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Database: PDB
Entry: 1LK9
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HEADER    LYASE                                   24-APR-02   1LK9              
TITLE     THE THREE-DIMENSIONAL STRUCTURE OF ALLIINASE FROM GARLIC              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALLIIN LYASE;                                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ALLIINASE, CYSTEINE SULPHOXIDE LYASE;                       
COMPND   5 EC: 4.4.1.4                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ALLIUM SATIVUM;                                 
SOURCE   3 ORGANISM_COMMON: GARLIC;                                             
SOURCE   4 ORGANISM_TAXID: 4682;                                                
SOURCE   5 OTHER_DETAILS: BULB                                                  
KEYWDS    EGF-LIKE DOMAIN, PLP TYPE 1, CHLORIDE BINDING, LYASE                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.B.KUETTNER,R.HILGENFELD,M.S.WEISS                                   
REVDAT   3   13-JUL-11 1LK9    1       VERSN                                    
REVDAT   2   24-FEB-09 1LK9    1       VERSN                                    
REVDAT   1   11-DEC-02 1LK9    0                                                
JRNL        AUTH   E.B.KUETTNER,R.HILGENFELD,M.S.WEISS                          
JRNL        TITL   THE ACTIVE PRINCIPLE OF GARLIC AT ATOMIC RESOLUTION          
JRNL        REF    J.BIOL.CHEM.                  V. 277 46402 2002              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   12235163                                                     
JRNL        DOI    10.1074/JBC.M208669200                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   E.B.KUETTNER,R.HILGENFELD,M.S.WEISS                          
REMARK   1  TITL   PURIFICATION, CHARACTERIZATION AND CRYSTALLIZATION OF        
REMARK   1  TITL 2 ALLIINASE FROM GARLIC                                        
REMARK   1  REF    ARCH.BIOCHEM.BIOPHYS.         V. 402   192 2002              
REMARK   1  REFN                   ISSN 0003-9861                               
REMARK   1  DOI    10.1016/S0003-9861(02)00088-7                                
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   E.B.KUETTNER,R.HILGENFELD,M.S.WEISS                          
REMARK   1  TITL   ERRATUM TO ``PURIFICATION, CHARACTERIZATION AND              
REMARK   1  TITL 2 CRYSTALLIZATION OF ALLIINASE FROM GARLIC. [ARCH. BIOCHEM.    
REMARK   1  TITL 3 BIOPHYS. 402, 192-200.]''                                    
REMARK   1  REF    ARCH.BIOCHEM.BIOPHYS.         V. 404   339 2002              
REMARK   1  REFN                   ISSN 0003-9861                               
REMARK   1  DOI    10.1016/S0003-9861(02)00368-5                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.53 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 4.0.6                                         
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.53                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 12.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 162892                         
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) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 3264                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6862                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 252                                     
REMARK   3   SOLVENT ATOMS            : 830                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.075         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.077         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.055         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.530         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.011 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.026 ; 0.040               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.030 ; 0.050               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.120 ; 0.150               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.174 ; 0.300               
REMARK   3    MULTIPLE TORSION                (A) : 0.190 ; 0.300               
REMARK   3    H-BOND (X...Y)                  (A) : 0.125 ; 0.300               
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : 3.900 ; 7.000               
REMARK   3    STAGGERED                 (DEGREES) : 13.400; 15.000              
REMARK   3    TRANSVERSE                (DEGREES) : 25.900; 20.000              
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 0.941 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.364 ; 2.500                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.366 ; 5.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.603 ; 10.000               
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1LK9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAY-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB016022.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-APR-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : BW7B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8423                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (TRUNCATE)                    
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 160747                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.530                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 12.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : 0.05500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.53                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.56                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS                        
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 5 MG/ML ALLIINASE, 5 MM HEPES   
REMARK 280  PH 7.4, 10 % (V/V) GLYCEROL, 0.25 MM PYRIDOXAL-5'-PHOSPHATE, 1 MM   
REMARK 280  S-ETHYL-L-CYSTEINE; PRECIPITANT: 2.9 M AMMONIUM SULFATE, 50 MM      
REMARK 280  HEPES PH 7.4 HANGING DROP METHOD(4 MICROL + 4 MICROL), VAPOUR       
REMARK 280  DIFFUSION, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       34.22500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       77.84500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       50.53500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       77.84500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       34.22500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       50.53500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14250 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 32330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -168.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ARG A   426                                                      
REMARK 465     LYS A   427                                                      
REMARK 465     THR A   428                                                      
REMARK 465     PRO A   429                                                      
REMARK 465     LEU A   430                                                      
REMARK 465     ILE A   431                                                      
REMARK 465     LYS A   432                                                      
REMARK 465     GLN A   433                                                      
REMARK 465     LEU A   434                                                      
REMARK 465     PHE A   435                                                      
REMARK 465     ILE A   436                                                      
REMARK 465     ASP A   437                                                      
REMARK 465     GLN A   438                                                      
REMARK 465     THR A   439                                                      
REMARK 465     GLU A   440                                                      
REMARK 465     THR A   441                                                      
REMARK 465     ALA A   442                                                      
REMARK 465     SER A   443                                                      
REMARK 465     ARG A   444                                                      
REMARK 465     ARG A   445                                                      
REMARK 465     PRO A   446                                                      
REMARK 465     PHE A   447                                                      
REMARK 465     ILE A   448                                                      
REMARK 465     THR B   428                                                      
REMARK 465     PRO B   429                                                      
REMARK 465     LEU B   430                                                      
REMARK 465     ILE B   431                                                      
REMARK 465     LYS B   432                                                      
REMARK 465     GLN B   433                                                      
REMARK 465     LEU B   434                                                      
REMARK 465     PHE B   435                                                      
REMARK 465     ILE B   436                                                      
REMARK 465     ASP B   437                                                      
REMARK 465     GLN B   438                                                      
REMARK 465     THR B   439                                                      
REMARK 465     GLU B   440                                                      
REMARK 465     THR B   441                                                      
REMARK 465     ALA B   442                                                      
REMARK 465     SER B   443                                                      
REMARK 465     ARG B   444                                                      
REMARK 465     ARG B   445                                                      
REMARK 465     PRO B   446                                                      
REMARK 465     PHE B   447                                                      
REMARK 465     ILE B   448                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A   1    N    CB   CG   CD   CE   NZ                         
REMARK 470     LYS B   1    N    CB   CG   CD   CE   NZ                         
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   O4   NAG A   502     O5   BMA A   503              2.11            
REMARK 500   OD2  ASP B   267     OG   SER B   269              2.15            
REMARK 500   O4   NAG B   502     O5   NAG B   503              2.16            
REMARK 500   O4   NAG A   504     O5   NAG A   505              2.16            
REMARK 500   O4   NAG A   500     O5   NAG A   502              2.18            
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  25   NE  -  CZ  -  NH1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG A  25   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    ARG A  89   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ASP A 123   N   -  CA  -  CB  ANGL. DEV. = -11.5 DEGREES          
REMARK 500    PHE A 128   CB  -  CG  -  CD2 ANGL. DEV. =  -5.1 DEGREES          
REMARK 500    PHE A 128   CB  -  CG  -  CD1 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    PRO A 208   N   -  CA  -  C   ANGL. DEV. =  17.0 DEGREES          
REMARK 500    ARG A 259   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A 287   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG A 323   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG A 357   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG B  89   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    PHE B 128   CB  -  CG  -  CD2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    PHE B 128   CB  -  CG  -  CD1 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    ARG B 213   NH1 -  CZ  -  NH2 ANGL. DEV. =   7.0 DEGREES          
REMARK 500    ARG B 213   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ARG B 259   NE  -  CZ  -  NH2 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG B 287   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG B 312   CD  -  NE  -  CZ  ANGL. DEV. =  10.5 DEGREES          
REMARK 500    ARG B 312   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG B 323   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG B 325   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ASP B 337   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG B 401   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 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    THR A   3      -91.90   -121.17                                   
REMARK 500    SER A  21     -148.14     57.17                                   
REMARK 500    ARG A  89       67.55     32.67                                   
REMARK 500    SER A  98       43.81   -152.97                                   
REMARK 500    ASP A 241       21.85   -144.51                                   
REMARK 500    SER A 360       61.23   -152.67                                   
REMARK 500    ARG A 384       31.30     76.58                                   
REMARK 500    GLU A 394       35.30     73.40                                   
REMARK 500    LYS A 406     -156.12    -88.29                                   
REMARK 500    THR B   3      -94.70   -126.35                                   
REMARK 500    ARG B  89       65.40     30.05                                   
REMARK 500    SER B  98       47.06   -151.03                                   
REMARK 500    GLN B 307       24.15   -140.55                                   
REMARK 500    SER B 360       61.31   -153.11                                   
REMARK 500    ARG B 384       34.29     75.68                                   
REMARK 500    GLU B 394       38.04     74.84                                   
REMARK 500    LYS B 406     -158.98    -91.38                                   
REMARK 500    ARG B 426      159.27    -49.94                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ASN A 146         0.07    SIDE CHAIN                              
REMARK 500    ASN B 146         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LYS A 122        23.0      L          L   OUTSIDE RANGE           
REMARK 500    ASP A 123        22.3      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1266        DISTANCE =  5.13 ANGSTROMS                       
REMARK 525    HOH A1279        DISTANCE =  5.11 ANGSTROMS                       
REMARK 525    HOH B1108        DISTANCE =  5.03 ANGSTROMS                       
REMARK 525    HOH B1111        DISTANCE =  6.40 ANGSTROMS                       
REMARK 525    HOH B1252        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH B1314        DISTANCE =  5.80 ANGSTROMS                       
REMARK 525    HOH B1416        DISTANCE =  5.56 ANGSTROMS                       
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 THE MOLECULES EPE AND DHA ARE ONLY PRESENT AT AN                     
REMARK 600 OCCUPANCY OF 50%. THEIR PRESENCE IS MUTUALLY EXCLUSIVE.              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 904                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 905                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 906                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 907                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 910                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 911                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 901                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 902                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 903                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 908                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 909                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP A 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 851                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 852                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PLP B 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DHA B 850                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THERE ARE TWO DIFFERENT SEQUENCES IN THE LITERATURE,                 
REMARK 999 ONE CONTAINS AN ASP IN POSITION 176 AND ONE CONTAINS ASN.            
REMARK 999 THE AUTHORS HAVE BUILT AND REFINED THE STRUCTURE WITH AN             
REMARK 999 ASP PRESENT IN THIS POSITION.                                        
DBREF  1LK9 A    1   448  UNP    Q01594   ALLN_ALLSA      39    486             
DBREF  1LK9 B    1   448  UNP    Q01594   ALLN_ALLSA      39    486             
SEQADV 1LK9 ASP A  176  UNP  Q01594    ASN   214 SEE REMARK 999                 
SEQADV 1LK9 ASP B  176  UNP  Q01594    ASN   214 SEE REMARK 999                 
SEQRES   1 A  448  LYS MET THR TRP THR MET LYS ALA ALA GLU GLU ALA GLU          
SEQRES   2 A  448  ALA VAL ALA ASN ILE ASN CYS SER GLU HIS GLY ARG ALA          
SEQRES   3 A  448  PHE LEU ASP GLY ILE ILE SER GLU GLY SER PRO LYS CYS          
SEQRES   4 A  448  GLU CYS ASN THR CYS TYR THR GLY PRO ASP CYS SER GLU          
SEQRES   5 A  448  LYS ILE GLN GLY CYS SER ALA ASP VAL ALA SER GLY ASP          
SEQRES   6 A  448  GLY LEU PHE LEU GLU GLU TYR TRP LYS GLN HIS LYS GLU          
SEQRES   7 A  448  ALA SER ALA VAL LEU VAL SER PRO TRP HIS ARG MET SER          
SEQRES   8 A  448  TYR PHE PHE ASN PRO VAL SER ASN PHE ILE SER PHE GLU          
SEQRES   9 A  448  LEU GLU LYS THR ILE LYS GLU LEU HIS GLU VAL VAL GLY          
SEQRES  10 A  448  ASN ALA ALA ALA LYS ASP ARG TYR ILE VAL PHE GLY VAL          
SEQRES  11 A  448  GLY VAL THR GLN LEU ILE HIS GLY LEU VAL ILE SER LEU          
SEQRES  12 A  448  SER PRO ASN MET THR ALA THR PRO ASP ALA PRO GLU SER          
SEQRES  13 A  448  LYS VAL VAL ALA HIS ALA PRO PHE TYR PRO VAL PHE ARG          
SEQRES  14 A  448  GLU GLN THR LYS TYR PHE ASP LYS LYS GLY TYR VAL TRP          
SEQRES  15 A  448  ALA GLY ASN ALA ALA ASN TYR VAL ASN VAL SER ASN PRO          
SEQRES  16 A  448  GLU GLN TYR ILE GLU MET VAL THR SER PRO ASN ASN PRO          
SEQRES  17 A  448  GLU GLY LEU LEU ARG HIS ALA VAL ILE LYS GLY CYS LYS          
SEQRES  18 A  448  SER ILE TYR ASP MET VAL TYR TYR TRP PRO HIS TYR THR          
SEQRES  19 A  448  PRO ILE LYS TYR LYS ALA ASP GLU ASP ILE LEU LEU PHE          
SEQRES  20 A  448  THR MET SER LYS PHE THR GLY HIS SER GLY SER ARG PHE          
SEQRES  21 A  448  GLY TRP ALA LEU ILE LYS ASP GLU SER VAL TYR ASN ASN          
SEQRES  22 A  448  LEU LEU ASN TYR MET THR LYS ASN THR GLU GLY THR PRO          
SEQRES  23 A  448  ARG GLU THR GLN LEU ARG SER LEU LYS VAL LEU LYS GLU          
SEQRES  24 A  448  VAL VAL ALA MET VAL LYS THR GLN LYS GLY THR MET ARG          
SEQRES  25 A  448  ASP LEU ASN THR PHE GLY PHE LYS LYS LEU ARG GLU ARG          
SEQRES  26 A  448  TRP VAL ASN ILE THR ALA LEU LEU ASP GLN SER ASP ARG          
SEQRES  27 A  448  PHE SER TYR GLN GLU LEU PRO GLN SER GLU TYR CYS ASN          
SEQRES  28 A  448  TYR PHE ARG ARG MET ARG PRO PRO SER PRO SER TYR ALA          
SEQRES  29 A  448  TRP VAL LYS CYS GLU TRP GLU GLU ASP LYS ASP CYS TYR          
SEQRES  30 A  448  GLN THR PHE GLN ASN GLY ARG ILE ASN THR GLN ASN GLY          
SEQRES  31 A  448  VAL GLY PHE GLU ALA SER SER ARG TYR VAL ARG LEU SER          
SEQRES  32 A  448  LEU ILE LYS THR GLN ASP ASP PHE ASP GLN LEU MET TYR          
SEQRES  33 A  448  TYR LEU LYS ASP MET VAL LYS ALA LYS ARG LYS THR PRO          
SEQRES  34 A  448  LEU ILE LYS GLN LEU PHE ILE ASP GLN THR GLU THR ALA          
SEQRES  35 A  448  SER ARG ARG PRO PHE ILE                                      
SEQRES   1 B  448  LYS MET THR TRP THR MET LYS ALA ALA GLU GLU ALA GLU          
SEQRES   2 B  448  ALA VAL ALA ASN ILE ASN CYS SER GLU HIS GLY ARG ALA          
SEQRES   3 B  448  PHE LEU ASP GLY ILE ILE SER GLU GLY SER PRO LYS CYS          
SEQRES   4 B  448  GLU CYS ASN THR CYS TYR THR GLY PRO ASP CYS SER GLU          
SEQRES   5 B  448  LYS ILE GLN GLY CYS SER ALA ASP VAL ALA SER GLY ASP          
SEQRES   6 B  448  GLY LEU PHE LEU GLU GLU TYR TRP LYS GLN HIS LYS GLU          
SEQRES   7 B  448  ALA SER ALA VAL LEU VAL SER PRO TRP HIS ARG MET SER          
SEQRES   8 B  448  TYR PHE PHE ASN PRO VAL SER ASN PHE ILE SER PHE GLU          
SEQRES   9 B  448  LEU GLU LYS THR ILE LYS GLU LEU HIS GLU VAL VAL GLY          
SEQRES  10 B  448  ASN ALA ALA ALA LYS ASP ARG TYR ILE VAL PHE GLY VAL          
SEQRES  11 B  448  GLY VAL THR GLN LEU ILE HIS GLY LEU VAL ILE SER LEU          
SEQRES  12 B  448  SER PRO ASN MET THR ALA THR PRO ASP ALA PRO GLU SER          
SEQRES  13 B  448  LYS VAL VAL ALA HIS ALA PRO PHE TYR PRO VAL PHE ARG          
SEQRES  14 B  448  GLU GLN THR LYS TYR PHE ASP LYS LYS GLY TYR VAL TRP          
SEQRES  15 B  448  ALA GLY ASN ALA ALA ASN TYR VAL ASN VAL SER ASN PRO          
SEQRES  16 B  448  GLU GLN TYR ILE GLU MET VAL THR SER PRO ASN ASN PRO          
SEQRES  17 B  448  GLU GLY LEU LEU ARG HIS ALA VAL ILE LYS GLY CYS LYS          
SEQRES  18 B  448  SER ILE TYR ASP MET VAL TYR TYR TRP PRO HIS TYR THR          
SEQRES  19 B  448  PRO ILE LYS TYR LYS ALA ASP GLU ASP ILE LEU LEU PHE          
SEQRES  20 B  448  THR MET SER LYS PHE THR GLY HIS SER GLY SER ARG PHE          
SEQRES  21 B  448  GLY TRP ALA LEU ILE LYS ASP GLU SER VAL TYR ASN ASN          
SEQRES  22 B  448  LEU LEU ASN TYR MET THR LYS ASN THR GLU GLY THR PRO          
SEQRES  23 B  448  ARG GLU THR GLN LEU ARG SER LEU LYS VAL LEU LYS GLU          
SEQRES  24 B  448  VAL VAL ALA MET VAL LYS THR GLN LYS GLY THR MET ARG          
SEQRES  25 B  448  ASP LEU ASN THR PHE GLY PHE LYS LYS LEU ARG GLU ARG          
SEQRES  26 B  448  TRP VAL ASN ILE THR ALA LEU LEU ASP GLN SER ASP ARG          
SEQRES  27 B  448  PHE SER TYR GLN GLU LEU PRO GLN SER GLU TYR CYS ASN          
SEQRES  28 B  448  TYR PHE ARG ARG MET ARG PRO PRO SER PRO SER TYR ALA          
SEQRES  29 B  448  TRP VAL LYS CYS GLU TRP GLU GLU ASP LYS ASP CYS TYR          
SEQRES  30 B  448  GLN THR PHE GLN ASN GLY ARG ILE ASN THR GLN ASN GLY          
SEQRES  31 B  448  VAL GLY PHE GLU ALA SER SER ARG TYR VAL ARG LEU SER          
SEQRES  32 B  448  LEU ILE LYS THR GLN ASP ASP PHE ASP GLN LEU MET TYR          
SEQRES  33 B  448  TYR LEU LYS ASP MET VAL LYS ALA LYS ARG LYS THR PRO          
SEQRES  34 B  448  LEU ILE LYS GLN LEU PHE ILE ASP GLN THR GLU THR ALA          
SEQRES  35 B  448  SER ARG ARG PRO PHE ILE                                      
MODRES 1LK9 ASN A  146  ASN  GLYCOSYLATION SITE                                 
MODRES 1LK9 ASN A  328  ASN  GLYCOSYLATION SITE                                 
MODRES 1LK9 ASN B  146  ASN  GLYCOSYLATION SITE                                 
MODRES 1LK9 ASN B  328  ASN  GLYCOSYLATION SITE                                 
HET    NAG  A 500      14                                                       
HET    FUC  A 501      10                                                       
HET    NAG  A 502      14                                                       
HET    BMA  A 503      11                                                       
HET    NAG  A 504      14                                                       
HET    NAG  A 505      14                                                       
HET    NAG  B 500      14                                                       
HET    FUC  B 501      10                                                       
HET    NAG  B 502      14                                                       
HET    NAG  B 503      14                                                       
HET    SO4  A 904       5                                                       
HET    SO4  A 905       5                                                       
HET    SO4  A 906       5                                                       
HET    SO4  A 907       5                                                       
HET    SO4  A 910       5                                                       
HET    SO4  A 911       5                                                       
HET     CL  A1001       1                                                       
HET    SO4  B 901       5                                                       
HET    SO4  B 902       5                                                       
HET    SO4  B 903       5                                                       
HET    SO4  B 908       5                                                       
HET    SO4  B 909       5                                                       
HET     CL  B1002       1                                                       
HET    PLP  A 600      15                                                       
HET    EPE  A 851      15                                                       
HET    EPE  A 852      15                                                       
HET    PLP  B 600      15                                                       
HET    DHA  B 850       6                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     PLP PYRIDOXAL-5'-PHOSPHATE                                           
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETNAM     DHA 2-AMINO-ACRYLIC ACID                                             
HETSYN     PLP VITAMIN B6 PHOSPHATE                                             
HETSYN     EPE HEPES                                                            
HETSYN     DHA 2,3-DIDEHYDROALANINE                                             
FORMUL   3  NAG    7(C8 H15 N O6)                                               
FORMUL   3  FUC    2(C6 H12 O5)                                                 
FORMUL   3  BMA    C6 H12 O6                                                    
FORMUL   7  SO4    11(O4 S 2-)                                                  
FORMUL  13   CL    2(CL 1-)                                                     
FORMUL  20  PLP    2(C8 H10 N O6 P)                                             
FORMUL  21  EPE    2(C8 H18 N2 O4 S)                                            
FORMUL  24  DHA    C3 H5 N O2                                                   
FORMUL  25  HOH   *830(H2 O)                                                    
HELIX    1   1 THR A    5  ASN A   17  1                                  13    
HELIX    2   2 GLY A   66  PHE A   68  5                                   3    
HELIX    3   3 LEU A   69  LYS A   74  1                                   6    
HELIX    4   4 HIS A   76  ALA A   81  1                                   6    
HELIX    5   5 SER A  102  GLY A  117  1                                  16    
HELIX    6   6 VAL A  130  SER A  144  1                                  15    
HELIX    7   7 TYR A  165  PHE A  175  1                                  11    
HELIX    8   8 ALA A  187  VAL A  190  5                                   4    
HELIX    9   9 ASN A  194  GLU A  196  5                                   3    
HELIX   10  10 MET A  249  THR A  253  1                                   5    
HELIX   11  11 HIS A  255  ARG A  259  5                                   5    
HELIX   12  12 ASP A  267  THR A  282  1                                  16    
HELIX   13  13 PRO A  286  LYS A  308  1                                  23    
HELIX   14  14 ASP A  313  ASP A  334  1                                  22    
HELIX   15  15 TRP A  370  LYS A  374  5                                   5    
HELIX   16  16 ASP A  375  GLY A  383  1                                   9    
HELIX   17  17 VAL A  391  GLU A  394  5                                   4    
HELIX   18  18 THR A  407  LYS A  423  1                                  17    
HELIX   19  19 THR B    5  ASN B   17  1                                  13    
HELIX   20  20 GLY B   66  PHE B   68  5                                   3    
HELIX   21  21 LEU B   69  LYS B   74  1                                   6    
HELIX   22  22 HIS B   76  ALA B   81  1                                   6    
HELIX   23  23 SER B  102  GLY B  117  1                                  16    
HELIX   24  24 VAL B  130  SER B  144  1                                  15    
HELIX   25  25 TYR B  165  PHE B  175  1                                  11    
HELIX   26  26 ALA B  187  VAL B  190  5                                   4    
HELIX   27  27 ASN B  194  GLU B  196  5                                   3    
HELIX   28  28 MET B  249  THR B  253  1                                   5    
HELIX   29  29 HIS B  255  ARG B  259  5                                   5    
HELIX   30  30 ASP B  267  GLU B  283  1                                  17    
HELIX   31  31 PRO B  286  LYS B  308  1                                  23    
HELIX   32  32 ASP B  313  ASP B  334  1                                  22    
HELIX   33  33 TRP B  370  LYS B  374  5                                   5    
HELIX   34  34 ASP B  375  GLY B  383  1                                   9    
HELIX   35  35 VAL B  391  GLU B  394  5                                   4    
HELIX   36  36 THR B  407  ALA B  424  1                                  18    
SHEET    1   A 2 GLY A  24  ARG A  25  0                                        
SHEET    2   A 2 GLU A  40  CYS A  41 -1  O  GLU A  40   N  ARG A  25           
SHEET    1   B 2 ILE A  32  SER A  33  0                                        
SHEET    2   B 2 SER A  36  PRO A  37 -1  O  SER A  36   N  SER A  33           
SHEET    1   C 2 TYR A  45  THR A  46  0                                        
SHEET    2   C 2 GLU A  52  LYS A  53 -1  O  GLU A  52   N  THR A  46           
SHEET    1   D 2 ALA A  59  ASP A  60  0                                        
SHEET    2   D 2 ILE A 385  ASN A 386  1  O  ASN A 386   N  ALA A  59           
SHEET    1   E 2 VAL A  82  VAL A  84  0                                        
SHEET    2   E 2 VAL B  82  VAL B  84 -1  O  VAL B  82   N  VAL A  84           
SHEET    1   F 7 TYR A 125  GLY A 129  0                                        
SHEET    2   F 7 GLY A 261  ILE A 265 -1  O  ILE A 265   N  TYR A 125           
SHEET    3   F 7 ILE A 244  THR A 248 -1  N  PHE A 247   O  TRP A 262           
SHEET    4   F 7 LYS A 221  ASP A 225  1  N  TYR A 224   O  LEU A 246           
SHEET    5   F 7 TYR A 198  THR A 203  1  N  VAL A 202   O  ASP A 225           
SHEET    6   F 7 SER A 156  ALA A 160  1  N  VAL A 159   O  MET A 201           
SHEET    7   F 7 TYR A 180  ASN A 185  1  O  ALA A 183   N  VAL A 158           
SHEET    1   G 4 PHE A 339  TYR A 341  0                                        
SHEET    2   G 4 TYR A 363  CYS A 368 -1  O  LYS A 367   N  SER A 340           
SHEET    3   G 4 TYR A 399  SER A 403 -1  O  LEU A 402   N  ALA A 364           
SHEET    4   G 4 GLN A 388  ASN A 389 -1  N  GLN A 388   O  ARG A 401           
SHEET    1   H 2 GLU A 348  CYS A 350  0                                        
SHEET    2   H 2 ARG A 355  ARG A 357 -1  O  ARG A 357   N  GLU A 348           
SHEET    1   I 2 GLY B  24  ARG B  25  0                                        
SHEET    2   I 2 GLU B  40  CYS B  41 -1  O  GLU B  40   N  ARG B  25           
SHEET    1   J 2 ILE B  32  SER B  33  0                                        
SHEET    2   J 2 SER B  36  PRO B  37 -1  O  SER B  36   N  SER B  33           
SHEET    1   K 2 TYR B  45  THR B  46  0                                        
SHEET    2   K 2 GLU B  52  LYS B  53 -1  O  GLU B  52   N  THR B  46           
SHEET    1   L 2 ALA B  59  ASP B  60  0                                        
SHEET    2   L 2 ILE B 385  ASN B 386  1  O  ASN B 386   N  ALA B  59           
SHEET    1   M 7 TYR B 125  GLY B 129  0                                        
SHEET    2   M 7 GLY B 261  ILE B 265 -1  O  ILE B 265   N  TYR B 125           
SHEET    3   M 7 ILE B 244  THR B 248 -1  N  PHE B 247   O  TRP B 262           
SHEET    4   M 7 LYS B 221  ASP B 225  1  N  TYR B 224   O  LEU B 246           
SHEET    5   M 7 TYR B 198  THR B 203  1  N  VAL B 202   O  ASP B 225           
SHEET    6   M 7 SER B 156  ALA B 160  1  N  VAL B 159   O  MET B 201           
SHEET    7   M 7 TYR B 180  ASN B 185  1  O  ALA B 183   N  VAL B 158           
SHEET    1   N 4 PHE B 339  TYR B 341  0                                        
SHEET    2   N 4 TYR B 363  CYS B 368 -1  O  LYS B 367   N  SER B 340           
SHEET    3   N 4 TYR B 399  SER B 403 -1  O  LEU B 402   N  ALA B 364           
SHEET    4   N 4 GLN B 388  ASN B 389 -1  N  GLN B 388   O  ARG B 401           
SHEET    1   O 2 GLU B 348  CYS B 350  0                                        
SHEET    2   O 2 ARG B 355  ARG B 357 -1  O  ARG B 357   N  GLU B 348           
SSBOND   1 CYS A   20    CYS A   39                          1555   1555  2.06  
SSBOND   2 CYS A   41    CYS A   50                          1555   1555  2.05  
SSBOND   3 CYS A   44    CYS A   57                          1555   1555  2.05  
SSBOND   4 CYS A  368    CYS A  376                          1555   1555  2.09  
SSBOND   5 CYS B   20    CYS B   39                          1555   1555  2.09  
SSBOND   6 CYS B   41    CYS B   50                          1555   1555  2.12  
SSBOND   7 CYS B   44    CYS B   57                          1555   1555  2.06  
SSBOND   8 CYS B  368    CYS B  376                          1555   1555  2.12  
LINK         ND2 ASN A 146                 C1  NAG A 500     1555   1555  1.45  
LINK         ND2 ASN A 328                 C1  NAG A 504     1555   1555  1.46  
LINK         ND2 ASN B 146                 C1  NAG B 500     1555   1555  1.46  
LINK         ND2 ASN B 328                 C1  NAG B 502     1555   1555  1.46  
LINK         O3  NAG A 500                 C1  FUC A 501     1555   1555  1.24  
LINK         O4  NAG A 500                 C1  NAG A 502     1555   1555  1.26  
LINK         O4  NAG A 504                 C1  NAG A 505     1555   1555  1.26  
LINK         O3  NAG B 500                 C1  FUC B 501     1555   1555  1.22  
LINK         O4  NAG B 502                 C1  NAG B 503     1555   1555  1.26  
LINK         NZ  LYS B 251                 C4A PLP B 600     1555   1555  1.46  
LINK         NZ  LYS A 251                 C4A PLP A 600     1555   1555  1.48  
LINK         O4  NAG A 502                 C1  BMA A 503     1555   1555  1.18  
LINK         C4A PLP B 600                 N  ADHA B 850     1555   1555  1.50  
CISPEP   1 ASN A   95    PRO A   96          0         0.51                     
CISPEP   2 ALA A  162    PRO A  163          0         1.78                     
CISPEP   3 SER A  204    PRO A  205          0        -4.02                     
CISPEP   4 ASN A  207    PRO A  208          0        18.14                     
CISPEP   5 ASN B   95    PRO B   96          0         2.12                     
CISPEP   6 ALA B  162    PRO B  163          0         3.81                     
CISPEP   7 SER B  204    PRO B  205          0        -9.66                     
CISPEP   8 ASN B  207    PRO B  208          0        24.58                     
SITE     1 AC1  7 ASN A 146  THR A 148  ALA A 149  FUC A 501                    
SITE     2 AC1  7 NAG A 502  HOH A1202  HOH A1309                               
SITE     1 AC2  5 NAG A 500  NAG A 502  HOH A1325  HOH A1330                    
SITE     2 AC2  5 HOH A1345                                                     
SITE     1 AC3  4 NAG A 500  FUC A 501  BMA A 503  HOH A1358                    
SITE     1 AC4  1 NAG A 502                                                     
SITE     1 AC5  5 ASN A 328  GLN A 408  PHE A 411  NAG A 505                    
SITE     2 AC5  5 HOH A1328                                                     
SITE     1 AC6  1 NAG A 504                                                     
SITE     1 AC7  4 HOH A1366  ASN B 146  THR B 148  FUC B 501                    
SITE     1 AC8  5 GLU A 170  TYR A 174  ASN B 276  LYS B 280                    
SITE     2 AC8  5 NAG B 500                                                     
SITE     1 AC9  5 ASN B 328  GLN B 408  PHE B 411  NAG B 503                    
SITE     2 AC9  5 HOH B1374                                                     
SITE     1 BC1  1 NAG B 502                                                     
SITE     1 BC2  3 LYS A 237  GLU A 348  ARG B 384                               
SITE     1 BC3  3 ARG A 323  HOH A1236  HOH A1310                               
SITE     1 BC4  5 ALA A 120  ALA A 121  LYS A 122  LYS A 239                    
SITE     2 BC4  5 HOH A1094                                                     
SITE     1 BC5  3 THR A 310  MET A 311  HOH A1306                               
SITE     1 BC6  9 GLU A  71  LYS A 321  THR A 407  GLN A 408                    
SITE     2 BC6  9 HOH A1075  HOH A1096  HOH A1101  HOH A1145                    
SITE     3 BC6  9 HOH A1308                                                     
SITE     1 BC7  3 ARG A 355  MET A 356  HOH A1376                               
SITE     1 BC8  5 PHE A  93  PHE A  94  SER A  98  ASN A  99                    
SITE     2 BC8  5 PHE A 100                                                     
SITE     1 BC9  6 LYS B  74  GLN B  75  HIS B  76  LYS B  77                    
SITE     2 BC9  6 GLU B  78  HOH B1117                                          
SITE     1 CC1  7 TRP B 370  GLU B 371  ARG B 426  HOH B1166                    
SITE     2 CC1  7 HOH B1269  HOH B1408  HOH B1409                               
SITE     1 CC2  8 HIS B 161  ALA B 187  LYS B 308  ARG B 354                    
SITE     2 CC2  8 HOH B1017  HOH B1103  HOH B1157  HOH B1208                    
SITE     1 CC3  6 GLU B 114  ALA B 120  ALA B 121  LYS B 122                    
SITE     2 CC3  6 LYS B 239  HOH B1246                                          
SITE     1 CC4  4 LYS B 367  TYR B 399  HOH B1165  HOH B1334                    
SITE     1 CC5  5 PHE B  93  PHE B  94  SER B  98  ASN B  99                    
SITE     2 CC5  5 PHE B 100                                                     
SITE     1 CC6 14 GLY A 131  VAL A 132  THR A 133  TYR A 165                    
SITE     2 CC6 14 THR A 203  ASN A 207  ASP A 225  VAL A 227                    
SITE     3 CC6 14 TYR A 228  THR A 248  SER A 250  LYS A 251                    
SITE     4 CC6 14 ARG A 259  TYR B  92                                          
SITE     1 CC7 10 TYR A  92  THR A 279  GLU A 283  HOH A1371                    
SITE     2 CC7 10 SER B  63  GLY B  64  TYR B 165  GLU B 170                    
SITE     3 CC7 10 GLN B 388  ARG B 401                                          
SITE     1 CC8 12 SER A  63  GLY A  64  TYR A 165  GLU A 170                    
SITE     2 CC8 12 GLN A 388  ARG A 401  HOH A1274  HOH A1363                    
SITE     3 CC8 12 HOH A1374  TYR B  92  THR B 279  GLU B 283                    
SITE     1 CC9 15 TYR A  92  GLY B 131  VAL B 132  THR B 133                    
SITE     2 CC9 15 TYR B 165  THR B 203  ASN B 207  ASP B 225                    
SITE     3 CC9 15 VAL B 227  TYR B 228  THR B 248  SER B 250                    
SITE     4 CC9 15 LYS B 251  ARG B 259  DHA B 850                               
SITE     1 DC1 10 TYR A  92  GLY B  64  TYR B 165  ASN B 207                    
SITE     2 DC1 10 TYR B 228  LYS B 251  TYR B 363  ARG B 401                    
SITE     3 DC1 10 PLP B 600  HOH B1380                                          
CRYST1   68.450  101.070  155.690  90.00  90.00  90.00 P 21 21 21    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      0.014610  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009894  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006423        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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