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LongText Report for: 6ob0-pdb

Name Class
6ob0-pdb
HEADER    HYDROLASE/PROTEIN BINDING               19-MAR-19   6OB0              
TITLE     COMPOUND 2 BOUND STRUCTURE OF WT LIPOPROTEIN LIPASE IN COMPLEX WITH   
TITLE    2 GPIHBP1 MUTANT N78D N82D PRODUCED IN HEK293-F CELLS                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LIPOPROTEIN LIPASE;                                        
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: LPL;                                                        
COMPND   5 EC: 3.1.1.34;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: GLYCOSYLPHOSPHATIDYLINOSITOL-ANCHORED HIGH DENSITY         
COMPND   9 LIPOPROTEIN-BINDING PROTEIN 1;                                       
COMPND  10 CHAIN: E, F, G, H;                                                   
COMPND  11 FRAGMENT: RESIDUES 21-151;                                           
COMPND  12 SYNONYM: GPI-ANCHORED HDL-BINDING PROTEIN 1,HIGH DENSITY LIPOPROTEIN-
COMPND  13 BINDING PROTEIN 1;                                                   
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GPIHBP1, HBP1;                                                 
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HEK293-F;                               
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: GPIHBP1, HBP1;                                                 
SOURCE  15 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  16 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  18 EXPRESSION_SYSTEM_CELL_LINE: HEK293-F                                
KEYWDS    LIPASE, HYDROLASE-PROTEIN BINDING COMPLEX                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.ARORA,P.A.HORTON,T.E.BENSON,M.J.ROMANOWSKI                          
REVDAT   1   08-MAY-19 6OB0    0                                                
JRNL        AUTH   R.ARORA,A.NIMONKAR,D.BAIRD,C.WANG,C.-H.CHIU,P.A.HORTON,      
JRNL        AUTH 2 S.HANRAHAN,R.CUBBON,S.WELDON,W.TSCHANTZ,S.MUELLER,R.BRUNNER, 
JRNL        AUTH 3 P.LEHR,P.MEIER,J.OTTL,A.VOZNESENSKY,P.PANDEY,T.SMITH,        
JRNL        AUTH 4 A.STOJANOVIC,A.FLYER,T.E.BENSON,M.J.ROMANOWSKI,J.TRAUGER     
JRNL        TITL   STRUCTURE OF LIPOPROTEIN LIPASE IN COMPLEX WITH GPIHBP1      
JRNL        REF    PROC.NATL.ACAD.SCI.USA                     2019              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        DOI    10.1073/PNAS.1820171116                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.81 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.7                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.81                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.15                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 69989                          
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)  : 0.200                          
REMARK   3   R VALUE            (WORKING SET)  : 0.198                          
REMARK   3   FREE R VALUE                      : 0.233                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.950                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 3465                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 50                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.81                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.83                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.63                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 1400                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2325                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 1323                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2293                   
REMARK   3   BIN FREE R VALUE                        : 0.2862                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.50                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 77                       
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 16511                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 436                                     
REMARK   3   SOLVENT ATOMS            : 226                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 67.92                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -20.53730                                            
REMARK   3    B22 (A**2) : -10.15820                                            
REMARK   3    B33 (A**2) : 30.69550                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.360               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 1.927               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.319               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 2.176               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.325               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.903                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.891                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 17461  ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 23708  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 6044   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : NULL   ; NULL   ; NULL                
REMARK   3    GENERAL PLANES            : 2923   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 17461  ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 1      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 2265   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 19024  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.16                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.01                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 20.99                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6OB0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAR-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000240333.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-MAR-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
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                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 70015                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.810                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 37.100                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : 0.14800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 12.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.81                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.82                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.01450                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: BUSTER 2.11.7                                         
REMARK 200 STARTING MODEL: 6OAZ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.05                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.15M CALCIUM ACETATE, 18% PEG3350,      
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       76.71500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       95.71000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       76.71500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       95.71000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: 2710 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24750 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 2800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: 2730 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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: 4                                                       
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: 2730 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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     ALA A    28                                                      
REMARK 465     ASP A    29                                                      
REMARK 465     LYS A   472                                                      
REMARK 465     LYS A   473                                                      
REMARK 465     SER A   474                                                      
REMARK 465     GLY A   475                                                      
REMARK 465     ALA B    28                                                      
REMARK 465     ASP B    29                                                      
REMARK 465     LYS B   472                                                      
REMARK 465     LYS B   473                                                      
REMARK 465     SER B   474                                                      
REMARK 465     GLY B   475                                                      
REMARK 465     ALA C    28                                                      
REMARK 465     ASP C    29                                                      
REMARK 465     LYS C   472                                                      
REMARK 465     LYS C   473                                                      
REMARK 465     SER C   474                                                      
REMARK 465     GLY C   475                                                      
REMARK 465     ALA D    28                                                      
REMARK 465     ASP D    29                                                      
REMARK 465     LYS D   472                                                      
REMARK 465     LYS D   473                                                      
REMARK 465     SER D   474                                                      
REMARK 465     GLY D   475                                                      
REMARK 465     GLN E    21                                                      
REMARK 465     THR E    22                                                      
REMARK 465     GLN E    23                                                      
REMARK 465     GLN E    24                                                      
REMARK 465     GLU E    25                                                      
REMARK 465     GLU E    26                                                      
REMARK 465     GLU E    27                                                      
REMARK 465     GLU E    28                                                      
REMARK 465     GLU E    29                                                      
REMARK 465     ASP E    30                                                      
REMARK 465     GLU E    31                                                      
REMARK 465     ASP E    32                                                      
REMARK 465     HIS E    33                                                      
REMARK 465     GLY E    34                                                      
REMARK 465     PRO E    35                                                      
REMARK 465     ASP E    36                                                      
REMARK 465     ASP E    37                                                      
REMARK 465     TYR E    38                                                      
REMARK 465     ASP E    39                                                      
REMARK 465     GLU E    40                                                      
REMARK 465     GLU E    41                                                      
REMARK 465     ASP E    42                                                      
REMARK 465     GLU E    43                                                      
REMARK 465     ASP E    44                                                      
REMARK 465     GLU E    45                                                      
REMARK 465     VAL E    46                                                      
REMARK 465     GLU E    47                                                      
REMARK 465     GLU E    48                                                      
REMARK 465     GLU E    49                                                      
REMARK 465     GLU E    50                                                      
REMARK 465     THR E    51                                                      
REMARK 465     ASN E    52                                                      
REMARK 465     ARG E    53                                                      
REMARK 465     LEU E    54                                                      
REMARK 465     PRO E    55                                                      
REMARK 465     GLY E    56                                                      
REMARK 465     GLY E    57                                                      
REMARK 465     ARG E    58                                                      
REMARK 465     SER E    59                                                      
REMARK 465     ARG E    60                                                      
REMARK 465     SER E   144                                                      
REMARK 465     ARG E   145                                                      
REMARK 465     VAL E   146                                                      
REMARK 465     GLN E   147                                                      
REMARK 465     ASP E   148                                                      
REMARK 465     PRO E   149                                                      
REMARK 465     THR E   150                                                      
REMARK 465     GLY E   151                                                      
REMARK 465     GLN F    21                                                      
REMARK 465     THR F    22                                                      
REMARK 465     GLN F    23                                                      
REMARK 465     GLN F    24                                                      
REMARK 465     GLU F    25                                                      
REMARK 465     GLU F    26                                                      
REMARK 465     GLU F    27                                                      
REMARK 465     GLU F    28                                                      
REMARK 465     GLU F    29                                                      
REMARK 465     ASP F    30                                                      
REMARK 465     GLU F    31                                                      
REMARK 465     ASP F    32                                                      
REMARK 465     HIS F    33                                                      
REMARK 465     GLY F    34                                                      
REMARK 465     PRO F    35                                                      
REMARK 465     ASP F    36                                                      
REMARK 465     ASP F    37                                                      
REMARK 465     TYR F    38                                                      
REMARK 465     ASP F    39                                                      
REMARK 465     GLU F    40                                                      
REMARK 465     GLU F    41                                                      
REMARK 465     ASP F    42                                                      
REMARK 465     GLU F    43                                                      
REMARK 465     ASP F    44                                                      
REMARK 465     GLU F    45                                                      
REMARK 465     VAL F    46                                                      
REMARK 465     GLU F    47                                                      
REMARK 465     GLU F    48                                                      
REMARK 465     GLU F    49                                                      
REMARK 465     GLU F    50                                                      
REMARK 465     THR F    51                                                      
REMARK 465     ASN F    52                                                      
REMARK 465     ARG F    53                                                      
REMARK 465     LEU F    54                                                      
REMARK 465     PRO F    55                                                      
REMARK 465     GLY F    56                                                      
REMARK 465     GLY F    57                                                      
REMARK 465     ARG F    58                                                      
REMARK 465     SER F    59                                                      
REMARK 465     ARG F    60                                                      
REMARK 465     VAL F    61                                                      
REMARK 465     LEU F    62                                                      
REMARK 465     SER F   144                                                      
REMARK 465     ARG F   145                                                      
REMARK 465     VAL F   146                                                      
REMARK 465     GLN F   147                                                      
REMARK 465     ASP F   148                                                      
REMARK 465     PRO F   149                                                      
REMARK 465     THR F   150                                                      
REMARK 465     GLY F   151                                                      
REMARK 465     GLN G    21                                                      
REMARK 465     THR G    22                                                      
REMARK 465     GLN G    23                                                      
REMARK 465     GLN G    24                                                      
REMARK 465     GLU G    25                                                      
REMARK 465     GLU G    26                                                      
REMARK 465     GLU G    27                                                      
REMARK 465     GLU G    28                                                      
REMARK 465     GLU G    29                                                      
REMARK 465     ASP G    30                                                      
REMARK 465     GLU G    31                                                      
REMARK 465     ASP G    32                                                      
REMARK 465     HIS G    33                                                      
REMARK 465     GLY G    34                                                      
REMARK 465     PRO G    35                                                      
REMARK 465     ASP G    36                                                      
REMARK 465     ASP G    37                                                      
REMARK 465     TYR G    38                                                      
REMARK 465     ASP G    39                                                      
REMARK 465     GLU G    40                                                      
REMARK 465     GLU G    41                                                      
REMARK 465     ASP G    42                                                      
REMARK 465     GLU G    43                                                      
REMARK 465     ASP G    44                                                      
REMARK 465     GLU G    45                                                      
REMARK 465     VAL G    46                                                      
REMARK 465     GLU G    47                                                      
REMARK 465     GLU G    48                                                      
REMARK 465     GLU G    49                                                      
REMARK 465     GLU G    50                                                      
REMARK 465     THR G    51                                                      
REMARK 465     ASN G    52                                                      
REMARK 465     ARG G    53                                                      
REMARK 465     LEU G    54                                                      
REMARK 465     PRO G    55                                                      
REMARK 465     GLY G    56                                                      
REMARK 465     GLY G    57                                                      
REMARK 465     ARG G    58                                                      
REMARK 465     SER G    59                                                      
REMARK 465     ARG G    60                                                      
REMARK 465     VAL G    61                                                      
REMARK 465     LEU G    62                                                      
REMARK 465     SER G   144                                                      
REMARK 465     ARG G   145                                                      
REMARK 465     VAL G   146                                                      
REMARK 465     GLN G   147                                                      
REMARK 465     ASP G   148                                                      
REMARK 465     PRO G   149                                                      
REMARK 465     THR G   150                                                      
REMARK 465     GLY G   151                                                      
REMARK 465     GLN H    21                                                      
REMARK 465     THR H    22                                                      
REMARK 465     GLN H    23                                                      
REMARK 465     GLN H    24                                                      
REMARK 465     GLU H    25                                                      
REMARK 465     GLU H    26                                                      
REMARK 465     GLU H    27                                                      
REMARK 465     GLU H    28                                                      
REMARK 465     GLU H    29                                                      
REMARK 465     ASP H    30                                                      
REMARK 465     GLU H    31                                                      
REMARK 465     ASP H    32                                                      
REMARK 465     HIS H    33                                                      
REMARK 465     GLY H    34                                                      
REMARK 465     PRO H    35                                                      
REMARK 465     ASP H    36                                                      
REMARK 465     ASP H    37                                                      
REMARK 465     TYR H    38                                                      
REMARK 465     ASP H    39                                                      
REMARK 465     GLU H    40                                                      
REMARK 465     GLU H    41                                                      
REMARK 465     ASP H    42                                                      
REMARK 465     GLU H    43                                                      
REMARK 465     ASP H    44                                                      
REMARK 465     GLU H    45                                                      
REMARK 465     VAL H    46                                                      
REMARK 465     GLU H    47                                                      
REMARK 465     GLU H    48                                                      
REMARK 465     GLU H    49                                                      
REMARK 465     GLU H    50                                                      
REMARK 465     THR H    51                                                      
REMARK 465     ASN H    52                                                      
REMARK 465     ARG H    53                                                      
REMARK 465     LEU H    54                                                      
REMARK 465     PRO H    55                                                      
REMARK 465     GLY H    56                                                      
REMARK 465     GLY H    57                                                      
REMARK 465     ARG H    58                                                      
REMARK 465     SER H    59                                                      
REMARK 465     ARG H    60                                                      
REMARK 465     VAL H    61                                                      
REMARK 465     LEU H    62                                                      
REMARK 465     SER H   144                                                      
REMARK 465     ARG H   145                                                      
REMARK 465     VAL H   146                                                      
REMARK 465     GLN H   147                                                      
REMARK 465     ASP H   148                                                      
REMARK 465     PRO H   149                                                      
REMARK 465     THR H   150                                                      
REMARK 465     GLY H   151                                                      
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    SER A 159     -123.95     55.44                                   
REMARK 500    TYR A 233       79.49   -116.36                                   
REMARK 500    GLU A 254     -138.10     57.08                                   
REMARK 500    GLU A 316       20.66    -73.14                                   
REMARK 500    LYS A 468      113.08   -165.68                                   
REMARK 500    GLN B 118       64.27   -102.61                                   
REMARK 500    SER B 159     -124.71     55.75                                   
REMARK 500    ASP B 183       74.74     35.36                                   
REMARK 500    TYR B 233       78.94   -116.63                                   
REMARK 500    GLU B 254     -133.24     56.42                                   
REMARK 500    LYS B 457     -168.10   -100.96                                   
REMARK 500    HIS B 466      149.80   -178.83                                   
REMARK 500    LYS B 468      110.97   -165.95                                   
REMARK 500    SER C 159     -121.62     61.10                                   
REMARK 500    ASP C 183       68.27     39.92                                   
REMARK 500    TYR C 233       79.57   -116.96                                   
REMARK 500    GLU C 254     -138.53     55.85                                   
REMARK 500    LYS C 457     -168.58   -101.37                                   
REMARK 500    LYS C 468      111.24   -164.35                                   
REMARK 500    HIS D  68       35.33     70.52                                   
REMARK 500    SER D 159     -117.64     53.93                                   
REMARK 500    ASP D 183       71.14     37.27                                   
REMARK 500    TYR D 233       79.95   -116.40                                   
REMARK 500    GLU D 254     -132.58     48.48                                   
REMARK 500    ARG D 255      -32.09    -38.49                                   
REMARK 500    LYS D 457     -166.70   -102.06                                   
REMARK 500    HIS D 466      148.93   -177.67                                   
REMARK 500    LYS D 468      111.53   -165.71                                   
REMARK 500    SER E  70       60.63     24.42                                   
REMARK 500    GLU E  75      124.64   -175.54                                   
REMARK 500    SER E 100       34.45    -89.17                                   
REMARK 500    ASP E 112      -75.27    -90.73                                   
REMARK 500    THR E 120       74.10   -110.87                                   
REMARK 500    TRP E 141        6.36    -68.11                                   
REMARK 500    SER F  70       68.08     27.31                                   
REMARK 500    ASP F  74       46.71    -94.24                                   
REMARK 500    SER F 100       45.21    -93.62                                   
REMARK 500    THR F 120       71.94   -109.97                                   
REMARK 500    ASN F 137       86.85    -67.62                                   
REMARK 500    SER G  70       53.11     32.21                                   
REMARK 500    ASP G  74       15.54    -69.50                                   
REMARK 500    SER G 100       43.11    -94.46                                   
REMARK 500    ASP G 112      -71.43    -88.94                                   
REMARK 500    THR G 120       73.90   -109.23                                   
REMARK 500    ASN G 137       83.82    -64.63                                   
REMARK 500    TRP G 141       14.21    -69.40                                   
REMARK 500    SER H  70       68.25     27.39                                   
REMARK 500    SER H 100       42.92    -94.06                                   
REMARK 500    ASP H 112      -71.45    -87.03                                   
REMARK 500    THR H 120       73.83   -110.91                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      51 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 507  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA A 194   O                                                      
REMARK 620 2 ARG A 197   O    68.6                                              
REMARK 620 3 SER A 199   OG   82.7  98.4                                        
REMARK 620 4 ASP A 202   OD1 152.2 139.1  89.2                                  
REMARK 620 5 ASP A 202   OD2 151.0  86.6  86.6  53.7                            
REMARK 620 6 HOH A 624   O    91.6  91.1 166.3  90.1 103.9                      
REMARK 620 7 HOH A 615   O    81.1 149.0  83.6  71.5 124.3  83.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 508  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA B 194   O                                                      
REMARK 620 2 ARG B 197   O    69.9                                              
REMARK 620 3 SER B 199   OG   85.2 104.0                                        
REMARK 620 4 ASP B 202   OD1 147.3 141.7  91.8                                  
REMARK 620 5 ASP B 202   OD2 158.5  90.6  91.2  53.8                            
REMARK 620 6 HOH B 608   O    79.2 148.7  77.5  68.4 120.7                      
REMARK 620 7 HOH B 625   O    89.2  91.1 161.0  83.1 100.4  83.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C 507  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA C 194   O                                                      
REMARK 620 2 ARG C 197   O    67.6                                              
REMARK 620 3 SER C 199   OG   79.4  98.5                                        
REMARK 620 4 ASP C 202   OD1 146.6 145.7  90.4                                  
REMARK 620 5 ASP C 202   OD2 153.7  91.3  88.9  55.7                            
REMARK 620 6 HOH C 619   O    73.0 140.4  77.4  73.8 127.5                      
REMARK 620 7 HOH C 622   O    92.1  87.5 166.8  91.2 102.8  90.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 507  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA D 194   O                                                      
REMARK 620 2 ARG D 197   O    66.3                                              
REMARK 620 3 SER D 199   OG   82.4  95.7                                        
REMARK 620 4 ASP D 202   OD1 157.2 136.5  92.2                                  
REMARK 620 5 ASP D 202   OD2 146.4  83.4  86.7  54.3                            
REMARK 620 6 HOH D 604   O    81.6 147.8  81.4  75.7 128.0                      
REMARK 620 7 HOH D 643   O    99.6  90.4 173.9  83.8  94.6  93.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue M3D A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue M3D A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 507                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue M3D B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue M3D B 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS B 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 508                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue M3D C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue M3D C 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA C 507                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue M3D D 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue M3D D 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA D 507                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 502 bound   
REMARK 800  to ASN A 70                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 501 bound   
REMARK 800  to ASN A 386                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 502 bound   
REMARK 800  to ASN B 70                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 501 bound   
REMARK 800  to ASN B 386                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 502 bound   
REMARK 800  to ASN C 70                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 501 bound   
REMARK 800  to ASN C 386                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 502 bound   
REMARK 800  to ASN D 70                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 501 bound   
REMARK 800  to ASN D 386                                                        
DBREF  6OB0 A   28   475  UNP    P06858   LIPL_HUMAN      28    475             
DBREF  6OB0 B   28   475  UNP    P06858   LIPL_HUMAN      28    475             
DBREF  6OB0 C   28   475  UNP    P06858   LIPL_HUMAN      28    475             
DBREF  6OB0 D   28   475  UNP    P06858   LIPL_HUMAN      28    475             
DBREF  6OB0 E   21   151  UNP    Q8IV16   HDBP1_HUMAN     21    151             
DBREF  6OB0 F   21   151  UNP    Q8IV16   HDBP1_HUMAN     21    151             
DBREF  6OB0 G   21   151  UNP    Q8IV16   HDBP1_HUMAN     21    151             
DBREF  6OB0 H   21   151  UNP    Q8IV16   HDBP1_HUMAN     21    151             
SEQADV 6OB0 ASP E   78  UNP  Q8IV16    ASN    78 ENGINEERED MUTATION            
SEQADV 6OB0 ASP E   82  UNP  Q8IV16    ASN    82 ENGINEERED MUTATION            
SEQADV 6OB0 ASP F   78  UNP  Q8IV16    ASN    78 ENGINEERED MUTATION            
SEQADV 6OB0 ASP F   82  UNP  Q8IV16    ASN    82 ENGINEERED MUTATION            
SEQADV 6OB0 ASP G   78  UNP  Q8IV16    ASN    78 ENGINEERED MUTATION            
SEQADV 6OB0 ASP G   82  UNP  Q8IV16    ASN    82 ENGINEERED MUTATION            
SEQADV 6OB0 ASP H   78  UNP  Q8IV16    ASN    78 ENGINEERED MUTATION            
SEQADV 6OB0 ASP H   82  UNP  Q8IV16    ASN    82 ENGINEERED MUTATION            
SEQRES   1 A  448  ALA ASP GLN ARG ARG ASP PHE ILE ASP ILE GLU SER LYS          
SEQRES   2 A  448  PHE ALA LEU ARG THR PRO GLU ASP THR ALA GLU ASP THR          
SEQRES   3 A  448  CYS HIS LEU ILE PRO GLY VAL ALA GLU SER VAL ALA THR          
SEQRES   4 A  448  CYS HIS PHE ASN HIS SER SER LYS THR PHE MET VAL ILE          
SEQRES   5 A  448  HIS GLY TRP THR VAL THR GLY MET TYR GLU SER TRP VAL          
SEQRES   6 A  448  PRO LYS LEU VAL ALA ALA LEU TYR LYS ARG GLU PRO ASP          
SEQRES   7 A  448  SER ASN VAL ILE VAL VAL ASP TRP LEU SER ARG ALA GLN          
SEQRES   8 A  448  GLU HIS TYR PRO VAL SER ALA GLY TYR THR LYS LEU VAL          
SEQRES   9 A  448  GLY GLN ASP VAL ALA ARG PHE ILE ASN TRP MET GLU GLU          
SEQRES  10 A  448  GLU PHE ASN TYR PRO LEU ASP ASN VAL HIS LEU LEU GLY          
SEQRES  11 A  448  TYR SER LEU GLY ALA HIS ALA ALA GLY ILE ALA GLY SER          
SEQRES  12 A  448  LEU THR ASN LYS LYS VAL ASN ARG ILE THR GLY LEU ASP          
SEQRES  13 A  448  PRO ALA GLY PRO ASN PHE GLU TYR ALA GLU ALA PRO SER          
SEQRES  14 A  448  ARG LEU SER PRO ASP ASP ALA ASP PHE VAL ASP VAL LEU          
SEQRES  15 A  448  HIS THR PHE THR ARG GLY SER PRO GLY ARG SER ILE GLY          
SEQRES  16 A  448  ILE GLN LYS PRO VAL GLY HIS VAL ASP ILE TYR PRO ASN          
SEQRES  17 A  448  GLY GLY THR PHE GLN PRO GLY CYS ASN ILE GLY GLU ALA          
SEQRES  18 A  448  ILE ARG VAL ILE ALA GLU ARG GLY LEU GLY ASP VAL ASP          
SEQRES  19 A  448  GLN LEU VAL LYS CYS SER HIS GLU ARG SER ILE HIS LEU          
SEQRES  20 A  448  PHE ILE ASP SER LEU LEU ASN GLU GLU ASN PRO SER LYS          
SEQRES  21 A  448  ALA TYR ARG CYS SER SER LYS GLU ALA PHE GLU LYS GLY          
SEQRES  22 A  448  LEU CYS LEU SER CYS ARG LYS ASN ARG CYS ASN ASN LEU          
SEQRES  23 A  448  GLY TYR GLU ILE ASN LYS VAL ARG ALA LYS ARG SER SER          
SEQRES  24 A  448  LYS MET TYR LEU LYS THR ARG SER GLN MET PRO TYR LYS          
SEQRES  25 A  448  VAL PHE HIS TYR GLN VAL LYS ILE HIS PHE SER GLY THR          
SEQRES  26 A  448  GLU SER GLU THR HIS THR ASN GLN ALA PHE GLU ILE SER          
SEQRES  27 A  448  LEU TYR GLY THR VAL ALA GLU SER GLU ASN ILE PRO PHE          
SEQRES  28 A  448  THR LEU PRO GLU VAL SER THR ASN LYS THR TYR SER PHE          
SEQRES  29 A  448  LEU ILE TYR THR GLU VAL ASP ILE GLY GLU LEU LEU MET          
SEQRES  30 A  448  LEU LYS LEU LYS TRP LYS SER ASP SER TYR PHE SER TRP          
SEQRES  31 A  448  SER ASP TRP TRP SER SER PRO GLY PHE ALA ILE GLN LYS          
SEQRES  32 A  448  ILE ARG VAL LYS ALA GLY GLU THR GLN LYS LYS VAL ILE          
SEQRES  33 A  448  PHE CYS SER ARG GLU LYS VAL SER HIS LEU GLN LYS GLY          
SEQRES  34 A  448  LYS ALA PRO ALA VAL PHE VAL LYS CYS HIS ASP LYS SER          
SEQRES  35 A  448  LEU ASN LYS LYS SER GLY                                      
SEQRES   1 B  448  ALA ASP GLN ARG ARG ASP PHE ILE ASP ILE GLU SER LYS          
SEQRES   2 B  448  PHE ALA LEU ARG THR PRO GLU ASP THR ALA GLU ASP THR          
SEQRES   3 B  448  CYS HIS LEU ILE PRO GLY VAL ALA GLU SER VAL ALA THR          
SEQRES   4 B  448  CYS HIS PHE ASN HIS SER SER LYS THR PHE MET VAL ILE          
SEQRES   5 B  448  HIS GLY TRP THR VAL THR GLY MET TYR GLU SER TRP VAL          
SEQRES   6 B  448  PRO LYS LEU VAL ALA ALA LEU TYR LYS ARG GLU PRO ASP          
SEQRES   7 B  448  SER ASN VAL ILE VAL VAL ASP TRP LEU SER ARG ALA GLN          
SEQRES   8 B  448  GLU HIS TYR PRO VAL SER ALA GLY TYR THR LYS LEU VAL          
SEQRES   9 B  448  GLY GLN ASP VAL ALA ARG PHE ILE ASN TRP MET GLU GLU          
SEQRES  10 B  448  GLU PHE ASN TYR PRO LEU ASP ASN VAL HIS LEU LEU GLY          
SEQRES  11 B  448  TYR SER LEU GLY ALA HIS ALA ALA GLY ILE ALA GLY SER          
SEQRES  12 B  448  LEU THR ASN LYS LYS VAL ASN ARG ILE THR GLY LEU ASP          
SEQRES  13 B  448  PRO ALA GLY PRO ASN PHE GLU TYR ALA GLU ALA PRO SER          
SEQRES  14 B  448  ARG LEU SER PRO ASP ASP ALA ASP PHE VAL ASP VAL LEU          
SEQRES  15 B  448  HIS THR PHE THR ARG GLY SER PRO GLY ARG SER ILE GLY          
SEQRES  16 B  448  ILE GLN LYS PRO VAL GLY HIS VAL ASP ILE TYR PRO ASN          
SEQRES  17 B  448  GLY GLY THR PHE GLN PRO GLY CYS ASN ILE GLY GLU ALA          
SEQRES  18 B  448  ILE ARG VAL ILE ALA GLU ARG GLY LEU GLY ASP VAL ASP          
SEQRES  19 B  448  GLN LEU VAL LYS CYS SER HIS GLU ARG SER ILE HIS LEU          
SEQRES  20 B  448  PHE ILE ASP SER LEU LEU ASN GLU GLU ASN PRO SER LYS          
SEQRES  21 B  448  ALA TYR ARG CYS SER SER LYS GLU ALA PHE GLU LYS GLY          
SEQRES  22 B  448  LEU CYS LEU SER CYS ARG LYS ASN ARG CYS ASN ASN LEU          
SEQRES  23 B  448  GLY TYR GLU ILE ASN LYS VAL ARG ALA LYS ARG SER SER          
SEQRES  24 B  448  LYS MET TYR LEU LYS THR ARG SER GLN MET PRO TYR LYS          
SEQRES  25 B  448  VAL PHE HIS TYR GLN VAL LYS ILE HIS PHE SER GLY THR          
SEQRES  26 B  448  GLU SER GLU THR HIS THR ASN GLN ALA PHE GLU ILE SER          
SEQRES  27 B  448  LEU TYR GLY THR VAL ALA GLU SER GLU ASN ILE PRO PHE          
SEQRES  28 B  448  THR LEU PRO GLU VAL SER THR ASN LYS THR TYR SER PHE          
SEQRES  29 B  448  LEU ILE TYR THR GLU VAL ASP ILE GLY GLU LEU LEU MET          
SEQRES  30 B  448  LEU LYS LEU LYS TRP LYS SER ASP SER TYR PHE SER TRP          
SEQRES  31 B  448  SER ASP TRP TRP SER SER PRO GLY PHE ALA ILE GLN LYS          
SEQRES  32 B  448  ILE ARG VAL LYS ALA GLY GLU THR GLN LYS LYS VAL ILE          
SEQRES  33 B  448  PHE CYS SER ARG GLU LYS VAL SER HIS LEU GLN LYS GLY          
SEQRES  34 B  448  LYS ALA PRO ALA VAL PHE VAL LYS CYS HIS ASP LYS SER          
SEQRES  35 B  448  LEU ASN LYS LYS SER GLY                                      
SEQRES   1 C  448  ALA ASP GLN ARG ARG ASP PHE ILE ASP ILE GLU SER LYS          
SEQRES   2 C  448  PHE ALA LEU ARG THR PRO GLU ASP THR ALA GLU ASP THR          
SEQRES   3 C  448  CYS HIS LEU ILE PRO GLY VAL ALA GLU SER VAL ALA THR          
SEQRES   4 C  448  CYS HIS PHE ASN HIS SER SER LYS THR PHE MET VAL ILE          
SEQRES   5 C  448  HIS GLY TRP THR VAL THR GLY MET TYR GLU SER TRP VAL          
SEQRES   6 C  448  PRO LYS LEU VAL ALA ALA LEU TYR LYS ARG GLU PRO ASP          
SEQRES   7 C  448  SER ASN VAL ILE VAL VAL ASP TRP LEU SER ARG ALA GLN          
SEQRES   8 C  448  GLU HIS TYR PRO VAL SER ALA GLY TYR THR LYS LEU VAL          
SEQRES   9 C  448  GLY GLN ASP VAL ALA ARG PHE ILE ASN TRP MET GLU GLU          
SEQRES  10 C  448  GLU PHE ASN TYR PRO LEU ASP ASN VAL HIS LEU LEU GLY          
SEQRES  11 C  448  TYR SER LEU GLY ALA HIS ALA ALA GLY ILE ALA GLY SER          
SEQRES  12 C  448  LEU THR ASN LYS LYS VAL ASN ARG ILE THR GLY LEU ASP          
SEQRES  13 C  448  PRO ALA GLY PRO ASN PHE GLU TYR ALA GLU ALA PRO SER          
SEQRES  14 C  448  ARG LEU SER PRO ASP ASP ALA ASP PHE VAL ASP VAL LEU          
SEQRES  15 C  448  HIS THR PHE THR ARG GLY SER PRO GLY ARG SER ILE GLY          
SEQRES  16 C  448  ILE GLN LYS PRO VAL GLY HIS VAL ASP ILE TYR PRO ASN          
SEQRES  17 C  448  GLY GLY THR PHE GLN PRO GLY CYS ASN ILE GLY GLU ALA          
SEQRES  18 C  448  ILE ARG VAL ILE ALA GLU ARG GLY LEU GLY ASP VAL ASP          
SEQRES  19 C  448  GLN LEU VAL LYS CYS SER HIS GLU ARG SER ILE HIS LEU          
SEQRES  20 C  448  PHE ILE ASP SER LEU LEU ASN GLU GLU ASN PRO SER LYS          
SEQRES  21 C  448  ALA TYR ARG CYS SER SER LYS GLU ALA PHE GLU LYS GLY          
SEQRES  22 C  448  LEU CYS LEU SER CYS ARG LYS ASN ARG CYS ASN ASN LEU          
SEQRES  23 C  448  GLY TYR GLU ILE ASN LYS VAL ARG ALA LYS ARG SER SER          
SEQRES  24 C  448  LYS MET TYR LEU LYS THR ARG SER GLN MET PRO TYR LYS          
SEQRES  25 C  448  VAL PHE HIS TYR GLN VAL LYS ILE HIS PHE SER GLY THR          
SEQRES  26 C  448  GLU SER GLU THR HIS THR ASN GLN ALA PHE GLU ILE SER          
SEQRES  27 C  448  LEU TYR GLY THR VAL ALA GLU SER GLU ASN ILE PRO PHE          
SEQRES  28 C  448  THR LEU PRO GLU VAL SER THR ASN LYS THR TYR SER PHE          
SEQRES  29 C  448  LEU ILE TYR THR GLU VAL ASP ILE GLY GLU LEU LEU MET          
SEQRES  30 C  448  LEU LYS LEU LYS TRP LYS SER ASP SER TYR PHE SER TRP          
SEQRES  31 C  448  SER ASP TRP TRP SER SER PRO GLY PHE ALA ILE GLN LYS          
SEQRES  32 C  448  ILE ARG VAL LYS ALA GLY GLU THR GLN LYS LYS VAL ILE          
SEQRES  33 C  448  PHE CYS SER ARG GLU LYS VAL SER HIS LEU GLN LYS GLY          
SEQRES  34 C  448  LYS ALA PRO ALA VAL PHE VAL LYS CYS HIS ASP LYS SER          
SEQRES  35 C  448  LEU ASN LYS LYS SER GLY                                      
SEQRES   1 D  448  ALA ASP GLN ARG ARG ASP PHE ILE ASP ILE GLU SER LYS          
SEQRES   2 D  448  PHE ALA LEU ARG THR PRO GLU ASP THR ALA GLU ASP THR          
SEQRES   3 D  448  CYS HIS LEU ILE PRO GLY VAL ALA GLU SER VAL ALA THR          
SEQRES   4 D  448  CYS HIS PHE ASN HIS SER SER LYS THR PHE MET VAL ILE          
SEQRES   5 D  448  HIS GLY TRP THR VAL THR GLY MET TYR GLU SER TRP VAL          
SEQRES   6 D  448  PRO LYS LEU VAL ALA ALA LEU TYR LYS ARG GLU PRO ASP          
SEQRES   7 D  448  SER ASN VAL ILE VAL VAL ASP TRP LEU SER ARG ALA GLN          
SEQRES   8 D  448  GLU HIS TYR PRO VAL SER ALA GLY TYR THR LYS LEU VAL          
SEQRES   9 D  448  GLY GLN ASP VAL ALA ARG PHE ILE ASN TRP MET GLU GLU          
SEQRES  10 D  448  GLU PHE ASN TYR PRO LEU ASP ASN VAL HIS LEU LEU GLY          
SEQRES  11 D  448  TYR SER LEU GLY ALA HIS ALA ALA GLY ILE ALA GLY SER          
SEQRES  12 D  448  LEU THR ASN LYS LYS VAL ASN ARG ILE THR GLY LEU ASP          
SEQRES  13 D  448  PRO ALA GLY PRO ASN PHE GLU TYR ALA GLU ALA PRO SER          
SEQRES  14 D  448  ARG LEU SER PRO ASP ASP ALA ASP PHE VAL ASP VAL LEU          
SEQRES  15 D  448  HIS THR PHE THR ARG GLY SER PRO GLY ARG SER ILE GLY          
SEQRES  16 D  448  ILE GLN LYS PRO VAL GLY HIS VAL ASP ILE TYR PRO ASN          
SEQRES  17 D  448  GLY GLY THR PHE GLN PRO GLY CYS ASN ILE GLY GLU ALA          
SEQRES  18 D  448  ILE ARG VAL ILE ALA GLU ARG GLY LEU GLY ASP VAL ASP          
SEQRES  19 D  448  GLN LEU VAL LYS CYS SER HIS GLU ARG SER ILE HIS LEU          
SEQRES  20 D  448  PHE ILE ASP SER LEU LEU ASN GLU GLU ASN PRO SER LYS          
SEQRES  21 D  448  ALA TYR ARG CYS SER SER LYS GLU ALA PHE GLU LYS GLY          
SEQRES  22 D  448  LEU CYS LEU SER CYS ARG LYS ASN ARG CYS ASN ASN LEU          
SEQRES  23 D  448  GLY TYR GLU ILE ASN LYS VAL ARG ALA LYS ARG SER SER          
SEQRES  24 D  448  LYS MET TYR LEU LYS THR ARG SER GLN MET PRO TYR LYS          
SEQRES  25 D  448  VAL PHE HIS TYR GLN VAL LYS ILE HIS PHE SER GLY THR          
SEQRES  26 D  448  GLU SER GLU THR HIS THR ASN GLN ALA PHE GLU ILE SER          
SEQRES  27 D  448  LEU TYR GLY THR VAL ALA GLU SER GLU ASN ILE PRO PHE          
SEQRES  28 D  448  THR LEU PRO GLU VAL SER THR ASN LYS THR TYR SER PHE          
SEQRES  29 D  448  LEU ILE TYR THR GLU VAL ASP ILE GLY GLU LEU LEU MET          
SEQRES  30 D  448  LEU LYS LEU LYS TRP LYS SER ASP SER TYR PHE SER TRP          
SEQRES  31 D  448  SER ASP TRP TRP SER SER PRO GLY PHE ALA ILE GLN LYS          
SEQRES  32 D  448  ILE ARG VAL LYS ALA GLY GLU THR GLN LYS LYS VAL ILE          
SEQRES  33 D  448  PHE CYS SER ARG GLU LYS VAL SER HIS LEU GLN LYS GLY          
SEQRES  34 D  448  LYS ALA PRO ALA VAL PHE VAL LYS CYS HIS ASP LYS SER          
SEQRES  35 D  448  LEU ASN LYS LYS SER GLY                                      
SEQRES   1 E  131  GLN THR GLN GLN GLU GLU GLU GLU GLU ASP GLU ASP HIS          
SEQRES   2 E  131  GLY PRO ASP ASP TYR ASP GLU GLU ASP GLU ASP GLU VAL          
SEQRES   3 E  131  GLU GLU GLU GLU THR ASN ARG LEU PRO GLY GLY ARG SER          
SEQRES   4 E  131  ARG VAL LEU LEU ARG CYS TYR THR CYS LYS SER LEU PRO          
SEQRES   5 E  131  ARG ASP GLU ARG CYS ASP LEU THR GLN ASP CYS SER HIS          
SEQRES   6 E  131  GLY GLN THR CYS THR THR LEU ILE ALA HIS GLY ASN THR          
SEQRES   7 E  131  GLU SER GLY LEU LEU THR THR HIS SER THR TRP CYS THR          
SEQRES   8 E  131  ASP SER CYS GLN PRO ILE THR LYS THR VAL GLU GLY THR          
SEQRES   9 E  131  GLN VAL THR MET THR CYS CYS GLN SER SER LEU CYS ASN          
SEQRES  10 E  131  VAL PRO PRO TRP GLN SER SER ARG VAL GLN ASP PRO THR          
SEQRES  11 E  131  GLY                                                          
SEQRES   1 F  131  GLN THR GLN GLN GLU GLU GLU GLU GLU ASP GLU ASP HIS          
SEQRES   2 F  131  GLY PRO ASP ASP TYR ASP GLU GLU ASP GLU ASP GLU VAL          
SEQRES   3 F  131  GLU GLU GLU GLU THR ASN ARG LEU PRO GLY GLY ARG SER          
SEQRES   4 F  131  ARG VAL LEU LEU ARG CYS TYR THR CYS LYS SER LEU PRO          
SEQRES   5 F  131  ARG ASP GLU ARG CYS ASP LEU THR GLN ASP CYS SER HIS          
SEQRES   6 F  131  GLY GLN THR CYS THR THR LEU ILE ALA HIS GLY ASN THR          
SEQRES   7 F  131  GLU SER GLY LEU LEU THR THR HIS SER THR TRP CYS THR          
SEQRES   8 F  131  ASP SER CYS GLN PRO ILE THR LYS THR VAL GLU GLY THR          
SEQRES   9 F  131  GLN VAL THR MET THR CYS CYS GLN SER SER LEU CYS ASN          
SEQRES  10 F  131  VAL PRO PRO TRP GLN SER SER ARG VAL GLN ASP PRO THR          
SEQRES  11 F  131  GLY                                                          
SEQRES   1 G  131  GLN THR GLN GLN GLU GLU GLU GLU GLU ASP GLU ASP HIS          
SEQRES   2 G  131  GLY PRO ASP ASP TYR ASP GLU GLU ASP GLU ASP GLU VAL          
SEQRES   3 G  131  GLU GLU GLU GLU THR ASN ARG LEU PRO GLY GLY ARG SER          
SEQRES   4 G  131  ARG VAL LEU LEU ARG CYS TYR THR CYS LYS SER LEU PRO          
SEQRES   5 G  131  ARG ASP GLU ARG CYS ASP LEU THR GLN ASP CYS SER HIS          
SEQRES   6 G  131  GLY GLN THR CYS THR THR LEU ILE ALA HIS GLY ASN THR          
SEQRES   7 G  131  GLU SER GLY LEU LEU THR THR HIS SER THR TRP CYS THR          
SEQRES   8 G  131  ASP SER CYS GLN PRO ILE THR LYS THR VAL GLU GLY THR          
SEQRES   9 G  131  GLN VAL THR MET THR CYS CYS GLN SER SER LEU CYS ASN          
SEQRES  10 G  131  VAL PRO PRO TRP GLN SER SER ARG VAL GLN ASP PRO THR          
SEQRES  11 G  131  GLY                                                          
SEQRES   1 H  131  GLN THR GLN GLN GLU GLU GLU GLU GLU ASP GLU ASP HIS          
SEQRES   2 H  131  GLY PRO ASP ASP TYR ASP GLU GLU ASP GLU ASP GLU VAL          
SEQRES   3 H  131  GLU GLU GLU GLU THR ASN ARG LEU PRO GLY GLY ARG SER          
SEQRES   4 H  131  ARG VAL LEU LEU ARG CYS TYR THR CYS LYS SER LEU PRO          
SEQRES   5 H  131  ARG ASP GLU ARG CYS ASP LEU THR GLN ASP CYS SER HIS          
SEQRES   6 H  131  GLY GLN THR CYS THR THR LEU ILE ALA HIS GLY ASN THR          
SEQRES   7 H  131  GLU SER GLY LEU LEU THR THR HIS SER THR TRP CYS THR          
SEQRES   8 H  131  ASP SER CYS GLN PRO ILE THR LYS THR VAL GLU GLY THR          
SEQRES   9 H  131  GLN VAL THR MET THR CYS CYS GLN SER SER LEU CYS ASN          
SEQRES  10 H  131  VAL PRO PRO TRP GLN SER SER ARG VAL GLN ASP PRO THR          
SEQRES  11 H  131  GLY                                                          
HET    NAG  A 501      14                                                       
HET    NAG  A 502      14                                                       
HET    M3D  A 503      35                                                       
HET    M3D  A 504      35                                                       
HET    EDO  A 505       4                                                       
HET    EDO  A 506       4                                                       
HET     CA  A 507       1                                                       
HET    NAG  B 501      14                                                       
HET    NAG  B 502      14                                                       
HET    M3D  B 503      35                                                       
HET    M3D  B 504      35                                                       
HET    EDO  B 505       4                                                       
HET    EDO  B 506       4                                                       
HET    TRS  B 507       8                                                       
HET     CA  B 508       1                                                       
HET    NAG  C 501      14                                                       
HET    NAG  C 502      14                                                       
HET    M3D  C 503      35                                                       
HET    M3D  C 504      35                                                       
HET    EDO  C 505       4                                                       
HET    EDO  C 506       4                                                       
HET     CA  C 507       1                                                       
HET    NAG  D 501      14                                                       
HET    NAG  D 502      14                                                       
HET    M3D  D 503      35                                                       
HET    M3D  D 504      35                                                       
HET    EDO  D 505       4                                                       
HET    EDO  D 506       4                                                       
HET     CA  D 507       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     M3D 7-(3-CYANO-4-HYDROXYPHENYL)-N-[2-(MORPHOLIN-4-YL)                
HETNAM   2 M3D  ETHYL]DIBENZO[B,F]OXEPINE-10-CARBOXAMIDE                        
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM      CA CALCIUM ION                                                      
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   9  NAG    8(C8 H15 N O6)                                               
FORMUL  11  M3D    8(C28 H25 N3 O4)                                             
FORMUL  13  EDO    8(C2 H6 O2)                                                  
FORMUL  15   CA    4(CA 2+)                                                     
FORMUL  22  TRS    C4 H12 N O3 1+                                               
FORMUL  38  HOH   *226(H2 O)                                                    
HELIX    1 AA1 GLN A   30  PHE A   34  5                                   5    
HELIX    2 AA2 ALA A   61  HIS A   68  1                                   8    
HELIX    3 AA3 SER A   90  GLU A  103  1                                  14    
HELIX    4 AA4 TRP A  113  GLN A  118  1                                   6    
HELIX    5 AA5 HIS A  120  ASN A  147  1                                  28    
HELIX    6 AA6 PRO A  149  ASP A  151  5                                   3    
HELIX    7 AA7 LEU A  160  THR A  172  1                                  13    
HELIX    8 AA8 GLU A  193  ARG A  197  5                                   5    
HELIX    9 AA9 SER A  199  ALA A  203  5                                   5    
HELIX   10 AB1 GLY A  246  GLU A  254  1                                   9    
HELIX   11 AB2 ASP A  259  LYS A  265  1                                   7    
HELIX   12 AB3 LYS A  265  ASN A  281  1                                  17    
HELIX   13 AB4 SER A  293  GLU A  298  1                                   6    
HELIX   14 AB5 CYS A  305  ASN A  308  5                                   4    
HELIX   15 AB6 GLN B   30  PHE B   34  5                                   5    
HELIX   16 AB7 VAL B   60  HIS B   68  1                                   9    
HELIX   17 AB8 SER B   90  GLU B  103  1                                  14    
HELIX   18 AB9 TRP B  113  GLN B  118  1                                   6    
HELIX   19 AC1 HIS B  120  ASN B  147  1                                  28    
HELIX   20 AC2 PRO B  149  ASP B  151  5                                   3    
HELIX   21 AC3 LEU B  160  THR B  172  1                                  13    
HELIX   22 AC4 GLU B  193  ARG B  197  5                                   5    
HELIX   23 AC5 SER B  199  ALA B  203  5                                   5    
HELIX   24 AC6 GLY B  246  GLU B  254  1                                   9    
HELIX   25 AC7 ASP B  259  LYS B  265  1                                   7    
HELIX   26 AC8 LYS B  265  ASN B  281  1                                  17    
HELIX   27 AC9 SER B  293  LYS B  299  1                                   7    
HELIX   28 AD1 GLN C   30  PHE C   34  5                                   5    
HELIX   29 AD2 ALA C   61  HIS C   68  1                                   8    
HELIX   30 AD3 SER C   90  GLU C  103  1                                  14    
HELIX   31 AD4 TRP C  113  GLN C  118  1                                   6    
HELIX   32 AD5 HIS C  120  ASN C  147  1                                  28    
HELIX   33 AD6 PRO C  149  ASP C  151  5                                   3    
HELIX   34 AD7 LEU C  160  THR C  172  1                                  13    
HELIX   35 AD8 GLU C  193  ARG C  197  5                                   5    
HELIX   36 AD9 SER C  199  ALA C  203  5                                   5    
HELIX   37 AE1 GLY C  246  GLU C  254  1                                   9    
HELIX   38 AE2 ASP C  259  LYS C  265  1                                   7    
HELIX   39 AE3 LYS C  265  ASN C  281  1                                  17    
HELIX   40 AE4 SER C  293  LYS C  299  1                                   7    
HELIX   41 AE5 CYS C  305  ASN C  308  5                                   4    
HELIX   42 AE6 GLN D   30  PHE D   34  5                                   5    
HELIX   43 AE7 ALA D   61  HIS D   68  1                                   8    
HELIX   44 AE8 SER D   90  GLU D  103  1                                  14    
HELIX   45 AE9 SER D  115  GLU D  119  5                                   5    
HELIX   46 AF1 HIS D  120  TYR D  127  1                                   8    
HELIX   47 AF2 TYR D  127  ASN D  147  1                                  21    
HELIX   48 AF3 PRO D  149  ASP D  151  5                                   3    
HELIX   49 AF4 SER D  159  THR D  172  1                                  14    
HELIX   50 AF5 GLU D  193  ARG D  197  5                                   5    
HELIX   51 AF6 SER D  199  ALA D  203  5                                   5    
HELIX   52 AF7 GLY D  246  GLU D  254  1                                   9    
HELIX   53 AF8 ASP D  259  LYS D  265  1                                   7    
HELIX   54 AF9 LYS D  265  ASN D  281  1                                  17    
HELIX   55 AG1 SER D  293  LYS D  299  1                                   7    
HELIX   56 AG2 PRO E  139  SER E  143  5                                   5    
SHEET    1 AA110 LYS A  40  ARG A  44  0                                        
SHEET    2 AA110 ASN A 107  ASP A 112 -1  O  ASP A 112   N  LYS A  40           
SHEET    3 AA110 THR A  75  ILE A  79  1  N  PHE A  76   O  ILE A 109           
SHEET    4 AA110 VAL A 153  TYR A 158  1  O  LEU A 156   N  ILE A  79           
SHEET    5 AA110 ARG A 178  LEU A 182  1  O  THR A 180   N  LEU A 155           
SHEET    6 AA110 PHE A 205  LEU A 209  1  O  ASP A 207   N  GLY A 181           
SHEET    7 AA110 VAL A 230  PRO A 234  1  O  ILE A 232   N  VAL A 208           
SHEET    8 AA110 SER A 326  LEU A 330  1  O  MET A 328   N  TYR A 233           
SHEET    9 AA110 LYS A 287  ARG A 290 -1  N  TYR A 289   O  TYR A 329           
SHEET   10 AA110 CYS A 310  ASN A 312 -1  O  ASN A 311   N  ALA A 288           
SHEET    1 AA2 8 GLU A 372  SER A 384  0                                        
SHEET    2 AA2 8 THR A 356  GLY A 368 -1  N  HIS A 357   O  VAL A 383           
SHEET    3 AA2 8 LEU A 402  TRP A 409 -1  O  LEU A 403   N  TYR A 367           
SHEET    4 AA2 8 ALA A 460  SER A 469 -1  O  ALA A 460   N  LEU A 407           
SHEET    5 AA2 8 LYS A 440  SER A 446 -1  N  CYS A 445   O  VAL A 463           
SHEET    6 AA2 8 LYS A 430  ALA A 435 -1  N  VAL A 433   O  VAL A 442           
SHEET    7 AA2 8 PHE A 341  PHE A 349 -1  N  LYS A 346   O  ARG A 432           
SHEET    8 AA2 8 LYS A 387  THR A 395 -1  O  ILE A 393   N  TYR A 343           
SHEET    1 AA3 2 GLY A 425  ILE A 428  0                                        
SHEET    2 AA3 2 SER A 451  GLN A 454 -1  O  LEU A 453   N  PHE A 426           
SHEET    1 AA410 LYS B  40  ARG B  44  0                                        
SHEET    2 AA410 ASN B 107  ASP B 112 -1  O  ASP B 112   N  LYS B  40           
SHEET    3 AA410 THR B  75  ILE B  79  1  N  PHE B  76   O  ILE B 109           
SHEET    4 AA410 VAL B 153  SER B 159  1  O  LEU B 156   N  ILE B  79           
SHEET    5 AA410 ARG B 178  PRO B 184  1  O  THR B 180   N  LEU B 155           
SHEET    6 AA410 PHE B 205  LEU B 209  1  O  LEU B 209   N  GLY B 181           
SHEET    7 AA410 VAL B 230  PRO B 234  1  O  ILE B 232   N  VAL B 208           
SHEET    8 AA410 SER B 326  LEU B 330  1  O  MET B 328   N  ASP B 231           
SHEET    9 AA410 LYS B 287  ARG B 290 -1  N  TYR B 289   O  TYR B 329           
SHEET   10 AA410 CYS B 310  ASN B 312 -1  O  ASN B 311   N  ALA B 288           
SHEET    1 AA5 8 GLU B 372  SER B 384  0                                        
SHEET    2 AA5 8 THR B 356  GLY B 368 -1  N  HIS B 357   O  VAL B 383           
SHEET    3 AA5 8 LEU B 402  TRP B 409 -1  O  LEU B 403   N  TYR B 367           
SHEET    4 AA5 8 ALA B 460  SER B 469 -1  O  ALA B 460   N  LEU B 407           
SHEET    5 AA5 8 LYS B 440  SER B 446 -1  N  CYS B 445   O  VAL B 463           
SHEET    6 AA5 8 LYS B 430  ALA B 435 -1  N  VAL B 433   O  VAL B 442           
SHEET    7 AA5 8 PHE B 341  PHE B 349 -1  N  LYS B 346   O  ARG B 432           
SHEET    8 AA5 8 LYS B 387  THR B 395 -1  O  LYS B 387   N  PHE B 349           
SHEET    1 AA6 2 GLY B 425  ILE B 428  0                                        
SHEET    2 AA6 2 SER B 451  GLN B 454 -1  O  LEU B 453   N  PHE B 426           
SHEET    1 AA710 LYS C  40  ARG C  44  0                                        
SHEET    2 AA710 ASN C 107  ASP C 112 -1  O  ASP C 112   N  LYS C  40           
SHEET    3 AA710 THR C  75  ILE C  79  1  N  PHE C  76   O  ILE C 109           
SHEET    4 AA710 VAL C 153  TYR C 158  1  O  LEU C 156   N  ILE C  79           
SHEET    5 AA710 ARG C 178  LEU C 182  1  O  THR C 180   N  LEU C 155           
SHEET    6 AA710 PHE C 205  LEU C 209  1  O  LEU C 209   N  GLY C 181           
SHEET    7 AA710 VAL C 230  PRO C 234  1  O  ILE C 232   N  VAL C 208           
SHEET    8 AA710 SER C 326  LEU C 330  1  O  MET C 328   N  TYR C 233           
SHEET    9 AA710 LYS C 287  ARG C 290 -1  N  TYR C 289   O  TYR C 329           
SHEET   10 AA710 CYS C 310  ASN C 312 -1  O  ASN C 311   N  ALA C 288           
SHEET    1 AA8 8 GLU C 372  SER C 384  0                                        
SHEET    2 AA8 8 THR C 356  GLY C 368 -1  N  PHE C 362   O  PHE C 378           
SHEET    3 AA8 8 LEU C 402  TRP C 409 -1  O  LEU C 403   N  TYR C 367           
SHEET    4 AA8 8 ALA C 460  SER C 469 -1  O  ALA C 460   N  LEU C 407           
SHEET    5 AA8 8 LYS C 440  SER C 446 -1  N  CYS C 445   O  VAL C 463           
SHEET    6 AA8 8 LYS C 430  ALA C 435 -1  N  VAL C 433   O  VAL C 442           
SHEET    7 AA8 8 PHE C 341  PHE C 349 -1  N  LYS C 346   O  ARG C 432           
SHEET    8 AA8 8 LYS C 387  THR C 395 -1  O  LYS C 387   N  PHE C 349           
SHEET    1 AA9 2 GLY C 425  ILE C 428  0                                        
SHEET    2 AA9 2 SER C 451  GLN C 454 -1  O  LEU C 453   N  PHE C 426           
SHEET    1 AB110 LYS D  40  ARG D  44  0                                        
SHEET    2 AB110 ASN D 107  ASP D 112 -1  O  ASP D 112   N  LYS D  40           
SHEET    3 AB110 THR D  75  ILE D  79  1  N  PHE D  76   O  ILE D 109           
SHEET    4 AB110 VAL D 153  TYR D 158  1  O  LEU D 156   N  MET D  77           
SHEET    5 AB110 ARG D 178  LEU D 182  1  O  THR D 180   N  LEU D 155           
SHEET    6 AB110 PHE D 205  LEU D 209  1  O  ASP D 207   N  GLY D 181           
SHEET    7 AB110 VAL D 230  PRO D 234  1  O  ILE D 232   N  VAL D 208           
SHEET    8 AB110 SER D 326  LEU D 330  1  O  MET D 328   N  TYR D 233           
SHEET    9 AB110 LYS D 287  ARG D 290 -1  N  TYR D 289   O  TYR D 329           
SHEET   10 AB110 CYS D 310  ASN D 312 -1  O  ASN D 311   N  ALA D 288           
SHEET    1 AB2 8 GLU D 372  SER D 384  0                                        
SHEET    2 AB2 8 THR D 356  GLY D 368 -1  N  HIS D 357   O  VAL D 383           
SHEET    3 AB2 8 LEU D 402  TRP D 409 -1  O  LYS D 408   N  GLU D 363           
SHEET    4 AB2 8 ALA D 460  SER D 469 -1  O  ALA D 460   N  LEU D 407           
SHEET    5 AB2 8 LYS D 440  SER D 446 -1  N  CYS D 445   O  VAL D 463           
SHEET    6 AB2 8 LYS D 430  ALA D 435 -1  N  VAL D 433   O  VAL D 442           
SHEET    7 AB2 8 PHE D 341  PHE D 349 -1  N  LYS D 346   O  ARG D 432           
SHEET    8 AB2 8 LYS D 387  THR D 395 -1  O  THR D 395   N  PHE D 341           
SHEET    1 AB3 2 GLY D 425  ILE D 428  0                                        
SHEET    2 AB3 2 SER D 451  GLN D 454 -1  O  LEU D 453   N  PHE D 426           
SHEET    1 AB4 2 ARG E  64  TYR E  66  0                                        
SHEET    2 AB4 2 THR E  80  ASP E  82 -1  O  GLN E  81   N  CYS E  65           
SHEET    1 AB5 5 CYS E  68  PRO E  72  0                                        
SHEET    2 AB5 5 GLY E 101  THR E 111 -1  O  HIS E 106   N  LEU E  71           
SHEET    3 AB5 5 THR E  88  THR E  98 -1  N  LEU E  92   O  SER E 107           
SHEET    4 AB5 5 THR E 124  CYS E 131 -1  O  GLN E 125   N  HIS E  95           
SHEET    5 AB5 5 ILE E 117  VAL E 121 -1  N  ILE E 117   O  MET E 128           
SHEET    1 AB6 2 ARG F  64  TYR F  66  0                                        
SHEET    2 AB6 2 THR F  80  ASP F  82 -1  O  GLN F  81   N  CYS F  65           
SHEET    1 AB7 5 CYS F  68  PRO F  72  0                                        
SHEET    2 AB7 5 GLY F 101  THR F 111 -1  O  HIS F 106   N  LEU F  71           
SHEET    3 AB7 5 THR F  88  THR F  98 -1  N  THR F  88   O  THR F 111           
SHEET    4 AB7 5 THR F 124  CYS F 131 -1  O  THR F 127   N  ILE F  93           
SHEET    5 AB7 5 ILE F 117  THR F 120 -1  N  ILE F 117   O  MET F 128           
SHEET    1 AB8 2 ARG G  64  TYR G  66  0                                        
SHEET    2 AB8 2 THR G  80  ASP G  82 -1  O  GLN G  81   N  CYS G  65           
SHEET    1 AB9 5 CYS G  68  PRO G  72  0                                        
SHEET    2 AB9 5 GLY G 101  THR G 111 -1  O  THR G 108   N  CYS G  68           
SHEET    3 AB9 5 THR G  88  THR G  98 -1  N  LEU G  92   O  SER G 107           
SHEET    4 AB9 5 GLN G 125  CYS G 131 -1  O  THR G 127   N  ILE G  93           
SHEET    5 AB9 5 ILE G 117  THR G 120 -1  N  ILE G 117   O  MET G 128           
SHEET    1 AC1 2 ARG H  64  TYR H  66  0                                        
SHEET    2 AC1 2 THR H  80  ASP H  82 -1  O  GLN H  81   N  CYS H  65           
SHEET    1 AC2 5 CYS H  68  PRO H  72  0                                        
SHEET    2 AC2 5 GLY H 101  THR H 111 -1  O  HIS H 106   N  LEU H  71           
SHEET    3 AC2 5 THR H  88  THR H  98 -1  N  LEU H  92   O  SER H 107           
SHEET    4 AC2 5 THR H 124  CYS H 131 -1  O  THR H 127   N  ILE H  93           
SHEET    5 AC2 5 ILE H 117  VAL H 121 -1  N  ILE H 117   O  MET H 128           
SSBOND   1 CYS A   54    CYS A   67                          1555   1555  2.06  
SSBOND   2 CYS A  243    CYS A  266                          1555   1555  2.08  
SSBOND   3 CYS A  291    CYS A  302                          1555   1555  2.04  
SSBOND   4 CYS A  305    CYS A  310                          1555   1555  2.06  
SSBOND   5 CYS A  445    CYS A  465                          1555   1555  2.09  
SSBOND   6 CYS B   54    CYS B   67                          1555   1555  2.05  
SSBOND   7 CYS B  243    CYS B  266                          1555   1555  2.07  
SSBOND   8 CYS B  291    CYS B  302                          1555   1555  2.04  
SSBOND   9 CYS B  305    CYS B  310                          1555   1555  2.07  
SSBOND  10 CYS B  445    CYS B  465                          1555   1555  2.09  
SSBOND  11 CYS C   54    CYS C   67                          1555   1555  2.05  
SSBOND  12 CYS C  243    CYS C  266                          1555   1555  2.09  
SSBOND  13 CYS C  291    CYS C  302                          1555   1555  2.04  
SSBOND  14 CYS C  305    CYS C  310                          1555   1555  2.08  
SSBOND  15 CYS C  445    CYS C  465                          1555   1555  2.09  
SSBOND  16 CYS D   54    CYS D   67                          1555   1555  2.06  
SSBOND  17 CYS D  243    CYS D  266                          1555   1555  2.08  
SSBOND  18 CYS D  291    CYS D  302                          1555   1555  2.06  
SSBOND  19 CYS D  305    CYS D  310                          1555   1555  2.07  
SSBOND  20 CYS D  445    CYS D  465                          1555   1555  2.08  
SSBOND  21 CYS E   65    CYS E   89                          1555   1555  2.05  
SSBOND  22 CYS E   68    CYS E   77                          1555   1555  2.05  
SSBOND  23 CYS E   83    CYS E  110                          1555   1555  2.05  
SSBOND  24 CYS E  114    CYS E  130                          1555   1555  2.04  
SSBOND  25 CYS E  131    CYS E  136                          1555   1555  2.05  
SSBOND  26 CYS F   65    CYS F   89                          1555   1555  2.04  
SSBOND  27 CYS F   68    CYS F   77                          1555   1555  2.05  
SSBOND  28 CYS F   83    CYS F  110                          1555   1555  2.05  
SSBOND  29 CYS F  114    CYS F  130                          1555   1555  2.04  
SSBOND  30 CYS F  131    CYS F  136                          1555   1555  2.05  
SSBOND  31 CYS G   65    CYS G   89                          1555   1555  2.03  
SSBOND  32 CYS G   68    CYS G   77                          1555   1555  2.05  
SSBOND  33 CYS G   83    CYS G  110                          1555   1555  2.05  
SSBOND  34 CYS G  114    CYS G  130                          1555   1555  2.05  
SSBOND  35 CYS G  131    CYS G  136                          1555   1555  2.04  
SSBOND  36 CYS H   65    CYS H   89                          1555   1555  2.04  
SSBOND  37 CYS H   68    CYS H   77                          1555   1555  2.06  
SSBOND  38 CYS H   83    CYS H  110                          1555   1555  2.06  
SSBOND  39 CYS H  114    CYS H  130                          1555   1555  2.05  
SSBOND  40 CYS H  131    CYS H  136                          1555   1555  2.05  
LINK         ND2 ASN A  70                 C1  NAG A 502     1555   1555  1.44  
LINK         O   ALA A 194                CA    CA A 507     1555   1555  2.21  
LINK         O   ARG A 197                CA    CA A 507     1555   1555  2.51  
LINK         OG  SER A 199                CA    CA A 507     1555   1555  2.40  
LINK         OD1 ASP A 202                CA    CA A 507     1555   1555  2.45  
LINK         OD2 ASP A 202                CA    CA A 507     1555   1555  2.41  
LINK         ND2 ASN A 386                 C1  NAG A 501     1555   1555  1.44  
LINK         ND2 ASN B  70                 C1  NAG B 502     1555   1555  1.44  
LINK         O   ALA B 194                CA    CA B 508     1555   1555  2.21  
LINK         O   ARG B 197                CA    CA B 508     1555   1555  2.45  
LINK         OG  SER B 199                CA    CA B 508     1555   1555  2.25  
LINK         OD1 ASP B 202                CA    CA B 508     1555   1555  2.49  
LINK         OD2 ASP B 202                CA    CA B 508     1555   1555  2.33  
LINK         ND2 ASN B 386                 C1  NAG B 501     1555   1555  1.43  
LINK         ND2 ASN C  70                 C1  NAG C 502     1555   1555  1.44  
LINK         O   ALA C 194                CA    CA C 507     1555   1555  2.32  
LINK         O   ARG C 197                CA    CA C 507     1555   1555  2.47  
LINK         OG  SER C 199                CA    CA C 507     1555   1555  2.41  
LINK         OD1 ASP C 202                CA    CA C 507     1555   1555  2.41  
LINK         OD2 ASP C 202                CA    CA C 507     1555   1555  2.27  
LINK         ND2 ASN C 386                 C1  NAG C 501     1555   1555  1.43  
LINK         ND2 ASN D  70                 C1  NAG D 502     1555   1555  1.44  
LINK         O   ALA D 194                CA    CA D 507     1555   1555  2.22  
LINK         O   ARG D 197                CA    CA D 507     1555   1555  2.64  
LINK         OG  SER D 199                CA    CA D 507     1555   1555  2.37  
LINK         OD1 ASP D 202                CA    CA D 507     1555   1555  2.38  
LINK         OD2 ASP D 202                CA    CA D 507     1555   1555  2.43  
LINK         ND2 ASN D 386                 C1  NAG D 501     1555   1555  1.44  
LINK        CA    CA A 507                 O   HOH A 624     1555   1555  2.56  
LINK        CA    CA A 507                 O   HOH A 615     1555   1555  2.16  
LINK        CA    CA B 508                 O   HOH B 608     1555   1555  2.33  
LINK        CA    CA B 508                 O   HOH B 625     1555   1555  2.47  
LINK        CA    CA C 507                 O   HOH C 619     1555   1555  2.28  
LINK        CA    CA C 507                 O   HOH C 622     1555   1555  2.61  
LINK        CA    CA D 507                 O   HOH D 604     1555   1555  2.48  
LINK        CA    CA D 507                 O   HOH D 643     1555   1555  2.13  
CISPEP   1 MET A  336    PRO A  337          0        -3.55                     
CISPEP   2 MET B  336    PRO B  337          0        -3.24                     
CISPEP   3 MET C  336    PRO C  337          0        -3.62                     
CISPEP   4 MET D  336    PRO D  337          0        -2.81                     
SITE     1 AC1 13 TRP A  82  VAL A  84  THR A  85  GLN A 262                    
SITE     2 AC1 13 LEU A 263  VAL A 264  LYS A 265  M3D A 504                    
SITE     3 AC1 13 HOH A 610  TYR B 414  PHE B 415  TRP B 417                    
SITE     4 AC1 13 EDO B 506                                                     
SITE     1 AC2 11 TRP A  82  TYR A 121  PRO A 122  SER A 159                    
SITE     2 AC2 11 PRO A 187  LYS A 265  HIS A 268  M3D A 503                    
SITE     3 AC2 11 PHE B 415  TRP B 420  TRP B 421                               
SITE     1 AC3  8 HIS A  80  GLY A  81  TRP A  82  MET A  87                    
SITE     2 AC3  8 TYR A  88  GLU A  89  TRP A  91  TYR A 158                    
SITE     1 AC4  5 TRP A 417  GLU B  89  SER B  90  GLU B 269                    
SITE     2 AC4  5 M3D B 503                                                     
SITE     1 AC5  6 ALA A 194  ARG A 197  SER A 199  ASP A 202                    
SITE     2 AC5  6 HOH A 615  HOH A 624                                          
SITE     1 AC6 13 TYR A 414  PHE A 415  TRP A 417  EDO A 506                    
SITE     2 AC6 13 TRP B  82  VAL B  84  THR B  85  GLN B 262                    
SITE     3 AC6 13 LEU B 263  VAL B 264  LYS B 265  M3D B 504                    
SITE     4 AC6 13 HOH B 628                                                     
SITE     1 AC7 10 TRP A 420  TRP A 421  TRP B  82  HIS B 120                    
SITE     2 AC7 10 TYR B 121  SER B 159  PRO B 187  LYS B 265                    
SITE     3 AC7 10 HIS B 268  M3D B 503                                          
SITE     1 AC8  8 HIS B  80  GLY B  81  TRP B  82  MET B  87                    
SITE     2 AC8  8 TYR B  88  GLU B  89  TRP B  91  TYR B 158                    
SITE     1 AC9  5 GLU A  89  SER A  90  GLU A 269  M3D A 503                    
SITE     2 AC9  5 TRP B 417                                                     
SITE     1 AD1  3 THR B  85  GLN B 118  GLU B 119                               
SITE     1 AD2  6 ALA B 194  ARG B 197  SER B 199  ASP B 202                    
SITE     2 AD2  6 HOH B 608  HOH B 625                                          
SITE     1 AD3 13 TRP C  82  VAL C  84  THR C  85  GLN C 262                    
SITE     2 AD3 13 LEU C 263  LYS C 265  M3D C 504  HOH C 616                    
SITE     3 AD3 13 HOH C 630  TYR D 414  PHE D 415  TRP D 417                    
SITE     4 AD3 13 EDO D 506                                                     
SITE     1 AD4 12 TRP C  82  TYR C 121  PRO C 122  SER C 159                    
SITE     2 AD4 12 PRO C 187  LYS C 265  HIS C 268  M3D C 503                    
SITE     3 AD4 12 HOH C 639  PHE D 415  TRP D 420  TRP D 421                    
SITE     1 AD5  6 HIS C  80  GLY C  81  TRP C  82  MET C  87                    
SITE     2 AD5  6 GLU C  89  TRP C  91                                          
SITE     1 AD6  5 TRP C 417  GLU D  89  SER D  90  GLU D 269                    
SITE     2 AD6  5 M3D D 503                                                     
SITE     1 AD7  6 ALA C 194  ARG C 197  SER C 199  ASP C 202                    
SITE     2 AD7  6 HOH C 619  HOH C 622                                          
SITE     1 AD8 14 TYR C 414  PHE C 415  TRP C 417  EDO C 506                    
SITE     2 AD8 14 TRP D  82  VAL D  84  THR D  85  GLN D 262                    
SITE     3 AD8 14 LEU D 263  VAL D 264  LYS D 265  M3D D 504                    
SITE     4 AD8 14 HOH D 616  HOH D 622                                          
SITE     1 AD9 11 PHE C 415  TRP C 420  TRP C 421  TRP D  82                    
SITE     2 AD9 11 MET D  87  TYR D 121  SER D 159  PRO D 187                    
SITE     3 AD9 11 LYS D 265  HIS D 268  M3D D 503                               
SITE     1 AE1  8 HIS D  80  GLY D  81  TRP D  82  MET D  87                    
SITE     2 AE1  8 TYR D  88  GLU D  89  TRP D  91  TYR D 158                    
SITE     1 AE2  6 GLU C  89  SER C  90  GLU C 269  M3D C 503                    
SITE     2 AE2  6 HOH C 616  TRP D 417                                          
SITE     1 AE3  6 ALA D 194  ARG D 197  SER D 199  ASP D 202                    
SITE     2 AE3  6 HOH D 604  HOH D 643                                          
SITE     1 AE4  3 ASN A  70  SER A  73  ASP A 105                               
SITE     1 AE5  4 GLY A 351  THR A 352  SER A 354  ASN A 386                    
SITE     1 AE6  3 ASN B  70  SER B  73  ASP B 105                               
SITE     1 AE7  4 GLY B 351  THR B 352  SER B 354  ASN B 386                    
SITE     1 AE8  3 ASN C  70  SER C  73  ASP C 105                               
SITE     1 AE9  4 GLY C 351  THR C 352  SER C 354  ASN C 386                    
SITE     1 AF1  3 ASN D  70  SER D  73  ASP D 105                               
SITE     1 AF2  4 GLY D 351  THR D 352  SER D 354  ASN D 386                    
CRYST1  153.430  191.420   97.180  90.00  90.00  90.00 P 21 21 2    16          
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      0.006518  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005224  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010290        0.00000                         
TER    3519      ASN A 471                                                      
TER    7031      ASN B 471                                                      
TER   10550      ASN C 471                                                      
TER   14069      ASN D 471                                                      
TER   14698      SER E 143                                                      
TER   15312      SER F 143                                                      
TER   15926      SER G 143                                                      
TER   16540      SER H 143                                                      
MASTER      727    0   29   56  108    0   61    617173    8  556  184          
END                                                                             

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
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