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LongText Report for: 4EY4-pdb

Name Class
4EY4-pdb
HEADER    HYDROLASE                               01-MAY-12   4EY4              
TITLE     CRYSTAL STRUCTURE OF RECOMBINANT HUMAN ACETYLCHOLINESTERASE IN THE APO
TITLE    2 STATE                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 33-574;                                       
COMPND   5 SYNONYM: ACHE;                                                       
COMPND   6 EC: 3.1.1.7;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ACHE;                                                          
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HEK293                                  
KEYWDS    ACETYLCHOLINESTERASE, HYDROLASE, APO                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.CHEUNG,M.RUDOLPH,F.BURSHTEYN,M.CASSIDY,E.GARY,J.LOVE,J.HEIGHT,      
AUTHOR   2 M.FRANKLIN                                                           
REVDAT   1   17-OCT-12 4EY4    0                                                
JRNL        AUTH   J.CHEUNG,M.J.RUDOLPH,F.BURSHTEYN,M.S.CASSIDY,E.N.GARY,       
JRNL        AUTH 2 J.LOVE,M.C.FRANKLIN,J.J.HEIGHT                               
JRNL        TITL   STRUCTURES OF HUMAN ACETYLCHOLINESTERASE IN COMPLEX WITH     
JRNL        TITL 2 PHARMACOLOGICALLY IMPORTANT LIGANDS.                         
JRNL        REF    J.MED.CHEM.                                2012              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   23035744                                                     
JRNL        DOI    10.1021/JM300871X                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.16 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8_1069)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.16                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.61                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 112096                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.185                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.220                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5594                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 46.6166 -  6.6927    0.92     3673   171  0.1726 0.2068        
REMARK   3     2  6.6927 -  5.3146    0.97     3653   209  0.1716 0.1907        
REMARK   3     3  5.3146 -  4.6435    0.96     3625   167  0.1412 0.1603        
REMARK   3     4  4.6435 -  4.2192    0.88     3236   173  0.1440 0.1814        
REMARK   3     5  4.2192 -  3.9170    0.88     3248   156  0.1604 0.1913        
REMARK   3     6  3.9170 -  3.6861    0.93     3398   190  0.1727 0.1872        
REMARK   3     7  3.6861 -  3.5016    0.95     3546   177  0.1826 0.2121        
REMARK   3     8  3.5016 -  3.3492    0.96     3488   196  0.1960 0.2262        
REMARK   3     9  3.3492 -  3.2203    0.97     3542   174  0.2054 0.2402        
REMARK   3    10  3.2203 -  3.1092    0.98     3584   189  0.2016 0.2399        
REMARK   3    11  3.1092 -  3.0120    0.98     3598   183  0.1993 0.2581        
REMARK   3    12  3.0120 -  2.9259    0.98     3595   191  0.1977 0.2433        
REMARK   3    13  2.9259 -  2.8489    0.99     3607   172  0.2064 0.2622        
REMARK   3    14  2.8489 -  2.7794    0.99     3579   202  0.2111 0.2641        
REMARK   3    15  2.7794 -  2.7162    0.99     3583   173  0.2105 0.2865        
REMARK   3    16  2.7162 -  2.6584    0.99     3563   200  0.2025 0.2642        
REMARK   3    17  2.6584 -  2.6053    0.99     3619   212  0.2113 0.2764        
REMARK   3    18  2.6053 -  2.5561    0.99     3605   172  0.2106 0.2720        
REMARK   3    19  2.5561 -  2.5105    0.99     3593   179  0.2055 0.2570        
REMARK   3    20  2.5105 -  2.4679    0.99     3505   226  0.2163 0.2594        
REMARK   3    21  2.4679 -  2.4281    0.99     3637   179  0.2176 0.2916        
REMARK   3    22  2.4281 -  2.3907    0.99     3592   185  0.2257 0.2654        
REMARK   3    23  2.3907 -  2.3556    0.99     3483   199  0.2363 0.2888        
REMARK   3    24  2.3556 -  2.3224    0.99     3610   189  0.2401 0.2970        
REMARK   3    25  2.3224 -  2.2910    0.99     3557   189  0.2375 0.2956        
REMARK   3    26  2.2910 -  2.2613    0.99     3589   169  0.2528 0.2897        
REMARK   3    27  2.2613 -  2.2330    0.99     3602   197  0.2622 0.3098        
REMARK   3    28  2.2330 -  2.2061    0.99     3534   196  0.2750 0.2944        
REMARK   3    29  2.2061 -  2.1805    0.99     3549   196  0.2841 0.3209        
REMARK   3    30  2.1805 -  2.1560    0.97     3509   183  0.2950 0.3439        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.40                                          
REMARK   3   SHRINKAGE RADIUS   : 1.20                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.250            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.760           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 7.13530                                              
REMARK   3    B22 (A**2) : 7.13530                                              
REMARK   3    B33 (A**2) : -14.27070                                            
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.010           8778                                  
REMARK   3   ANGLE     :  1.174          11971                                  
REMARK   3   CHIRALITY :  0.083           1281                                  
REMARK   3   PLANARITY :  0.006           1578                                  
REMARK   3   DIHEDRAL  : 13.756           3193                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4EY4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-MAY-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB072214.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.075                              
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 112311                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.19                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55100                            
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: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 4EY7                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 72.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12 TO 18% PEG 3350, 0.2M POTASSIUM       
REMARK 280  NITRATE, PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      108.12933            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      216.25867            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      216.25867            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      108.12933            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 28.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     PRO A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     THR A   262                                                      
REMARK 465     GLY A   263                                                      
REMARK 465     GLY A   264                                                      
REMARK 465     PRO A   495                                                      
REMARK 465     LYS A   496                                                      
REMARK 465     ALA A   497                                                      
REMARK 465     THR A   543                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     GLY B   261                                                      
REMARK 465     ARG B   493                                                      
REMARK 465     ASP B   494                                                      
REMARK 465     THR B   543                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NE2  GLN B   527     O    HOH B   846              2.07            
REMARK 500   NE2  GLN A   527     O    HOH A   884              2.09            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A  47       -7.62     77.39                                   
REMARK 500    ALA A  62       52.73   -113.28                                   
REMARK 500    ALA A 167       77.71   -152.72                                   
REMARK 500    SER A 203     -123.05     59.96                                   
REMARK 500    ASP A 306      -91.12    -92.62                                   
REMARK 500    VAL A 407      -61.77   -126.73                                   
REMARK 500    PHE B  47       -4.24     76.94                                   
REMARK 500    ALA B 167       71.56   -155.67                                   
REMARK 500    ASN B 170       16.77     54.14                                   
REMARK 500    SER B 203     -118.16     46.90                                   
REMARK 500    ASP B 306      -82.96    -91.89                                   
REMARK 500    VAL B 407      -63.78   -127.08                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO3 B 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PE8 B 608                 
DBREF  4EY4 A    2   543  UNP    P22303   ACES_HUMAN      33    574             
DBREF  4EY4 B    2   543  UNP    P22303   ACES_HUMAN      33    574             
SEQRES   1 A  542  GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY          
SEQRES   2 A  542  GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY          
SEQRES   3 A  542  PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO          
SEQRES   4 A  542  PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS          
SEQRES   5 A  542  GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN          
SEQRES   6 A  542  SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY          
SEQRES   7 A  542  PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU          
SEQRES   8 A  542  SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR          
SEQRES   9 A  542  PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE          
SEQRES  10 A  542  TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP          
SEQRES  11 A  542  VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR          
SEQRES  12 A  542  VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY          
SEQRES  13 A  542  PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN          
SEQRES  14 A  542  VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL          
SEQRES  15 A  542  GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER          
SEQRES  16 A  542  VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL          
SEQRES  17 A  542  GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE          
SEQRES  18 A  542  HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO          
SEQRES  19 A  542  TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA          
SEQRES  20 A  542  THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY          
SEQRES  21 A  542  THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG          
SEQRES  22 A  542  THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS          
SEQRES  23 A  542  VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL          
SEQRES  24 A  542  PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU          
SEQRES  25 A  542  ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL          
SEQRES  26 A  542  LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU          
SEQRES  27 A  542  VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER          
SEQRES  28 A  542  LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL          
SEQRES  29 A  542  GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL          
SEQRES  30 A  542  VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO          
SEQRES  31 A  542  ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP          
SEQRES  32 A  542  HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG          
SEQRES  33 A  542  LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE          
SEQRES  34 A  542  GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP MET          
SEQRES  35 A  542  GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY          
SEQRES  36 A  542  ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU          
SEQRES  37 A  542  LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN          
SEQRES  38 A  542  PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO          
SEQRES  39 A  542  LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN          
SEQRES  40 A  542  GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG          
SEQRES  41 A  542  ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG          
SEQRES  42 A  542  PHE LEU PRO LYS LEU LEU SER ALA THR                          
SEQRES   1 B  542  GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY          
SEQRES   2 B  542  GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY          
SEQRES   3 B  542  PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO          
SEQRES   4 B  542  PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS          
SEQRES   5 B  542  GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN          
SEQRES   6 B  542  SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY          
SEQRES   7 B  542  PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU          
SEQRES   8 B  542  SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR          
SEQRES   9 B  542  PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE          
SEQRES  10 B  542  TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP          
SEQRES  11 B  542  VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR          
SEQRES  12 B  542  VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY          
SEQRES  13 B  542  PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN          
SEQRES  14 B  542  VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL          
SEQRES  15 B  542  GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER          
SEQRES  16 B  542  VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL          
SEQRES  17 B  542  GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE          
SEQRES  18 B  542  HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO          
SEQRES  19 B  542  TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA          
SEQRES  20 B  542  THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY          
SEQRES  21 B  542  THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG          
SEQRES  22 B  542  THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS          
SEQRES  23 B  542  VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL          
SEQRES  24 B  542  PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU          
SEQRES  25 B  542  ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL          
SEQRES  26 B  542  LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU          
SEQRES  27 B  542  VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER          
SEQRES  28 B  542  LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL          
SEQRES  29 B  542  GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL          
SEQRES  30 B  542  VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO          
SEQRES  31 B  542  ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP          
SEQRES  32 B  542  HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG          
SEQRES  33 B  542  LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE          
SEQRES  34 B  542  GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP MET          
SEQRES  35 B  542  GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY          
SEQRES  36 B  542  ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU          
SEQRES  37 B  542  LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN          
SEQRES  38 B  542  PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO          
SEQRES  39 B  542  LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN          
SEQRES  40 B  542  GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG          
SEQRES  41 B  542  ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG          
SEQRES  42 B  542  PHE LEU PRO LYS LEU LEU SER ALA THR                          
MODRES 4EY4 ASN B  350  ASN  GLYCOSYLATION SITE                                 
MODRES 4EY4 ASN A  350  ASN  GLYCOSYLATION SITE                                 
MODRES 4EY4 ASN B  265  ASN  GLYCOSYLATION SITE                                 
HET    FUC  A 601      10                                                       
HET    NAG  A 602      14                                                       
HET    NAG  A 603      14                                                       
HET    EDO  A 604       4                                                       
HET    EDO  A 605       4                                                       
HET    FUC  B 601      10                                                       
HET    NAG  B 602      14                                                       
HET    NAG  B 603      14                                                       
HET    NAG  B 604      14                                                       
HET    EDO  B 605       4                                                       
HET    NO3  B 606       4                                                       
HET    NO3  B 607       4                                                       
HET    PE8  B 608      25                                                       
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     NO3 NITRATE ION                                                      
HETNAM     PE8 3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL                    
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  FUC    2(C6 H12 O5)                                                 
FORMUL   3  NAG    5(C8 H15 N O6)                                               
FORMUL   4  EDO    3(C2 H6 O2)                                                  
FORMUL   9  NO3    2(N O3 1-)                                                   
FORMUL  11  PE8    C16 H34 O9                                                   
FORMUL  12  HOH   *397(H2 O)                                                    
HELIX    1   1 ASP A    5  GLU A    7  5                                   3    
HELIX    2   2 MET A   42  ARG A   46  5                                   5    
HELIX    3   3 PHE A   80  MET A   85  1                                   6    
HELIX    4   4 LEU A  130  ASP A  134  5                                   5    
HELIX    5   5 GLY A  135  ARG A  143  1                                   9    
HELIX    6   6 VAL A  153  LEU A  159  1                                   7    
HELIX    7   7 ASN A  170  VAL A  187  1                                  18    
HELIX    8   8 ALA A  188  PHE A  190  5                                   3    
HELIX    9   9 SER A  203  LEU A  214  1                                  12    
HELIX   10  10 SER A  215  GLY A  220  1                                   6    
HELIX   11  11 MET A  241  VAL A  255  1                                  15    
HELIX   12  12 ASP A  266  THR A  275  1                                  10    
HELIX   13  13 PRO A  277  GLU A  285  1                                   9    
HELIX   14  14 TRP A  286  LEU A  289  5                                   4    
HELIX   15  15 THR A  311  ALA A  318  1                                   8    
HELIX   16  16 GLY A  335  VAL A  340  1                                   6    
HELIX   17  17 SER A  355  VAL A  367  1                                  13    
HELIX   18  18 SER A  371  THR A  383  1                                  13    
HELIX   19  19 ASP A  390  VAL A  407  1                                  18    
HELIX   20  20 VAL A  407  GLN A  421  1                                  15    
HELIX   21  21 PRO A  440  GLY A  444  5                                   5    
HELIX   22  22 GLU A  450  PHE A  455  1                                   6    
HELIX   23  23 GLY A  456  ASP A  460  5                                   5    
HELIX   24  24 THR A  466  GLY A  487  1                                  22    
HELIX   25  25 ARG A  525  ARG A  534  1                                  10    
HELIX   26  26 ARG A  534  ALA A  542  1                                   9    
HELIX   27  27 ASP B    5  GLU B    7  5                                   3    
HELIX   28  28 MET B   42  ARG B   46  5                                   5    
HELIX   29  29 PHE B   80  MET B   85  1                                   6    
HELIX   30  30 LEU B  130  ASP B  134  5                                   5    
HELIX   31  31 GLY B  135  ARG B  143  1                                   9    
HELIX   32  32 VAL B  153  LEU B  159  1                                   7    
HELIX   33  33 ASN B  170  VAL B  187  1                                  18    
HELIX   34  34 ALA B  188  PHE B  190  5                                   3    
HELIX   35  35 SER B  203  LEU B  214  1                                  12    
HELIX   36  36 SER B  215  GLY B  220  1                                   6    
HELIX   37  37 GLY B  240  VAL B  255  1                                  16    
HELIX   38  38 ASN B  265  ARG B  274  1                                  10    
HELIX   39  39 PRO B  277  ASN B  283  1                                   7    
HELIX   40  40 HIS B  284  LEU B  289  5                                   6    
HELIX   41  41 THR B  311  ALA B  318  1                                   8    
HELIX   42  42 GLY B  335  VAL B  340  1                                   6    
HELIX   43  43 SER B  355  VAL B  367  1                                  13    
HELIX   44  44 SER B  371  THR B  383  1                                  13    
HELIX   45  45 ASP B  390  VAL B  407  1                                  18    
HELIX   46  46 VAL B  407  GLN B  421  1                                  15    
HELIX   47  47 PRO B  440  GLY B  444  5                                   5    
HELIX   48  48 GLU B  450  PHE B  455  1                                   6    
HELIX   49  49 GLY B  456  ASP B  460  5                                   5    
HELIX   50  50 THR B  466  GLY B  487  1                                  22    
HELIX   51  51 ARG B  525  ARG B  534  1                                  10    
HELIX   52  52 PHE B  535  ALA B  542  1                                   8    
SHEET    1   A 3 LEU A   9  VAL A  12  0                                        
SHEET    2   A 3 GLY A  15  ARG A  18 -1  O  LEU A  17   N  VAL A  10           
SHEET    3   A 3 VAL A  59  ASP A  61  1  O  VAL A  60   N  ARG A  16           
SHEET    1   B11 ILE A  20  LEU A  22  0                                        
SHEET    2   B11 VAL A  29  PRO A  36 -1  O  VAL A  29   N  LEU A  22           
SHEET    3   B11 TYR A  98  PRO A 104 -1  O  THR A 103   N  SER A  30           
SHEET    4   B11 VAL A 145  MET A 149 -1  O  SER A 148   N  ASN A 100           
SHEET    5   B11 THR A 112  ILE A 118  1  N  LEU A 115   O  VAL A 145           
SHEET    6   B11 GLY A 192  GLU A 202  1  O  THR A 198   N  VAL A 114           
SHEET    7   B11 ARG A 224  GLN A 228  1  O  GLN A 228   N  GLY A 201           
SHEET    8   B11 GLN A 325  VAL A 331  1  O  LEU A 327   N  LEU A 227           
SHEET    9   B11 ARG A 424  PHE A 430  1  O  TYR A 426   N  VAL A 328           
SHEET   10   B11 GLN A 509  LEU A 513  1  O  LEU A 513   N  VAL A 429           
SHEET   11   B11 GLU A 519  ARG A 522 -1  O  ARG A 521   N  TYR A 510           
SHEET    1   C 2 VAL A  68  CYS A  69  0                                        
SHEET    2   C 2 LEU A  92  SER A  93  1  O  SER A  93   N  VAL A  68           
SHEET    1   D 2 VAL A 239  GLY A 240  0                                        
SHEET    2   D 2 VAL A 302  VAL A 303  1  O  VAL A 303   N  VAL A 239           
SHEET    1   E 3 LEU B   9  VAL B  12  0                                        
SHEET    2   E 3 GLY B  15  ARG B  18 -1  O  LEU B  17   N  VAL B  10           
SHEET    3   E 3 VAL B  59  ASP B  61  1  O  VAL B  60   N  ARG B  16           
SHEET    1   F11 ILE B  20  LEU B  22  0                                        
SHEET    2   F11 VAL B  29  PRO B  36 -1  O  VAL B  29   N  LEU B  22           
SHEET    3   F11 TYR B  98  PRO B 104 -1  O  LEU B  99   N  ILE B  35           
SHEET    4   F11 VAL B 145  MET B 149 -1  O  LEU B 146   N  TRP B 102           
SHEET    5   F11 THR B 112  ILE B 118  1  N  TRP B 117   O  VAL B 147           
SHEET    6   F11 GLY B 192  GLU B 202  1  O  THR B 198   N  VAL B 114           
SHEET    7   F11 ARG B 224  GLN B 228  1  O  GLN B 228   N  GLY B 201           
SHEET    8   F11 GLN B 325  VAL B 331  1  O  LEU B 327   N  LEU B 227           
SHEET    9   F11 ARG B 424  PHE B 430  1  O  TYR B 426   N  VAL B 328           
SHEET   10   F11 GLN B 509  LEU B 513  1  O  LEU B 513   N  VAL B 429           
SHEET   11   F11 GLU B 519  ARG B 522 -1  O  ARG B 521   N  TYR B 510           
SHEET    1   G 2 VAL B  68  CYS B  69  0                                        
SHEET    2   G 2 LEU B  92  SER B  93  1  O  SER B  93   N  VAL B  68           
SSBOND   1 CYS A   69    CYS A   96                          1555   1555  2.08  
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.07  
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.03  
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.08  
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.07  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.04  
LINK         O4  NAG B 602                 C1  NAG B 603     1555   1555  1.45  
LINK         O4  NAG A 602                 C1  NAG A 603     1555   1555  1.46  
LINK         C1  FUC A 601                 O6  NAG A 602     1555   1555  1.46  
LINK         C1  FUC B 601                 O6  NAG B 602     1555   1555  1.47  
LINK         ND2 ASN B 350                 C1  NAG B 602     1555   1555  1.47  
LINK         ND2 ASN A 350                 C1  NAG A 602     1555   1555  1.48  
LINK         ND2 ASN B 265                 C1  NAG B 604     1555   1555  1.53  
CISPEP   1 TYR A  105    PRO A  106          0        -1.66                     
CISPEP   2 TYR B  105    PRO B  106          0         6.06                     
CISPEP   3 CYS B  257    PRO B  258          0        -6.19                     
SITE     1 AC1  2 SER A 347  NAG A 602                                          
SITE     1 AC2  6 PHE A 346  SER A 347  ASN A 350  FUC A 601                    
SITE     2 AC2  6 NAG A 603  HOH A 860                                          
SITE     1 AC3  4 PRO A 344  GLY A 345  PHE A 346  NAG A 602                    
SITE     1 AC4  8 TYR A 382  THR A 383  ASP A 384  HIS A 387                    
SITE     2 AC4  8 ARG A 393  LEU A 394  ALA A 397  HOH A 746                    
SITE     1 AC5  6 ALA A 526  ALA A 530  ARG A 534  HOH A 820                    
SITE     2 AC5  6 HOH A 825  HOH B 816                                          
SITE     1 AC6  2 SER B 347  NAG B 602                                          
SITE     1 AC7  4 SER B 347  ASN B 350  FUC B 601  NAG B 603                    
SITE     1 AC8  3 PRO B 344  GLY B 345  NAG B 602                               
SITE     1 AC9  3 ASN B 265  GLU B 268  HOH B 829                               
SITE     1 BC1  8 TYR B 382  THR B 383  ASP B 384  HIS B 387                    
SITE     2 BC1  8 PRO B 388  ARG B 393  LEU B 394  HOH B 799                    
SITE     1 BC2  7 VAL A 255  VAL A 280  HIS A 284  PRO B 162                    
SITE     2 BC2  7 MET B 241  GLY B 242  ARG B 245                               
SITE     1 BC3  4 HOH A 747  ALA B 526  ARG B 534  HOH B 818                    
SITE     1 BC4  6 GLY B 163  ASP B 304  GLY B 305  ASP B 306                    
SITE     2 BC4  6 SER B 309  HOH B 757                                          
CRYST1  106.178  106.178  324.388  90.00  90.00 120.00 P 31 2 1     12          
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      0.009418  0.005438  0.000000        0.00000                         
SCALE2      0.000000  0.010875  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003083        0.00000                         
TER    4190      ALA A 542                                                      
TER    8375      ALA B 542                                                      
MASTER      349    0   13   52   34    0   19    6 8816    2  150   84          
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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