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LongText Report for: 4BBZ-pdb

Name Class
4BBZ-pdb
HEADER    HYDROLASE                               30-SEP-12   4BBZ              
TITLE     STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY CBDP ( 2-MIN    
TITLE    2 SOAK): CRESYL-PHOSPHOSERINE ADDUCT                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLINESTERASE;                                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 29-557;                         
COMPND   5 SYNONYM: ACYLCHOLINE ACYLHYDROLASE, BUTYRYLCHOLINE ESTERASE,         
COMPND   6  CHOLINE ESTERASE II, PSEUDOCHOLINESTERASE;                          
COMPND   7 EC: 3.1.1.8;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 OTHER_DETAILS: CRESYL-PHOSPHATE ADDUCT ON S198                       
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, ACETYLCHOLINESTERASE, NERVE TRANSMISSION, INHIBITION,      
KEYWDS   2 ALPHA-BETA HYDROLASE                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.CARLETTI,J.-P.COLLETIER,L.M.SCHOPFER,G.SANTONI,P.MASSON,            
AUTHOR   2 O.LOCKRIDGE,F.NACHON,M.WEIK                                          
REVDAT   1   06-FEB-13 4BBZ    0                                                
JRNL        AUTH   E.CARLETTI,J.-P.COLLETIER,L.M.SCHOPFER,G.SANTONI,P.MASSON,   
JRNL        AUTH 2 O.LOCKRIDGE,F.NACHON,M.WEIK                                  
JRNL        TITL   INHIBITION PATHWAYS OF THE POTENT ORGANOPHOSPHATE CBDP WITH  
JRNL        TITL 2 CHOLINESTERASES REVEALED BY X-RAY CRYSTALLOGRAPHIC           
JRNL        TITL 3 SNAPSHOTS AND MASS SPECTROMETRY                              
JRNL        REF    CHEM.RES.TOXICOL.                          2013              
JRNL        REFN                   ESSN 1520-5010                               
JRNL        PMID   23339663                                                     
JRNL        DOI    10.1021/TX3004505                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.1_1168)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 54.688                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.35                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.14                          
REMARK   3   NUMBER OF REFLECTIONS             : 21049                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1693                          
REMARK   3   R VALUE            (WORKING SET) : 0.1663                          
REMARK   3   FREE R VALUE                     : 0.2248                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1053                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 54.6988 -  5.3987    0.96     2602   137  0.1815 0.2212        
REMARK   3     2  5.3987 -  4.2856    0.98     2510   133  0.1454 0.1948        
REMARK   3     3  4.2856 -  3.7440    0.98     2503   131  0.1430 0.2186        
REMARK   3     4  3.7440 -  3.4018    0.98     2475   130  0.1545 0.2021        
REMARK   3     5  3.4018 -  3.1580    0.99     2464   130  0.1768 0.2329        
REMARK   3     6  3.1580 -  2.9718    0.99     2495   131  0.1853 0.2914        
REMARK   3     7  2.9718 -  2.8230    0.99     2477   131  0.1983 0.2715        
REMARK   3     8  2.8230 -  2.7001    0.99     2470   130  0.2015 0.2752        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.28             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.19            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           4534                                  
REMARK   3   ANGLE     :  1.269           6176                                  
REMARK   3   CHIRALITY :  0.088            674                                  
REMARK   3   PLANARITY :  0.004            775                                  
REMARK   3   DIHEDRAL  : 19.883           1681                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 3:316)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -14.7815 -32.1307 -35.3739              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2526 T22:   0.1341                                     
REMARK   3      T33:   0.1826 T12:  -0.0817                                     
REMARK   3      T13:  -0.0397 T23:  -0.1293                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7111 L22:   1.6131                                     
REMARK   3      L33:   2.5274 L12:   0.4409                                     
REMARK   3      L13:   0.1482 L23:   0.4177                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0536 S12:   0.3157 S13:  -0.2752                       
REMARK   3      S21:  -0.4094 S22:   0.1311 S23:  -0.0890                       
REMARK   3      S31:   0.1528 S32:   0.0362 S33:   0.0492                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 317:529)                           
REMARK   3    ORIGIN FOR THE GROUP (A): -19.4174 -31.9835 -10.8545              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1418 T22:   0.1915                                     
REMARK   3      T33:   0.1819 T12:  -0.0458                                     
REMARK   3      T13:  -0.0752 T23:  -0.0754                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2429 L22:   2.1013                                     
REMARK   3      L33:   2.2652 L12:   0.0125                                     
REMARK   3      L13:   0.4689 L23:  -0.2786                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0000 S12:  -0.4443 S13:  -0.1678                       
REMARK   3      S21:   0.1672 S22:   0.1314 S23:   0.0708                       
REMARK   3      S31:   0.1157 S32:  -0.3262 S33:   0.0746                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4BBZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-SEP-12.                  
REMARK 100 THE PDBE ID CODE IS EBI-54212.                                       
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        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9765                             
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   : 21049                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.70                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 54.70                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 10.1                               
REMARK 200  R MERGE                    (I) : 0.07                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 29.00                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 9.2                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.46                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 5.20                               
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   (%): 61                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM 2.1 M      
REMARK 280  AMMONIUM SULFATE, 0.1 M MES BUFFER PH 6.5.                          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z                                                 
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      11555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290      12555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290      13555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      14555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      15555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       77.34000            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       77.34000            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       63.49500            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       77.34000            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       77.34000            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       63.49500            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       77.34000            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       77.34000            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       63.49500            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       77.34000            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       77.34000            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       63.49500            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       77.34000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       77.34000            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       63.49500            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       77.34000            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       77.34000            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       63.49500            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       77.34000            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       77.34000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       63.49500            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       77.34000            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       77.34000            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       63.49500            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLU A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG A   40   CD                                                  
REMARK 480     GLU A  432   CD                                                  
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    57     C1   NAG A   540              1.44            
REMARK 500   ND2  ASN A   241     C1   NAG A   560              1.46            
REMARK 500   ND2  ASN A   341     C1   NAG A   570              1.44            
REMARK 500   ND2  ASN A   485     C2   NAG A   580              2.18            
REMARK 500   ND2  ASN A   485     C1   NAG A   580              1.44            
REMARK 500  UNK   UNX A   706    UNK   UNX A   709              1.83            
REMARK 500  UNK   UNX A   707    UNK   UNX A   709              2.00            
REMARK 500  UNK   UNX A   707    UNK   UNX A   710              2.10            
REMARK 500   O    HOH A  2071     O    HOH A  2090              2.15            
REMARK 500   O    HOH A  2072     O    HOH A  2090              2.11            
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   NH2  ARG A   509     O2   SO4 A   703     7555     2.19            
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    SER A 198   CA    SER A 198   CB      0.123                       
REMARK 500    SER A 198   CB    SER A 198   OG      0.257                       
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    SER A 198   CA  -  CB  -  OG  ANGL. DEV. =  16.9 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       -8.00     70.66                                   
REMARK 500    LYS A  45      157.47    -48.01                                   
REMARK 500    ASP A  54     -170.66     60.17                                   
REMARK 500    ASP A  87      134.88    -37.44                                   
REMARK 500    SER A  89      149.52   -173.49                                   
REMARK 500    LYS A 103      120.79    -34.63                                   
REMARK 500    ASN A 106       59.73   -144.99                                   
REMARK 500    ASN A 159      109.35    -48.10                                   
REMARK 500    ALA A 162       75.11   -161.37                                   
REMARK 500    SER A 198     -123.45     59.38                                   
REMARK 500    ASP A 297      -77.19   -136.33                                   
REMARK 500    ASP A 378       84.20     62.48                                   
REMARK 500    ASP A 379      -59.26   -138.42                                   
REMARK 500    PHE A 398      -62.93   -136.97                                   
REMARK 500    PRO A 480       48.97    -83.83                                   
REMARK 500    ASN A 485       62.71   -116.56                                   
REMARK 500    ASN A 486       46.83     39.62                                   
REMARK 500    THR A 496      -58.61     72.34                                   
REMARK 500    GLU A 506      -73.23    -93.13                                   
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        21.4      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG A 580                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A 713                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4OJ A1530                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG A 550 BOUND TO ASN A 106                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG A 590 BOUND TO ASN A 256                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF POLYSACCHARIDE         
REMARK 800   RESIDUES  540 TO  541                                              
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF POLYSACCHARIDE         
REMARK 800   RESIDUES  560 TO  562                                              
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF POLYSACCHARIDE         
REMARK 800   RESIDUES  570 TO  572                                              
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1EHO   RELATED DB: PDB                                   
REMARK 900  MODEL OF (-)-COCAINE-BOUND BCHE COMPLEX.                            
REMARK 900 RELATED ID: 1EHQ   RELATED DB: PDB                                   
REMARK 900  MODEL OF (+)-COCAINE-BOUND BCHE COMPLEX                             
REMARK 900 RELATED ID: 1KCJ   RELATED DB: PDB                                   
REMARK 900  MODEL OF (-)-COCAINE-BOUND (-)-COCAINE HYDROLASE COMPLEX            
REMARK 900 RELATED ID: 1P0I   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN BUTYRYL CHOLINESTERASE                   
REMARK 900 RELATED ID: 1P0M   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF HUMAN BUTYRYL CHOLINESTERASE                   
REMARK 900  INCOMPLEX WITH A CHOLINE MOLECULE                                   
REMARK 900 RELATED ID: 1P0P   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN                               
REMARK 900  BUTYRYLCHOLINESTERASE IN COMPLEX WITH THE SUBSTRATE                 
REMARK 900  ANALOGBUTYRYLTHIOCHOLINE                                            
REMARK 900 RELATED ID: 1P0Q   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN BUTYRYL                       
REMARK 900  CHOLINESTERASE                                                      
REMARK 900 RELATED ID: 1XLU   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF DI-ISOPROPYL-PHOSPHORO-FLUORIDATE (              
REMARK 900  DFP)INHIBITED BUTYRYLCHOLINESTERASE AFTER AGING                     
REMARK 900 RELATED ID: 1XLV   RELATED DB: PDB                                   
REMARK 900  ETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (AGED) OBTAINEDBY         
REMARK 900  REACTION WITH ECHOTHIOPHATE                                         
REMARK 900 RELATED ID: 1XLW   RELATED DB: PDB                                   
REMARK 900  DIETHYLPHOSPHORYLATED BUTYRYLCHOLINESTERASE (NONAGED)OBTAINED       
REMARK 900  BY REACTION WITH ECHOTHIOPHATE                                      
REMARK 900 RELATED ID: 2J4C   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH            
REMARK 900  10MM HGCL2                                                          
REMARK 900 RELATED ID: 2WID   RELATED DB: PDB                                   
REMARK 900  AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY               
REMARK 900  TABUN ANALOGUE TA1                                                  
REMARK 900 RELATED ID: 2WIF   RELATED DB: PDB                                   
REMARK 900  AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY               
REMARK 900  TABUN ANALOGUE TA1                                                  
REMARK 900 RELATED ID: 2WIG   RELATED DB: PDB                                   
REMARK 900  NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY            
REMARK 900  TABUN ANALOGUE TA4                                                  
REMARK 900 RELATED ID: 2WIJ   RELATED DB: PDB                                   
REMARK 900  NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY            
REMARK 900  TABUN ANALOGUE TA5                                                  
REMARK 900 RELATED ID: 2WIK   RELATED DB: PDB                                   
REMARK 900  NONAGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY            
REMARK 900  TABUN ANALOGUE TA6                                                  
REMARK 900 RELATED ID: 2WIL   RELATED DB: PDB                                   
REMARK 900  AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY               
REMARK 900  TABUN ANALOGUE TA5                                                  
REMARK 900 RELATED ID: 2WSL   RELATED DB: PDB                                   
REMARK 900  AGED FORM OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY               
REMARK 900  TABUN ANALOGUE TA4                                                  
REMARK 900 RELATED ID: 2XMB   RELATED DB: PDB                                   
REMARK 900  G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX              
REMARK 900  WITH SULFATE                                                        
REMARK 900 RELATED ID: 2XMC   RELATED DB: PDB                                   
REMARK 900  G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX              
REMARK 900  WITH FLUORIDE ANION                                                 
REMARK 900 RELATED ID: 2XMD   RELATED DB: PDB                                   
REMARK 900  G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX              
REMARK 900  WITH ECHOTHIOPHATE                                                  
REMARK 900 RELATED ID: 2XMG   RELATED DB: PDB                                   
REMARK 900  G117H MUTANT OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX              
REMARK 900  WITH VX                                                             
REMARK 900 RELATED ID: 2XQF   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED            
REMARK 900  BY RACEMIC VX                                                       
REMARK 900 RELATED ID: 2XQG   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED            
REMARK 900  BY RACEMIC VR                                                       
REMARK 900 RELATED ID: 2XQI   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED            
REMARK 900  BY RACEMIC CVX                                                      
REMARK 900 RELATED ID: 2XQJ   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED            
REMARK 900  BY PURE ENANTIOMER VX-(R)                                           
REMARK 900 RELATED ID: 2XQK   RELATED DB: PDB                                   
REMARK 900  X-RAY STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED            
REMARK 900  BY PURE ENANTIOMER VX-(S)                                           
REMARK 900 RELATED ID: 2Y1K   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY CBDP          
REMARK 900   (12H SOAK): PHOSPHOSERINE ADDUCT                                   
REMARK 900 RELATED ID: 4AQD   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF FULLY GLYCOSYLATED HUMAN                       
REMARK 900  BUTYRYLCHOLINESTERASE                                               
REMARK 900 RELATED ID: 4AXB   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN                               
REMARK 900  BUTYRYLCHOLINESTERASE IN COMPLEX WITH 2-PAM                         
REMARK 900 RELATED ID: 4B0O   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN                               
REMARK 900  BUTYRYLCHOLINESTERASE IN COMPLEX WITH BENZYL PYRIDINIUM-4           
REMARK 900  -METHYLTRICHLOROACETIMIDATE                                         
REMARK 900 RELATED ID: 4B0P   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF SOMAN-AGED HUMAN                               
REMARK 900  BUTYRYLCHOLINESTERASE IN COMPLEX WITH METHYL 2-(                    
REMARK 900  PENTAFLUOROBENZYLOXYIMINO)PYRIDINIUM                                
REMARK 900 RELATED ID: 4BC0   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY CBDP           
REMARK 900   (12-H SOAK): CRESYL-PHOSPHOSERINE ADDUCT                           
REMARK 900 RELATED ID: 4BC1   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY CBDP           
REMARK 900   (30-MIN SOAK): CRESYL-SALIGENIN-PHOSPHOSERINE ADDUCT               
DBREF  4BBZ A    1   529  UNP    P06276   CHLE_HUMAN      29    557             
SEQADV 4BBZ GLN A   17  UNP  P06276    ASN    45 ENGINEERED MUTATION            
SEQADV 4BBZ GLN A  455  UNP  P06276    ASN   483 ENGINEERED MUTATION            
SEQADV 4BBZ 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 SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU          
SEQRES  17 A  529  LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE          
SEQRES  18 A  529  LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR          
SEQRES  19 A  529  SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA          
SEQRES  20 A  529  LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE          
SEQRES  21 A  529  ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU          
SEQRES  22 A  529  LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU          
SEQRES  23 A  529  SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU          
SEQRES  24 A  529  THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE          
SEQRES  25 A  529  LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU          
SEQRES  26 A  529  GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER          
SEQRES  27 A  529  LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN          
SEQRES  28 A  529  GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE          
SEQRES  29 A  529  GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL          
SEQRES  30 A  529  ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY          
SEQRES  31 A  529  ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU          
SEQRES  32 A  529  GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA          
SEQRES  33 A  529  PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO          
SEQRES  34 A  529  TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE          
SEQRES  35 A  529  GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP GLN          
SEQRES  36 A  529  TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL          
SEQRES  37 A  529  LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO GLN          
SEQRES  38 A  529  GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS          
SEQRES  39 A  529  SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER          
SEQRES  40 A  529  THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG          
SEQRES  41 A  529  PHE TRP THR SER PHE PHE PRO LYS VAL                          
HET    NAG  A 540      14                                                       
HET    FUL  A 541      10                                                       
HET    NAG  A 550      14                                                       
HET    NAG  A 560      14                                                       
HET    NAG  A 561      14                                                       
HET    FUL  A 562      10                                                       
HET    NAG  A 570      14                                                       
HET    NAG  A 571      14                                                       
HET    FUL  A 572      10                                                       
HET    NAG  A 580      14                                                       
HET    NAG  A 590      14                                                       
HET    SO4  A 700       5                                                       
HET    SO4  A 701       5                                                       
HET    SO4  A 702       5                                                       
HET    SO4  A 703       5                                                       
HET    SO4  A 704       5                                                       
HET    UNX  A 705       1                                                       
HET    UNX  A 706       1                                                       
HET    UNX  A 707       1                                                       
HET    UNX  A 709       1                                                       
HET    UNX  A 710       1                                                       
HET    UNX  A 711       1                                                       
HET    UNX  A 712       1                                                       
HET     CL  A 713       1                                                       
HET    4OJ  A1530      11                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUL BETA-L-FUCOSE                                                    
HETNAM     SO4 SULFATE ION                                                      
HETNAM     UNX UNKNOWN ATOM OR ION                                              
HETNAM      CL CHLORIDE ION                                                     
HETNAM     4OJ (2-METHYLPHENYL) DIHYDROGEN PHOSPHATE                            
HETSYN     FUL 6-DEOXY-BETA-L-GALACTOSE                                         
HETSYN     4OJ O-CRESYL-PHOSPHATE                                               
FORMUL   2  NAG    8(C8 H15 N O6)                                               
FORMUL   3  FUL    3(C6 H12 O5)                                                 
FORMUL   4  SO4    5(O4 S 2-)                                                   
FORMUL   5  UNX    7(X)                                                         
FORMUL   6   CL    CL 1-                                                        
FORMUL   7  4OJ    C7 H9 O4 P                                                   
FORMUL   8  HOH   *139(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 GLY A  149  LEU A  154  1                                   6    
HELIX    6   6 ASN A  165  ILE A  182  1                                  18    
HELIX    7   7 ALA A  183  PHE A  185  5                                   3    
HELIX    8   8 SER A  198  SER A  210  1                                  13    
HELIX    9   9 PRO A  211  PHE A  217  5                                   7    
HELIX   10  10 SER A  235  THR A  250  1                                  16    
HELIX   11  11 ASN A  256  ASN A  266  1                                  11    
HELIX   12  12 ASP A  268  GLU A  276  1                                   9    
HELIX   13  13 ALA A  277  VAL A  279  5                                   3    
HELIX   14  14 MET A  302  LEU A  309  1                                   8    
HELIX   15  15 GLY A  326  VAL A  331  1                                   6    
HELIX   16  16 THR A  346  PHE A  358  1                                  13    
HELIX   17  17 SER A  362  THR A  374  1                                  13    
HELIX   18  18 GLU A  383  PHE A  398  1                                  16    
HELIX   19  19 PHE A  398  GLU A  411  1                                  14    
HELIX   20  20 PRO A  431  GLY A  435  5                                   5    
HELIX   21  21 GLU A  441  PHE A  446  1                                   6    
HELIX   22  22 GLY A  447  GLU A  451  5                                   5    
HELIX   23  23 THR A  457  GLY A  478  1                                  22    
HELIX   24  24 ARG A  515  PHE A  525  1                                  11    
HELIX   25  25 PHE A  526  VAL A  529  5                                   4    
SHEET    1  AA 3 ILE A   5  THR A   8  0                                        
SHEET    2  AA 3 GLY A  11  ARG A  14 -1  O  GLY A  11   N  THR A   8           
SHEET    3  AA 3 ILE A  55  ASN A  57  1  O  TRP A  56   N  ARG A  14           
SHEET    1  AB11 MET A  16  VAL A  20  0                                        
SHEET    2  AB11 GLY A  23  PRO A  32 -1  O  GLY A  23   N  VAL A  20           
SHEET    3  AB11 TYR A  94  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           
SHEET    1  AC 2 SER A  64  CYS A  65  0                                        
SHEET    2  AC 2 LEU A  88  SER A  89  1  N  SER A  89   O  SER A  64           
SSBOND   1 CYS A   65    CYS A   92                          1555   1555  2.04  
SSBOND   2 CYS A  252    CYS A  263                          1555   1555  2.04  
SSBOND   3 CYS A  400    CYS A  519                          1555   1555  2.04  
LINK         ND2 ASN A 106                 C1  NAG A 550     1555   1555  1.46  
LINK         OG  SER A 198                 P13 4OJ A1530     1555   1555  2.02  
LINK         ND2 ASN A 256                 C1  NAG A 590     1555   1555  1.44  
LINK         O6  NAG A 540                 C1  FUL A 541     1555   1555  1.44  
LINK         O4  NAG A 560                 C1  NAG A 561     1555   1555  1.46  
LINK         O6  NAG A 560                 C1  FUL A 562     1555   1555  1.44  
LINK         O6  NAG A 570                 C1  FUL A 572     1555   1555  1.45  
LINK         O4  NAG A 570                 C1  NAG A 571     1555   1555  1.45  
CISPEP   1 ALA A  101    PRO A  102          0         2.82                     
CISPEP   2 ASP A  378    ASP A  379          0       -16.83                     
CISPEP   3 ASP A  379    GLN A  380          0        -3.81                     
SITE     1 AC1  2 ARG A 465  ASN A 485                                          
SITE     1 AC2  4 GLN A 316  GLY A 413  ASN A 414  ASN A 415                    
SITE     1 AC3  5 LYS A 323  TYR A 420  ARG A 509  ARG A 515                    
SITE     2 AC3  5 SO4 A 703                                                     
SITE     1 AC4  2 ARG A 347  GLN A 351                                          
SITE     1 AC5  4 ARG A 509  LEU A 514  ARG A 515  SO4 A 701                    
SITE     1 AC6  2 THR A 488  THR A 508                                          
SITE     1 AC7  1 LYS A  45                                                     
SITE     1 AC8  7 GLY A 116  GLY A 117  SER A 198  TRP A 231                    
SITE     2 AC8  7 LEU A 286  VAL A 288  HIS A 438                               
SITE     1 AC9  3 ASN A 106  ASN A 188  LYS A 190                               
SITE     1 BC1  2 ASN A 256  THR A 258                                          
SITE     1 BC2  2 ARG A  14  ASN A  57                                          
SITE     1 BC3  4 ASN A 241  ASN A 245  LEU A 249  PHE A 278                    
SITE     1 BC4  4 SER A 338  ASN A 341  GLU A 349  HOH A2075                    
CRYST1  154.680  154.680  126.990  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      0.006465  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006465  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007875        0.00000                         
TER    4223      VAL A 529                                                      
MASTER      584    0   25   25   16    0   15    6 4547    1  192   41          
END                                                                             

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
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