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LongText Report for: 2WIG-pdb

Name Class
2WIG-pdb
HEADER    HYDROLASE                               11-MAY-09   2WIG              
TITLE     NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY              
TITLE    2 TABUN ANALOGUE TA4                                                   
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  CHOLINE ESTERASE II, BUTYRYLCHOLINE ESTERASE,                       
COMPND   7  PSEUDOCHOLINESTERASE;                                               
COMPND   8 EC: 3.1.1.8;                                                         
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES;                                                       
COMPND  11 OTHER_DETAILS: S198 IS PHOSPHORAMIDYLATED                            
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_TAXID: 10029;                                      
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: CHO-K1;                                    
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: OVARY CELLS;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGS                                       
KEYWDS    TABUN, AGING, HYDROLASE, INHIBITION, POLYMORPHISM,                    
KEYWDS   2 GLYCOPROTEIN, DISULFIDE BOND, SERINE ESTERASE, DISEASE               
KEYWDS   3 MUTATION, BUTYRYLCHOLINESTERASE                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.CARLETTI,N.AURBEK,E.GILLON,M.LOIODICE,Y.NICOLET,                    
AUTHOR   2 J.FONTECILLA,P.MASSON,H.THIERMANN,F.NACHON,F.WOREK                   
REVDAT   1   19-MAY-09 2WIG    0                                                
JRNL        AUTH   E.CARLETTI,N.AURBEK,E.GILLON,M.LOIODICE,Y.NICOLET,           
JRNL        AUTH 2 J.FONTECILLA,P.MASSON,H.THIERMANN,F.NACHON,F.WOREK           
JRNL        TITL   STRUCTURE-ACTIVITY ANALYSIS OF AGING AND                     
JRNL        TITL 2 REACTIVATION OF HUMAN BUTYRYLCHOLINESTERASE                  
JRNL        TITL 3 INHIBITED BY ANALOGUES OF TABUN                              
JRNL        REF    BIOCHEM.J.                                 2009              
JRNL        REFN                   ESSN 1470-8728                               
JRNL        PMID   19368529                                                     
JRNL        DOI    10.1042/BJ20090091                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0069                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.09                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.00                         
REMARK   3   NUMBER OF REFLECTIONS             : 40659                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.19060                         
REMARK   3   R VALUE            (WORKING SET) : 0.18868                         
REMARK   3   FREE R VALUE                     : 0.25296                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1258                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.150                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.206                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2927                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.254                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 91                           
REMARK   3   BIN FREE R VALUE                    : 0.363                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4226                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 164                                     
REMARK   3   SOLVENT ATOMS            : 343                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.280                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00                                                 
REMARK   3    B22 (A**2) : 0.00                                                 
REMARK   3    B33 (A**2) : 0.00                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.191         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.187         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.141         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.566         
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.925                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4514 ; 0.018 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6150 ; 1.875 ; 1.983       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   529 ; 6.778 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   206 ;36.006 ;24.078       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   700 ;17.521 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;17.242 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   673 ; 0.144 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3404 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2632 ; 1.065 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4251 ; 1.929 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1882 ; 2.820 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1897 ; 4.417 ; 4.500       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   4                                                                      
REMARK   4 2WIG COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-MAY-09.                  
REMARK 100 THE PDBE ID CODE IS EBI-39779.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-SEP-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
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                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
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   : 41918                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.15                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 7.2                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 25.80                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.2                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.29                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 4.30                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: XDS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1P0I                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.5                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.1 M AMMONIUM SULFATE, 100 MM           
REMARK 280  MES PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE              
REMARK 280  293K                                                                
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       77.50500            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       77.50500            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       63.42000            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       77.50500            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       77.50500            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       63.42000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       77.50500            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       77.50500            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       63.42000            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       77.50500            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       77.50500            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       63.42000            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       77.50500            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       77.50500            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       63.42000            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       77.50500            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       77.50500            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       63.42000            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       77.50500            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       77.50500            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       63.42000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       77.50500            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       77.50500            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       63.42000            
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 GENERATING THE BIOMOLECULE                                           
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: OCTAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 47540 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 153490 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -334.64 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  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   6  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN  45 TO GLN                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 483 TO GLN                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 509 TO GLN                        
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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 528    CA                                                  
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;                                
REMARK 480 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 480 I=INSERTION CODE):                                                   
REMARK 480   M RES CSSEQI  ATOMS                                                
REMARK 480     LYS A  51    CB   CG   CD   CE   NZ                              
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   N    ASN A   106  -  O    HOH A  2092              2.09            
REMARK 500   N    THR A   496  -  O    HOH A  2294              2.12            
REMARK 500   NH2  ARG A   509  -  O    HOH A  2305              2.13            
REMARK 500   O    HOH A  2002  -  O    HOH A  2138              2.04            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 359   C   -  N   -  CA  ANGL. DEV. =  13.2 DEGREES          
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 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    THR A  53       64.13    178.18                                   
REMARK 500    ASP A  54      120.96    100.77                                   
REMARK 500    ALA A  58       73.59   -103.59                                   
REMARK 500    GLN A  67      148.54   -174.79                                   
REMARK 500    ASN A 106       61.61   -163.07                                   
REMARK 500    PRO A 160        0.30    -69.15                                   
REMARK 500    ASN A 165       15.87     58.33                                   
REMARK 500    SER A 198     -121.96     52.42                                   
REMARK 500    VAL A 279       -0.61    -59.88                                   
REMARK 500    ASP A 297      -78.39   -134.39                                   
REMARK 500    ASP A 324       53.93   -114.66                                   
REMARK 500    ILE A 344      104.37    -59.70                                   
REMARK 500    PRO A 359      -59.50    -20.95                                   
REMARK 500    VAL A 361       80.61     51.50                                   
REMARK 500    SER A 362      156.32    -48.52                                   
REMARK 500    ASP A 379       10.76    -56.84                                   
REMARK 500    GLN A 380      -71.02    -77.91                                   
REMARK 500    ARG A 381      110.68    -20.83                                   
REMARK 500    PHE A 398      -55.74   -125.38                                   
REMARK 500    ARG A 453       -6.75    -54.57                                   
REMARK 500    THR A 496      -90.97     93.62                                   
REMARK 500    GLU A 506      -84.95    -70.02                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY A  360     VAL A  361                   34.23                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL A 361         6.0      L          D   EXPECTING SP3           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TC3 A1530                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA A1531                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1532                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1533                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1534                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1535                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1536                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1538                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1539                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUL A1540                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1541                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUL A1542                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1543                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1544                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1546                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1547                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUL A1548                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1EHQ   RELATED DB: PDB                                   
REMARK 900  MODEL OF (+)-COCAINE-BOUND BCHE COMPLEX                             
REMARK 900 RELATED ID: 1P0Q   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN                               
REMARK 900  BUTYRYL CHOLINESTERASE                                              
REMARK 900 RELATED ID: 2J4C   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE IN                         
REMARK 900  COMPLEX WITH 10MM HGCL2                                             
REMARK 900 RELATED ID: 1KCJ   RELATED DB: PDB                                   
REMARK 900  MODEL OF (-)-COCAINE-BOUND (-)-COCAINE                              
REMARK 900  HYDROLASE COMPLEX                                                   
REMARK 900 RELATED ID: 1P0P   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN                               
REMARK 900  BUTYRYLCHOLINESTERASE IN COMPLEX WITH THE                           
REMARK 900  SUBSTRATE ANALOGBUTYRYLTHIOCHOLINE                                  
REMARK 900 RELATED ID: 1XLU   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF DI-ISOPROPYL-PHOSPHORO-                          
REMARK 900  FLUORIDATE (DFP)INHIBITED BUTYRYLCHOLINESTERASE                     
REMARK 900  AFTER AGING                                                         
REMARK 900 RELATED ID: 1XLV   RELATED DB: PDB                                   
REMARK 900  ETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (AGED)                    
REMARK 900  OBTAINEDBY REACTION WITH ECHOTHIOPHATE                              
REMARK 900 RELATED ID: 1EHO   RELATED DB: PDB                                   
REMARK 900  MODEL OF (-)-COCAINE-BOUND BCHE COMPLEX.                            
REMARK 900 RELATED ID: 1P0M   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN BUTYRYL                                  
REMARK 900  CHOLINESTERASE INCOMPLEX WITH A CHOLINE                             
REMARK 900  MOLECULE                                                            
REMARK 900 RELATED ID: 1XLW   RELATED DB: PDB                                   
REMARK 900  DIETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (NONAGED                
REMARK 900  )OBTAINED BY REACTION WITH ECHOTHIOPHATE                            
REMARK 900 RELATED ID: 1P0I   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN BUTYRYL                                  
REMARK 900  CHOLINESTERASE                                                      
REMARK 900 RELATED ID: 2WIK   RELATED DB: PDB                                   
REMARK 900  NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE                         
REMARK 900  INHIBITED BY TABUN ANALOGUE TA6                                     
REMARK 900 RELATED ID: 2WIF   RELATED DB: PDB                                   
REMARK 900  NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE                         
REMARK 900  INHIBITED BY TABUN ANALOGUE TA1                                     
REMARK 900 RELATED ID: 2WID   RELATED DB: PDB                                   
REMARK 900  AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE                            
REMARK 900  INHIBITED BY TABUN ANALOGUE TA1                                     
REMARK 900 RELATED ID: 2WIJ   RELATED DB: PDB                                   
REMARK 900  NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE                         
REMARK 900  INHIBITED BY TABUN ANALOGUE TA5                                     
DBREF  2WIG A    1   529  UNP    P06276   CHLE_HUMAN      29    557             
SEQADV 2WIG GLN A   17  UNP  P06276    ASN    45 ENGINEERED MUTATION            
SEQADV 2WIG THR A   53  UNP  P06276    SER    81 CONFLICT                       
SEQADV 2WIG GLN A  455  UNP  P06276    ASN   483 ENGINEERED MUTATION            
SEQADV 2WIG GLN A  481  UNP  P06276    ASN   509 ENGINEERED MUTATION            
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  THR 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 SER 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 ASN 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                          
HET    TC3  A1530       7                                                       
HET     NA  A1531       1                                                       
HET    SO4  A1532       5                                                       
HET     CL  A1533       1                                                       
HET     CL  A1534       1                                                       
HET     CL  A1535       1                                                       
HET    SO4  A1536       5                                                       
HET     CL  A1537       1                                                       
HET    NAG  A1538      14                                                       
HET    NAG  A1539      14                                                       
HET    FUL  A1540      10                                                       
HET    NAG  A1541      14                                                       
HET    FUL  A1542      10                                                       
HET    NAG  A1543      14                                                       
HET    NAG  A1544      14                                                       
HET    NAG  A1545      14                                                       
HET    NAG  A1546      14                                                       
HET    NAG  A1547      14                                                       
HET    FUL  A1548      10                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM      NA SODIUM ION                                                       
HETNAM     FUL BETA-L-FUCOSE                                                    
HETNAM     TC3 ETHYL HYDROGEN METHYLAMIDOPHOSPHATE                              
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   2  SO4    2(O4 S 2-)                                                   
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   4   CL    4(CL 1-)                                                     
FORMUL   5   NA    NA 1+                                                        
FORMUL   6  FUL    3(C6 H12 O5)                                                 
FORMUL   7  TC3    C3 H10 N1 O3 P1                                              
FORMUL   8  NAG    8(C8 H15 N O6)                                               
FORMUL   9  HOH   *343(H2 O1)                                                   
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 GLY A  149  LEU A  154  1                                   6    
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 SER A  198  SER A  210  1                                  13    
HELIX    9   9 PRO A  211  PHE A  217  5                                   7    
HELIX   10  10 SER A  235  THR A  250  1                                  16    
HELIX   11  11 ASN A  256  ARG A  265  1                                  10    
HELIX   12  12 ASP A  268  ALA A  277  1                                  10    
HELIX   13  13 MET A  302  LEU A  309  1                                   8    
HELIX   14  14 GLY A  326  GLY A  333  5                                   8    
HELIX   15  15 THR A  346  PHE A  358  1                                  13    
HELIX   16  16 SER A  362  THR A  374  1                                  13    
HELIX   17  17 GLU A  383  PHE A  398  1                                  16    
HELIX   18  18 PHE A  398  GLU A  411  1                                  14    
HELIX   19  19 PRO A  431  GLY A  435  5                                   5    
HELIX   20  20 GLU A  441  PHE A  446  1                                   6    
HELIX   21  21 GLY A  447  GLU A  451  5                                   5    
HELIX   22  22 GLU A  451  GLN A  455  5                                   5    
HELIX   23  23 THR A  457  GLY A  478  1                                  22    
HELIX   24  24 ARG A  515  SER A  524  1                                  10    
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 ILE A  55  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  ALA A 101 -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  GLU A 197  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 ILE A 510  THR A 512 -1  O  MET A 511   N  TYR A 500           
SSBOND   1 CYS A   65    CYS A   92                          1555   1555  2.10  
SSBOND   2 CYS A  252    CYS A  263                          1555   1555  2.06  
SSBOND   3 CYS A  400    CYS A  519                          1555   1555  2.08  
LINK         ND2 ASN A  57                 C1  NAG A1543     1555   1555  1.47  
LINK         ND2 ASN A 106                 C1  NAG A1541     1555   1555  1.46  
LINK         OG  SER A 198                 P   TC3 A1530     1555   1555  1.65  
LINK         ND2 ASN A 241                 C1  NAG A1546     1555   1555  1.47  
LINK         ND2 ASN A 256                 C1  NAG A1545     1555   1555  1.45  
LINK         ND2 ASN A 341                 C1  NAG A1538     1555   1555  1.43  
LINK         ND2 ASN A 485                 C1  NAG A1544     1555   1555  1.45  
LINK         O6  NAG A1538                 C1  FUL A1540     1555   1555  1.43  
LINK         O4  NAG A1538                 C1  NAG A1539     1555   1555  1.42  
LINK         O6  NAG A1541                 C1  FUL A1542     1555   1555  1.44  
LINK         O6  NAG A1546                 C1  FUL A1548     1555   1555  1.44  
LINK         O4  NAG A1546                 C1  NAG A1547     1555   1555  1.44  
CISPEP   1 THR A   53    ASP A   54          0       -14.38                     
CISPEP   2 ALA A  101    PRO A  102          0        -0.65                     
CISPEP   3 VAL A  377    ASP A  378          0         3.47                     
SITE     1 AC1  7 GLY A 116  GLY A 117  SER A 198  ALA A 199                    
SITE     2 AC1  7 LEU A 286  PHE A 398  HIS A 438                               
SITE     1 AC2  1 PHE A 525                                                     
SITE     1 AC3  5 LYS A 323  TYR A 420  ARG A 515  HOH A2191                    
SITE     2 AC3  5 HOH A2328                                                     
SITE     1 AC4  2 HIS A  77  HOH A2025                                          
SITE     1 AC5  2 ASP A 378  GLN A 380                                          
SITE     1 AC6  2 ARG A 515  HOH A2321                                          
SITE     1 AC7  4 GLN A 316  GLY A 413  ASN A 414  ASN A 415                    
SITE     1 AC8  5 SER A 338  ASN A 341  NAG A1539  FUL A1540                    
SITE     2 AC8  5 HOH A2201                                                     
SITE     1 AC9  2 GLY A 336  NAG A1538                                          
SITE     1 BC1  1 NAG A1538                                                     
SITE     1 BC2  4 ASN A 106  ASN A 188  LYS A 190  FUL A1542                    
SITE     1 BC3  7 ASN A 188  LYS A 190  SER A 191  LYS A 476                    
SITE     2 BC3  7 NAG A1541  HOH A2093  HOH A2331                               
SITE     1 BC4  2 ASN A  57  HOH A2333                                          
SITE     1 BC5  4 ARG A 465  ASN A 485  HOH A2336  HOH A2337                    
SITE     1 BC6  3 ASN A 256  GLU A 259  HOH A2339                               
SITE     1 BC7  7 TYR A 237  ASN A 241  ASN A 245  NAG A1547                    
SITE     2 BC7  7 FUL A1548  HOH A2164  HOH A2340                               
SITE     1 BC8  3 NAG A1546  FUL A1548  HOH A2341                               
SITE     1 BC9  6 ASN A 245  LEU A 249  PHE A 278  NAG A1546                    
SITE     2 BC9  6 NAG A1547  HOH A2343                                          
CRYST1  155.010  155.010  126.840  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      0.006451  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006451  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007884        0.00000                         
TER    4227      VAL A 529                                                      
MASTER      561    0   19   24   14    0   24    6 4733    1  172   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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