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LongText Report for: 2XQK-pdb

Name Class
2XQK-pdb
HEADER    HYDROLASE                               02-SEP-10   2XQK              
TITLE     X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY           
TITLE    2 PURE ENANTIOMER VX-(S)                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLINESTERASE;                                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 31-557;                                           
COMPND   5 SYNONYM: ACYLCHOLINE ACYLHYDROLASE, CHOLINE ESTERASE II,             
COMPND   6  BUTYRYLCHOLINE ESTERASE, PSEUDOCHOLINESTERASE;                      
COMPND   7 EC: 3.1.1.8;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: CHO K1;                                 
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGS                                       
KEYWDS    HYDROLASE, NERVE AGENT, BIOSCAVENGER                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.WANDHAMMER,E.CARLETTI,E.GILLON,P.MASSON,M.GOELDNER,D.NOORT,         
AUTHOR   2 F.NACHON                                                             
REVDAT   1   23-MAR-11 2XQK    0                                                
JRNL        AUTH   M.WANDHAMMER,E.CARLETTI,M.VANDERSCHANS,E.GILLON,Y.NICOLET,   
JRNL        AUTH 2 P.MASSON,M.GOELDNER,D.NOORT,F.NACHON                         
JRNL        TITL   STRUCTURAL STUDY OF THE COMPLEX STEREOSELECTIVITY OF HUMAN   
JRNL        TITL 2 BUTYRYLCHOLINESTERASE FOR THE NEUROTOXIC V-AGENTS            
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.53                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.55                          
REMARK   3   NUMBER OF REFLECTIONS             : 29176                          
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) : 0.15959                         
REMARK   3   R VALUE            (WORKING SET) : 0.15720                         
REMARK   3   FREE R VALUE                     : 0.21721                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1216                            
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) : 2.400                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.462                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2119                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.41                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.197                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 88                           
REMARK   3   BIN FREE R VALUE                    : 0.233                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4265                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 183                                     
REMARK   3   SOLVENT ATOMS            : 323                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.242                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.42                                                 
REMARK   3    B22 (A**2) : 1.42                                                 
REMARK   3    B33 (A**2) : -2.84                                                
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): 0.264         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.214         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.142         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.243        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.931                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4555 ; 0.022 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6209 ; 1.954 ; 1.979       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   547 ; 6.711 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   211 ;36.882 ;24.218       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   721 ;17.688 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;18.228 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   674 ; 0.136 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3486 ; 0.011 ; 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):  2661 ; 1.064 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4307 ; 1.928 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1894 ; 3.231 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1892 ; 5.060 ; 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  : 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): -22.6430 -28.7140 -45.3810              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3229 T22:   0.1979                                     
REMARK   3      T33:   0.4664 T12:  -0.0550                                     
REMARK   3      T13:  -0.1102 T23:  -0.0398                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1814 L22:   1.8630                                     
REMARK   3      L33:   1.8541 L12:  -0.1798                                     
REMARK   3      L13:   0.2277 L23:   0.2246                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0470 S12:   0.5564 S13:   0.0525                       
REMARK   3      S21:  -0.6936 S22:  -0.0040 S23:   0.1183                       
REMARK   3      S31:  -0.0914 S32:  -0.1534 S33:   0.0509                       
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   259                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.9010 -31.3510 -33.2410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1036 T22:   0.0545                                     
REMARK   3      T33:   0.4574 T12:  -0.0310                                     
REMARK   3      T13:  -0.0208 T23:  -0.0679                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9387 L22:   1.2737                                     
REMARK   3      L33:   1.7068 L12:   0.0588                                     
REMARK   3      L13:   0.2172 L23:   0.0919                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0297 S12:   0.1926 S13:  -0.0873                       
REMARK   3      S21:  -0.3142 S22:   0.0896 S23:  -0.0410                       
REMARK   3      S31:   0.0351 S32:   0.0473 S33:  -0.0599                       
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   260        A   323                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.1940 -37.4700 -28.8750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0977 T22:   0.0583                                     
REMARK   3      T33:   0.5087 T12:   0.0063                                     
REMARK   3      T13:  -0.0056 T23:  -0.0730                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2577 L22:   1.1107                                     
REMARK   3      L33:   1.4417 L12:  -0.0254                                     
REMARK   3      L13:   0.0416 L23:   0.2862                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0053 S12:   0.0820 S13:  -0.2626                       
REMARK   3      S21:  -0.1694 S22:   0.0800 S23:  -0.1697                       
REMARK   3      S31:   0.1925 S32:   0.1428 S33:  -0.0747                       
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   324        A   401                          
REMARK   3    ORIGIN FOR THE GROUP (A): -15.4190 -45.6100  -5.8740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1535 T22:   0.0780                                     
REMARK   3      T33:   0.4810 T12:  -0.0434                                     
REMARK   3      T13:  -0.1030 T23:   0.0138                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8256 L22:   2.0102                                     
REMARK   3      L33:   2.2991 L12:   0.2383                                     
REMARK   3      L13:   1.6405 L23:  -0.5970                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2257 S12:  -0.4146 S13:  -0.4456                       
REMARK   3      S21:   0.1837 S22:   0.0842 S23:  -0.0142                       
REMARK   3      S31:   0.3305 S32:  -0.2335 S33:  -0.3098                       
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   402        A   469                          
REMARK   3    ORIGIN FOR THE GROUP (A): -25.8710 -27.1870 -16.6370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0321 T22:   0.0800                                     
REMARK   3      T33:   0.4458 T12:   0.0043                                     
REMARK   3      T13:  -0.0337 T23:  -0.0464                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6482 L22:   1.7806                                     
REMARK   3      L33:   1.7461 L12:   0.5137                                     
REMARK   3      L13:   0.3753 L23:  -0.0801                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0114 S12:  -0.1410 S13:   0.0107                       
REMARK   3      S21:  -0.0238 S22:   0.0414 S23:   0.2409                       
REMARK   3      S31:  -0.0229 S32:  -0.3080 S33:  -0.0300                       
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   470        A   529                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.2470 -21.4310  -9.7760              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0821 T22:   0.1073                                     
REMARK   3      T33:   0.4520 T12:   0.0179                                     
REMARK   3      T13:  -0.0272 T23:  -0.0624                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4819 L22:   4.0841                                     
REMARK   3      L33:   1.8744 L12:  -0.0900                                     
REMARK   3      L13:   0.3078 L23:  -0.3826                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1228 S12:  -0.1399 S13:   0.2096                       
REMARK   3      S21:   0.3304 S22:   0.0779 S23:  -0.0734                       
REMARK   3      S31:  -0.2445 S32:  -0.1917 S33:   0.0449                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 2XQK COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-SEP-10.                  
REMARK 100 THE PDBE ID CODE IS EBI-45266.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-DEC-09                          
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                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.954                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CDD                                
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   : 30395                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.40                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.50                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 7.1                                
REMARK 200  R MERGE                    (I) : 0.07                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 9.90                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.9                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.45                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 5.30                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1P0I                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.8                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE 2.1 M,                  
REMARK 280  2-(N-MORPHOLINO)-ETHANESULFONIC ACID 0.1 M, PH 6.5, VAPOR           
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298.0K .                       
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       77.46000            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       77.46000            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       63.69500            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       77.46000            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       77.46000            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       63.69500            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       77.46000            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       77.46000            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       63.69500            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       77.46000            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       77.46000            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       63.69500            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       77.46000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       77.46000            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       63.69500            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       77.46000            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       77.46000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       63.69500            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       77.46000            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       77.46000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       63.69500            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       77.46000            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       77.46000            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       63.69500            
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: 43200 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 160820 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -255.9 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375  K     K A1538   LIES ON A SPECIAL POSITION.                         
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 400 ENGINEERED RESIDUE IN CHAIN A, ASN 514 TO GLN                        
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   ND2  ASN A   241     C1   NAG A  1546              2.08            
REMARK 500   OE2  GLU A   497     O    HOH A  2290              2.16            
REMARK 500   O6   NAG A  1542     O    HOH A  2321              2.15            
REMARK 500   O    HOH A  2114     O    HOH A  2266              2.18            
REMARK 500   O    HOH A  2139     O    HOH A  2142              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 255   CB    GLU A 255   CG      0.155                       
REMARK 500    GLU A 404   CG    GLU A 404   CD      0.091                       
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    ARG A 219   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    LEU A 370   CA  -  CB  -  CG  ANGL. DEV. =  17.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A  43       -2.93     80.55                                   
REMARK 500    LYS A  51      140.94    121.51                                   
REMARK 500    ASP A  54      179.74     55.98                                   
REMARK 500    ALA A  58       62.96   -102.44                                   
REMARK 500    CYS A  92       13.61   -140.18                                   
REMARK 500    LYS A 103      124.55    -24.71                                   
REMARK 500    ASN A 106       60.02   -156.10                                   
REMARK 500    PHE A 118       13.59     56.21                                   
REMARK 500    ALA A 162       72.12   -154.81                                   
REMARK 500    SER A 198     -124.68     63.07                                   
REMARK 500    ASP A 297      -77.51   -140.81                                   
REMARK 500    ASP A 324       57.25   -119.74                                   
REMARK 500    ASP A 379      156.44    -40.72                                   
REMARK 500    GLN A 380       57.58    -91.00                                   
REMARK 500    PHE A 398      -56.64   -125.26                                   
REMARK 500    THR A 496      -87.72     98.77                                   
REMARK 500    GLU A 506      -78.87    -79.90                                   
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    GLN A 380        24.7      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     FUC A 1541                                                       
REMARK 610     NAG A 1543                                                       
REMARK 610     NAG A 1545                                                       
REMARK 610     NAG A 1546                                                       
REMARK 610     NAG A 1547                                                       
REMARK 610     FUC A 1548                                                       
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                              CA A1534  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 443   OE1                                                    
REMARK 620 2 HOH A2246   O    69.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A1535  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2056   O                                                      
REMARK 620 2 GLU A  80   OE1  50.2                                              
REMARK 620 3 HOH A2059   O   117.4  82.5                                        
REMARK 620 4 HOH A2059   O    72.1 111.5  97.2                                  
REMARK 620 5 HOH A2055   O    95.2  53.4  81.0 164.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY A1531                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  VX A1530                 
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 SO4 A1533                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CA A1534                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  NA A1535                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1536                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1537                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC A1541                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1542                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1543                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1544                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1546                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A1547                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FUC A1548                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF                        
REMARK 800     SUGAR BOUND TO ASN A 341 RESIDUES 1539 TO 1540                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
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: 2XMG   RELATED DB: PDB                                   
REMARK 900  G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN                      
REMARK 900   COMPLEX WITH VX                                                    
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: 1KCJ   RELATED DB: PDB                                   
REMARK 900  MODEL OF (-)-COCAINE-BOUND (-)-COCAINE                              
REMARK 900  HYDROLASE COMPLEX                                                   
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: 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: 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: 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: 2WID   RELATED DB: PDB                                   
REMARK 900  AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE                            
REMARK 900  INHIBITED BY TABUN ANALOGUE TA1                                     
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: 2WIL   RELATED DB: PDB                                   
REMARK 900  AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE                            
REMARK 900  INHIBITED BY TABUN ANALOGUE TA5                                     
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 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: 2XQG   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE                      
REMARK 900   INHIBITED BY RACEMIC VR                                            
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: 2XQF   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE                      
REMARK 900   INHIBITED BY RACEMIC VX                                            
DBREF  2XQK A    3   529  UNP    P06276   CHLE_HUMAN      31    557             
SEQADV 2XQK GLN A   17  UNP  P06276    ASN    45 ENGINEERED MUTATION            
SEQADV 2XQK GLN A  455  UNP  P06276    ASN   483 ENGINEERED MUTATION            
SEQADV 2XQK GLN A  481  UNP  P06276    ASN   509 ENGINEERED MUTATION            
SEQADV 2XQK GLN A  486  UNP  P06276    ASN   514 ENGINEERED MUTATION            
SEQRES   1 A  527  ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL ARG GLY          
SEQRES   2 A  527  MET GLN LEU THR VAL PHE GLY GLY THR VAL THR ALA PHE          
SEQRES   3 A  527  LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY ARG LEU          
SEQRES   4 A  527  ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP SER ASP          
SEQRES   5 A  527  ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS CYS GLN          
SEQRES   6 A  527  ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY SER GLU          
SEQRES   7 A  527  MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP CYS LEU          
SEQRES   8 A  527  TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO LYS ASN          
SEQRES   9 A  527  ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY PHE GLN          
SEQRES  10 A  527  THR GLY THR SER SER LEU HIS VAL TYR ASP GLY LYS PHE          
SEQRES  11 A  527  LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER MET ASN          
SEQRES  12 A  527  TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU PRO GLY          
SEQRES  13 A  527  ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE ASP GLN          
SEQRES  14 A  527  GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE ALA ALA          
SEQRES  15 A  527  PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE GLY GLU          
SEQRES  16 A  527  SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU LEU SER          
SEQRES  17 A  527  PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE LEU GLN          
SEQRES  18 A  527  SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR SER LEU          
SEQRES  19 A  527  TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA LYS LEU          
SEQRES  20 A  527  THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE ILE LYS          
SEQRES  21 A  527  CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU LEU ASN          
SEQRES  22 A  527  GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU SER VAL          
SEQRES  23 A  527  ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU THR ASP          
SEQRES  24 A  527  MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE LYS LYS          
SEQRES  25 A  527  THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU GLY THR          
SEQRES  26 A  527  ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER LYS ASP          
SEQRES  27 A  527  ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN GLU GLY          
SEQRES  28 A  527  LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE GLY LYS          
SEQRES  29 A  527  GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL ASP ASP          
SEQRES  30 A  527  GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY ASP VAL          
SEQRES  31 A  527  VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU GLU PHE          
SEQRES  32 A  527  THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA PHE PHE          
SEQRES  33 A  527  TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO TRP PRO          
SEQRES  34 A  527  GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE GLU PHE          
SEQRES  35 A  527  VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP GLN TYR THR          
SEQRES  36 A  527  LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL LYS ARG          
SEQRES  37 A  527  TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO GLN GLU THR          
SEQRES  38 A  527  GLN ASN GLN SER THR SER TRP PRO VAL PHE LYS SER THR          
SEQRES  39 A  527  GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER THR ARG          
SEQRES  40 A  527  ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG PHE TRP          
SEQRES  41 A  527  THR SER PHE PHE PRO LYS VAL                                  
HET    GLY  A1531       5                                                       
HET     VX  A1530       6                                                       
HET    SO4  A1532       5                                                       
HET    SO4  A1533       5                                                       
HET     CA  A1534       1                                                       
HET     NA  A1535       1                                                       
HET     CL  A1536       1                                                       
HET     CL  A1537       1                                                       
HET      K  A1538       1                                                       
HET    NAG  A1539      14                                                       
HET    NAG  A1540      14                                                       
HET    FUC  A1541      10                                                       
HET    NAG  A1542      14                                                       
HET    NAG  A1543      14                                                       
HET    NAG  A1544      14                                                       
HET    NAG  A1545      14                                                       
HET    NAG  A1546      14                                                       
HET    NAG  A1547      14                                                       
HET    FUC  A1548      10                                                       
HET    UNX  A1549       1                                                       
HET    UNX  A1550       1                                                       
HET    UNX  A1551       1                                                       
HET    UNX  A1552       1                                                       
HET    UNX  A1553       1                                                       
HET    UNX  A1554       1                                                       
HET    UNX  A1555       1                                                       
HET    UNX  A1556       1                                                       
HET    UNX  A1557       1                                                       
HET    UNX  A1558       1                                                       
HET    UNX  A1559       1                                                       
HET    UNX  A1560       1                                                       
HET    UNX  A1561       1                                                       
HET    UNX  A1562       1                                                       
HET    UNX  A1563       1                                                       
HET    UNX  A1564       1                                                       
HET    UNX  A1565       1                                                       
HET    UNX  A1566       1                                                       
HET    UNX  A1567       1                                                       
HET    UNX  A1568       1                                                       
HET    UNX  A1569       1                                                       
HET    UNX  A1570       1                                                       
HET    UNX  A1571       1                                                       
HET    UNX  A1572       1                                                       
HET    UNX  A1573       1                                                       
HETNAM     GLY GLYCINE                                                          
HETNAM      VX O-ETHYLMETHYLPHOSPHONIC ACID ESTER GROUP                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CA CALCIUM ION                                                      
HETNAM      NA SODIUM ION                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM       K POTASSIUM ION                                                    
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     UNX UNKNOWN ATOM OR ION                                              
FORMUL   2  GLY    C2 H5 N O2                                                   
FORMUL   3   VX    C3 H9 O3 P                                                   
FORMUL   4  SO4    2(O4 S 2-)                                                   
FORMUL   5   CA    CA 2+                                                        
FORMUL   6   NA    NA 1+                                                        
FORMUL   7   CL    2(CL 1-)                                                     
FORMUL   8    K    K 1+                                                         
FORMUL   9  NAG    8(C8 H15 N O6)                                               
FORMUL  10  FUC    2(C6 H12 O5)                                                 
FORMUL  11  UNX    25(X)                                                        
FORMUL  12  HOH   *323(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 SER A  198  LEU A  208  1                                  11    
HELIX    9   9 SER A  210  PHE A  217  5                                   8    
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  PHE A  525  1                                  11    
HELIX   26  26 PHE A  526  VAL A  529  5                                   4    
SHEET    1  AA 3 ILE A   5  ALA A   7  0                                        
SHEET    2  AA 3 LYS A  12  ARG A  14 -1  O  VAL A  13   N  ILE A   6           
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  2.08  
SSBOND   2 CYS A  252    CYS A  263                          1555   1555  2.11  
SSBOND   3 CYS A  400    CYS A  519                          1555   1555  2.08  
LINK         ND2 ASN A 106                 C1  NAG A1542     1555   1555  1.45  
LINK         OG  SER A 198                 P1   VX A1530     1555   1555  1.73  
LINK         ND2 ASN A 341                 C1  NAG A1539     1555   1555  1.42  
LINK         ND2 ASN A 485                 C1  NAG A1544     1555   1555  1.44  
LINK        CA    CA A1534                 OE1 GLU A 443     1555   1555  3.19  
LINK        CA    CA A1534                 O   HOH A2246     1555   1555  2.54  
LINK        NA    NA A1535                 O   HOH A2056     1555   1555  3.10  
LINK        NA    NA A1535                 OE1 GLU A  80     1555   1555  2.80  
LINK        NA    NA A1535                 O   HOH A2059     1555   1555  2.53  
LINK        NA    NA A1535                 O   HOH A2059     1555  16444  2.33  
LINK        NA    NA A1535                 O   HOH A2055     1555   1555  2.89  
LINK         O4  NAG A1539                 C1  NAG A1540     1555   1555  1.43  
CISPEP   1 ALA A  101    PRO A  102          0         0.57                     
CISPEP   2 VAL A  377    ASP A  378          0       -20.43                     
SITE     1 AC1  4 LEU A  18  TRP A  98  ASP A 129  LYS A 131                    
SITE     1 AC2  7 GLY A 116  GLY A 117  SER A 198  ALA A 199                    
SITE     2 AC2  7 HIS A 438  HOH A2165  HOH A2318                               
SITE     1 AC3  4 GLN A 316  GLY A 413  ASN A 414  ASN A 415                    
SITE     1 AC4  3 HIS A 372  PHE A 521  PHE A 525                               
SITE     1 AC5  2 GLU A 443  HOH A2246                                          
SITE     1 AC6  3 GLU A  80  HOH A2055  HOH A2059                               
SITE     1 AC7  2 ARG A 347  GLN A 351                                          
SITE     1 AC8  2 THR A 512  HOH A2295                                          
SITE     1 AC9  3 SER A 338  NAG A1539  NAG A1540                               
SITE     1 BC1  5 ASN A 106  ASN A 188  LYS A 190  HOH A2320                    
SITE     2 BC1  5 HOH A2321                                                     
SITE     1 BC2  1 ASN A  57                                                     
SITE     1 BC3  2 ARG A 465  ASN A 485                                          
SITE     1 BC4  1 ASN A 256                                                     
SITE     1 BC5  7 TYR A 237  GLU A 238  ASN A 241  ASN A 245                    
SITE     2 BC5  7 PRO A 281  NAG A1547  FUC A1548                               
SITE     1 BC6  2 NAG A1546  FUC A1548                                          
SITE     1 BC7  7 ASN A 245  PHE A 278  VAL A 280  PRO A 281                    
SITE     2 BC7  7 NAG A1546  NAG A1547  HOH A2323                               
SITE     1 BC8  7 PHE A 337  SER A 338  ASN A 341  ASN A 342                    
SITE     2 BC8  7 FUC A1541  HOH A2195  HOH A2319                               
CRYST1  154.920  154.920  127.390  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      0.006455  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006455  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007850        0.00000                         
TER    4266      VAL A 529                                                      
MASTER      715    0   44   26   14    0   22    6 4771    1  166   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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