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LongText Report for: 6fat-pdb

Name Class
6fat-pdb
HEADER    HYDROLASE                               17-DEC-17   6FAT              
TITLE     THE CRYSTAL STRUCTURE OF A FERULOYL ESTERASE C FROM FUSARIUM          
TITLE    2 OXYSPORUM.                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CARBOXYLIC ESTER HYDROLASE;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.1.1.-;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: FUSARIUM OXYSPORUM;                             
SOURCE   3 ORGANISM_COMMON: FUSARIUM VASCULAR WILT;                             
SOURCE   4 ORGANISM_TAXID: 5507;                                                
SOURCE   5 GENE: FAEC;                                                          
SOURCE   6 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4922                                        
KEYWDS    FERULIC ACID ESTERASE, HYDROLASE                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.DIMAROGONA,E.D.CHRYSINA                                             
REVDAT   1   30-JAN-19 6FAT    0                                                
JRNL        AUTH   M.DIMAROGONA,E.D.CHRYSINA                                    
JRNL        TITL   THE CRYSTAL STRUCTURE OF A FERULOYL ESTERASE C FROM FUSARIUM 
JRNL        TITL 2 OXYSPORUM.                                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.MOUKOULI,E.TOPAKAS,P.CHRISTAKOPOULOS                       
REMARK   1  TITL   CLONING, CHARACTERIZATION AND FUNCTIONAL EXPRESSION OF AN    
REMARK   1  TITL 2 ALKALITOLERANT TYPE C FERULOYL ESTERASE FROM FUSARIUM        
REMARK   1  TITL 3 OXYSPORUM.                                                   
REMARK   1  REF    APPL. MICROBIOL. BIOTECHNOL.  V.  79   245 2008              
REMARK   1  REFN                   ISSN 0175-7598                               
REMARK   1  PMID   18414848                                                     
REMARK   1  DOI    10.1007/S00253-008-1432-3                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 102.35                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 49493                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : FREE R-VALUE                    
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2634                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3638                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.26                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3190                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 191                          
REMARK   3   BIN FREE R VALUE                    : 0.3100                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7910                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 407                                     
REMARK   3   SOLVENT ATOMS            : 357                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.96                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.86000                                             
REMARK   3    B22 (A**2) : -0.15000                                             
REMARK   3    B33 (A**2) : 2.91000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -4.12000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.373         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.231         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.218         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.882         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8600 ; 0.007 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  7454 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11731 ; 1.072 ; 1.989       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 17324 ; 0.862 ; 3.003       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1056 ;17.770 ; 5.398       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   380 ;34.272 ;24.132       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1222 ;11.272 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    41 ;13.997 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1316 ; 0.058 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9357 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1753 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4068 ; 0.565 ; 3.532       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4067 ; 0.565 ; 3.531       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5077 ; 1.051 ; 5.296       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  5078 ; 1.051 ; 5.297       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4532 ; 0.437 ; 3.665       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  4532 ; 0.437 ; 3.665       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  6654 ; 0.807 ; 5.482       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  9554 ; 1.994 ;41.463       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  9497 ; 1.926 ;41.417       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 6FAT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-DEC-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200008019.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-JAN-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PETRA III, EMBL C/O DESY           
REMARK 200  BEAMLINE                       : P14 (MX2)                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.2395                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 300K               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 52149                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 102.350                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.09600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 0.0950                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.37                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 3WMT                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% (V/V) PEG400, 0.1M TRIS-HCL PH 8.5   
REMARK 280  BUFFER, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289.15K          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       43.73350            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLN A   544                                                      
REMARK 465     LYS A   545                                                      
REMARK 465     LEU A   546                                                      
REMARK 465     ILE A   547                                                      
REMARK 465     SER A   548                                                      
REMARK 465     GLU A   549                                                      
REMARK 465     GLU A   550                                                      
REMARK 465     ASP A   551                                                      
REMARK 465     LEU A   552                                                      
REMARK 465     ASN A   553                                                      
REMARK 465     SER A   554                                                      
REMARK 465     ALA A   555                                                      
REMARK 465     VAL A   556                                                      
REMARK 465     ASP A   557                                                      
REMARK 465     HIS A   558                                                      
REMARK 465     HIS A   559                                                      
REMARK 465     HIS A   560                                                      
REMARK 465     HIS A   561                                                      
REMARK 465     HIS A   562                                                      
REMARK 465     HIS A   563                                                      
REMARK 465     GLN B   544                                                      
REMARK 465     LYS B   545                                                      
REMARK 465     LEU B   546                                                      
REMARK 465     ILE B   547                                                      
REMARK 465     SER B   548                                                      
REMARK 465     GLU B   549                                                      
REMARK 465     GLU B   550                                                      
REMARK 465     ASP B   551                                                      
REMARK 465     LEU B   552                                                      
REMARK 465     ASN B   553                                                      
REMARK 465     SER B   554                                                      
REMARK 465     ALA B   555                                                      
REMARK 465     VAL B   556                                                      
REMARK 465     ASP B   557                                                      
REMARK 465     HIS B   558                                                      
REMARK 465     HIS B   559                                                      
REMARK 465     HIS B   560                                                      
REMARK 465     HIS B   561                                                      
REMARK 465     HIS B   562                                                      
REMARK 465     HIS B   563                                                      
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    TYR A 170      -39.06   -143.06                                   
REMARK 500    SER A 201     -111.26     62.36                                   
REMARK 500    ALA A 225       55.26     36.15                                   
REMARK 500    ALA A 227       38.08    -83.44                                   
REMARK 500    ASP A 270      -80.15    -77.17                                   
REMARK 500    LYS A 302      -68.39   -145.87                                   
REMARK 500    PHE A 317       35.84    -93.06                                   
REMARK 500    ASN A 383       72.47     39.73                                   
REMARK 500    CYS A 453      -46.98     73.26                                   
REMARK 500    LYS A 472       51.95   -119.54                                   
REMARK 500    LYS A 527      -52.21   -161.21                                   
REMARK 500    TYR B 170      -33.81   -147.84                                   
REMARK 500    SER B 201     -112.93     67.00                                   
REMARK 500    ALA B 225       54.12     33.05                                   
REMARK 500    ALA B 227       40.43    -82.38                                   
REMARK 500    ASP B 270      -80.73    -80.28                                   
REMARK 500    PHE B 317       34.57    -91.36                                   
REMARK 500    CYS B 453      -39.38     74.67                                   
REMARK 500    LYS B 527      -61.47   -128.62                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 897        DISTANCE =  6.82 ANGSTROMS                       
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 613  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 270   OD1                                                    
REMARK 620 2 ASP A 274   OD1 105.3                                              
REMARK 620 3 ASP A 274   OD2  84.9  46.3                                        
REMARK 620 4 VAL A 276   O    90.0  81.8 123.4                                  
REMARK 620 5 ASP A 278   OD1  96.4 149.6 159.6  77.0                            
REMARK 620 6 ILE A 280   O    70.9 123.1  77.3 151.3  83.9                      
REMARK 620 7 HOH A 745   O   154.4  86.2  87.1 114.5  83.0  83.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 622  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 270   OD1                                                    
REMARK 620 2 ASP B 274   OD1 110.6                                              
REMARK 620 3 ASP B 274   OD2  92.3  46.2                                        
REMARK 620 4 VAL B 276   O    87.2  82.8 124.9                                  
REMARK 620 5 ASP B 278   OD1  89.0 151.1 158.1  76.9                            
REMARK 620 6 ILE B 280   O    68.4 124.2  78.1 148.1  82.2                      
REMARK 620 7 HOH B 799   O   152.2  89.9  88.8 114.6  80.2  84.7                
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 CA A 613                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA B 622                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  601 through BMA A 603 bound to ASN A 66                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 604 bound   
REMARK 800  to ASN A 101                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  605 through BMA A 607 bound to ASN A 151                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  608 through MAN A 612 bound to ASN A 362                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  601 through NAG B 602 bound to ASN B 66                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 603 bound   
REMARK 800  to ASN B 101                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  604 through MAN B 610 bound to ASN B 151                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  611 through MAN B 621 bound to ASN B 362                            
DBREF1 6FAT A   36   563  UNP                  A0A1D3S5H0_FUSOX                 
DBREF2 6FAT A     A0A1D3S5H0                         36         563             
DBREF1 6FAT B   36   563  UNP                  A0A1D3S5H0_FUSOX                 
DBREF2 6FAT B     A0A1D3S5H0                         36         563             
SEQRES   1 A  528  ASP PHE ALA ALA LYS CYS ALA GLY PHE LYS THR SER LEU          
SEQRES   2 A  528  LYS LEU PRO ASN THR LYS VAL TRP PHE THR GLU HIS VAL          
SEQRES   3 A  528  PRO ALA GLY LYS ASN ILE THR PHE PRO ASP ASN HIS PRO          
SEQRES   4 A  528  THR CYS THR PRO LYS SER THR ILE THR ASP VAL GLU ILE          
SEQRES   5 A  528  CYS ARG VAL ALA MET PHE VAL THR THR GLY PRO LYS SER          
SEQRES   6 A  528  ASN LEU THR LEU GLU ALA TRP LEU PRO SER ASN TRP THR          
SEQRES   7 A  528  GLY ARG PHE LEU SER THR GLY ASN GLY GLY MET ALA GLY          
SEQRES   8 A  528  CYS ILE GLN TYR ASP ASP VAL ALA TYR GLY ALA GLY PHE          
SEQRES   9 A  528  GLY PHE ALA THR VAL GLY ALA ASN ASN GLY HIS ASN GLY          
SEQRES  10 A  528  THR SER ALA VAL SER MET TYR LYS ASN SER GLY VAL VAL          
SEQRES  11 A  528  GLU ASP TYR VAL TYR ARG SER VAL HIS THR GLY THR VAL          
SEQRES  12 A  528  LEU GLY LYS GLU LEU THR LYS LYS PHE TYR GLY LYS LYS          
SEQRES  13 A  528  HIS THR LYS SER TYR TYR LEU GLY CYS SER THR GLY GLY          
SEQRES  14 A  528  ARG GLN GLY TRP LYS GLU ALA GLN SER PHE PRO ASP ASP          
SEQRES  15 A  528  PHE ASP GLY ILE VAL ALA GLY ALA PRO ALA MET ARG PHE          
SEQRES  16 A  528  ASN GLY LEU GLN SER ARG SER GLY SER PHE TRP GLY ILE          
SEQRES  17 A  528  THR GLY PRO PRO GLY ALA PRO THR HIS LEU SER PRO GLU          
SEQRES  18 A  528  GLU TRP ALA MET VAL GLN LYS ASN VAL LEU VAL GLN CYS          
SEQRES  19 A  528  ASP GLU PRO LEU ASP GLY VAL ALA ASP GLY ILE LEU GLU          
SEQRES  20 A  528  ASP PRO ASN LEU CYS GLN TYR ARG PRO GLU ALA LEU VAL          
SEQRES  21 A  528  CYS SER LYS GLY GLN THR LYS ASN CYS LEU THR GLY PRO          
SEQRES  22 A  528  GLN ILE GLU THR VAL ARG LYS VAL PHE GLY PRO LEU TYR          
SEQRES  23 A  528  GLY ASN ASN GLY THR TYR ILE TYR PRO ARG ILE PRO PRO          
SEQRES  24 A  528  GLY ALA ASP GLN GLY PHE GLY PHE ALA ILE GLY GLU GLN          
SEQRES  25 A  528  PRO PHE PRO TYR SER THR GLU TRP PHE GLN TYR VAL ILE          
SEQRES  26 A  528  TRP ASN ASP THR LYS TRP ASP PRO ASN THR ILE GLY PRO          
SEQRES  27 A  528  ASN ASP TYR GLN LYS ALA SER GLU VAL ASN PRO PHE ASN          
SEQRES  28 A  528  VAL GLU THR TRP GLU GLY ASP LEU SER LYS PHE ARG LYS          
SEQRES  29 A  528  ARG GLY SER LYS ILE ILE HIS TRP HIS GLY LEU GLU ASP          
SEQRES  30 A  528  GLY LEU ILE SER SER ASP ASN SER MET GLU TYR TYR ASN          
SEQRES  31 A  528  HIS VAL SER ALA THR MET GLY LEU SER ASN THR GLU LEU          
SEQRES  32 A  528  ASP GLU PHE TYR ARG TYR PHE ARG VAL SER GLY CYS GLY          
SEQRES  33 A  528  HIS CYS SER GLY GLY ILE GLY ALA ASN ARG ILE GLY ASN          
SEQRES  34 A  528  ASN ARG ALA ASN LEU GLY GLY LYS GLU ALA LYS ASN ASN          
SEQRES  35 A  528  VAL LEU LEU ALA LEU VAL LYS TRP VAL GLU GLU GLY GLN          
SEQRES  36 A  528  ALA PRO GLU THR ILE THR GLY VAL ARG TYR VAL ASN GLY          
SEQRES  37 A  528  ALA THR THR GLY LYS VAL GLU VAL GLU ARG ARG HIS CYS          
SEQRES  38 A  528  ARG TYR PRO TYR ARG ASN VAL TRP ASP ARG LYS GLY ASN          
SEQRES  39 A  528  TYR LYS ASN PRO ASP SER TRP LYS CYS GLU LEU PRO LEU          
SEQRES  40 A  528  GLU GLN LYS LEU ILE SER GLU GLU ASP LEU ASN SER ALA          
SEQRES  41 A  528  VAL ASP HIS HIS HIS HIS HIS HIS                              
SEQRES   1 B  528  ASP PHE ALA ALA LYS CYS ALA GLY PHE LYS THR SER LEU          
SEQRES   2 B  528  LYS LEU PRO ASN THR LYS VAL TRP PHE THR GLU HIS VAL          
SEQRES   3 B  528  PRO ALA GLY LYS ASN ILE THR PHE PRO ASP ASN HIS PRO          
SEQRES   4 B  528  THR CYS THR PRO LYS SER THR ILE THR ASP VAL GLU ILE          
SEQRES   5 B  528  CYS ARG VAL ALA MET PHE VAL THR THR GLY PRO LYS SER          
SEQRES   6 B  528  ASN LEU THR LEU GLU ALA TRP LEU PRO SER ASN TRP THR          
SEQRES   7 B  528  GLY ARG PHE LEU SER THR GLY ASN GLY GLY MET ALA GLY          
SEQRES   8 B  528  CYS ILE GLN TYR ASP ASP VAL ALA TYR GLY ALA GLY PHE          
SEQRES   9 B  528  GLY PHE ALA THR VAL GLY ALA ASN ASN GLY HIS ASN GLY          
SEQRES  10 B  528  THR SER ALA VAL SER MET TYR LYS ASN SER GLY VAL VAL          
SEQRES  11 B  528  GLU ASP TYR VAL TYR ARG SER VAL HIS THR GLY THR VAL          
SEQRES  12 B  528  LEU GLY LYS GLU LEU THR LYS LYS PHE TYR GLY LYS LYS          
SEQRES  13 B  528  HIS THR LYS SER TYR TYR LEU GLY CYS SER THR GLY GLY          
SEQRES  14 B  528  ARG GLN GLY TRP LYS GLU ALA GLN SER PHE PRO ASP ASP          
SEQRES  15 B  528  PHE ASP GLY ILE VAL ALA GLY ALA PRO ALA MET ARG PHE          
SEQRES  16 B  528  ASN GLY LEU GLN SER ARG SER GLY SER PHE TRP GLY ILE          
SEQRES  17 B  528  THR GLY PRO PRO GLY ALA PRO THR HIS LEU SER PRO GLU          
SEQRES  18 B  528  GLU TRP ALA MET VAL GLN LYS ASN VAL LEU VAL GLN CYS          
SEQRES  19 B  528  ASP GLU PRO LEU ASP GLY VAL ALA ASP GLY ILE LEU GLU          
SEQRES  20 B  528  ASP PRO ASN LEU CYS GLN TYR ARG PRO GLU ALA LEU VAL          
SEQRES  21 B  528  CYS SER LYS GLY GLN THR LYS ASN CYS LEU THR GLY PRO          
SEQRES  22 B  528  GLN ILE GLU THR VAL ARG LYS VAL PHE GLY PRO LEU TYR          
SEQRES  23 B  528  GLY ASN ASN GLY THR TYR ILE TYR PRO ARG ILE PRO PRO          
SEQRES  24 B  528  GLY ALA ASP GLN GLY PHE GLY PHE ALA ILE GLY GLU GLN          
SEQRES  25 B  528  PRO PHE PRO TYR SER THR GLU TRP PHE GLN TYR VAL ILE          
SEQRES  26 B  528  TRP ASN ASP THR LYS TRP ASP PRO ASN THR ILE GLY PRO          
SEQRES  27 B  528  ASN ASP TYR GLN LYS ALA SER GLU VAL ASN PRO PHE ASN          
SEQRES  28 B  528  VAL GLU THR TRP GLU GLY ASP LEU SER LYS PHE ARG LYS          
SEQRES  29 B  528  ARG GLY SER LYS ILE ILE HIS TRP HIS GLY LEU GLU ASP          
SEQRES  30 B  528  GLY LEU ILE SER SER ASP ASN SER MET GLU TYR TYR ASN          
SEQRES  31 B  528  HIS VAL SER ALA THR MET GLY LEU SER ASN THR GLU LEU          
SEQRES  32 B  528  ASP GLU PHE TYR ARG TYR PHE ARG VAL SER GLY CYS GLY          
SEQRES  33 B  528  HIS CYS SER GLY GLY ILE GLY ALA ASN ARG ILE GLY ASN          
SEQRES  34 B  528  ASN ARG ALA ASN LEU GLY GLY LYS GLU ALA LYS ASN ASN          
SEQRES  35 B  528  VAL LEU LEU ALA LEU VAL LYS TRP VAL GLU GLU GLY GLN          
SEQRES  36 B  528  ALA PRO GLU THR ILE THR GLY VAL ARG TYR VAL ASN GLY          
SEQRES  37 B  528  ALA THR THR GLY LYS VAL GLU VAL GLU ARG ARG HIS CYS          
SEQRES  38 B  528  ARG TYR PRO TYR ARG ASN VAL TRP ASP ARG LYS GLY ASN          
SEQRES  39 B  528  TYR LYS ASN PRO ASP SER TRP LYS CYS GLU LEU PRO LEU          
SEQRES  40 B  528  GLU GLN LYS LEU ILE SER GLU GLU ASP LEU ASN SER ALA          
SEQRES  41 B  528  VAL ASP HIS HIS HIS HIS HIS HIS                              
MODRES 6FAT CYS A   41  CYS  S                                                  
MODRES 6FAT CYS A   76  CYS  S                                                  
MODRES 6FAT CYS A  200  CYS  S                                                  
MODRES 6FAT CYS A  269  CYS  S                                                  
MODRES 6FAT CYS A  296  CYS  S                                                  
MODRES 6FAT CYS A  516  CYS  S                                                  
MODRES 6FAT CYS A   88  CYS  S                                                  
MODRES 6FAT CYS A  127  CYS  S                                                  
MODRES 6FAT CYS A  453  CYS  S                                                  
MODRES 6FAT CYS A  287  CYS  S                                                  
MODRES 6FAT CYS A  304  CYS  S                                                  
MODRES 6FAT CYS A  538  CYS  S                                                  
MODRES 6FAT CYS B   41  CYS  S                                                  
MODRES 6FAT CYS B   76  CYS  S                                                  
MODRES 6FAT CYS B  200  CYS  S                                                  
MODRES 6FAT CYS B  269  CYS  S                                                  
MODRES 6FAT CYS B  296  CYS  S                                                  
MODRES 6FAT CYS B  516  CYS  S                                                  
MODRES 6FAT CYS B   88  CYS  S                                                  
MODRES 6FAT CYS B  127  CYS  S                                                  
MODRES 6FAT CYS B  453  CYS  S                                                  
MODRES 6FAT CYS B  287  CYS  S                                                  
MODRES 6FAT CYS B  304  CYS  S                                                  
MODRES 6FAT CYS B  538  CYS  S                                                  
HET    NAG  A 601      14                                                       
HET    NAG  A 602      14                                                       
HET    BMA  A 603      11                                                       
HET    NAG  A 604      14                                                       
HET    NAG  A 605      14                                                       
HET    NAG  A 606      14                                                       
HET    BMA  A 607      11                                                       
HET    NAG  A 608      14                                                       
HET    NAG  A 609      14                                                       
HET    BMA  A 610      11                                                       
HET    MAN  A 611      11                                                       
HET    MAN  A 612      11                                                       
HET     CA  A 613       1                                                       
HET    NAG  B 601      14                                                       
HET    NAG  B 602      14                                                       
HET    NAG  B 603      14                                                       
HET    NAG  B 604      14                                                       
HET    NAG  B 605      14                                                       
HET    BMA  B 606      11                                                       
HET    MAN  B 607      11                                                       
HET    MAN  B 608      11                                                       
HET    MAN  B 609      11                                                       
HET    MAN  B 610      11                                                       
HET    NAG  B 611      14                                                       
HET    NAG  B 612      14                                                       
HET    BMA  B 613      11                                                       
HET    MAN  B 614      11                                                       
HET    MAN  B 615      11                                                       
HET    MAN  B 616      11                                                       
HET    MAN  B 617      11                                                       
HET    MAN  B 618      11                                                       
HET    MAN  B 619      11                                                       
HET    MAN  B 620      11                                                       
HET    MAN  B 621      11                                                       
HET     CA  B 622       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM      CA CALCIUM ION                                                      
FORMUL   3  NAG    14(C8 H15 N O6)                                              
FORMUL   3  BMA    5(C6 H12 O6)                                                 
FORMUL   6  MAN    14(C6 H12 O6)                                                
FORMUL   7   CA    2(CA 2+)                                                     
FORMUL  13  HOH   *357(H2 O)                                                    
HELIX    1 AA1 ASP A   36  LEU A   48  1                                  13    
HELIX    2 AA2 GLN A  129  PHE A  139  1                                  11    
HELIX    3 AA3 ALA A  155  TYR A  159  5                                   5    
HELIX    4 AA4 ASN A  161  TYR A  170  1                                  10    
HELIX    5 AA5 TYR A  170  GLY A  189  1                                  20    
HELIX    6 AA6 SER A  201  PHE A  214  1                                  14    
HELIX    7 AA7 ARG A  229  GLY A  245  1                                  17    
HELIX    8 AA8 SER A  254  ASP A  270  1                                  17    
HELIX    9 AA9 ASP A  270  GLY A  275  1                                   6    
HELIX   10 AB1 ARG A  290  VAL A  295  5                                   6    
HELIX   11 AB2 THR A  306  PHE A  317  1                                  12    
HELIX   12 AB3 ASN A  323  GLY A  325  5                                   3    
HELIX   13 AB4 GLY A  339  ILE A  344  1                                   6    
HELIX   14 AB5 PHE A  349  VAL A  359  1                                  11    
HELIX   15 AB6 ASP A  367  ILE A  371  5                                   5    
HELIX   16 AB7 GLY A  372  ASN A  383  1                                  12    
HELIX   17 AB8 PRO A  384  VAL A  387  5                                   4    
HELIX   18 AB9 LEU A  394  ARG A  400  1                                   7    
HELIX   19 AC1 SER A  416  GLY A  432  1                                  17    
HELIX   20 AC2 SER A  434  ASP A  439  1                                   6    
HELIX   21 AC3 GLU A  473  ASN A  476  5                                   4    
HELIX   22 AC4 ASN A  477  GLY A  489  1                                  13    
HELIX   23 AC5 ASN A  502  ALA A  504  5                                   3    
HELIX   24 AC6 ASN A  532  ASP A  534  5                                   3    
HELIX   25 AC7 PHE B   37  LEU B   48  1                                  12    
HELIX   26 AC8 GLN B  129  PHE B  139  1                                  11    
HELIX   27 AC9 ALA B  155  TYR B  159  5                                   5    
HELIX   28 AD1 ASN B  161  TYR B  170  1                                  10    
HELIX   29 AD2 TYR B  170  GLY B  189  1                                  20    
HELIX   30 AD3 SER B  201  PHE B  214  1                                  14    
HELIX   31 AD4 PRO B  215  PHE B  218  5                                   4    
HELIX   32 AD5 ARG B  229  GLY B  245  1                                  17    
HELIX   33 AD6 SER B  254  ASP B  270  1                                  17    
HELIX   34 AD7 ASP B  270  GLY B  275  1                                   6    
HELIX   35 AD8 ASP B  283  CYS B  287  5                                   5    
HELIX   36 AD9 ARG B  290  VAL B  295  5                                   6    
HELIX   37 AE1 THR B  306  PHE B  317  1                                  12    
HELIX   38 AE2 ASN B  323  GLY B  325  5                                   3    
HELIX   39 AE3 PHE B  349  VAL B  359  1                                  11    
HELIX   40 AE4 GLY B  372  ASN B  383  1                                  12    
HELIX   41 AE5 PRO B  384  VAL B  387  5                                   4    
HELIX   42 AE6 LEU B  394  GLY B  401  1                                   8    
HELIX   43 AE7 SER B  416  GLY B  432  1                                  17    
HELIX   44 AE8 SER B  434  ASP B  439  1                                   6    
HELIX   45 AE9 GLU B  473  ASN B  476  5                                   4    
HELIX   46 AF1 ASN B  477  GLU B  488  1                                  12    
HELIX   47 AF2 ASN B  502  ALA B  504  5                                   3    
HELIX   48 AF3 ASN B  532  ASP B  534  5                                   3    
SHEET    1 AA1 9 THR A  53  VAL A  61  0                                        
SHEET    2 AA1 9 ILE A  87  GLY A  97 -1  O  ARG A  89   N  GLU A  59           
SHEET    3 AA1 9 SER A 100  PRO A 109 -1  O  LEU A 102   N  VAL A  94           
SHEET    4 AA1 9 ALA A 142  GLY A 145 -1  O  THR A 143   N  TRP A 107           
SHEET    5 AA1 9 PHE A 116  THR A 119  1  N  THR A 119   O  VAL A 144           
SHEET    6 AA1 9 SER A 195  CYS A 200  1  O  LEU A 198   N  SER A 118           
SHEET    7 AA1 9 GLY A 220  GLY A 224  1  O  GLY A 224   N  GLY A 199           
SHEET    8 AA1 9 LYS A 403  GLY A 409  1  O  ILE A 405   N  ILE A 221           
SHEET    9 AA1 9 TYR A 442  VAL A 447  1  O  PHE A 445   N  HIS A 406           
SHEET    1 AA2 2 ASN A  66  THR A  68  0                                        
SHEET    2 AA2 2 SER A  80  ILE A  82 -1  O  THR A  81   N  ILE A  67           
SHEET    1 AA3 2 LEU A 320  TYR A 321  0                                        
SHEET    2 AA3 2 TYR A 327  TYR A 329 -1  O  TYR A 329   N  LEU A 320           
SHEET    1 AA4 2 THR A 494  TYR A 500  0                                        
SHEET    2 AA4 2 VAL A 509  CYS A 516 -1  O  VAL A 511   N  ARG A 499           
SHEET    1 AA5 2 ARG A 521  TRP A 524  0                                        
SHEET    2 AA5 2 TRP A 536  GLU A 539 -1  O  LYS A 537   N  VAL A 523           
SHEET    1 AA6 9 THR B  53  VAL B  61  0                                        
SHEET    2 AA6 9 ILE B  87  GLY B  97 -1  O  ARG B  89   N  GLU B  59           
SHEET    3 AA6 9 SER B 100  PRO B 109 -1  O  LEU B 102   N  VAL B  94           
SHEET    4 AA6 9 ALA B 142  ALA B 146 -1  O  THR B 143   N  TRP B 107           
SHEET    5 AA6 9 PHE B 116  THR B 119  1  N  LEU B 117   O  ALA B 142           
SHEET    6 AA6 9 SER B 195  CYS B 200  1  O  TYR B 196   N  PHE B 116           
SHEET    7 AA6 9 GLY B 220  GLY B 224  1  O  GLY B 224   N  GLY B 199           
SHEET    8 AA6 9 LYS B 403  GLY B 409  1  O  ILE B 405   N  ILE B 221           
SHEET    9 AA6 9 TYR B 442  VAL B 447  1  O  PHE B 445   N  HIS B 406           
SHEET    1 AA7 2 ASN B  66  THR B  68  0                                        
SHEET    2 AA7 2 SER B  80  ILE B  82 -1  O  THR B  81   N  ILE B  67           
SHEET    1 AA8 2 LEU B 320  TYR B 321  0                                        
SHEET    2 AA8 2 TYR B 327  TYR B 329 -1  O  TYR B 329   N  LEU B 320           
SHEET    1 AA9 2 THR B 494  TYR B 500  0                                        
SHEET    2 AA9 2 VAL B 509  CYS B 516 -1  O  GLU B 510   N  ARG B 499           
SHEET    1 AB1 2 ARG B 521  TRP B 524  0                                        
SHEET    2 AB1 2 TRP B 536  GLU B 539 -1  O  GLU B 539   N  ARG B 521           
SSBOND   1 CYS A   41    CYS A   88                          1555   1555  2.04  
SSBOND   2 CYS A   76    CYS A  127                          1555   1555  2.03  
SSBOND   3 CYS A  200    CYS A  453                          1555   1555  2.04  
SSBOND   4 CYS A  269    CYS A  287                          1555   1555  2.04  
SSBOND   5 CYS A  296    CYS A  304                          1555   1555  2.03  
SSBOND   6 CYS A  516    CYS A  538                          1555   1555  2.03  
SSBOND   7 CYS B   41    CYS B   88                          1555   1555  2.04  
SSBOND   8 CYS B   76    CYS B  127                          1555   1555  2.03  
SSBOND   9 CYS B  200    CYS B  453                          1555   1555  2.04  
SSBOND  10 CYS B  269    CYS B  287                          1555   1555  2.04  
SSBOND  11 CYS B  296    CYS B  304                          1555   1555  2.04  
SSBOND  12 CYS B  516    CYS B  538                          1555   1555  2.03  
LINK         ND2 ASN A  66                 C1  NAG A 601     1555   1555  1.44  
LINK         ND2 ASN A 101                 C1  NAG A 604     1555   1555  1.45  
LINK         ND2 ASN A 151                 C1  NAG A 605     1555   1555  1.44  
LINK         OD1 ASP A 270                CA    CA A 613     1555   1555  2.32  
LINK         OD1 ASP A 274                CA    CA A 613     1555   1555  2.33  
LINK         OD2 ASP A 274                CA    CA A 613     1555   1555  3.01  
LINK         O   VAL A 276                CA    CA A 613     1555   1555  2.33  
LINK         OD1 ASP A 278                CA    CA A 613     1555   1555  2.32  
LINK         O   ILE A 280                CA    CA A 613     1555   1555  2.32  
LINK         ND2 ASN A 362                 C1  NAG A 608     1555   1555  1.44  
LINK         ND2 ASN B  66                 C1  NAG B 601     1555   1555  1.45  
LINK         ND2 ASN B 101                 C1  NAG B 603     1555   1555  1.44  
LINK         ND2 ASN B 151                 C1  NAG B 604     1555   1555  1.44  
LINK         OD1 ASP B 270                CA    CA B 622     1555   1555  2.32  
LINK         OD1 ASP B 274                CA    CA B 622     1555   1555  2.33  
LINK         OD2 ASP B 274                CA    CA B 622     1555   1555  3.01  
LINK         O   VAL B 276                CA    CA B 622     1555   1555  2.33  
LINK         OD1 ASP B 278                CA    CA B 622     1555   1555  2.32  
LINK         O   ILE B 280                CA    CA B 622     1555   1555  2.33  
LINK         ND2 ASN B 362                 C1  NAG B 611     1555   1555  1.44  
LINK         O4  NAG A 601                 C1  NAG A 602     1555   1555  1.44  
LINK         O4  NAG A 602                 C1  BMA A 603     1555   1555  1.44  
LINK         O4  NAG A 605                 C1  NAG A 606     1555   1555  1.44  
LINK         O4  NAG A 606                 C1  BMA A 607     1555   1555  1.45  
LINK         O4  NAG A 608                 C1  NAG A 609     1555   1555  1.45  
LINK         O4  NAG A 609                 C1  BMA A 610     1555   1555  1.44  
LINK         O6  BMA A 610                 C1  MAN A 611     1555   1555  1.45  
LINK         O3  MAN A 611                 C1  MAN A 612     1555   1555  1.45  
LINK        CA    CA A 613                 O   HOH A 745     1555   1555  2.50  
LINK         O4  NAG B 601                 C1  NAG B 602     1555   1555  1.44  
LINK         O4  NAG B 604                 C1  NAG B 605     1555   1555  1.44  
LINK         O4  NAG B 605                 C1  BMA B 606     1555   1555  1.44  
LINK         O3  BMA B 606                 C1  MAN B 608     1555   1555  1.44  
LINK         O6  BMA B 606                 C1  MAN B 607     1555   1555  1.44  
LINK         O2  MAN B 608                 C1  MAN B 609     1555   1555  1.44  
LINK         O2  MAN B 609                 C1  MAN B 610     1555   1555  1.44  
LINK         O4  NAG B 611                 C1  NAG B 612     1555   1555  1.44  
LINK         O4  NAG B 612                 C1  BMA B 613     1555   1555  1.44  
LINK         O3  BMA B 613                 C1  MAN B 618     1555   1555  1.44  
LINK         O6  BMA B 613                 C1  MAN B 614     1555   1555  1.44  
LINK         O3  MAN B 614                 C1  MAN B 615     1555   1555  1.44  
LINK         O6  MAN B 614                 C1  MAN B 616     1555   1555  1.45  
LINK         O2  MAN B 616                 C1  MAN B 617     1555   1555  1.45  
LINK         O2  MAN B 618                 C1  MAN B 620     1555   1555  1.44  
LINK         O6  MAN B 618                 C1  MAN B 619     1555   1555  1.46  
LINK         O2  MAN B 620                 C1  MAN B 621     1555   1555  1.44  
LINK        CA    CA B 622                 O   HOH B 799     1555   1555  2.41  
CISPEP   1 THR A   77    PRO A   78          0         1.27                     
CISPEP   2 TYR A  518    PRO A  519          0         8.49                     
CISPEP   3 THR B   77    PRO B   78          0         0.52                     
CISPEP   4 TYR B  518    PRO B  519          0         8.57                     
SITE     1 AC1  6 ASP A 270  ASP A 274  VAL A 276  ASP A 278                    
SITE     2 AC1  6 ILE A 280  HOH A 745                                          
SITE     1 AC2  6 ASP B 270  ASP B 274  VAL B 276  ASP B 278                    
SITE     2 AC2  6 ILE B 280  HOH B 799                                          
SITE     1 AC3  3 ASN A  66  SER A  80  HOH A 785                               
SITE     1 AC4  5 PHE A  93  LYS A  99  ASN A 101  VAL A 164                    
SITE     2 AC4  5 LYS A 298                                                     
SITE     1 AC5  7 TRP A  56  PHE A  57  ASP A  71  ASN A  72                    
SITE     2 AC5  7 GLU A 105  ASN A 151  HOH A 790                               
SITE     1 AC6 17 ILE A 360  TRP A 361  ASN A 362  LYS A 378                    
SITE     2 AC6 17 VAL A 382  ASN A 383  PRO A 384  PHE A 385                    
SITE     3 AC6 17 ASN A 386  HOH A 720  HOH A 730  LYS B 194                    
SITE     4 AC6 17 ARG B 400  LYS B 403  GLU B 440  GLY B 489                    
SITE     5 AC6 17 HOH B 832                                                     
SITE     1 AC7  5 ASN B  66  THR B  68  SER B  80  ILE B  82                    
SITE     2 AC7  5 HOH B 714                                                     
SITE     1 AC8  4 ASN B 101  GLY B 149  VAL B 164  HOH B 756                    
SITE     1 AC9 10 TRP B  56  PHE B  57  ASP B  71  ASN B 101                    
SITE     2 AC9 10 THR B 103  GLU B 105  ASN B 151  HOH B 760                    
SITE     3 AC9 10 HOH B 816  HOH B 857                                          
SITE     1 AD1 24 SER B 162  ILE B 360  TRP B 361  ASN B 362                    
SITE     2 AD1 24 LYS B 378  SER B 380  GLU B 381  VAL B 382                    
SITE     3 AD1 24 ASN B 383  PRO B 384  ASN B 386  GLU B 388                    
SITE     4 AD1 24 TRP B 390  GLU B 391  HOH B 706  HOH B 722                    
SITE     5 AD1 24 HOH B 738  HOH B 745  HOH B 780  HOH B 790                    
SITE     6 AD1 24 HOH B 793  HOH B 800  HOH B 818  HOH B 827                    
CRYST1   67.536   87.467  106.565  90.00 106.18  90.00 P 1 21 1      4          
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      0.014807  0.000000  0.004295        0.00000                         
SCALE2      0.000000  0.011433  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009771        0.00000                         
TER    3956      GLU A 543                                                      
TER    7915      GLU B 543                                                      
MASTER      416    0   35   48   34    0   26    6 8674    2  455   82          
END                                                                             

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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.
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