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LongText Report for: 4B0P-pdb

Name Class
4B0P-pdb
HEADER    HYDROLASE                               04-JUL-12   4B0P              
TITLE     CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN BUTYRYLCHOLINESTERASE IN        
TITLE    2 COMPLEX WITH METHYL 2-(PENTAFLUOROBENZYLOXYIMINO) PYRIDINIUM         
CAVEAT     4B0P    NAG A 2181 C1 HAS INCORRECT CHIRALITY                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLINESTERASE;                                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 29-557;                                           
COMPND   5 SYNONYM: BUTYRYLCHOLINESTERASE, ACYLCHOLINE ACYLHYDROLASE,           
COMPND   6  BUTYRYLCHOLINE ESTERASE, CHOLINE ESTERASE II,                       
COMPND   7  PSEUDOCHOLINESTERASE;                                               
COMPND   8 EC: 3.1.1.8;                                                         
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: CHO-K1;                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGS                                       
KEYWDS    HYDROLASE, AGING                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.WANDHAMMER,M.DE KONING,M.VAN GROL,D.NOORT,M.GOELDNER,F.NACHON       
REVDAT   1   29-AUG-12 4B0P    0                                                
JRNL        AUTH   M.WANDHAMMER,M.DE KONING,M.VAN GROL,M.LOIODICE,L.SAUREL,     
JRNL        AUTH 2 D.NOORT,M.GOELDNER,F.NACHON                                  
JRNL        TITL   A STEP TOWARD THE REACTIVATION OF AGED CHOLINESTERASES -     
JRNL        TITL 2 CRYSTAL STRUCTURE OF LIGANDS BINDING TO AGED HUMAN           
JRNL        TITL 3 BUTYRYLCHOLINESTERASE                                        
JRNL        REF    CHEM.BIOL.INTERACT                         2012              
JRNL        REFN                   ESSN 1872-7786                               
JRNL        DOI    10.1016/J.CBI.2012.08.005                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.500                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.878                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.36                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.70                          
REMARK   3   NUMBER OF REFLECTIONS             : 27798                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1663                          
REMARK   3   R VALUE            (WORKING SET) : 0.1644                          
REMARK   3   FREE R VALUE                     : 0.2120                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1112                            
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 30.8808 -  4.9939    0.95     3392   141  0.1684 0.2111        
REMARK   3     2  4.9939 -  3.9664    0.98     3345   139  0.1283 0.1378        
REMARK   3     3  3.9664 -  3.4658    0.99     3324   139  0.1471 0.2062        
REMARK   3     4  3.4658 -  3.1493    1.00     3353   140  0.1753 0.2610        
REMARK   3     5  3.1493 -  2.9237    1.00     3331   139  0.1930 0.2779        
REMARK   3     6  2.9237 -  2.7515    1.00     3322   138  0.1994 0.2422        
REMARK   3     7  2.7515 -  2.6137    1.00     3313   138  0.2071 0.2914        
REMARK   3     8  2.6137 -  2.5000    0.99     3306   138  0.1969 0.2461        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.354                                         
REMARK   3   B_SOL              : 58.980                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.25             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.85            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 45.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  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      :  0.006           4535                                  
REMARK   3   ANGLE     :  1.259           6175                                  
REMARK   3   CHIRALITY :  0.091            671                                  
REMARK   3   PLANARITY :  0.005            782                                  
REMARK   3   DIHEDRAL  : 21.089           1684                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 3 THROUGH 242)                      
REMARK   3    ORIGIN FOR THE GROUP (A):  29.6377  17.6955  37.8462              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3115 T22:   0.3797                                     
REMARK   3      T33:   0.2918 T12:  -0.0748                                     
REMARK   3      T13:  -0.0363 T23:  -0.0817                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9780 L22:   1.8861                                     
REMARK   3      L33:   2.3284 L12:   0.2613                                     
REMARK   3      L13:   0.3384 L23:   0.3588                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1645 S12:  -0.4942 S13:   0.1018                       
REMARK   3      S21:   0.4672 S22:  -0.0819 S23:  -0.0560                       
REMARK   3      S31:  -0.1036 S32:   0.0094 S33:  -0.0681                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 243 THROUGH 322)                    
REMARK   3    ORIGIN FOR THE GROUP (A):  40.8139   3.2360  33.1803              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3971 T22:   0.4499                                     
REMARK   3      T33:   0.4974 T12:   0.0071                                     
REMARK   3      T13:  -0.1547 T23:  -0.0578                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7067 L22:   1.8618                                     
REMARK   3      L33:   3.0680 L12:   0.0063                                     
REMARK   3      L13:   1.3526 L23:  -0.3177                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1511 S12:  -0.2532 S13:  -0.3263                       
REMARK   3      S21:   0.4397 S22:  -0.0796 S23:  -0.5735                       
REMARK   3      S31:   0.3436 S32:   0.6100 S33:  -0.1093                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 323 THROUGH 529)                    
REMARK   3    ORIGIN FOR THE GROUP (A):  32.4078  19.0139  12.2258              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3271 T22:   0.2907                                     
REMARK   3      T33:   0.2484 T12:  -0.0466                                     
REMARK   3      T13:  -0.0545 T23:  -0.0457                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1868 L22:   2.3365                                     
REMARK   3      L33:   2.2759 L12:  -0.2495                                     
REMARK   3      L13:  -0.5045 L23:   0.9473                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0195 S12:   0.2242 S13:   0.1411                       
REMARK   3      S21:  -0.3737 S22:   0.1141 S23:  -0.0932                       
REMARK   3      S31:  -0.2717 S32:   0.1716 S33:  -0.1257                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN A AND (RESID 1178 THROUGH 1178)                  
REMARK   3    ORIGIN FOR THE GROUP (A):  26.0479  29.6894  32.4666              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1944 T22:   0.1275                                     
REMARK   3      T33:   0.2615 T12:  -0.1003                                     
REMARK   3      T13:   0.0236 T23:   0.0388                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.6804 L22:   1.2667                                     
REMARK   3      L33:   4.4780 L12:   2.1396                                     
REMARK   3      L13:   5.7230 L23:   0.6878                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0461 S12:   0.3860 S13:  -0.3821                       
REMARK   3      S21:  -0.0075 S22:   0.4091 S23:  -0.0882                       
REMARK   3      S31:   0.1327 S32:   0.3411 S33:  -0.4192                       
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 4B0P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JUN-12.                  
REMARK 100 THE PDBE ID CODE IS EBI-52875.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-SEP-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00407                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (QUANTUM Q315R)                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27807                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.50                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.88                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 3.2                                
REMARK 200  R MERGE                    (I) : 0.01                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 21.40                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.2                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.06                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.58                               
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 1P0I                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.1 M AMMONIUM SULFATE, 0.1 M            
REMARK 280  MES BUFFER PH 6.5                                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z                                                 
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      11555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290      12555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290      13555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      14555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      15555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  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  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       77.11500            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       77.11500            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       66.93000            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       77.11500            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       77.11500            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       66.93000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       77.11500            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       77.11500            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       66.93000            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       77.11500            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       77.11500            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       66.93000            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       77.11500            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       77.11500            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       66.93000            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       77.11500            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       77.11500            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       66.93000            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       77.11500            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       77.11500            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       66.93000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       77.11500            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       77.11500            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       66.93000            
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: 9020 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 41880 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -104.3 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000 -1.000000  0.000000       77.11500            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000       77.11500            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       66.93000            
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     GLU A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     TYR A  237   CZ                                                  
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   NH1  ARG A    14     OD1  ASN A    57              2.20            
REMARK 500   NH1  ARG A   240     OE2  GLU A   257              2.12            
REMARK 500   ND2  ASN A   256     C2   NAG A  2188              2.18            
REMARK 500   NZ   LYS A   262     O    HOH A  3098              2.19            
REMARK 500   O    HOH A  3071     O    HOH A  3123              2.10            
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  43       -4.12     75.06                                   
REMARK 500    LYS A  51      141.91     88.46                                   
REMARK 500    ASP A  54      166.56     63.39                                   
REMARK 500    ASN A 106       56.65   -155.05                                   
REMARK 500    ALA A 162       79.25   -158.03                                   
REMARK 500    GLU A 257      -33.69    -39.52                                   
REMARK 500    ASP A 297      -73.43   -132.41                                   
REMARK 500    TRP A 376      151.81    -47.70                                   
REMARK 500    VAL A 377       60.79   -118.80                                   
REMARK 500    ASP A 378       46.56    -99.71                                   
REMARK 500    GLN A 380       73.80   -115.61                                   
REMARK 500    PHE A 398      -57.81   -134.10                                   
REMARK 500    ASN A 485       58.78   -105.93                                   
REMARK 500    ASN A 486       34.71     35.59                                   
REMARK 500    THR A 496      -72.45    -68.54                                   
REMARK 500    GLU A 506     -107.16    -96.34                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A2190  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 443   OE1                                                    
REMARK 620 2 HOH A3145   O    77.6                                              
REMARK 620 3 HOH A3187   O   111.2 117.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A1171   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SBG A 198   O2                                                     
REMARK 620 2 HOH A3021   O    86.9                                              
REMARK 620 3 HOH A3064   O   144.4  74.6                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY A1178                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA A1170                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE   K A1171                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MF5 A1179                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA A2190                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2191                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A2193                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A2194                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A2195                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2197                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A2198                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG A2179 BOUND TO ASN A  57                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG A2180 BOUND TO ASN A 106                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO         
REMARK 800   ASN A 241 RESIDUES 2181 TO 2183                                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG A2188 BOUND TO ASN A 256                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO         
REMARK 800   ASN A 341 RESIDUES 2184 TO 2186                                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG A2187 BOUND TO ASN A 485                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1EHO   RELATED DB: PDB                                   
REMARK 900  MODEL OF (-)-COCAINE-BOUND BCHE COMPLEX.                            
REMARK 900 RELATED ID: 1EHQ   RELATED DB: PDB                                   
REMARK 900  MODEL OF (+)-COCAINE-BOUND BCHE COMPLEX                             
REMARK 900 RELATED ID: 1KCJ   RELATED DB: PDB                                   
REMARK 900  MODEL OF (-)-COCAINE-BOUND (-)-COCAINE HYDROLASE COMPLEX            
REMARK 900 RELATED ID: 1P0I   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN BUTYRYL CHOLINESTERASE                   
REMARK 900 RELATED ID: 1P0M   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN BUTYRYL CHOLINESTERASE                   
REMARK 900  INCOMPLEX WITH A CHOLINE MOLECULE                                   
REMARK 900 RELATED ID: 1P0P   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN                               
REMARK 900  BUTYRYLCHOLINESTERASE IN COMPLEX WITH THE SUBSTRATE                 
REMARK 900  ANALOGBUTYRYLTHIOCHOLINE                                            
REMARK 900 RELATED ID: 1P0Q   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN BUTYRYL                       
REMARK 900  CHOLINESTERASE                                                      
REMARK 900 RELATED ID: 1XLU   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF DI-ISOPROPYL-PHOSPHORO-FLUORIDATE (              
REMARK 900  DFP)INHIBITED BUTYRYLCHOLINESTERASE AFTER AGING                     
REMARK 900 RELATED ID: 1XLV   RELATED DB: PDB                                   
REMARK 900  ETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (AGED) OBTAINEDBY         
REMARK 900  REACTION WITH ECHOTHIOPHATE                                         
REMARK 900 RELATED ID: 1XLW   RELATED DB: PDB                                   
REMARK 900  DIETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (NONAGED)OBTAINED       
REMARK 900  BY REACTION WITH ECHOTHIOPHATE                                      
REMARK 900 RELATED ID: 2J4C   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH            
REMARK 900  10MM HGCL2                                                          
REMARK 900 RELATED ID: 2WID   RELATED DB: PDB                                   
REMARK 900  AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY               
REMARK 900  TABUN ANALOGUE TA1                                                  
REMARK 900 RELATED ID: 2WIF   RELATED DB: PDB                                   
REMARK 900  AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY               
REMARK 900  TABUN ANALOGUE TA1                                                  
REMARK 900 RELATED ID: 2WIG   RELATED DB: PDB                                   
REMARK 900  NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY            
REMARK 900  TABUN ANALOGUE TA4                                                  
REMARK 900 RELATED ID: 2WIJ   RELATED DB: PDB                                   
REMARK 900  NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY            
REMARK 900  TABUN ANALOGUE TA5                                                  
REMARK 900 RELATED ID: 2WIK   RELATED DB: PDB                                   
REMARK 900  NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY            
REMARK 900  TABUN ANALOGUE TA6                                                  
REMARK 900 RELATED ID: 2WIL   RELATED DB: PDB                                   
REMARK 900  AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY               
REMARK 900  TABUN ANALOGUE TA5                                                  
REMARK 900 RELATED ID: 2WSL   RELATED DB: PDB                                   
REMARK 900  AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY               
REMARK 900  TABUN ANALOGUE TA4                                                  
REMARK 900 RELATED ID: 2XMB   RELATED DB: PDB                                   
REMARK 900  G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX              
REMARK 900  WITH SULFATE                                                        
REMARK 900 RELATED ID: 2XMC   RELATED DB: PDB                                   
REMARK 900  G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX              
REMARK 900  WITH FLUORIDE ANION                                                 
REMARK 900 RELATED ID: 2XMD   RELATED DB: PDB                                   
REMARK 900  G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX              
REMARK 900  WITH ECHOTHIOPHATE                                                  
REMARK 900 RELATED ID: 2XMG   RELATED DB: PDB                                   
REMARK 900  G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX              
REMARK 900  WITH VX                                                             
REMARK 900 RELATED ID: 2XQF   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED            
REMARK 900  BY RACEMIC VX                                                       
REMARK 900 RELATED ID: 2XQG   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED            
REMARK 900  BY RACEMIC VR                                                       
REMARK 900 RELATED ID: 2XQI   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED            
REMARK 900  BY RACEMIC CVX                                                      
REMARK 900 RELATED ID: 2XQJ   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED            
REMARK 900  BY PURE ENANTIOMER VX-(R)                                           
REMARK 900 RELATED ID: 2XQK   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED            
REMARK 900  BY PURE ENANTIOMER VX-(S)                                           
REMARK 900 RELATED ID: 2Y1K   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY CBDP          
REMARK 900   (12H SOAK): PHOSPHOSERINE ADDUCT                                   
REMARK 900 RELATED ID: 4AQD   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF FULLY GLYCOSYLATED HUMAN                       
REMARK 900  BUTYRYLCHOLINESTERASE                                               
REMARK 900 RELATED ID: 4AXB   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN                               
REMARK 900  BUTYRYLCHOLINESTERASE IN COMPLEX WITH 2-PAM                         
REMARK 900 RELATED ID: 4B0O   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN                               
REMARK 900  BUTYRYLCHOLINESTERASE IN COMPLEX WITH BENZYL PYRIDINIUM-4           
REMARK 900  -METHYLTRICHLOROACETIMIDATE                                         
DBREF  4B0P A    1   529  UNP    P06276   CHLE_HUMAN      29    557             
SEQADV 4B0P GLN A   17  UNP  P06276    ASN    45 CONFLICT                       
SEQADV 4B0P GLN A  384  UNP  P06276    ASN   412 CONFLICT                       
SEQADV 4B0P GLN A  455  UNP  P06276    ASN   483 CONFLICT                       
SEQADV 4B0P GLN A  481  UNP  P06276    ASN   509 CONFLICT                       
SEQRES   1 A  529  GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL          
SEQRES   2 A  529  ARG GLY MET GLN LEU THR VAL PHE GLY GLY THR VAL THR          
SEQRES   3 A  529  ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY          
SEQRES   4 A  529  ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP          
SEQRES   5 A  529  SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS          
SEQRES   6 A  529  CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY          
SEQRES   7 A  529  SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP          
SEQRES   8 A  529  CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO          
SEQRES   9 A  529  LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY          
SEQRES  10 A  529  PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY          
SEQRES  11 A  529  LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER          
SEQRES  12 A  529  MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU          
SEQRES  13 A  529  PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE          
SEQRES  14 A  529  ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE          
SEQRES  15 A  529  ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE          
SEQRES  16 A  529  GLY GLU SBG ALA GLY ALA ALA SER VAL SER LEU HIS LEU          
SEQRES  17 A  529  LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE          
SEQRES  18 A  529  LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR          
SEQRES  19 A  529  SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA          
SEQRES  20 A  529  LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE          
SEQRES  21 A  529  ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU          
SEQRES  22 A  529  LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU          
SEQRES  23 A  529  SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU          
SEQRES  24 A  529  THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE          
SEQRES  25 A  529  LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU          
SEQRES  26 A  529  GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER          
SEQRES  27 A  529  LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN          
SEQRES  28 A  529  GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE          
SEQRES  29 A  529  GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL          
SEQRES  30 A  529  ASP ASP GLN ARG PRO GLU GLN TYR ARG GLU ALA LEU GLY          
SEQRES  31 A  529  ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU          
SEQRES  32 A  529  GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA          
SEQRES  33 A  529  PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO          
SEQRES  34 A  529  TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE          
SEQRES  35 A  529  GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP GLN          
SEQRES  36 A  529  TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL          
SEQRES  37 A  529  LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO GLN          
SEQRES  38 A  529  GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS          
SEQRES  39 A  529  SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER          
SEQRES  40 A  529  THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG          
SEQRES  41 A  529  PHE TRP THR SER PHE PHE PRO LYS VAL                          
MODRES 4B0P SBG A  198  SER  MODIFIED SERINE                                    
HET    SBG  A 198      10                                                       
HET    GLY  A1178       5                                                       
HET     NA  A1170       1                                                       
HET      K  A1171       1                                                       
HET    MF5  A1179      22                                                       
HET    NAG  A2179      14                                                       
HET    NAG  A2180      14                                                       
HET    NAG  A2181      14                                                       
HET    NAG  A2182      14                                                       
HET    FUL  A2183      10                                                       
HET    NAG  A2184      14                                                       
HET    NAG  A2185      14                                                       
HET    FUL  A2186      10                                                       
HET    NAG  A2187      14                                                       
HET    NAG  A2188      14                                                       
HET     NA  A2190       1                                                       
HET     CA  A2191       1                                                       
HET     CA  A2192       1                                                       
HET     CL  A2193       1                                                       
HET     CL  A2194       1                                                       
HET     CL  A2195       1                                                       
HET     CL  A2196       1                                                       
HET     CA  A2197       1                                                       
HET     CA  A2198       1                                                       
HETNAM     SBG O-[(S)-HYDROXY(METHYL)PHOSPHORYL]-L-SERINE                       
HETNAM     GLY GLYCINE                                                          
HETNAM      NA SODIUM ION                                                       
HETNAM       K POTASSIUM ION                                                    
HETNAM     MF5 1-(1-METHYLPYRIDIN-1-IUM-2-YL)-N-[[2,3,4,5,6-PENTAKIS(FLUORANYL) 
HETNAM   2 MF5 PHENYL]METHOXY]METHANIMINE                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUL BETA-L-FUCOSE                                                    
HETNAM      CA CALCIUM ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETSYN     MF5 METHYL2-(PENTAFLUOROBENZYLOXYIMINO)PYRIDINIUM                    
HETSYN     FUL 6-DEOXY-BETA-L-GALACTOSE                                         
FORMUL   1  SBG    C4 H10 N O5 P                                                
FORMUL   2  GLY    C2 H5 N O2                                                   
FORMUL   3   NA    2(NA 1+)                                                     
FORMUL   4    K    K 1+                                                         
FORMUL   5  MF5    C14 H10 F5 N2 O 1+                                           
FORMUL   6  NAG    8(C8 H15 N O6)                                               
FORMUL   7  FUL    2(C6 H12 O5)                                                 
FORMUL   8   CA    4(CA 2+)                                                     
FORMUL   9   CL    4(CL 1-)                                                     
FORMUL  10  HOH   *188(H2 O)                                                    
HELIX    1   1 LEU A   38  ARG A   42  5                                   5    
HELIX    2   2 PHE A   76  MET A   81  1                                   6    
HELIX    3   3 LEU A  125  ASP A  129  5                                   5    
HELIX    4   4 GLY A  130  ARG A  138  1                                   9    
HELIX    5   5 VAL A  148  LEU A  154  1                                   7    
HELIX    6   6 ASN A  165  ILE A  182  1                                  18    
HELIX    7   7 ALA A  183  PHE A  185  5                                   3    
HELIX    8   8 ALA A  199  SER A  210  1                                  12    
HELIX    9   9 PRO A  211  HIS A  214  5                                   4    
HELIX   10  10 SER A  235  THR A  250  1                                  16    
HELIX   11  11 ASN A  256  ASN A  266  1                                  11    
HELIX   12  12 ASP A  268  ALA A  277  1                                  10    
HELIX   13  13 PHE A  278  VAL A  280  5                                   3    
HELIX   14  14 MET A  302  LEU A  309  1                                   8    
HELIX   15  15 GLY A  326  VAL A  331  1                                   6    
HELIX   16  16 THR A  346  PHE A  358  1                                  13    
HELIX   17  17 SER A  362  THR A  374  1                                  13    
HELIX   18  18 GLU A  383  PHE A  398  1                                  16    
HELIX   19  19 PHE A  398  GLU A  411  1                                  14    
HELIX   20  20 PRO A  431  GLY A  435  5                                   5    
HELIX   21  21 GLU A  441  PHE A  446  1                                   6    
HELIX   22  22 GLY A  447  GLU A  451  5                                   5    
HELIX   23  23 GLU A  451  GLN A  455  5                                   5    
HELIX   24  24 THR A  457  GLY A  478  1                                  22    
HELIX   25  25 ARG A  515  PHE A  525  1                                  11    
HELIX   26  26 PHE A  526  VAL A  529  5                                   4    
SHEET    1  AA 3 ILE A   5  THR A   8  0                                        
SHEET    2  AA 3 GLY A  11  ARG A  14 -1  O  GLY A  11   N  THR A   8           
SHEET    3  AA 3 TRP A  56  ASN A  57  1  O  TRP A  56   N  ARG A  14           
SHEET    1  AB11 MET A  16  VAL A  20  0                                        
SHEET    2  AB11 GLY A  23  PRO A  32 -1  O  GLY A  23   N  VAL A  20           
SHEET    3  AB11 TYR A  94  PRO A 100 -1  O  LEU A  95   N  ILE A  31           
SHEET    4  AB11 ILE A 140  MET A 144 -1  O  VAL A 141   N  TRP A  98           
SHEET    5  AB11 ALA A 107  ILE A 113  1  O  THR A 108   N  ILE A 140           
SHEET    6  AB11 GLY A 187  GLY A 196  1  N  ASN A 188   O  ALA A 107           
SHEET    7  AB11 ARG A 219  GLN A 223  1  O  ARG A 219   N  LEU A 194           
SHEET    8  AB11 ILE A 317  ASN A 322  1  O  LEU A 318   N  LEU A 222           
SHEET    9  AB11 ALA A 416  PHE A 421  1  O  PHE A 417   N  VAL A 319           
SHEET   10  AB11 LYS A 499  LEU A 503  1  O  LEU A 501   N  TYR A 420           
SHEET   11  AB11 ARG A 509  THR A 512 -1  O  ARG A 509   N  THR A 502           
SHEET    1  AC 2 SER A  64  CYS A  65  0                                        
SHEET    2  AC 2 LEU A  88  SER A  89  1  N  SER A  89   O  SER A  64           
SSBOND   1 CYS A   65    CYS A   92                          1555   1555  2.04  
SSBOND   2 CYS A  252    CYS A  263                          1555   1555  2.04  
SSBOND   3 CYS A  400    CYS A  519                          1555   1555  2.05  
LINK         ND2 ASN A  57                 C1  NAG A2179     1555   1555  1.46  
LINK         ND2 ASN A 106                 C1  NAG A2180     1555   1555  1.46  
LINK         O2  SBG A 198                 K     K A1171     1555   1555  3.29  
LINK         N   SBG A 198                 C   GLU A 197     1555   1555  1.33  
LINK         C   SBG A 198                 N   ALA A 199     1555   1555  1.33  
LINK         ND2 ASN A 241                 C1  NAG A2181     1555   1555  1.46  
LINK         ND2 ASN A 256                 C1  NAG A2188     1555   1555  1.44  
LINK         ND2 ASN A 341                 C1  NAG A2184     1555   1555  1.44  
LINK         ND2 ASN A 485                 C1  NAG A2187     1555   1555  1.45  
LINK         K     K A1171                 O   HOH A3021     1555   1555  2.84  
LINK         K     K A1171                 O   HOH A3064     1555   1555  2.86  
LINK         O6  NAG A2181                 C1  FUL A2183     1555   1555  1.44  
LINK         O4  NAG A2181                 C1  NAG A2182     1555   1555  1.46  
LINK         O6  NAG A2184                 C1  FUL A2186     1555   1555  1.44  
LINK         O4  NAG A2184                 C1  NAG A2185     1555   1555  1.44  
LINK        NA    NA A2190                 O   HOH A3187     1555   1555  2.66  
LINK        NA    NA A2190                 O   HOH A3145     1555   1555  2.50  
LINK        NA    NA A2190                 OE1 GLU A 443     1555   1555  2.97  
LINK        CA    CA A2197                 SG  CYS A  66     1555   1555  2.72  
CISPEP   1 ALA A  101    PRO A  102          0        -2.80                     
CISPEP   2 VAL A  377    ASP A  378          0       -19.12                     
SITE     1 AC1  5 LEU A  18  TYR A  61  TRP A  98  ASP A 129                    
SITE     2 AC1  5 LYS A 131                                                     
SITE     1 AC2  2 GLU A  80  ASN A  83                                          
SITE     1 AC3  3 SBG A 198  HOH A3021  HOH A3064                               
SITE     1 AC4 11 ASP A  70  TRP A  82  GLY A 116  GLU A 197                    
SITE     2 AC4 11 PRO A 285  ALA A 328  PHE A 329  TYR A 332                    
SITE     3 AC4 11 HIS A 438  GLY A 439  HOH A3041                               
SITE     1 AC5  4 MET A  81  GLU A 443  HOH A3145  HOH A3187                    
SITE     1 AC6  1 TYR A 420                                                     
SITE     1 AC7  2 ARG A 242  VAL A 288                                          
SITE     1 AC8  1 ARG A 347                                                     
SITE     1 AC9  2 THR A 512  LYS A 513                                          
SITE     1 BC1  2 CYS A  66  GLN A 270                                          
SITE     1 BC2  1 PHE A 217                                                     
SITE     1 BC3  2 ARG A  14  ASN A  57                                          
SITE     1 BC4  4 ASN A 106  ASN A 188  LYS A 190  HOH A3184                    
SITE     1 BC5  6 TYR A 237  ASN A 241  ASN A 245  LEU A 249                    
SITE     2 BC5  6 PHE A 278  PRO A 281                                          
SITE     1 BC6  1 ASN A 256                                                     
SITE     1 BC7  7 PRO A 335  GLY A 336  PHE A 337  SER A 338                    
SITE     2 BC7  7 ASN A 341  ASN A 342  HOH A3185                               
SITE     1 BC8  4 ARG A 465  GLU A 482  ASN A 485  HOH A3186                    
CRYST1  154.230  154.230  133.860  90.00  90.00  90.00 I 4 2 2      16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006484  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006484  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007470        0.00000                         
TER    4238      VAL A 529                                                      
MASTER      562    0   24   26   16    0   22    6 4595    1  192   41          
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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