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LongText Report for: 2Y1K-pdb

Name Class
2Y1K-pdb
HEADER    HYDROLASE                               08-DEC-10   2Y1K              
TITLE     STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY CBDP (          
TITLE    2 12H SOAK): PHOSPHOSERINE ADDUCT                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLINESTERASE;                                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 29-557;                                           
COMPND   5 EC: 3.1.1.8;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 OTHER_DETAILS:                                                       
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, INHIBITION, AGING                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.CARLETTI,J.P.COLLETIER,F.NACHON,M.WEIK                              
REVDAT   1   29-JUN-11 2Y1K    0                                                
JRNL        AUTH   E.CARLETTI,L.M.SCHOPFER,J.P.COLLETIER,M.T.FROMENT,F.NACHON,  
JRNL        AUTH 2 M.WEIK,O.LOCKRIDGE,P.MASSON                                  
JRNL        TITL   REACTION OF CRESYL SALIGENIN PHOSPHATE, THE                  
JRNL        TITL 2 ORGANOPHOSPHORUS AGENT IMPLICATED IN AEROTOXIC SYNDROME,     
JRNL        TITL 3 WITH HUMAN CHOLINESTERASES: MECHANISTIC STUDIES EMPLOYING    
JRNL        TITL 4 KINETICS, MASS SPECTROMETRY, AND X-RAY STRUCTURE ANALYSIS.   
JRNL        REF    CHEM.RES.TOXICOL.             V.  24   797 2011              
JRNL        REFN                   ISSN 0893-228X                               
JRNL        PMID   21438623                                                     
JRNL        DOI    10.1021/TX100447K                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0093                                      
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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.38                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.79                          
REMARK   3   NUMBER OF REFLECTIONS             : 24577                          
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) : 0.18480                         
REMARK   3   R VALUE            (WORKING SET) : 0.18281                         
REMARK   3   FREE R VALUE                     : 0.24706                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 760                             
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) : 2.500                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.565                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1713                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.19                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.265                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 53                           
REMARK   3   BIN FREE R VALUE                    : 0.432                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4193                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 175                                     
REMARK   3   SOLVENT ATOMS            : 229                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 61.361                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.02                                                 
REMARK   3    B22 (A**2) : 0.02                                                 
REMARK   3    B33 (A**2) : -0.04                                                
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): 0.405         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.275         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.211         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 18.173        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4484 ; 0.018 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6097 ; 1.933 ; 1.984       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   527 ; 7.481 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   201 ;37.736 ;24.030       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   700 ;18.567 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;15.683 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   673 ; 0.151 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3378 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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 : 6                                           
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     3        A    70                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.5889  28.8405  18.6809              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4925 T22:   0.3015                                     
REMARK   3      T33:   0.0393 T12:  -0.0887                                     
REMARK   3      T13:   0.1153 T23:   0.0227                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1174 L22:   4.3716                                     
REMARK   3      L33:   2.6680 L12:  -1.2092                                     
REMARK   3      L13:  -0.1780 L23:  -0.3635                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0095 S12:   0.9061 S13:   0.1341                       
REMARK   3      S21:  -1.2883 S22:  -0.0816 S23:  -0.3160                       
REMARK   3      S31:   0.2084 S32:   0.3469 S33:   0.0912                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    71        A   233                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.6657  28.3397  31.0946              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1602 T22:   0.0797                                     
REMARK   3      T33:   0.0264 T12:  -0.0663                                     
REMARK   3      T13:   0.0206 T23:   0.0191                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1968 L22:   2.4159                                     
REMARK   3      L33:   2.6600 L12:  -0.0049                                     
REMARK   3      L13:  -0.6708 L23:  -0.0284                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1515 S12:   0.2055 S13:   0.0925                       
REMARK   3      S21:  -0.3452 S22:   0.1520 S23:  -0.0099                       
REMARK   3      S31:   0.1843 S32:   0.0987 S33:  -0.0005                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   234        A   282                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.2214  49.8386  27.0455              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4594 T22:   0.3087                                     
REMARK   3      T33:   0.5078 T12:   0.0479                                     
REMARK   3      T13:  -0.0633 T23:   0.1842                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6554 L22:   6.4919                                     
REMARK   3      L33:   9.4734 L12:  -0.1429                                     
REMARK   3      L13:  -0.0324 L23:  -2.1078                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0360 S12:  -0.0011 S13:   0.9013                       
REMARK   3      S21:  -0.0403 S22:   0.2320 S23:   0.4281                       
REMARK   3      S31:  -1.1427 S32:  -0.7709 S33:  -0.1959                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   283        A   373                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.4193  39.9844  49.4328              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1406 T22:   0.1351                                     
REMARK   3      T33:   0.2263 T12:  -0.0005                                     
REMARK   3      T13:   0.0990 T23:  -0.0035                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0609 L22:   2.3653                                     
REMARK   3      L33:   3.1414 L12:   0.8796                                     
REMARK   3      L13:   0.0899 L23:   0.8209                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0698 S12:  -0.1961 S13:   0.3864                       
REMARK   3      S21:  -0.0054 S22:   0.0620 S23:   0.4718                       
REMARK   3      S31:  -0.4771 S32:  -0.0738 S33:  -0.1318                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   374        A   472                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.4372  30.4890  50.5303              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0527 T22:   0.4568                                     
REMARK   3      T33:   0.0665 T12:  -0.0196                                     
REMARK   3      T13:   0.0151 T23:  -0.0576                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3627 L22:   5.5425                                     
REMARK   3      L33:   3.1475 L12:  -0.1568                                     
REMARK   3      L13:  -0.6040 L23:   0.5251                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0315 S12:  -0.7712 S13:   0.1040                       
REMARK   3      S21:   0.2718 S22:   0.0816 S23:  -0.4190                       
REMARK   3      S31:  -0.0515 S32:   0.5795 S33:  -0.1131                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   473        A   529                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.5166  21.7678  54.6426              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1220 T22:   0.3879                                     
REMARK   3      T33:   0.2665 T12:  -0.0811                                     
REMARK   3      T13:  -0.0249 T23:   0.2653                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9092 L22:   8.6307                                     
REMARK   3      L33:   4.4235 L12:  -1.0811                                     
REMARK   3      L13:  -2.3015 L23:   3.0835                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0138 S12:  -0.7168 S13:  -0.4035                       
REMARK   3      S21:   0.4044 S22:  -0.0681 S23:   0.3276                       
REMARK   3      S31:   0.2460 S32:   0.4220 S33:   0.0543                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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. THE ADPS OF THE ATOMS IN THE  PHOPHONO GROUP     
REMARK   3   OF SER 198 WERE REFINED SEPARATELY (AS ISOTROPIC) AND NOT          
REMARK   3   INCLUDED IN THE TLS REFINEMENT OF RESIDUES 71-233.                 
REMARK   4                                                                      
REMARK   4 2Y1K COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-DEC-10                   
REMARK 100 THE PDBE ID CODE IS EBI-46641                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
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) : 0.9765                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (QUANTUM 315R)                 
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   : 25339                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.50                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 4.8                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.8                               
REMARK 200  DATA REDUNDANCY                : 6.7                                
REMARK 200  R MERGE                    (I) : 0.09                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 26.00                              
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     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.0                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.40                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 4.80                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
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   (%): 61.0                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M MES PH 6.5, 2.1 M AMMONIUM         
REMARK 280  SULFATE.                                                            
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       76.88500            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       76.88500            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       63.80000            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       76.88500            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       76.88500            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       63.80000            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       76.88500            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       76.88500            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       63.80000            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       76.88500            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       76.88500            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       63.80000            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       76.88500            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       76.88500            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       63.80000            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       76.88500            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       76.88500            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       63.80000            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       76.88500            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       76.88500            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       63.80000            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       76.88500            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       76.88500            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       63.80000            
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: OCTAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 51750 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 155080 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -515.6 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      127.60000            
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      127.60000            
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      127.60000            
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      127.60000            
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 465     ASP A   379                                                      
REMARK 465     GLN A   380                                                      
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     ASP A  54    CG   OD1  OD2                                       
REMARK 470     TYR A 282    CG   CD1  CD2  CE1  CE2  CZ   OH                    
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 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ASP A   391     O    HOH A  2144              1.52            
REMARK 500   O    TRP A   522     O    HOH A  2214              1.66            
REMARK 500   N    ASP A   395     O    HOH A  2144              1.82            
REMARK 500   O4   NAG A  1536     O5   NAG A  1538              1.86            
REMARK 500   O    LEU A   514     O    HOH A  2210              1.89            
REMARK 500   O    TYR A   500     O    HOH A  2199              1.89            
REMARK 500   NH1  ARG A   347     O    HOH A  2129              1.93            
REMARK 500   O    ILE A   510     O    HOH A  2204              1.96            
REMARK 500   CB   ALA A   475     O    HOH A  2179              1.98            
REMARK 500   O4   NAG A  1536     C1   NAG A  1538              2.00            
REMARK 500   O    HOH A  2072     O    HOH A  2134              2.00            
REMARK 500   N    THR A   496     O    HOH A  2192              2.01            
REMARK 500   N    ARG A   381     O    HOH A  2138              2.01            
REMARK 500   C    TRP A   522     O    HOH A  2214              2.06            
REMARK 500   CG2  THR A   300     O    HOH A  2111              2.10            
REMARK 500   O    PRO A   157     O    HOH A  2078              2.14            
REMARK 500   NE2  GLN A   172     O    HOH A  2081              2.17            
REMARK 500  CL     CL A  1533     O    HOH A  2186              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  2089     O    HOH A  2091     7556     1.50            
REMARK 500   O    HOH A  2198     O    HOH A  2207     7556     2.11            
REMARK 500   O    HOH A  2204     O    HOH A  2208     7556     1.56            
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    ILE A   4       76.43   -159.39                                   
REMARK 500    PHE A  43      -14.89     88.73                                   
REMARK 500    THR A  50      -73.41    -23.26                                   
REMARK 500    LYS A  51      172.90    137.85                                   
REMARK 500    TRP A  52      136.33    169.20                                   
REMARK 500    ASP A  54      169.92     58.21                                   
REMARK 500    ALA A  58       65.06   -104.53                                   
REMARK 500    GLN A  67      142.23    169.34                                   
REMARK 500    SER A  89      145.30   -172.09                                   
REMARK 500    LYS A 103      123.42    -32.26                                   
REMARK 500    ASN A 106       52.46   -164.88                                   
REMARK 500    ALA A 162       80.80   -153.24                                   
REMARK 500    SEP A 198     -123.34     57.87                                   
REMARK 500    TYR A 237      -71.26    -56.51                                   
REMARK 500    PRO A 281      -95.16    -46.54                                   
REMARK 500    ASP A 297      -83.90   -141.65                                   
REMARK 500    VAL A 361       98.53     41.19                                   
REMARK 500    PHE A 398      -59.14   -123.06                                   
REMARK 500    LEU A 428      122.67    -39.39                                   
REMARK 500    PRO A 480       46.93    -94.49                                   
REMARK 500    ASN A 485       60.03   -100.23                                   
REMARK 500    ASN A 486       48.64     36.74                                   
REMARK 500    THR A 496      -77.99    111.80                                   
REMARK 500    GLU A 506     -115.96   -101.76                                   
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 LEU A  156     PRO A  157                 -148.97                    
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 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
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        13.5      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 CATALYTIC SERINE 198 IS PHOSPHORYLATED (SEP).                        
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 A1532  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2072   O                                                      
REMARK 620 2 HOH A2073   O   101.1                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1531                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA A1532                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1533                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A1534                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1535                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1540                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1541                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1542                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FU4 A1543                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1544                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1546                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1547                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1548                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FU4 A1549                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF                        
REMARK 800  SUGAR BOUND TO ASN A 341 RESIDUES 1536 TO 1539                      
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2XQK   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE                      
REMARK 900   INHIBITED BY PURE ENANTIOMER VX-(S)                                
REMARK 900 RELATED ID: 2WSL   RELATED DB: PDB                                   
REMARK 900  AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE                            
REMARK 900  INHIBITED BY TABUN ANALOGUE TA4                                     
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: 2XMB   RELATED DB: PDB                                   
REMARK 900  G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN                      
REMARK 900   COMPLEX WITH SULFATE                                               
REMARK 900 RELATED ID: 2XMG   RELATED DB: PDB                                   
REMARK 900  G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN                      
REMARK 900   COMPLEX WITH VX                                                    
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: 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: 2WIJ   RELATED DB: PDB                                   
REMARK 900  NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE                         
REMARK 900  INHIBITED BY TABUN ANALOGUE TA5                                     
REMARK 900 RELATED ID: 2XMD   RELATED DB: PDB                                   
REMARK 900  G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN                      
REMARK 900   COMPLEX WITH ECHOTHIOPHATE                                         
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: 2XQI   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE                      
REMARK 900   INHIBITED BY RACEMIC CVX                                           
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: 2XQJ   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE                      
REMARK 900   INHIBITED BY PURE ENANTIOMER VX-(R)                                
REMARK 900 RELATED ID: 1XLW   RELATED DB: PDB                                   
REMARK 900  DIETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (NONAGED                
REMARK 900  )OBTAINED BY REACTION WITH ECHOTHIOPHATE                            
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: 2XMC   RELATED DB: PDB                                   
REMARK 900  G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN                      
REMARK 900   COMPLEX WITH FLUORIDE ANION                                        
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: 2XQF   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE                      
REMARK 900   INHIBITED BY RACEMIC VX                                            
REMARK 900 RELATED ID: 2WIL   RELATED DB: PDB                                   
REMARK 900  AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE                            
REMARK 900  INHIBITED BY TABUN ANALOGUE TA5                                     
REMARK 900 RELATED ID: 2XQG   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE                      
REMARK 900   INHIBITED BY RACEMIC VR                                            
REMARK 900 RELATED ID: 2WIF   RELATED DB: PDB                                   
REMARK 900  AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE                            
REMARK 900  INHIBITED BY TABUN ANALOGUE TA1                                     
REMARK 900 RELATED ID: 1P0I   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN BUTYRYL                                  
REMARK 900  CHOLINESTERASE                                                      
REMARK 900 RELATED ID: 2WIG   RELATED DB: PDB                                   
REMARK 900  NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE                         
REMARK 900  INHIBITED BY TABUN ANALOGUE TA4                                     
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 RESIDUE NUMBERING IS FOR THE MATURE PROTEIN SEQUENCE.                
DBREF  2Y1K A    1   529  UNP    P06276   CHLE_HUMAN      29    557             
SEQADV 2Y1K GLN A   17  UNP  P06276    ASN    45 ENGINEERED MUTATION            
SEQADV 2Y1K GLN A  455  UNP  P06276    ASN   483 ENGINEERED MUTATION            
SEQADV 2Y1K 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  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 SEP 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                          
MODRES 2Y1K SEP A  198  SER  PHOSPHOSERINE                                      
HET    SEP  A 198      10                                                       
HET    SO4  A1531       5                                                       
HET     NA  A1532       1                                                       
HET     CL  A1533       1                                                       
HET    GOL  A1534       6                                                       
HET    SO4  A1535       5                                                       
HET    NAG  A1536      14                                                       
HET    FUC  A1539      10                                                       
HET    SO4  A1537       5                                                       
HET    NAG  A1538      14                                                       
HET    SO4  A1540       5                                                       
HET    SO4  A1541       5                                                       
HET    NAG  A1542      14                                                       
HET    FU4  A1543      10                                                       
HET    NAG  A1544      14                                                       
HET    NAG  A1545      14                                                       
HET    NAG  A1546      14                                                       
HET    NAG  A1547      14                                                       
HET    NAG  A1548      14                                                       
HET    FU4  A1549      10                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     SO4 SULFATE ION                                                      
HETNAM      NA SODIUM ION                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     FU4 2,6-ANHYDRO-1-DEOXY-D-GALACTITOL                                 
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     GOL GLYCERIN                                                         
FORMUL   1  SEP    C3 H8 N O6 P                                                 
FORMUL   2  SO4    5(O4 S 2-)                                                   
FORMUL   3   NA    NA 1+                                                        
FORMUL   4   CL    CL 1-                                                        
FORMUL   5  GOL    C3 H8 O3                                                     
FORMUL   6  NAG    8(C8 H15 N O6)                                               
FORMUL   7  FUC    C6 H12 O5                                                    
FORMUL   8  FU4    2(C6 H12 O4)                                                 
FORMUL   9  HOH   *229(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 SEP 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  GLU A  276  1                                   9    
HELIX   13  13 ALA A  277  VAL A  280  5                                   4    
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  SER A  524  1                                  10    
HELIX   26  26 PHE A  525  VAL A  529  5                                   5    
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  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  2.06  
SSBOND   2 CYS A  252    CYS A  263                          1555   1555  2.07  
SSBOND   3 CYS A  400    CYS A  519                          1555   1555  2.10  
LINK         C   GLU A 197                 N   SEP A 198     1555   1555  1.34  
LINK         C   SEP A 198                 N   ALA A 199     1555   1555  1.35  
LINK         ND2 ASN A 341                 C1  NAG A1536     1555   1555  1.42  
LINK        NA    NA A1532                 O   HOH A2073     1555   5556  2.37  
LINK        NA    NA A1532                 O   HOH A2072     1555   5556  2.44  
LINK         O6  NAG A1536                 C1  FUC A1539     1555   1555  1.46  
CISPEP   1 ALA A  101    PRO A  102          0         1.44                     
CISPEP   2 GLY A  360    VAL A  361          0        24.46                     
SITE     1 AC1  2 ARG A 347  GLN A 351                                          
SITE     1 AC2  4 PHE A 521  PHE A 525  HOH A2072  HOH A2073                    
SITE     1 AC3  3 THR A 488  THR A 508  HOH A2186                               
SITE     1 AC4  5 LEU A  18  TYR A  61  TRP A  98  ASP A 129                    
SITE     2 AC4  5 LYS A 131                                                     
SITE     1 AC5  5 GLN A 316  GLY A 413  ASN A 414  ASN A 415                    
SITE     2 AC5  5 HOH A2121                                                     
SITE     1 AC6  7 LYS A 323  TYR A 420  ARG A 509  ARG A 515                    
SITE     2 AC6  7 SO4 A1541  HOH A2219  HOH A2220                               
SITE     1 AC7  7 ARG A 509  LEU A 514  ARG A 515  GLN A 518                    
SITE     2 AC7  7 SO4 A1540  HOH A2206  HOH A2220                               
SITE     1 AC8  5 ASN A 106  ASN A 188  LYS A 190  FU4 A1543                    
SITE     2 AC8  5 HOH A2221                                                     
SITE     1 AC9  5 ASN A 188  LYS A 190  SER A 191  NAG A1542                    
SITE     2 AC9  5 HOH A2223                                                     
SITE     1 BC1  3 ARG A  14  ASN A  57  HOH A2224                               
SITE     1 BC2  3 ARG A 465  GLU A 482  ASN A 485                               
SITE     1 BC3  2 ASN A 256  THR A 258                                          
SITE     1 BC4  4 TYR A 237  ASN A 241  ASN A 245  NAG A1548                    
SITE     1 BC5  4 LYS A 248  NAG A1547  FU4 A1549  HOH A2226                    
SITE     1 BC6  4 ASN A 245  PHE A 278  VAL A 280  NAG A1548                    
SITE     1 BC7  8 ARG A 242  LEU A 286  SER A 287  VAL A 288                    
SITE     2 BC7  8 SER A 338  ASN A 341  HOH A2217  HOH A2218                    
CRYST1  153.770  153.770  127.600  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      0.006503  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006503  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007837        0.00000                         
TER    4194      VAL A 529                                                      
MASTER      724    0   20   26   14    0   23    6 4597    1  192   41          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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