   1555  1.43  
LINK         O6  BMA A1139                 C1  MAN A1140     1555   1555  1.43  
LINK         O2  MAN A1152                 C1  MAN A1154     1555   1555  1.43  
LINK         O3  MAN A1140                 C1  MAN A1141     1555   1555  1.43  
LINK         O4  NAG A1132                 C1  BMA A1133     1555   1555  1.44  
LINK         O4  NAG A1137                 C1  NAG A1138     1555   1555  1.44  
LINK         O4  NAG A1149                 C1  BMA A1150     1555   1555  1.44  
LINK         O6  BMA A1150                 C1  MAN A1151     1555   1555  1.44  
LINK         O3  BMA A1150                 C1  MAN A1152     1555   1555  1.44  
LINK         O2  MAN A1142                 C1  MAN A1143     1555   1555  1.44  
LINK         O2  MAN A1154                 C1  MAN A1155     1555   1555  1.44  
LINK         O4  NAG A1131                 C1  NAG A1132     1555   1555  1.44  
LINK         O4  NAG A1138                 C1  BMA A1139     1555   1555  1.44  
LINK         O4  NAG A1144                 C1  NAG A1145     1555   1555  1.44  
LINK         O3  BMA A1133                 C1  MAN A1134     1555   1555  1.44  
LINK         ND2 ASN A 914                 C1  NAG A1148     1555   1555  1.45  
LINK         O6  MAN A1151                 C1  MAN A1157     1555   1555  1.45  
LINK         O2  MAN A1134                 C1  MAN A1135     1555   1555  1.45  
LINK         ND2 ASN A 760                 C1  NAG A1144     1555   1555  1.45  
LINK         ND2 ASN A 622                 C1  NAG A1137     1555   1555  1.45  
LINK         ND2 ASN A 777                 C1  NAG A1146     1555   1555  1.45  
LINK         O4  NAG A1146                 C1  NAG A1147     1555   1555  1.46  
LINK         ND2 ASN A 373                 C1  NAG A1131     1555   1555  1.46  
LINK         ND2 ASN A 402                 C1  NAG A1136     1555   1555  1.46  
LINK         OE1 GLU A 460                CD    CD A1104     1555   1555  2.40  
LINK        CD    CD A1105                 O   HOH A3077     1555   1555  2.49  
LINK        CD    CD A1104                 O   HOH A3076     1555   1555  2.53  
LINK         OE2 GLU A 460                CD    CD A1104     1555   1555  2.54  
LINK         OD2 ASP A 547                CD    CD A1105     1555   1555  2.56  
LINK         OE1 GLU A 804                CD    CD A1108     1555   1555  2.56  
LINK         OD2 ASP A 803                CD    CD A1103     1555   1555  2.57  
LINK        CD    CD A1103                 O   HOH A3075     1555   1555  2.57  
LINK         OE2 GLU A 112                CD    CD A1102     1555   1555  2.57  
LINK        CD    CD A1103                 O   HOH A3074     1555   1555  2.58  
LINK        CD    CD A1102                 O   HOH A3080     1555   1555  2.61  
LINK         OD2 ASP A 163                CD    CD A1109     1555   1555  2.62  
LINK         OE1 GLU A 126                CD    CD A1101     1555   1555  2.63  
LINK         OE2 GLU A 142                CD    CD A1108     1555   1555  2.64  
LINK         OD1 ASP A 122                CD    CD A1107     1555   1555  2.64  
LINK         OD1 ASP A 803                CD    CD A1103     1555   1555  2.65  
LINK         OE1 GLU A 313                CD    CD A1113     1555   1555  2.65  
LINK         OE1 GLU A 991                CD    CD A1129     1555   1555  2.65  
LINK        CD    CD A1104                 O   HOH A3079     1555   1555  2.66  
LINK         OD1 ASN A 815                CD    CD A1124     1555   1555  2.66  
LINK         OE2 GLU A 804                CD    CD A1108     1555   1555  2.66  
LINK         OD1 ASP A 699                CD    CD A1122     1555   1555  2.66  
LINK         OE1 GLU A 112                CD    CD A1102     1555   1555  2.66  
LINK        CD    CD A1105                 O   HOH A3078     1555   1555  2.67  
LINK         OD1 ASP A 214                CD    CD A1110     1555   1555  2.67  
LINK        CD    CD A1105                 O   HOH A3250     1555   1555  2.67  
LINK        CD    CD A1103                 O   HOH A3224     1555   1555  2.68  
LINK         OD1 ASP A 227                CD    CD A1112     1555   1555  2.68  
LINK         OE2 GLU A 322                CD    CD A1114     1555   1555  2.68  
LINK         OD2 ASP A 828                CD    CD A1126     1555   1555  2.70  
LINK         O4  BMA A1159                 C1  NAG A1161     1555   1555  1.44  
LINK         C1  NAG A1158                 O4  BMA A1160     1555   1555  1.44  
LINK         O3  NAG A1164                 C1  BMA A1165     1555   1555  1.44  
LINK         O4  BMA A1165                 C1  NAG A1166     1555   1555  1.45  
LINK         O3  NAG A1158                 C1  BMA A1159     1555   1555  1.45  
LINK        CD    CD A1102                 O6  BMA A1160     1555   1555  2.52  
LINK        CD    CD A1128                 O6  BMA A1165     1555   1555  2.55  
LINK         C1  BMA A1160                 O4  BMA A1162     1555   1555  1.42  
LINK         O3  NAG A1161                 C1  M6D A1163     1555   1555  1.45  
LINK         O4  M6D A1163                 C1  NAG A1164     1555   1555  1.30  
CISPEP   1 GLY A  136    SER A  137          0        16.36                     
CISPEP   2 TYR A  342    MET A  343          0       -16.80                     
CISPEP   3 ILE A  456    PRO A  457          0        -0.55                     
CISPEP   4 GLY A  938    PRO A  939          0         4.44                     
SITE     1 AC1  4 GLU A 126   CD A1128  NAG A1164  BMA A1165                    
SITE     1 AC2  4 GLU A 112  GLU A 999  BMA A1160  HOH A3080                    
SITE     1 AC3  4 ASP A 803  HOH A3074  HOH A3075  HOH A3224                    
SITE     1 AC4  4 GLU A 460  GLU A 761  HOH A3076  HOH A3079                    
SITE     1 AC5  5 ASP A 547  HOH A3077  HOH A3078  HOH A3079                    
SITE     2 AC5  5 HOH A3250                                                     
SITE     1 AC6  1 ASP A  40                                                     
SITE     1 AC7  1 ASP A 122                                                     
SITE     1 AC8  4 ASN A 140  GLU A 142  GLU A 804  GAL A1130                    
SITE     1 AC9  2 THR A 158  ASP A 163                                          
SITE     1 BC1  1 ASP A 214                                                     
SITE     1 BC2  2 THR A 249  NAG A1148                                          
SITE     1 BC3  1 ASP A 227                                                     
SITE     1 BC4  2 GLU A 313  HOH A3159                                          
SITE     1 BC5  2 GLU A 322  GLN A 438                                          
SITE     1 BC6  2 ASP A 410  GLU A 882                                          
SITE     1 BC7  2 ASP A 410  LYS A 446                                          
SITE     1 BC8  3 ASP A 413  GLU A 873   CD A1121                               
SITE     1 BC9  1 ASP A 530                                                     
SITE     1 CC1  1 ASP A 614                                                     
SITE     1 CC2  1 GLU A 644                                                     
SITE     1 CC3  3 ASP A 413  ASP A 676   CD A1117                               
SITE     1 CC4  1 ASP A 699                                                     
SITE     1 CC5  1 ASP A 711                                                     
SITE     1 CC6  2 HIS A 707  ASN A 815                                          
SITE     1 CC7  1 HIS A 355                                                     
SITE     1 CC8  2 ASP A 828  SER A 830                                          
SITE     1 CC9  1 ASP A 844                                                     
SITE     1 DC1  3 ASP A 899   CD A1101  BMA A1165                               
SITE     1 DC2  2 GLU A 991  M6D A1163                                          
SITE     1 DC3 15 TYR A  96  ILE A 139  ASN A 140  ALA A 141                    
SITE     2 DC3 15 GLU A 142  ASN A 199  GLU A 200  ASN A 235                    
SITE     3 DC3 15 ASP A 258  TYR A 260  GLU A 298  PHE A 304                    
SITE     4 DC3 15 TYR A 342  TYR A 364   CD A1108                               
SITE     1 DC4 11 ASP A 363  THR A 369  THR A 371  ASN A 373                    
SITE     2 DC4 11 TYR A 909  THR A 980  THR A 981  NAG A1132                    
SITE     3 DC4 11 NAG A1137  HOH A3066  HOH A3267                               
SITE     1 DC5  5 GLU A 313  SER A 942  NAG A1131  BMA A1133                    
SITE     2 DC5  5 HOH A3266                                                     
SITE     1 DC6  2 NAG A1132  MAN A1134                                          
SITE     1 DC7  4 ASN A 911  GLU A 976  BMA A1133  MAN A1135                    
SITE     1 DC8  1 MAN A1134                                                     
SITE     1 DC9  3 ASP A 279  ASN A 402  LEU A 403                               
SITE     1 EC1  6 TYR A 603  ASN A 622  THR A 981  NAG A1131                    
SITE     2 EC1  6 NAG A1138  HOH A3014                                          
SITE     1 EC2  6 THR A 375  GLU A 377  TYR A 571  NAG A1137                    
SITE     2 EC2  6 BMA A1139  HOH A3070                                          
SITE     1 EC3  5 GLU A 377  NAG A1138  MAN A1140  MAN A1142                    
SITE     2 EC3  5 HOH A3042                                                     
SITE     1 EC4  5 GLU A 377  ASN A 568  BMA A1139  MAN A1141                    
SITE     2 EC4  5 HOH A3242                                                     
SITE     1 EC5  4 HIS A 321  GLU A 322  ARG A 325  MAN A1140                    
SITE     1 EC6  3 ASN A 320  BMA A1139  MAN A1143                               
SITE     1 EC7  1 MAN A1142                                                     
SITE     1 EC8  7 SER A 688  ASN A 760  ASN A 790  TYR A 791                    
SITE     2 EC8  7 VAL A 792  NAG A1145  HOH A3136                               
SITE     1 EC9  3 TYR A 690  ASN A 790  NAG A1144                               
SITE     1 FC1  4 ARG A 746  ASP A 775  ASN A 777  NAG A1147                    
SITE     1 FC2  2 ARG A 746  NAG A1146                                          
SITE     1 FC3 11 ASN A 914  THR A 916  PHE A 933  GLY A 935                    
SITE     2 FC3 11 VAL A 937  GLY A 938  PRO A 939  GLN A 940                    
SITE     3 FC3 11 THR A 941   CD A1111  NAG A1149                               
SITE     1 FC4  7 GLY A 248  GLY A 308  VAL A 937  NAG A1148                    
SITE     2 FC4  7 BMA A1150  MAN A1153  HOH A3257                               
SITE     1 FC5  8 GLY A 246  GLY A 248  ASP A 771  TYR A 772                    
SITE     2 FC5  8 NAG A1149  MAN A1151  MAN A1152  HOH A3122                    
SITE     1 FC6  5 GLY A 246  TYR A 772  BMA A1150  MAN A1156                    
SITE     2 FC6  5 MAN A1157                                                     
SITE     1 FC7  7 PRO A 245  GLY A 246  ALA A 251  BMA A1150                    
SITE     2 FC7  7 MAN A1153  MAN A1154  HOH A3094                               
SITE     1 FC8  9 GLY A 248  THR A 249  ALA A 267  GLY A 308                    
SITE     2 FC8  9 GLY A 309  PRO A 310  NAG A1149  MAN A1152                    
SITE     3 FC8  9 MAN A1154                                                     
SITE     1 FC9  6 ASP A 265  GLY A 308  MAN A1152  MAN A1153                    
SITE     2 FC9  6 MAN A1155  HOH A3264                                          
SITE     1 GC1  3 ASP A 771  MAN A1154  HOH A3264                               
SITE     1 GC2  4 GLY A 241  SER A 247  GLN A 288  MAN A1151                    
SITE     1 GC3  1 MAN A1151                                                     
SITE     1 GC4  6 GLU A 112  LYS A 848  GLU A 994  PRO A 996                    
SITE     2 GC4  6 BMA A1159  BMA A1160                                          
SITE     1 GC5  5 GLY A 113  GLU A 994  GLN A 995  NAG A1158                    
SITE     2 GC5  5 NAG A1161                                                     
SITE     1 GC6  6 ARG A 110  LYS A 848  GLU A 999   CD A1102                    
SITE     2 GC6  6 NAG A1158  BMA A1162                                          
SITE     1 GC7  6 PRO A 119  PRO A 993  GLU A 994  GLN A 995                    
SITE     2 GC7  6 BMA A1159  M6D A1163                                          
SITE     1 GC8  2 ARG A 110  BMA A1160                                          
SITE     1 GC9  6 ASP A 122  ARG A 953   CD A1129  NAG A1161                    
SITE     2 GC9  6 NAG A1164  HOH A3280                                          
SITE     1 HC1  4  CD A1101  M6D A1163  BMA A1165  HOH A3214                    
SITE     1 HC2  8 LEU A  79  GLU A 126  ASP A 899  LYS A 902                    
SITE     2 HC2  8  CD A1101   CD A1128  NAG A1164  NAG A1166                    
SITE     1 HC3  6 HIS A 609  ASP A 899  PRO A 901  LYS A 902                    
SITE     2 HC3  6 ARG A 953  BMA A1165                                          
CRYST1  146.380  146.380  136.330  90.00  90.00 120.00 P 32 2 1      6          
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      0.006832  0.003944  0.000000        0.00000                         
SCALE2      0.000000  0.007888  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007335        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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