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LongText Report for: 4EY8-pdb

Name Class
4EY8-pdb
HEADER    HYDROLASE/HYDROLASE INHIBITOR           01-MAY-12   4EY8              
TITLE     CRYSTAL STRUCTURE OF RECOMBINANT HUMAN ACETYLCHOLINESTERASE IN COMPLEX
TITLE    2 WITH FASCICULIN-2                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 33-574;                                       
COMPND   5 SYNONYM: ACHE;                                                       
COMPND   6 EC: 3.1.1.7;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: FASCICULIN-2;                                              
COMPND  10 CHAIN: B;                                                            
COMPND  11 SYNONYM: FAS-2, FAS2, ACETYLCHOLINESTERASE TOXIN F-VII, FASCICULIN-  
COMPND  12 II, FAS-II, TOXIN TA1                                                
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_TISSUE: HEK-293;                                   
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: DENDROASPIS ANGUSTICEPS;                        
SOURCE  11 ORGANISM_COMMON: EASTERN GREEN MAMBA;                                
SOURCE  12 ORGANISM_TAXID: 8618;                                                
SOURCE  13 SECRETION: VENOM                                                     
KEYWDS    ACETYLCHOLINESTERASE, HYDROLASE, FASCICULIN 2, SNAKE VENOM TOXIN,     
KEYWDS   2 INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR COMPLEX                     
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 4EY8    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.    2.60 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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.38                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 33413                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1681                            
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 46.3880 -  5.9391    0.98     2795   136  0.1613 0.1875        
REMARK   3     2  5.9391 -  4.7155    0.99     2703   147  0.1631 0.1857        
REMARK   3     3  4.7155 -  4.1199    0.98     2638   162  0.1574 0.2096        
REMARK   3     4  4.1199 -  3.7434    0.97     2646   130  0.1779 0.2310        
REMARK   3     5  3.7434 -  3.4752    0.98     2618   161  0.2144 0.2980        
REMARK   3     6  3.4752 -  3.2703    0.99     2652   131  0.2417 0.3020        
REMARK   3     7  3.2703 -  3.1066    0.99     2667   129  0.2484 0.3220        
REMARK   3     8  3.1066 -  2.9714    0.99     2659   134  0.2349 0.3074        
REMARK   3     9  2.9714 -  2.8570    0.99     2653   141  0.2508 0.3374        
REMARK   3    10  2.8570 -  2.7584    0.99     2654   143  0.2581 0.3179        
REMARK   3    11  2.7584 -  2.6722    0.98     2616   142  0.2617 0.3539        
REMARK   3    12  2.6722 -  2.5958    0.90     2431   125  0.2887 0.3804        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.30                                          
REMARK   3   SHRINKAGE RADIUS   : 1.10                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.350            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.820           
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) : 15.70660                                             
REMARK   3    B22 (A**2) : 15.70660                                             
REMARK   3    B33 (A**2) : -31.41320                                            
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      :  0.008           4829                                  
REMARK   3   ANGLE     :  1.187           6590                                  
REMARK   3   CHIRALITY :  0.079            713                                  
REMARK   3   PLANARITY :  0.006            859                                  
REMARK   3   DIHEDRAL  : 17.080           1765                                  
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 4EY8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAY-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB072218.                                      
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                             : 7.5 - 7.8                          
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4C                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.990                              
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33704                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.596                              
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     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.05400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29000                            
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: 1B41                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.14                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 TO 2.0M AMMONIUM SULPHATE, 0.1M      
REMARK 280  HEPES PH 7.5 - 7.8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE      
REMARK 280  283K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-Z                                              
REMARK 290       7555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       8555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       9555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290      10555   Y+2/3,X+1/3,-Z+1/3                                      
REMARK 290      11555   X-Y+2/3,-Y+1/3,-Z+1/3                                   
REMARK 290      12555   -X+2/3,-X+Y+1/3,-Z+1/3                                  
REMARK 290      13555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290      14555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290      15555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290      16555   Y+1/3,X+2/3,-Z+2/3                                      
REMARK 290      17555   X-Y+1/3,-Y+2/3,-Z+2/3                                   
REMARK 290      18555   -X+1/3,-X+Y+2/3,-Z+2/3                                  
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        0.00000            
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        0.00000            
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        0.00000            
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        0.00000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000       75.85250            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       43.79346            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       82.62067            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       75.85250            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       43.79346            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       82.62067            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       75.85250            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       43.79346            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       82.62067            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       75.85250            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       43.79346            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       82.62067            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       75.85250            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       43.79346            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       82.62067            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       75.85250            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       43.79346            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       82.62067            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       87.58692            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000      165.24133            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000       87.58692            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000      165.24133            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000       87.58692            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      165.24133            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000       87.58692            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      165.24133            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       87.58692            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000      165.24133            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000       87.58692            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000      165.24133            
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 300 REMARK: DIMER                                                        
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: 2180 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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     GLU A     4                                                      
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 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   C1   FUC A   605     C6   NAG A   606              2.17            
REMARK 500   O5   FUC A   605     O6   NAG A   606              2.18            
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    PRO A  25      -28.36    -37.53                                   
REMARK 500    PHE A  47      -16.67     77.40                                   
REMARK 500    ALA A  62       44.16   -109.88                                   
REMARK 500    PHE A 123        3.27     57.12                                   
REMARK 500    SER A 203     -120.46     60.58                                   
REMARK 500    PRO A 217       -9.10    -54.95                                   
REMARK 500    PRO A 290      -71.02    -56.90                                   
REMARK 500    ASP A 306      -85.77    -93.87                                   
REMARK 500    VAL A 407      -61.74   -131.59                                   
REMARK 500    ASN A 464       46.43    -97.86                                   
REMARK 500    ASP A 488      116.11   -160.05                                   
REMARK 500    ARG A 493     -150.56   -125.51                                   
REMARK 500    SER A 541        1.83    -69.73                                   
REMARK 500    HIS B   6      158.52    172.16                                   
REMARK 500    THR B   7     -162.28   -100.38                                   
REMARK 500    ASP B  45     -167.87   -165.12                                   
REMARK 500    PRO B  56     -145.67    -83.41                                   
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 SO4 A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 609                 
DBREF  4EY8 A    2   543  UNP    P22303   ACES_HUMAN      33    574             
DBREF  4EY8 B    1    61  UNP    P0C1Z0   TXFA2_DENAN      1     61             
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   61  THR MET CYS TYR SER HIS THR THR THR SER ARG ALA ILE          
SEQRES   2 B   61  LEU THR ASN CYS GLY GLU ASN SER CYS TYR ARG LYS SER          
SEQRES   3 B   61  ARG ARG HIS PRO PRO LYS MET VAL LEU GLY ARG GLY CYS          
SEQRES   4 B   61  GLY CYS PRO PRO GLY ASP ASP ASN LEU GLU VAL LYS CYS          
SEQRES   5 B   61  CYS THR SER PRO ASP LYS CYS ASN TYR                          
MODRES 4EY8 ASN A  464  ASN  GLYCOSYLATION SITE                                 
MODRES 4EY8 ASN A  350  ASN  GLYCOSYLATION SITE                                 
HET    SO4  A 601       5                                                       
HET    SO4  A 602       5                                                       
HET    SO4  A 603       5                                                       
HET    SO4  A 604       5                                                       
HET    FUC  A 605      10                                                       
HET    NAG  A 606      14                                                       
HET    NAG  A 607      14                                                       
HET    BMA  A 608      11                                                       
HET    NAG  A 609      14                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
FORMUL   3  SO4    4(O4 S 2-)                                                   
FORMUL   7  FUC    C6 H12 O5                                                    
FORMUL   7  NAG    3(C8 H15 N O6)                                               
FORMUL   7  BMA    C6 H12 O6                                                    
FORMUL   9  HOH   *44(H2 O)                                                     
HELIX    1   1 MET A   42  ARG A   46  5                                   5    
HELIX    2   2 PHE A   80  MET A   85  1                                   6    
HELIX    3   3 LEU A  130  ASP A  134  5                                   5    
HELIX    4   4 GLY A  135  ARG A  143  1                                   9    
HELIX    5   5 VAL A  153  LEU A  159  1                                   7    
HELIX    6   6 ASN A  170  VAL A  187  1                                  18    
HELIX    7   7 ALA A  188  PHE A  190  5                                   3    
HELIX    8   8 SER A  203  LEU A  213  1                                  11    
HELIX    9   9 SER A  215  PHE A  222  5                                   8    
HELIX   10  10 GLY A  240  VAL A  255  1                                  16    
HELIX   11  11 ASP A  266  ARG A  276  1                                  11    
HELIX   12  12 PRO A  277  TRP A  286  1                                  10    
HELIX   13  13 HIS A  287  LEU A  289  5                                   3    
HELIX   14  14 THR A  311  GLY A  319  1                                   9    
HELIX   15  15 GLY A  335  GLY A  342  5                                   8    
HELIX   16  16 SER A  355  VAL A  367  1                                  13    
HELIX   17  17 SER A  371  THR A  383  1                                  13    
HELIX   18  18 ASP A  390  VAL A  407  1                                  18    
HELIX   19  19 VAL A  407  ALA A  420  1                                  14    
HELIX   20  20 PRO A  440  GLY A  444  5                                   5    
HELIX   21  21 GLU A  450  PHE A  455  1                                   6    
HELIX   22  22 GLY A  456  ASP A  460  5                                   5    
HELIX   23  23 THR A  466  GLY A  487  1                                  22    
HELIX   24  24 ARG A  525  ARG A  534  1                                  10    
HELIX   25  25 ARG A  534  SER A  541  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  VAL A 101   N  PHE A  32           
SHEET    4   B11 VAL A 145  MET A 149 -1  O  LEU A 146   N  TRP A 102           
SHEET    5   B11 THR A 112  ILE A 118  1  N  TRP A 117   O  VAL A 147           
SHEET    6   B11 GLY A 192  GLU A 202  1  O  PHE A 200   N  VAL A 116           
SHEET    7   B11 ARG A 224  GLN A 228  1  O  VAL A 226   N  LEU A 199           
SHEET    8   B11 GLN A 325  VAL A 331  1  O  LEU A 327   N  ALA A 225           
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  VAL A 511   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 ALA A  38  GLU A  39  0                                        
SHEET    2   C 2 GLU A  51  PRO A  52 -1  O  GLU A  51   N  GLU A  39           
SHEET    1   D 2 VAL A  68  CYS A  69  0                                        
SHEET    2   D 2 LEU A  92  SER A  93  1  O  SER A  93   N  VAL A  68           
SHEET    1   E 2 MET B   2  SER B   5  0                                        
SHEET    2   E 2 ILE B  13  ASN B  16 -1  O  ILE B  13   N  SER B   5           
SHEET    1   F 3 VAL B  34  CYS B  39  0                                        
SHEET    2   F 3 CYS B  22  ARG B  27 -1  N  LYS B  25   O  GLY B  36           
SHEET    3   F 3 LEU B  48  CYS B  53 -1  O  GLU B  49   N  SER B  26           
SSBOND   1 CYS A   69    CYS A   96                          1555   1555  2.06  
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.06  
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.07  
SSBOND   4 CYS B    3    CYS B   22                          1555   1555  2.03  
SSBOND   5 CYS B   17    CYS B   39                          1555   1555  2.04  
SSBOND   6 CYS B   41    CYS B   52                          1555   1555  2.05  
SSBOND   7 CYS B   53    CYS B   59                          1555   1555  2.04  
LINK         C1  FUC A 605                 O6  NAG A 606     1555   1555  1.21  
LINK         ND2 ASN A 464                 C1  NAG A 609     1555   1555  1.48  
LINK         ND2 ASN A 350                 C1  NAG A 606     1555   1555  1.53  
LINK         O4  NAG A 607                 C1  BMA A 608     1555   1555  1.55  
LINK         O4  NAG A 606                 C1  NAG A 607     1555   1555  1.55  
CISPEP   1 TYR A  105    PRO A  106          0         3.10                     
CISPEP   2 PRO A  492    ARG A  493          0         2.85                     
CISPEP   3 PRO B   30    PRO B   31          0         4.70                     
CISPEP   4 SER B   55    PRO B   56          0        -5.37                     
SITE     1 AC1  4 ARG A 525  ALA A 526  GLN A 527  ALA A 528                    
SITE     1 AC2  3 GLY A 240  MET A 241  GLY A 242                               
SITE     1 AC3  3 THR A 504  GLY A 506  ALA A 507                               
SITE     1 AC4  4 ARG A  16  SER A  57  GLY A  58  ARG A 165                    
SITE     1 AC5  2 SER A 347  NAG A 606                                          
SITE     1 AC6  4 SER A 347  ASN A 350  FUC A 605  NAG A 607                    
SITE     1 AC7  3 GLY A 345  NAG A 606  BMA A 608                               
SITE     1 AC8  1 NAG A 607                                                     
SITE     1 AC9  2 SER A 462  ASN A 464                                          
CRYST1  151.705  151.705  247.862  90.00  90.00 120.00 H 3 2        18          
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      0.006592  0.003806  0.000000        0.00000                         
SCALE2      0.000000  0.007611  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004035        0.00000                         
TER    4140      THR A 543                                                      
TER    4605      TYR B  61                                                      
MASTER      363    0    9   25   23    0    9    6 4719    2   99   47          
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:
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