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Database: PDB
Entry: 5UN8
LinkDB: 5UN8
Original site: 5UN8 
HEADER    HYDROLASE                               30-JAN-17   5UN8              
TITLE     CRYSTAL STRUCTURE OF HUMAN O-GLCNACASE IN COMPLEX WITH GLYCOPEPTIDE   
TITLE    2 P53                                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN O-GLCNACASE;                                       
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 60-400 AND 553-704;                           
COMPND   5 SYNONYM: OGA,BETA-N-ACETYLGLUCOSAMINIDASE,BETA-N-                    
COMPND   6 ACETYLHEXOSAMINIDASE,BETA-HEXOSAMINIDASE,MENINGIOMA-EXPRESSED ANTIGEN
COMPND   7 5,N-ACETYL-BETA-D-GLUCOSAMINIDASE,N-ACETYL-BETA-GLUCOSAMINIDASE,     
COMPND   8 NUCLEAR CYTOPLASMIC O-GLCNACASE AND ACETYLTRANSFERASE,NCOAT;         
COMPND   9 EC: 3.2.1.169,3.2.1.-;                                               
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 2;                                                           
COMPND  12 MOLECULE: P53 PEPTIDE;                                               
COMPND  13 CHAIN: E, F, G, H;                                                   
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 OTHER_DETAILS: SER WAS O-GLCNACYLATED; NAG STANDS FOR O-GLCNAC       
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MGEA5, HEXC, KIAA0679, MEA5;                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI-PICHIA PASTORIS SHUTTLE VECTOR   
SOURCE   7 PPPARG4;                                                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 1182032;                                    
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 SYNTHETIC: YES;                                                      
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_TAXID: 9606                                                 
KEYWDS    HUMAN O-GLCNACASE; GLYCOPEPTIDE, HYDROLASE                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.LI,J.JIANG                                                          
REVDAT   3   19-APR-17 5UN8    1       JRNL                                     
REVDAT   2   05-APR-17 5UN8    1       JRNL                                     
REVDAT   1   15-MAR-17 5UN8    0                                                
JRNL        AUTH   B.LI,H.LI,L.LU,J.JIANG                                       
JRNL        TITL   STRUCTURES OF HUMAN O-GLCNACASE AND ITS COMPLEXES REVEAL A   
JRNL        TITL 2 NEW SUBSTRATE RECOGNITION MODE.                              
JRNL        REF    NAT. STRUCT. MOL. BIOL.       V.  24   362 2017              
JRNL        REFN                   ESSN 1545-9985                               
JRNL        PMID   28319083                                                     
JRNL        DOI    10.1038/NSMB.3390                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.13 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0131                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.13                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 148.24                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 128753                         
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) : 0.187                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6796                            
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) : 2.13                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.19                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7287                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 74.42                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2650                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 403                          
REMARK   3   BIN FREE R VALUE                    : 0.2950                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 14264                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 56                                      
REMARK   3   SOLVENT ATOMS            : 1232                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.02                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.22000                                             
REMARK   3    B22 (A**2) : -0.10000                                             
REMARK   3    B33 (A**2) : 0.36000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.19000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.195         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.175         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.125         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.878         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 14717 ; 0.020 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 19930 ; 1.874 ; 1.953       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1718 ; 6.401 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   706 ;35.428 ;23.541       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2493 ;15.629 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    92 ;15.540 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2111 ; 0.127 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11202 ; 0.010 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  6938 ; 2.719 ; 2.704       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8634 ; 3.925 ; 4.032       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  7779 ; 4.344 ; 3.048       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 24271 ; 8.143 ;24.029       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : MASK                                                 
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: NULL                                      
REMARK   4                                                                      
REMARK   4 5UN8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000224404.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-JUN-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.978                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 139265                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.130                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 148.240                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.14                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
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: 5TKE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.93                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.032 M AMMONIUM CITRATE TRIBASIC (PH    
REMARK 280  7.0), 0.02 M MES MONOHYDRATE, 0.016 M IMIDAZOLE, 0.002 M ZINC       
REMARK 280  SULFATE HEPTAHYDRATE, 0.128 M POTASSIUM THIOCYANATE, 12.8% W/V      
REMARK 280  POLYETHYLENE GLYCOL 3,350, 3.2% W/V POLYETHYLENE GLYCOL             
REMARK 280  MONOMETHYL ETHER 2,000, AND 5% W/V POLYETHYLENE GLYCOL              
REMARK 280  MONOMETHYL ETHER 550., EVAPORATION, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       47.69650            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, E, G                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9820 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 33440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, F, H                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   334                                                      
REMARK 465     ASN A   335                                                      
REMARK 465     MET A   336                                                      
REMARK 465     ASN A   337                                                      
REMARK 465     GLY A   338                                                      
REMARK 465     VAL A   339                                                      
REMARK 465     ARG A   340                                                      
REMARK 465     LYS A   341                                                      
REMARK 465     ASP A   342                                                      
REMARK 465     VAL A   343                                                      
REMARK 465     VAL A   344                                                      
REMARK 465     MET A   345                                                      
REMARK 465     THR A   346                                                      
REMARK 465     ASP A   347                                                      
REMARK 465     SER A   348                                                      
REMARK 465     GLU A   349                                                      
REMARK 465     ASP A   350                                                      
REMARK 465     SER A   351                                                      
REMARK 465     THR A   352                                                      
REMARK 465     VAL A   353                                                      
REMARK 465     SER A   354                                                      
REMARK 465     ILE A   355                                                      
REMARK 465     GLN A   356                                                      
REMARK 465     ILE A   357                                                      
REMARK 465     LYS A   358                                                      
REMARK 465     LEU A   359                                                      
REMARK 465     GLU A   360                                                      
REMARK 465     ASN A   361                                                      
REMARK 465     GLU A   362                                                      
REMARK 465     GLY A   363                                                      
REMARK 465     SER A   364                                                      
REMARK 465     ASP A   365                                                      
REMARK 465     GLU A   366                                                      
REMARK 465     ASP A   367                                                      
REMARK 465     ILE A   368                                                      
REMARK 465     GLU A   369                                                      
REMARK 465     THR A   370                                                      
REMARK 465     ASP A   371                                                      
REMARK 465     VAL A   372                                                      
REMARK 465     LEU A   373                                                      
REMARK 465     SER A   541                                                      
REMARK 465     ARG A   542                                                      
REMARK 465     GLY A   543                                                      
REMARK 465     GLY A   544                                                      
REMARK 465     GLY A   545                                                      
REMARK 465     GLY A   546                                                      
REMARK 465     SER A   547                                                      
REMARK 465     GLY A   548                                                      
REMARK 465     GLY A   549                                                      
REMARK 465     GLY A   550                                                      
REMARK 465     GLY A   551                                                      
REMARK 465     SER A   552                                                      
REMARK 465     SER A   593                                                      
REMARK 465     VAL A   594                                                      
REMARK 465     ASN A   595                                                      
REMARK 465     CYS A   596                                                      
REMARK 465     LYS A   597                                                      
REMARK 465     GLY A   598                                                      
REMARK 465     LYS A   599                                                      
REMARK 465     ASP A   600                                                      
REMARK 465     SER A   601                                                      
REMARK 465     GLU A   602                                                      
REMARK 465     LYS A   603                                                      
REMARK 465     HIS A   666                                                      
REMARK 465     SER A   667                                                      
REMARK 465     SER A   668                                                      
REMARK 465     ALA A   669                                                      
REMARK 465     GLN A   670                                                      
REMARK 465     PHE A   671                                                      
REMARK 465     LEU A   672                                                      
REMARK 465     ILE A   673                                                      
REMARK 465     GLY A   674                                                      
REMARK 465     ASP A   675                                                      
REMARK 465     GLN A   676                                                      
REMARK 465     GLU A   677                                                      
REMARK 465     PRO A   678                                                      
REMARK 465     LEU A   701                                                      
REMARK 465     PHE A   702                                                      
REMARK 465     PHE A   703                                                      
REMARK 465     GLN A   704                                                      
REMARK 465     SER B   334                                                      
REMARK 465     ASN B   335                                                      
REMARK 465     MET B   336                                                      
REMARK 465     ASN B   337                                                      
REMARK 465     GLY B   338                                                      
REMARK 465     VAL B   339                                                      
REMARK 465     ARG B   340                                                      
REMARK 465     LYS B   341                                                      
REMARK 465     ASP B   342                                                      
REMARK 465     VAL B   343                                                      
REMARK 465     VAL B   344                                                      
REMARK 465     MET B   345                                                      
REMARK 465     THR B   346                                                      
REMARK 465     ASP B   347                                                      
REMARK 465     SER B   348                                                      
REMARK 465     GLU B   349                                                      
REMARK 465     ASP B   350                                                      
REMARK 465     SER B   351                                                      
REMARK 465     THR B   352                                                      
REMARK 465     VAL B   353                                                      
REMARK 465     SER B   354                                                      
REMARK 465     ILE B   355                                                      
REMARK 465     GLN B   356                                                      
REMARK 465     ILE B   357                                                      
REMARK 465     LYS B   358                                                      
REMARK 465     LEU B   359                                                      
REMARK 465     GLU B   360                                                      
REMARK 465     ASN B   361                                                      
REMARK 465     GLU B   362                                                      
REMARK 465     GLY B   363                                                      
REMARK 465     SER B   364                                                      
REMARK 465     ASP B   365                                                      
REMARK 465     GLU B   366                                                      
REMARK 465     ASP B   367                                                      
REMARK 465     ILE B   368                                                      
REMARK 465     GLU B   369                                                      
REMARK 465     THR B   370                                                      
REMARK 465     ASP B   371                                                      
REMARK 465     VAL B   372                                                      
REMARK 465     LEU B   373                                                      
REMARK 465     SER B   541                                                      
REMARK 465     ARG B   542                                                      
REMARK 465     GLY B   543                                                      
REMARK 465     GLY B   544                                                      
REMARK 465     GLY B   545                                                      
REMARK 465     GLY B   546                                                      
REMARK 465     SER B   547                                                      
REMARK 465     GLY B   548                                                      
REMARK 465     GLY B   549                                                      
REMARK 465     GLY B   550                                                      
REMARK 465     GLY B   551                                                      
REMARK 465     SER B   593                                                      
REMARK 465     VAL B   594                                                      
REMARK 465     ASN B   595                                                      
REMARK 465     CYS B   596                                                      
REMARK 465     LYS B   597                                                      
REMARK 465     GLY B   598                                                      
REMARK 465     LYS B   599                                                      
REMARK 465     ASP B   600                                                      
REMARK 465     SER B   601                                                      
REMARK 465     GLU B   602                                                      
REMARK 465     HIS B   666                                                      
REMARK 465     SER B   667                                                      
REMARK 465     SER B   668                                                      
REMARK 465     ALA B   669                                                      
REMARK 465     GLN B   670                                                      
REMARK 465     PHE B   671                                                      
REMARK 465     LEU B   672                                                      
REMARK 465     ILE B   673                                                      
REMARK 465     GLY B   674                                                      
REMARK 465     ASP B   675                                                      
REMARK 465     GLN B   676                                                      
REMARK 465     GLU B   677                                                      
REMARK 465     PRO B   678                                                      
REMARK 465     LEU B   701                                                      
REMARK 465     PHE B   702                                                      
REMARK 465     PHE B   703                                                      
REMARK 465     GLN B   704                                                      
REMARK 465     ASN C   337                                                      
REMARK 465     GLY C   338                                                      
REMARK 465     VAL C   339                                                      
REMARK 465     ARG C   340                                                      
REMARK 465     LYS C   341                                                      
REMARK 465     ASP C   342                                                      
REMARK 465     VAL C   343                                                      
REMARK 465     VAL C   344                                                      
REMARK 465     MET C   345                                                      
REMARK 465     THR C   346                                                      
REMARK 465     ASP C   347                                                      
REMARK 465     SER C   348                                                      
REMARK 465     GLU C   349                                                      
REMARK 465     ASP C   350                                                      
REMARK 465     SER C   351                                                      
REMARK 465     THR C   352                                                      
REMARK 465     VAL C   353                                                      
REMARK 465     SER C   354                                                      
REMARK 465     ILE C   355                                                      
REMARK 465     GLN C   356                                                      
REMARK 465     ILE C   357                                                      
REMARK 465     LYS C   358                                                      
REMARK 465     LEU C   359                                                      
REMARK 465     GLU C   360                                                      
REMARK 465     ASN C   361                                                      
REMARK 465     GLU C   362                                                      
REMARK 465     GLY C   363                                                      
REMARK 465     SER C   364                                                      
REMARK 465     ASP C   365                                                      
REMARK 465     GLU C   366                                                      
REMARK 465     ASP C   367                                                      
REMARK 465     ILE C   368                                                      
REMARK 465     GLU C   369                                                      
REMARK 465     THR C   370                                                      
REMARK 465     ASP C   371                                                      
REMARK 465     VAL C   372                                                      
REMARK 465     GLY C   534                                                      
REMARK 465     VAL C   535                                                      
REMARK 465     PRO C   536                                                      
REMARK 465     HIS C   537                                                      
REMARK 465     GLN C   538                                                      
REMARK 465     TYR C   539                                                      
REMARK 465     SER C   540                                                      
REMARK 465     SER C   541                                                      
REMARK 465     ARG C   542                                                      
REMARK 465     GLY C   543                                                      
REMARK 465     GLY C   544                                                      
REMARK 465     GLY C   545                                                      
REMARK 465     GLY C   546                                                      
REMARK 465     SER C   547                                                      
REMARK 465     GLY C   548                                                      
REMARK 465     GLY C   549                                                      
REMARK 465     GLY C   550                                                      
REMARK 465     GLY C   551                                                      
REMARK 465     SER C   593                                                      
REMARK 465     VAL C   594                                                      
REMARK 465     ASN C   595                                                      
REMARK 465     CYS C   596                                                      
REMARK 465     LYS C   597                                                      
REMARK 465     GLY C   598                                                      
REMARK 465     LYS C   599                                                      
REMARK 465     ASP C   600                                                      
REMARK 465     SER C   601                                                      
REMARK 465     GLU C   602                                                      
REMARK 465     LYS C   603                                                      
REMARK 465     ILE C   695                                                      
REMARK 465     ASP C   696                                                      
REMARK 465     GLY C   697                                                      
REMARK 465     ALA C   698                                                      
REMARK 465     ASN C   699                                                      
REMARK 465     ASP C   700                                                      
REMARK 465     LEU C   701                                                      
REMARK 465     PHE C   702                                                      
REMARK 465     PHE C   703                                                      
REMARK 465     GLN C   704                                                      
REMARK 465     ASN D   337                                                      
REMARK 465     GLY D   338                                                      
REMARK 465     VAL D   339                                                      
REMARK 465     ARG D   340                                                      
REMARK 465     LYS D   341                                                      
REMARK 465     ASP D   342                                                      
REMARK 465     VAL D   343                                                      
REMARK 465     VAL D   344                                                      
REMARK 465     MET D   345                                                      
REMARK 465     THR D   346                                                      
REMARK 465     ASP D   347                                                      
REMARK 465     SER D   348                                                      
REMARK 465     GLU D   349                                                      
REMARK 465     ASP D   350                                                      
REMARK 465     SER D   351                                                      
REMARK 465     THR D   352                                                      
REMARK 465     VAL D   353                                                      
REMARK 465     SER D   354                                                      
REMARK 465     ILE D   355                                                      
REMARK 465     GLN D   356                                                      
REMARK 465     ILE D   357                                                      
REMARK 465     LYS D   358                                                      
REMARK 465     LEU D   359                                                      
REMARK 465     GLU D   360                                                      
REMARK 465     ASN D   361                                                      
REMARK 465     GLU D   362                                                      
REMARK 465     GLY D   363                                                      
REMARK 465     SER D   364                                                      
REMARK 465     ASP D   365                                                      
REMARK 465     GLU D   366                                                      
REMARK 465     ASP D   367                                                      
REMARK 465     ILE D   368                                                      
REMARK 465     GLU D   369                                                      
REMARK 465     THR D   370                                                      
REMARK 465     ASP D   371                                                      
REMARK 465     VAL D   372                                                      
REMARK 465     GLY D   534                                                      
REMARK 465     VAL D   535                                                      
REMARK 465     PRO D   536                                                      
REMARK 465     HIS D   537                                                      
REMARK 465     GLN D   538                                                      
REMARK 465     TYR D   539                                                      
REMARK 465     SER D   540                                                      
REMARK 465     SER D   541                                                      
REMARK 465     ARG D   542                                                      
REMARK 465     GLY D   543                                                      
REMARK 465     GLY D   544                                                      
REMARK 465     GLY D   545                                                      
REMARK 465     GLY D   546                                                      
REMARK 465     SER D   547                                                      
REMARK 465     GLY D   548                                                      
REMARK 465     GLY D   549                                                      
REMARK 465     GLY D   550                                                      
REMARK 465     GLY D   551                                                      
REMARK 465     SER D   593                                                      
REMARK 465     VAL D   594                                                      
REMARK 465     ASN D   595                                                      
REMARK 465     CYS D   596                                                      
REMARK 465     LYS D   597                                                      
REMARK 465     GLY D   598                                                      
REMARK 465     LYS D   599                                                      
REMARK 465     ASP D   600                                                      
REMARK 465     SER D   601                                                      
REMARK 465     GLU D   602                                                      
REMARK 465     LYS D   603                                                      
REMARK 465     ILE D   695                                                      
REMARK 465     ASP D   696                                                      
REMARK 465     GLY D   697                                                      
REMARK 465     ALA D   698                                                      
REMARK 465     ASN D   699                                                      
REMARK 465     ASP D   700                                                      
REMARK 465     LEU D   701                                                      
REMARK 465     PHE D   702                                                      
REMARK 465     PHE D   703                                                      
REMARK 465     GLN D   704                                                      
REMARK 465     GLN E   144                                                      
REMARK 465     LEU E   145                                                      
REMARK 465     PRO E   153                                                      
REMARK 465     GLY E   154                                                      
REMARK 465     GLN F   144                                                      
REMARK 465     LEU F   145                                                      
REMARK 465     GLY F   154                                                      
REMARK 465     GLN G   144                                                      
REMARK 465     LEU G   145                                                      
REMARK 465     GLN H   144                                                      
REMARK 465     LEU H   145                                                      
REMARK 465     GLY H   154                                                      
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   O    HOH A  1086     O    HOH A  1111              2.03            
REMARK 500   O    HOH A  1039     O    HOH A  1061              2.03            
REMARK 500   O    HOH B   844     O    HOH D   818              2.04            
REMARK 500   NE2  HIS D   666     O    HOH D   801              2.06            
REMARK 500   O    HOH B   804     O    HOH B   810              2.09            
REMARK 500   CB   SER C   231     O    HOH C   801              2.09            
REMARK 500   O    HOH B  1037     O    HOH B  1057              2.14            
REMARK 500   SG   CYS D   663     O    HOH D   801              2.14            
REMARK 500   N    LYS B   603     O    HOH B   801              2.16            
REMARK 500   O    HOH A  1055     O    HOH A  1067              2.16            
REMARK 500   O    HOH A  1055     O    HOH A  1070              2.17            
REMARK 500   N    HIS B    59     O    HOH B   802              2.18            
REMARK 500   OG   SER C   231     O    HOH C   801              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   SG   CYS A   663     SG   CYS C   663     2856     1.53            
REMARK 500   SG   CYS B   663     O    HOH D   801     2755     2.13            
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    CYS A 663   CA    CYS A 663   CB      0.132                       
REMARK 500    CYS A 663   CB    CYS A 663   SG      0.205                       
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    ARG A  83   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    CYS A 663   N   -  CA  -  CB  ANGL. DEV. =   9.1 DEGREES          
REMARK 500    CYS A 663   CA  -  CB  -  SG  ANGL. DEV. =  35.0 DEGREES          
REMARK 500    CYS A 663   N   -  CA  -  C   ANGL. DEV. = -16.8 DEGREES          
REMARK 500    ARG B  83   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG B  83   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG B 127   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ASP C 100   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    MET C 640   CG  -  SD  -  CE  ANGL. DEV. = -10.1 DEGREES          
REMARK 500    CYS C 663   CB  -  CA  -  C   ANGL. DEV. =  10.7 DEGREES          
REMARK 500    ARG D 104   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    MET D 640   CG  -  SD  -  CE  ANGL. DEV. = -11.9 DEGREES          
REMARK 500    ARG D 691   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG D 691   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.9 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    ALA A  96       48.72   -156.23                                   
REMARK 500    ARG A 104      -78.13   -144.80                                   
REMARK 500    PRO A 314     -158.86   -102.46                                   
REMARK 500    TYR A 566      -84.70    -96.43                                   
REMARK 500    ARG A 664      -49.15    -27.23                                   
REMARK 500    ALA B  96       48.40   -151.41                                   
REMARK 500    ARG B 104      -71.85   -136.50                                   
REMARK 500    PHE B 106       51.17   -116.48                                   
REMARK 500    PRO B 314     -162.21   -101.27                                   
REMARK 500    TYR B 566      -86.74    -98.94                                   
REMARK 500    PRO B 694       -6.13    -59.05                                   
REMARK 500    ALA C  96       43.36   -151.32                                   
REMARK 500    ARG C 104      -70.60   -145.85                                   
REMARK 500    ASP C 142        6.42   -152.52                                   
REMARK 500    HIS C 178        9.29    -69.93                                   
REMARK 500    LYS C 272       35.57     73.93                                   
REMARK 500    PRO C 314     -159.37    -99.31                                   
REMARK 500    ASN C 335       29.17   -153.54                                   
REMARK 500    TYR C 566      -87.86    -99.80                                   
REMARK 500    ALA D  96       42.74   -149.46                                   
REMARK 500    ARG D 104      -70.83   -139.00                                   
REMARK 500    ASP D 142       11.11   -150.66                                   
REMARK 500    LYS D 272       32.33     70.05                                   
REMARK 500    ASN D 335       30.16   -143.66                                   
REMARK 500    TYR D 566      -88.39    -99.34                                   
REMARK 500    ASP F 148     -172.09   -173.46                                   
REMARK 500    PRO G 152      159.34    -49.69                                   
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 Mono-Saccharide NAG E 200 bound   
REMARK 800  to SER E 149                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG F 200 bound   
REMARK 800  to SER F 149                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG G 200 bound   
REMARK 800  to SER G 149                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG H 200 bound   
REMARK 800  to SER H 149                                                        
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5UN9   RELATED DB: PDB                                   
DBREF  5UN8 A   60   542  UNP    O60502   OGA_HUMAN       60    400             
DBREF  5UN8 A  553   704  UNP    O60502   OGA_HUMAN      553    704             
DBREF  5UN8 B   60   542  UNP    O60502   OGA_HUMAN       60    400             
DBREF  5UN8 B  553   704  UNP    O60502   OGA_HUMAN      553    704             
DBREF  5UN8 C   60   542  UNP    O60502   OGA_HUMAN       60    400             
DBREF  5UN8 C  553   704  UNP    O60502   OGA_HUMAN      553    704             
DBREF  5UN8 D   60   542  UNP    O60502   OGA_HUMAN       60    400             
DBREF  5UN8 D  553   704  UNP    O60502   OGA_HUMAN      553    704             
DBREF  5UN8 E  144   154  PDB    5UN8     5UN8           144    154             
DBREF  5UN8 F  144   154  PDB    5UN8     5UN8           144    154             
DBREF  5UN8 G  144   154  PDB    5UN8     5UN8           144    154             
DBREF  5UN8 H  144   154  PDB    5UN8     5UN8           144    154             
SEQADV 5UN8 HIS A   59  UNP  O60502              EXPRESSION TAG                 
SEQADV 5UN8 ASN A  175  UNP  O60502    ASP   175 CONFLICT                       
SEQADV 5UN8 GLY A  543  UNP  O60502              LINKER                         
SEQADV 5UN8 GLY A  544  UNP  O60502              LINKER                         
SEQADV 5UN8 GLY A  545  UNP  O60502              LINKER                         
SEQADV 5UN8 GLY A  546  UNP  O60502              LINKER                         
SEQADV 5UN8 SER A  547  UNP  O60502              LINKER                         
SEQADV 5UN8 GLY A  548  UNP  O60502              LINKER                         
SEQADV 5UN8 GLY A  549  UNP  O60502              LINKER                         
SEQADV 5UN8 GLY A  550  UNP  O60502              LINKER                         
SEQADV 5UN8 GLY A  551  UNP  O60502              LINKER                         
SEQADV 5UN8 SER A  552  UNP  O60502              LINKER                         
SEQADV 5UN8 HIS B   59  UNP  O60502              EXPRESSION TAG                 
SEQADV 5UN8 ASN B  175  UNP  O60502    ASP   175 CONFLICT                       
SEQADV 5UN8 GLY B  543  UNP  O60502              LINKER                         
SEQADV 5UN8 GLY B  544  UNP  O60502              LINKER                         
SEQADV 5UN8 GLY B  545  UNP  O60502              LINKER                         
SEQADV 5UN8 GLY B  546  UNP  O60502              LINKER                         
SEQADV 5UN8 SER B  547  UNP  O60502              LINKER                         
SEQADV 5UN8 GLY B  548  UNP  O60502              LINKER                         
SEQADV 5UN8 GLY B  549  UNP  O60502              LINKER                         
SEQADV 5UN8 GLY B  550  UNP  O60502              LINKER                         
SEQADV 5UN8 GLY B  551  UNP  O60502              LINKER                         
SEQADV 5UN8 SER B  552  UNP  O60502              LINKER                         
SEQADV 5UN8 HIS C   59  UNP  O60502              EXPRESSION TAG                 
SEQADV 5UN8 ASN C  175  UNP  O60502    ASP   175 CONFLICT                       
SEQADV 5UN8 GLY C  543  UNP  O60502              LINKER                         
SEQADV 5UN8 GLY C  544  UNP  O60502              LINKER                         
SEQADV 5UN8 GLY C  545  UNP  O60502              LINKER                         
SEQADV 5UN8 GLY C  546  UNP  O60502              LINKER                         
SEQADV 5UN8 SER C  547  UNP  O60502              LINKER                         
SEQADV 5UN8 GLY C  548  UNP  O60502              LINKER                         
SEQADV 5UN8 GLY C  549  UNP  O60502              LINKER                         
SEQADV 5UN8 GLY C  550  UNP  O60502              LINKER                         
SEQADV 5UN8 GLY C  551  UNP  O60502              LINKER                         
SEQADV 5UN8 SER C  552  UNP  O60502              LINKER                         
SEQADV 5UN8 HIS D   59  UNP  O60502              EXPRESSION TAG                 
SEQADV 5UN8 ASN D  175  UNP  O60502    ASP   175 CONFLICT                       
SEQADV 5UN8 GLY D  543  UNP  O60502              LINKER                         
SEQADV 5UN8 GLY D  544  UNP  O60502              LINKER                         
SEQADV 5UN8 GLY D  545  UNP  O60502              LINKER                         
SEQADV 5UN8 GLY D  546  UNP  O60502              LINKER                         
SEQADV 5UN8 SER D  547  UNP  O60502              LINKER                         
SEQADV 5UN8 GLY D  548  UNP  O60502              LINKER                         
SEQADV 5UN8 GLY D  549  UNP  O60502              LINKER                         
SEQADV 5UN8 GLY D  550  UNP  O60502              LINKER                         
SEQADV 5UN8 GLY D  551  UNP  O60502              LINKER                         
SEQADV 5UN8 SER D  552  UNP  O60502              LINKER                         
SEQRES   1 A  504  HIS PHE LEU CYS GLY VAL VAL GLU GLY PHE TYR GLY ARG          
SEQRES   2 A  504  PRO TRP VAL MET GLU GLN ARG LYS GLU LEU PHE ARG ARG          
SEQRES   3 A  504  LEU GLN LYS TRP GLU LEU ASN THR TYR LEU TYR ALA PRO          
SEQRES   4 A  504  LYS ASP ASP TYR LYS HIS ARG MET PHE TRP ARG GLU MET          
SEQRES   5 A  504  TYR SER VAL GLU GLU ALA GLU GLN LEU MET THR LEU ILE          
SEQRES   6 A  504  SER ALA ALA ARG GLU TYR GLU ILE GLU PHE ILE TYR ALA          
SEQRES   7 A  504  ILE SER PRO GLY LEU ASP ILE THR PHE SER ASN PRO LYS          
SEQRES   8 A  504  GLU VAL SER THR LEU LYS ARG LYS LEU ASP GLN VAL SER          
SEQRES   9 A  504  GLN PHE GLY CYS ARG SER PHE ALA LEU LEU PHE ASP ASN          
SEQRES  10 A  504  ILE ASP HIS ASN MET CYS ALA ALA ASP LYS GLU VAL PHE          
SEQRES  11 A  504  SER SER PHE ALA HIS ALA GLN VAL SER ILE THR ASN GLU          
SEQRES  12 A  504  ILE TYR GLN TYR LEU GLY GLU PRO GLU THR PHE LEU PHE          
SEQRES  13 A  504  CYS PRO THR GLU TYR CYS GLY THR PHE CYS TYR PRO ASN          
SEQRES  14 A  504  VAL SER GLN SER PRO TYR LEU ARG THR VAL GLY GLU LYS          
SEQRES  15 A  504  LEU LEU PRO GLY ILE GLU VAL LEU TRP THR GLY PRO LYS          
SEQRES  16 A  504  VAL VAL SER LYS GLU ILE PRO VAL GLU SER ILE GLU GLU          
SEQRES  17 A  504  VAL SER LYS ILE ILE LYS ARG ALA PRO VAL ILE TRP ASP          
SEQRES  18 A  504  ASN ILE HIS ALA ASN ASP TYR ASP GLN LYS ARG LEU PHE          
SEQRES  19 A  504  LEU GLY PRO TYR LYS GLY ARG SER THR GLU LEU ILE PRO          
SEQRES  20 A  504  ARG LEU LYS GLY VAL LEU THR ASN PRO ASN CYS GLU PHE          
SEQRES  21 A  504  GLU ALA ASN TYR VAL ALA ILE HIS THR LEU ALA THR TRP          
SEQRES  22 A  504  TYR LYS SER ASN MET ASN GLY VAL ARG LYS ASP VAL VAL          
SEQRES  23 A  504  MET THR ASP SER GLU ASP SER THR VAL SER ILE GLN ILE          
SEQRES  24 A  504  LYS LEU GLU ASN GLU GLY SER ASP GLU ASP ILE GLU THR          
SEQRES  25 A  504  ASP VAL LEU TYR SER PRO GLN MET ALA LEU LYS LEU ALA          
SEQRES  26 A  504  LEU THR GLU TRP LEU GLN GLU PHE GLY VAL PRO HIS GLN          
SEQRES  27 A  504  TYR SER SER ARG GLY GLY GLY GLY SER GLY GLY GLY GLY          
SEQRES  28 A  504  SER VAL THR LEU GLU ASP LEU GLN LEU LEU ALA ASP LEU          
SEQRES  29 A  504  PHE TYR LEU PRO TYR GLU HIS GLY PRO LYS GLY ALA GLN          
SEQRES  30 A  504  MET LEU ARG GLU PHE GLN TRP LEU ARG ALA ASN SER SER          
SEQRES  31 A  504  VAL VAL SER VAL ASN CYS LYS GLY LYS ASP SER GLU LYS          
SEQRES  32 A  504  ILE GLU GLU TRP ARG SER ARG ALA ALA LYS PHE GLU GLU          
SEQRES  33 A  504  MET CYS GLY LEU VAL MET GLY MET PHE THR ARG LEU SER          
SEQRES  34 A  504  ASN CYS ALA ASN ARG THR ILE LEU TYR ASP MET TYR SER          
SEQRES  35 A  504  TYR VAL TRP ASP ILE LYS SER ILE MET SER MET VAL LYS          
SEQRES  36 A  504  SER PHE VAL GLN TRP LEU GLY CYS ARG SER HIS SER SER          
SEQRES  37 A  504  ALA GLN PHE LEU ILE GLY ASP GLN GLU PRO TRP ALA PHE          
SEQRES  38 A  504  ARG GLY GLY LEU ALA GLY GLU PHE GLN ARG LEU LEU PRO          
SEQRES  39 A  504  ILE ASP GLY ALA ASN ASP LEU PHE PHE GLN                      
SEQRES   1 B  504  HIS PHE LEU CYS GLY VAL VAL GLU GLY PHE TYR GLY ARG          
SEQRES   2 B  504  PRO TRP VAL MET GLU GLN ARG LYS GLU LEU PHE ARG ARG          
SEQRES   3 B  504  LEU GLN LYS TRP GLU LEU ASN THR TYR LEU TYR ALA PRO          
SEQRES   4 B  504  LYS ASP ASP TYR LYS HIS ARG MET PHE TRP ARG GLU MET          
SEQRES   5 B  504  TYR SER VAL GLU GLU ALA GLU GLN LEU MET THR LEU ILE          
SEQRES   6 B  504  SER ALA ALA ARG GLU TYR GLU ILE GLU PHE ILE TYR ALA          
SEQRES   7 B  504  ILE SER PRO GLY LEU ASP ILE THR PHE SER ASN PRO LYS          
SEQRES   8 B  504  GLU VAL SER THR LEU LYS ARG LYS LEU ASP GLN VAL SER          
SEQRES   9 B  504  GLN PHE GLY CYS ARG SER PHE ALA LEU LEU PHE ASP ASN          
SEQRES  10 B  504  ILE ASP HIS ASN MET CYS ALA ALA ASP LYS GLU VAL PHE          
SEQRES  11 B  504  SER SER PHE ALA HIS ALA GLN VAL SER ILE THR ASN GLU          
SEQRES  12 B  504  ILE TYR GLN TYR LEU GLY GLU PRO GLU THR PHE LEU PHE          
SEQRES  13 B  504  CYS PRO THR GLU TYR CYS GLY THR PHE CYS TYR PRO ASN          
SEQRES  14 B  504  VAL SER GLN SER PRO TYR LEU ARG THR VAL GLY GLU LYS          
SEQRES  15 B  504  LEU LEU PRO GLY ILE GLU VAL LEU TRP THR GLY PRO LYS          
SEQRES  16 B  504  VAL VAL SER LYS GLU ILE PRO VAL GLU SER ILE GLU GLU          
SEQRES  17 B  504  VAL SER LYS ILE ILE LYS ARG ALA PRO VAL ILE TRP ASP          
SEQRES  18 B  504  ASN ILE HIS ALA ASN ASP TYR ASP GLN LYS ARG LEU PHE          
SEQRES  19 B  504  LEU GLY PRO TYR LYS GLY ARG SER THR GLU LEU ILE PRO          
SEQRES  20 B  504  ARG LEU LYS GLY VAL LEU THR ASN PRO ASN CYS GLU PHE          
SEQRES  21 B  504  GLU ALA ASN TYR VAL ALA ILE HIS THR LEU ALA THR TRP          
SEQRES  22 B  504  TYR LYS SER ASN MET ASN GLY VAL ARG LYS ASP VAL VAL          
SEQRES  23 B  504  MET THR ASP SER GLU ASP SER THR VAL SER ILE GLN ILE          
SEQRES  24 B  504  LYS LEU GLU ASN GLU GLY SER ASP GLU ASP ILE GLU THR          
SEQRES  25 B  504  ASP VAL LEU TYR SER PRO GLN MET ALA LEU LYS LEU ALA          
SEQRES  26 B  504  LEU THR GLU TRP LEU GLN GLU PHE GLY VAL PRO HIS GLN          
SEQRES  27 B  504  TYR SER SER ARG GLY GLY GLY GLY SER GLY GLY GLY GLY          
SEQRES  28 B  504  SER VAL THR LEU GLU ASP LEU GLN LEU LEU ALA ASP LEU          
SEQRES  29 B  504  PHE TYR LEU PRO TYR GLU HIS GLY PRO LYS GLY ALA GLN          
SEQRES  30 B  504  MET LEU ARG GLU PHE GLN TRP LEU ARG ALA ASN SER SER          
SEQRES  31 B  504  VAL VAL SER VAL ASN CYS LYS GLY LYS ASP SER GLU LYS          
SEQRES  32 B  504  ILE GLU GLU TRP ARG SER ARG ALA ALA LYS PHE GLU GLU          
SEQRES  33 B  504  MET CYS GLY LEU VAL MET GLY MET PHE THR ARG LEU SER          
SEQRES  34 B  504  ASN CYS ALA ASN ARG THR ILE LEU TYR ASP MET TYR SER          
SEQRES  35 B  504  TYR VAL TRP ASP ILE LYS SER ILE MET SER MET VAL LYS          
SEQRES  36 B  504  SER PHE VAL GLN TRP LEU GLY CYS ARG SER HIS SER SER          
SEQRES  37 B  504  ALA GLN PHE LEU ILE GLY ASP GLN GLU PRO TRP ALA PHE          
SEQRES  38 B  504  ARG GLY GLY LEU ALA GLY GLU PHE GLN ARG LEU LEU PRO          
SEQRES  39 B  504  ILE ASP GLY ALA ASN ASP LEU PHE PHE GLN                      
SEQRES   1 C  504  HIS PHE LEU CYS GLY VAL VAL GLU GLY PHE TYR GLY ARG          
SEQRES   2 C  504  PRO TRP VAL MET GLU GLN ARG LYS GLU LEU PHE ARG ARG          
SEQRES   3 C  504  LEU GLN LYS TRP GLU LEU ASN THR TYR LEU TYR ALA PRO          
SEQRES   4 C  504  LYS ASP ASP TYR LYS HIS ARG MET PHE TRP ARG GLU MET          
SEQRES   5 C  504  TYR SER VAL GLU GLU ALA GLU GLN LEU MET THR LEU ILE          
SEQRES   6 C  504  SER ALA ALA ARG GLU TYR GLU ILE GLU PHE ILE TYR ALA          
SEQRES   7 C  504  ILE SER PRO GLY LEU ASP ILE THR PHE SER ASN PRO LYS          
SEQRES   8 C  504  GLU VAL SER THR LEU LYS ARG LYS LEU ASP GLN VAL SER          
SEQRES   9 C  504  GLN PHE GLY CYS ARG SER PHE ALA LEU LEU PHE ASP ASN          
SEQRES  10 C  504  ILE ASP HIS ASN MET CYS ALA ALA ASP LYS GLU VAL PHE          
SEQRES  11 C  504  SER SER PHE ALA HIS ALA GLN VAL SER ILE THR ASN GLU          
SEQRES  12 C  504  ILE TYR GLN TYR LEU GLY GLU PRO GLU THR PHE LEU PHE          
SEQRES  13 C  504  CYS PRO THR GLU TYR CYS GLY THR PHE CYS TYR PRO ASN          
SEQRES  14 C  504  VAL SER GLN SER PRO TYR LEU ARG THR VAL GLY GLU LYS          
SEQRES  15 C  504  LEU LEU PRO GLY ILE GLU VAL LEU TRP THR GLY PRO LYS          
SEQRES  16 C  504  VAL VAL SER LYS GLU ILE PRO VAL GLU SER ILE GLU GLU          
SEQRES  17 C  504  VAL SER LYS ILE ILE LYS ARG ALA PRO VAL ILE TRP ASP          
SEQRES  18 C  504  ASN ILE HIS ALA ASN ASP TYR ASP GLN LYS ARG LEU PHE          
SEQRES  19 C  504  LEU GLY PRO TYR LYS GLY ARG SER THR GLU LEU ILE PRO          
SEQRES  20 C  504  ARG LEU LYS GLY VAL LEU THR ASN PRO ASN CYS GLU PHE          
SEQRES  21 C  504  GLU ALA ASN TYR VAL ALA ILE HIS THR LEU ALA THR TRP          
SEQRES  22 C  504  TYR LYS SER ASN MET ASN GLY VAL ARG LYS ASP VAL VAL          
SEQRES  23 C  504  MET THR ASP SER GLU ASP SER THR VAL SER ILE GLN ILE          
SEQRES  24 C  504  LYS LEU GLU ASN GLU GLY SER ASP GLU ASP ILE GLU THR          
SEQRES  25 C  504  ASP VAL LEU TYR SER PRO GLN MET ALA LEU LYS LEU ALA          
SEQRES  26 C  504  LEU THR GLU TRP LEU GLN GLU PHE GLY VAL PRO HIS GLN          
SEQRES  27 C  504  TYR SER SER ARG GLY GLY GLY GLY SER GLY GLY GLY GLY          
SEQRES  28 C  504  SER VAL THR LEU GLU ASP LEU GLN LEU LEU ALA ASP LEU          
SEQRES  29 C  504  PHE TYR LEU PRO TYR GLU HIS GLY PRO LYS GLY ALA GLN          
SEQRES  30 C  504  MET LEU ARG GLU PHE GLN TRP LEU ARG ALA ASN SER SER          
SEQRES  31 C  504  VAL VAL SER VAL ASN CYS LYS GLY LYS ASP SER GLU LYS          
SEQRES  32 C  504  ILE GLU GLU TRP ARG SER ARG ALA ALA LYS PHE GLU GLU          
SEQRES  33 C  504  MET CYS GLY LEU VAL MET GLY MET PHE THR ARG LEU SER          
SEQRES  34 C  504  ASN CYS ALA ASN ARG THR ILE LEU TYR ASP MET TYR SER          
SEQRES  35 C  504  TYR VAL TRP ASP ILE LYS SER ILE MET SER MET VAL LYS          
SEQRES  36 C  504  SER PHE VAL GLN TRP LEU GLY CYS ARG SER HIS SER SER          
SEQRES  37 C  504  ALA GLN PHE LEU ILE GLY ASP GLN GLU PRO TRP ALA PHE          
SEQRES  38 C  504  ARG GLY GLY LEU ALA GLY GLU PHE GLN ARG LEU LEU PRO          
SEQRES  39 C  504  ILE ASP GLY ALA ASN ASP LEU PHE PHE GLN                      
SEQRES   1 D  504  HIS PHE LEU CYS GLY VAL VAL GLU GLY PHE TYR GLY ARG          
SEQRES   2 D  504  PRO TRP VAL MET GLU GLN ARG LYS GLU LEU PHE ARG ARG          
SEQRES   3 D  504  LEU GLN LYS TRP GLU LEU ASN THR TYR LEU TYR ALA PRO          
SEQRES   4 D  504  LYS ASP ASP TYR LYS HIS ARG MET PHE TRP ARG GLU MET          
SEQRES   5 D  504  TYR SER VAL GLU GLU ALA GLU GLN LEU MET THR LEU ILE          
SEQRES   6 D  504  SER ALA ALA ARG GLU TYR GLU ILE GLU PHE ILE TYR ALA          
SEQRES   7 D  504  ILE SER PRO GLY LEU ASP ILE THR PHE SER ASN PRO LYS          
SEQRES   8 D  504  GLU VAL SER THR LEU LYS ARG LYS LEU ASP GLN VAL SER          
SEQRES   9 D  504  GLN PHE GLY CYS ARG SER PHE ALA LEU LEU PHE ASP ASN          
SEQRES  10 D  504  ILE ASP HIS ASN MET CYS ALA ALA ASP LYS GLU VAL PHE          
SEQRES  11 D  504  SER SER PHE ALA HIS ALA GLN VAL SER ILE THR ASN GLU          
SEQRES  12 D  504  ILE TYR GLN TYR LEU GLY GLU PRO GLU THR PHE LEU PHE          
SEQRES  13 D  504  CYS PRO THR GLU TYR CYS GLY THR PHE CYS TYR PRO ASN          
SEQRES  14 D  504  VAL SER GLN SER PRO TYR LEU ARG THR VAL GLY GLU LYS          
SEQRES  15 D  504  LEU LEU PRO GLY ILE GLU VAL LEU TRP THR GLY PRO LYS          
SEQRES  16 D  504  VAL VAL SER LYS GLU ILE PRO VAL GLU SER ILE GLU GLU          
SEQRES  17 D  504  VAL SER LYS ILE ILE LYS ARG ALA PRO VAL ILE TRP ASP          
SEQRES  18 D  504  ASN ILE HIS ALA ASN ASP TYR ASP GLN LYS ARG LEU PHE          
SEQRES  19 D  504  LEU GLY PRO TYR LYS GLY ARG SER THR GLU LEU ILE PRO          
SEQRES  20 D  504  ARG LEU LYS GLY VAL LEU THR ASN PRO ASN CYS GLU PHE          
SEQRES  21 D  504  GLU ALA ASN TYR VAL ALA ILE HIS THR LEU ALA THR TRP          
SEQRES  22 D  504  TYR LYS SER ASN MET ASN GLY VAL ARG LYS ASP VAL VAL          
SEQRES  23 D  504  MET THR ASP SER GLU ASP SER THR VAL SER ILE GLN ILE          
SEQRES  24 D  504  LYS LEU GLU ASN GLU GLY SER ASP GLU ASP ILE GLU THR          
SEQRES  25 D  504  ASP VAL LEU TYR SER PRO GLN MET ALA LEU LYS LEU ALA          
SEQRES  26 D  504  LEU THR GLU TRP LEU GLN GLU PHE GLY VAL PRO HIS GLN          
SEQRES  27 D  504  TYR SER SER ARG GLY GLY GLY GLY SER GLY GLY GLY GLY          
SEQRES  28 D  504  SER VAL THR LEU GLU ASP LEU GLN LEU LEU ALA ASP LEU          
SEQRES  29 D  504  PHE TYR LEU PRO TYR GLU HIS GLY PRO LYS GLY ALA GLN          
SEQRES  30 D  504  MET LEU ARG GLU PHE GLN TRP LEU ARG ALA ASN SER SER          
SEQRES  31 D  504  VAL VAL SER VAL ASN CYS LYS GLY LYS ASP SER GLU LYS          
SEQRES  32 D  504  ILE GLU GLU TRP ARG SER ARG ALA ALA LYS PHE GLU GLU          
SEQRES  33 D  504  MET CYS GLY LEU VAL MET GLY MET PHE THR ARG LEU SER          
SEQRES  34 D  504  ASN CYS ALA ASN ARG THR ILE LEU TYR ASP MET TYR SER          
SEQRES  35 D  504  TYR VAL TRP ASP ILE LYS SER ILE MET SER MET VAL LYS          
SEQRES  36 D  504  SER PHE VAL GLN TRP LEU GLY CYS ARG SER HIS SER SER          
SEQRES  37 D  504  ALA GLN PHE LEU ILE GLY ASP GLN GLU PRO TRP ALA PHE          
SEQRES  38 D  504  ARG GLY GLY LEU ALA GLY GLU PHE GLN ARG LEU LEU PRO          
SEQRES  39 D  504  ILE ASP GLY ALA ASN ASP LEU PHE PHE GLN                      
SEQRES   1 E   11  GLN LEU TRP VAL ASP SER THR PRO PRO PRO GLY                  
SEQRES   1 F   11  GLN LEU TRP VAL ASP SER THR PRO PRO PRO GLY                  
SEQRES   1 G   11  GLN LEU TRP VAL ASP SER THR PRO PRO PRO GLY                  
SEQRES   1 H   11  GLN LEU TRP VAL ASP SER THR PRO PRO PRO GLY                  
HET    NAG  E 200      14                                                       
HET    NAG  F 200      14                                                       
HET    NAG  G 200      14                                                       
HET    NAG  H 200      14                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   9  NAG    4(C8 H15 N O6)                                               
FORMUL  13  HOH   *1232(H2 O)                                                   
HELIX    1 AA1 VAL A   74  TRP A   88  1                                  15    
HELIX    2 AA2 ASP A  100  ARG A  104  5                                   5    
HELIX    3 AA3 SER A  112  TYR A  129  1                                  18    
HELIX    4 AA4 ASN A  147  GLN A  163  1                                  17    
HELIX    5 AA5 CYS A  181  PHE A  188  1                                   8    
HELIX    6 AA6 SER A  190  LEU A  206  1                                  17    
HELIX    7 AA7 CYS A  220  CYS A  224  5                                   5    
HELIX    8 AA8 SER A  231  LEU A  241  1                                  11    
HELIX    9 AA9 PRO A  260  LYS A  272  1                                  13    
HELIX   10 AB1 SER A  300  LEU A  307  5                                   8    
HELIX   11 AB2 GLU A  317  ALA A  320  5                                   4    
HELIX   12 AB3 ASN A  321  LYS A  333  1                                  13    
HELIX   13 AB4 SER A  375  GLN A  389  1                                  15    
HELIX   14 AB5 THR A  554  PHE A  565  1                                  12    
HELIX   15 AB6 GLY A  572  ASN A  588  1                                  17    
HELIX   16 AB7 SER A  589  VAL A  592  5                                   4    
HELIX   17 AB8 GLU A  605  SER A  629  1                                  25    
HELIX   18 AB9 ASN A  633  GLY A  662  1                                  30    
HELIX   19 AC1 GLY A  683  LEU A  693  1                                  11    
HELIX   20 AC2 VAL B   74  TRP B   88  1                                  15    
HELIX   21 AC3 ASP B  100  ARG B  104  5                                   5    
HELIX   22 AC4 SER B  112  TYR B  129  1                                  18    
HELIX   23 AC5 ASN B  147  PHE B  164  1                                  18    
HELIX   24 AC6 CYS B  181  PHE B  188  1                                   8    
HELIX   25 AC7 SER B  190  LEU B  206  1                                  17    
HELIX   26 AC8 CYS B  220  CYS B  224  5                                   5    
HELIX   27 AC9 SER B  231  LEU B  241  1                                  11    
HELIX   28 AD1 PRO B  260  LYS B  272  1                                  13    
HELIX   29 AD2 SER B  300  LEU B  307  5                                   8    
HELIX   30 AD3 GLU B  317  ALA B  320  5                                   4    
HELIX   31 AD4 ASN B  321  LYS B  333  1                                  13    
HELIX   32 AD5 SER B  375  GLN B  389  1                                  15    
HELIX   33 AD6 THR B  554  PHE B  565  1                                  12    
HELIX   34 AD7 GLY B  572  ASN B  588  1                                  17    
HELIX   35 AD8 SER B  589  VAL B  592  5                                   4    
HELIX   36 AD9 ILE B  604  SER B  629  1                                  26    
HELIX   37 AE1 ASN B  633  GLY B  662  1                                  30    
HELIX   38 AE2 GLY B  683  LEU B  693  1                                  11    
HELIX   39 AE3 VAL C   74  TRP C   88  1                                  15    
HELIX   40 AE4 SER C  112  TYR C  129  1                                  18    
HELIX   41 AE5 ASN C  147  GLN C  163  1                                  17    
HELIX   42 AE6 CYS C  181  PHE C  188  1                                   8    
HELIX   43 AE7 SER C  190  LEU C  206  1                                  17    
HELIX   44 AE8 CYS C  220  CYS C  224  5                                   5    
HELIX   45 AE9 SER C  231  LEU C  241  1                                  11    
HELIX   46 AF1 PRO C  260  LYS C  272  1                                  13    
HELIX   47 AF2 SER C  300  LEU C  307  5                                   8    
HELIX   48 AF3 GLU C  317  ALA C  320  5                                   4    
HELIX   49 AF4 ASN C  321  SER C  334  1                                  14    
HELIX   50 AF5 SER C  375  GLN C  389  1                                  15    
HELIX   51 AF6 THR C  554  PHE C  565  1                                  12    
HELIX   52 AF7 GLY C  572  ASN C  588  1                                  17    
HELIX   53 AF8 SER C  589  VAL C  592  5                                   4    
HELIX   54 AF9 GLU C  605  ASN C  630  1                                  26    
HELIX   55 AG1 ASN C  633  CYS C  663  1                                  31    
HELIX   56 AG2 ARG C  664  HIS C  666  5                                   3    
HELIX   57 AG3 GLU C  677  PHE C  681  5                                   5    
HELIX   58 AG4 GLY C  683  LEU C  692  1                                  10    
HELIX   59 AG5 VAL D   74  TRP D   88  1                                  15    
HELIX   60 AG6 SER D  112  TYR D  129  1                                  18    
HELIX   61 AG7 ASN D  147  PHE D  164  1                                  18    
HELIX   62 AG8 CYS D  181  GLU D  186  1                                   6    
HELIX   63 AG9 SER D  190  LEU D  206  1                                  17    
HELIX   64 AH1 CYS D  220  CYS D  224  5                                   5    
HELIX   65 AH2 SER D  231  LEU D  241  1                                  11    
HELIX   66 AH3 PRO D  260  LYS D  272  1                                  13    
HELIX   67 AH4 SER D  300  LEU D  307  5                                   8    
HELIX   68 AH5 GLU D  317  ALA D  320  5                                   4    
HELIX   69 AH6 ASN D  321  ASN D  335  1                                  15    
HELIX   70 AH7 SER D  375  GLN D  389  1                                  15    
HELIX   71 AH8 THR D  554  PHE D  565  1                                  12    
HELIX   72 AH9 GLY D  572  ASN D  588  1                                  17    
HELIX   73 AI1 SER D  589  VAL D  592  5                                   4    
HELIX   74 AI2 GLU D  605  ASN D  630  1                                  26    
HELIX   75 AI3 ASN D  633  CYS D  663  1                                  31    
HELIX   76 AI4 ARG D  664  HIS D  666  5                                   3    
HELIX   77 AI5 GLU D  677  PHE D  681  5                                   5    
HELIX   78 AI6 GLY D  683  LEU D  692  1                                  10    
SHEET    1 AA1 9 LEU A  61  GLU A  66  0                                        
SHEET    2 AA1 9 THR A  92  TYR A  95  1  O  LEU A  94   N  GLU A  66           
SHEET    3 AA1 9 GLU A 132  ILE A 137  1  O  ILE A 134   N  TYR A  93           
SHEET    4 AA1 9 SER A 168  LEU A 172  1  O  LEU A 172   N  ILE A 137           
SHEET    5 AA1 9 PHE A 212  CYS A 215  1  O  LEU A 213   N  LEU A 171           
SHEET    6 AA1 9 GLU A 246  TRP A 249  1  O  LEU A 248   N  PHE A 214           
SHEET    7 AA1 9 VAL A 276  ASP A 279  1  O  VAL A 276   N  VAL A 247           
SHEET    8 AA1 9 GLY A 309  THR A 312  1  O  LEU A 311   N  ILE A 277           
SHEET    9 AA1 9 LEU A  61  GLU A  66  1  N  GLY A  63   O  THR A 312           
SHEET    1 AA2 9 LEU B  61  GLU B  66  0                                        
SHEET    2 AA2 9 THR B  92  TYR B  95  1  O  LEU B  94   N  GLU B  66           
SHEET    3 AA2 9 GLU B 132  ILE B 137  1  O  ILE B 134   N  TYR B  95           
SHEET    4 AA2 9 SER B 168  LEU B 172  1  O  LEU B 172   N  ILE B 137           
SHEET    5 AA2 9 PHE B 212  CYS B 215  1  O  CYS B 215   N  LEU B 171           
SHEET    6 AA2 9 GLU B 246  TRP B 249  1  O  LEU B 248   N  PHE B 214           
SHEET    7 AA2 9 VAL B 276  ASP B 279  1  O  VAL B 276   N  VAL B 247           
SHEET    8 AA2 9 GLY B 309  THR B 312  1  O  LEU B 311   N  ASP B 279           
SHEET    9 AA2 9 LEU B  61  GLU B  66  1  N  GLY B  63   O  THR B 312           
SHEET    1 AA3 9 LEU C  61  GLU C  66  0                                        
SHEET    2 AA3 9 THR C  92  TYR C  95  1  O  LEU C  94   N  VAL C  64           
SHEET    3 AA3 9 GLU C 132  ILE C 137  1  O  ILE C 134   N  TYR C  95           
SHEET    4 AA3 9 SER C 168  LEU C 172  1  O  SER C 168   N  TYR C 135           
SHEET    5 AA3 9 PHE C 212  CYS C 215  1  O  CYS C 215   N  LEU C 171           
SHEET    6 AA3 9 GLU C 246  TRP C 249  1  O  LEU C 248   N  PHE C 214           
SHEET    7 AA3 9 VAL C 276  ASP C 279  1  O  VAL C 276   N  VAL C 247           
SHEET    8 AA3 9 GLY C 309  THR C 312  1  O  LEU C 311   N  ILE C 277           
SHEET    9 AA3 9 LEU C  61  GLU C  66  1  N  GLY C  63   O  THR C 312           
SHEET    1 AA4 9 LEU D  61  GLU D  66  0                                        
SHEET    2 AA4 9 THR D  92  TYR D  95  1  O  LEU D  94   N  VAL D  64           
SHEET    3 AA4 9 GLU D 132  ILE D 137  1  O  ILE D 134   N  TYR D  95           
SHEET    4 AA4 9 SER D 168  LEU D 172  1  O  SER D 168   N  TYR D 135           
SHEET    5 AA4 9 PHE D 212  CYS D 215  1  O  CYS D 215   N  LEU D 171           
SHEET    6 AA4 9 GLU D 246  TRP D 249  1  O  GLU D 246   N  PHE D 212           
SHEET    7 AA4 9 VAL D 276  ASP D 279  1  O  VAL D 276   N  VAL D 247           
SHEET    8 AA4 9 GLY D 309  THR D 312  1  O  LEU D 311   N  ILE D 277           
SHEET    9 AA4 9 LEU D  61  GLU D  66  1  N  GLY D  63   O  THR D 312           
LINK         OG  SER E 149                 C1  NAG E 200     1555   1555  1.36  
LINK         OG  SER F 149                 C1  NAG F 200     1555   1555  1.36  
LINK         OG  SER G 149                 C1  NAG G 200     1555   1555  1.36  
LINK         OG  SER H 149                 C1  NAG H 200     1555   1555  1.36  
CISPEP   1 TYR A  225    PRO A  226          0        -4.11                     
CISPEP   2 TYR B  225    PRO B  226          0         1.46                     
CISPEP   3 TYR C  225    PRO C  226          0         1.01                     
CISPEP   4 TYR D  225    PRO D  226          0        -1.07                     
SITE     1 AC1 14 GLY A  67  PHE A  68  LYS A  98  ASP A 174                    
SITE     2 AC1 14 ASN A 175  TYR A 219  VAL A 254  TRP A 278                    
SITE     3 AC1 14 ASN A 280  ASP A 285  TYR A 286  ASN A 313                    
SITE     4 AC1 14 SER E 149  HOH E 306                                          
SITE     1 AC2 14 GLY B  67  PHE B  68  LYS B  98  ASP B 174                    
SITE     2 AC2 14 ASN B 175  TYR B 219  VAL B 254  TRP B 278                    
SITE     3 AC2 14 ASN B 280  ASP B 285  TYR B 286  ASN B 313                    
SITE     4 AC2 14 SER F 149  HOH F 302                                          
SITE     1 AC3 13 GLY C  67  PHE C  68  TYR C  69  LYS C  98                    
SITE     2 AC3 13 ASP C 174  ASN C 175  VAL C 254  TRP C 278                    
SITE     3 AC3 13 ASN C 280  ASP C 285  ASN C 313  SER G 149                    
SITE     4 AC3 13 HOH G 301                                                     
SITE     1 AC4 14 GLY D  67  PHE D  68  TYR D  69  LYS D  98                    
SITE     2 AC4 14 ASP D 174  ASN D 175  THR D 250  VAL D 254                    
SITE     3 AC4 14 TRP D 278  ASN D 280  ASP D 285  ASN D 313                    
SITE     4 AC4 14 SER H 149  HOH H 304                                          
CRYST1   89.909   95.393  149.320  90.00  96.91  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011122  0.000000  0.001347        0.00000                         
SCALE2      0.000000  0.010483  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006746        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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