Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 4AQD-pdb

Name Class
4AQD-pdb
HEADER    HYDROLASE                               16-APR-12   4AQD              
TITLE     CRYSTAL STRUCTURE OF FULLY GLYCOSYLATED HUMAN BUTYRYLCHOLINESTERASE   
CAVEAT     4AQD    NAG A 651 HAS WRONG CHIRALITY AT ATOM C1                     
CAVEAT     4AQD    NAG B 641 HAS WRONG CHIRALITY AT ATOM C1                     
CAVEAT     4AQD    NAG A 671 HAS WRONG CHIRALITY AT ATOM C1                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BUTYRYLCHOLINESTERASE;                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 27-557;                                           
COMPND   5 EC: 3.1.1.8;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: S2;                                     
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMT-BIP                                   
KEYWDS    HYDROLASE, ACETYLCHOLINESTERASE, EXPRESSION, HUPRINE, SERINE          
KEYWDS   2 HYDROLASE, CATALYTIC TRIAD, INSECT CELLS, GLYCOSYLATIONS             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.BRAZZOLOTTO,M.WANDHAMMER,C.RONCO,M.TROVASLET,L.JEAN,O.LOCKRIDGE,    
AUTHOR   2 P.Y.RENARD,F.NACHON                                                  
REVDAT   1   04-JUL-12 4AQD    0                                                
JRNL        AUTH   X.BRAZZOLOTTO,M.WANDHAMMER,C.RONCO,M.TROVASLET,L.JEAN,       
JRNL        AUTH 2 O.LOCKRIDGE,P.Y.RENARD,F.NACHON                              
JRNL        TITL   HUMAN BUTYRYLCHOLINESTERASE PRODUCED IN INSECT CELLS:        
JRNL        TITL 2 HUPRINE-BASED AFFINITY PURIFICATION, CRYSTAL STRUCTURE       
JRNL        REF    FEBS J.                                    2012              
JRNL        REFN                   ESSN 1742-4658                               
JRNL        DOI    10.1111/J.1742-4658.2012.08672.X                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.500                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.041                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.36                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.39                          
REMARK   3   NUMBER OF REFLECTIONS             : 46071                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1652                          
REMARK   3   R VALUE            (WORKING SET) : 0.1632                          
REMARK   3   FREE R VALUE                     : 0.2320                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1381                            
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 39.0453 -  5.3823    0.99     4716   145  0.1708 0.2153        
REMARK   3     2  5.3823 -  4.2738    1.00     4532   140  0.1366 0.1978        
REMARK   3     3  4.2738 -  3.7340    1.00     4533   140  0.1394 0.1991        
REMARK   3     4  3.7340 -  3.3928    1.00     4464   138  0.1637 0.2370        
REMARK   3     5  3.3928 -  3.1498    1.00     4439   138  0.1691 0.2790        
REMARK   3     6  3.1498 -  2.9641    1.00     4461   138  0.1636 0.2576        
REMARK   3     7  2.9641 -  2.8157    1.00     4412   136  0.1720 0.2477        
REMARK   3     8  2.8157 -  2.6932    1.00     4399   136  0.1862 0.2446        
REMARK   3     9  2.6932 -  2.5895    0.99     4426   137  0.2142 0.3217        
REMARK   3    10  2.5895 -  2.5002    0.98     4308   133  0.2453 0.3135        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.98                                          
REMARK   3   K_SOL              : 0.362                                         
REMARK   3   B_SOL              : 61.675                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.35             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.76            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 46.58                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.5507                                               
REMARK   3    B22 (A**2) : -5.2688                                              
REMARK   3    B33 (A**2) : 0.7181                                               
REMARK   3    B12 (A**2) : 0.0000                                               
REMARK   3    B13 (A**2) : 0.0000                                               
REMARK   3    B23 (A**2) : 0.0000                                               
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           9212                                  
REMARK   3   ANGLE     :  1.231          12488                                  
REMARK   3   CHIRALITY :  0.077           1386                                  
REMARK   3   PLANARITY :  0.005           1550                                  
REMARK   3   DIHEDRAL  : 22.726           3471                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 3:315)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -10.8838 -10.3045  -8.4504              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2550 T22:   0.2297                                     
REMARK   3      T33:   0.1640 T12:  -0.0305                                     
REMARK   3      T13:  -0.0073 T23:   0.0793                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8420 L22:   2.0559                                     
REMARK   3      L33:   1.7580 L12:  -0.1064                                     
REMARK   3      L13:  -0.3574 L23:   0.0401                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0176 S12:  -0.3549 S13:  -0.2566                       
REMARK   3      S21:   0.2116 S22:  -0.0029 S23:   0.0995                       
REMARK   3      S31:   0.2822 S32:   0.0970 S33:  -0.0173                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 316:529)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   4.2755   0.7050 -25.0057              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2518 T22:   0.1438                                     
REMARK   3      T33:   0.0841 T12:  -0.0554                                     
REMARK   3      T13:  -0.0240 T23:   0.0332                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3869 L22:   1.8759                                     
REMARK   3      L33:   2.4847 L12:  -0.5403                                     
REMARK   3      L13:  -0.7871 L23:   0.5015                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0004 S12:  -0.0652 S13:   0.0247                       
REMARK   3      S21:  -0.2249 S22:   0.0287 S23:  -0.2040                       
REMARK   3      S31:  -0.1154 S32:   0.3819 S33:  -0.0039                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 4:315)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -31.9127  25.0871 -37.2007              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2116 T22:   0.2144                                     
REMARK   3      T33:   0.2053 T12:   0.0130                                     
REMARK   3      T13:  -0.0229 T23:   0.0015                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2006 L22:   3.2124                                     
REMARK   3      L33:   2.4515 L12:   0.7362                                     
REMARK   3      L13:  -0.1416 L23:  -0.6667                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1855 S12:  -0.0179 S13:   0.1313                       
REMARK   3      S21:   0.2722 S22:   0.0193 S23:   0.5592                       
REMARK   3      S31:  -0.0716 S32:  -0.4262 S33:  -0.0881                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 316:529)                           
REMARK   3    ORIGIN FOR THE GROUP (A): -16.2567  37.8569 -51.8162              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5127 T22:   0.1228                                     
REMARK   3      T33:   0.2338 T12:  -0.0139                                     
REMARK   3      T13:  -0.0571 T23:   0.1000                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4876 L22:   1.7886                                     
REMARK   3      L33:   2.6521 L12:   0.5247                                     
REMARK   3      L13:  -0.4438 L23:  -0.3396                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0827 S12:   0.2510 S13:   0.4237                       
REMARK   3      S21:  -0.4997 S22:   0.0629 S23:   0.0607                       
REMARK   3      S31:  -0.7299 S32:   0.0650 S33:  -0.0501                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: A BETA-ALANINE WAS MODELED AT BOND        
REMARK   3   DISTANCE TO THE CATALYTIC SERINE. A PEAK OF ELECTRON DENSITY       
REMARK   3   CLOSE TO A PEAK OF ELECTRON DENSITY CLOSE TO TRP82 WAS MODELED     
REMARK   3   AS DUMMY ATOMS (RESIDUES UNX).                                     
REMARK   4                                                                      
REMARK   4 4AQD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-APR-12.                  
REMARK 100 THE PDBE ID CODE IS EBI-52078.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-MAY-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.4                                
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) : 0.97939                            
REMARK 200  MONOCHROMATOR                  : SILICON (1 1 1)                    
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   : 46071                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.50                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 6.1                                
REMARK 200  R MERGE                    (I) : 0.06                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 22.30                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.3                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.64                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.30                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX AUTOMR                                         
REMARK 200 STARTING MODEL: PDB ENTRY 1P0I                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.7                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM            
REMARK 280  20% PEG 3350, 0.2 M NH4OAC PH 7.4, AT 293 K                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
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       36.37500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.60000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.63000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      113.60000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.37500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.63000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 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 IN ADDITION APPLY THE FOLLOWING TO CHAINS: B                         
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000      -39.63000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000     -113.60000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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     ARG A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     GLU A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     ARG B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     GLU B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     ASP B     3                                                      
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     GLN A  380   CB   CG   CD   OE1                                  
REMARK 480     ARG A  453   CD   NE   CZ   NH1  NH2                             
REMARK 480     GLU A  506   CD   OE1  OE2                                       
REMARK 480     ILE B    4   O    CG1  CG2  CD1                                  
REMARK 480     LYS B   51   CB   CG   CD   CE   NZ                              
REMARK 480     SER B   53   CB   OG                                             
REMARK 480     ASP B   54   CB   CG   OD1  OD2                                  
REMARK 480     GLN B  484   CG   CD   OE1  NE2                                  
REMARK 480     ASN B  485   CB   CG   OD1  ND2                                  
REMARK 480     ASN B  486   CG   OD1  ND2                                       
REMARK 480     GLU B  506   CG   CD   OE1                                       
REMARK 480     SER B  507   CB   OG                                             
REMARK 480     ARG B  509   NE   CZ   NH1  NH2                                  
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    17     C2   NAG A   601              2.14            
REMARK 500   OG   SER A   198     C    BAL A   550              2.07            
REMARK 500   NH2B ARG A   465     O    HOH A  2129              2.17            
REMARK 500   OE1  GLU A   497     O    HOH A  2145              2.12            
REMARK 500   ND2  ASN B    17     C2   NAG B   601              1.64            
REMARK 500   ND2  ASN B    57     C2   NAG B   611              2.16            
REMARK 500   OG   SER B   198     C    BAL B   550              2.08            
REMARK 500   ND2  ASN B   241     C2   NAG B   631              2.11            
REMARK 500   O    ASN B   455     O1   EDO B  1534              2.13            
REMARK 500   O4   NAG A   651     X    UNX B  1548              1.94            
REMARK 500   X    UNX A  1542     X    UNX A  1544              2.04            
REMARK 500   X    UNX B  1542     X    UNX B  1544              1.80            
REMARK 500   X    UNX B  1543     X    UNX B  1545              2.16            
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      -13.39     76.55                                   
REMARK 500    THR A  50      -83.70    -75.56                                   
REMARK 500    ASP A  54     -150.46     59.93                                   
REMARK 500    ASN A 106       55.60   -160.24                                   
REMARK 500    ALA A 162       68.27   -161.18                                   
REMARK 500    SER A 198     -117.64     60.88                                   
REMARK 500    GLU A 255      -74.98    -45.84                                   
REMARK 500    ASP A 297      -72.74   -105.40                                   
REMARK 500    ASP A 324       60.43   -119.85                                   
REMARK 500    ARG A 381       90.99     24.40                                   
REMARK 500    PHE A 398      -61.89   -127.22                                   
REMARK 500    GLU A 482      -74.29   -109.91                                   
REMARK 500    ASN A 485      133.01     82.14                                   
REMARK 500    PHE B  43      -16.24     81.02                                   
REMARK 500    LYS B  51      153.18    -49.52                                   
REMARK 500    ASP B  54     -157.69    -75.39                                   
REMARK 500    ASN B 106       52.76   -155.55                                   
REMARK 500    ASP B 129      109.16    -57.38                                   
REMARK 500    ALA B 162       75.95   -161.39                                   
REMARK 500    SER B 198     -115.24     58.91                                   
REMARK 500    THR B 218      -55.66   -120.78                                   
REMARK 500    ASP B 297      -77.91   -127.68                                   
REMARK 500    ASP B 324       62.15   -118.71                                   
REMARK 500    TYR B 332       38.32    -99.92                                   
REMARK 500    SER B 338      142.03   -174.92                                   
REMARK 500    PHE B 398      -63.48   -128.98                                   
REMARK 500    ASN B 455     -154.43     66.35                                   
REMARK 500    TYR B 456      151.25     78.83                                   
REMARK 500    THR B 483     -142.98    -83.23                                   
REMARK 500    GLN B 484       95.44     51.65                                   
REMARK 500    ASN B 485      -20.07    -38.90                                   
REMARK 500    ASN B 486      -76.90    -65.61                                   
REMARK 500    SER B 487     -148.69     50.38                                   
REMARK 500    THR B 488        6.61   -170.29                                   
REMARK 500    SER B 489       97.42     54.98                                   
REMARK 500    GLU B 506       77.36   -101.37                                   
REMARK 500    SER B 507      112.16     75.56                                   
REMARK 500    PRO B 527        2.96    -61.95                                   
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 BAL A 550                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A1530                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A1531                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1532                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1533                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1534                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1535                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1536                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1537                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1538                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1539                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1540                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1546                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A1547                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY A1643                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BAL B 550                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1530                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG B1531                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1532                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1533                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1534                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1535                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1536                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1537                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1538                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1539                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1540                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1541                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1546                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL B1547                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLY B1642                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO         
REMARK 800   ASN A  17 RESIDUES  601 TO  602                                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO         
REMARK 800   ASN A  57 RESIDUES  611 TO  613                                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO         
REMARK 800   ASN A 106 RESIDUES  621 TO  622                                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO         
REMARK 800   ASN A 241 RESIDUES  631 TO  633                                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG A 651 BOUND TO ASN A 341                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO         
REMARK 800   ASN A 481 RESIDUES  671 TO  673                                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN A OF SUGAR BOUND TO         
REMARK 800   ASN A 486 RESIDUES  681 TO  683                                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG B 601 BOUND TO ASN B  17                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG B 611 BOUND TO ASN B  57                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG B 621 BOUND TO ASN B 106                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO         
REMARK 800   ASN B 241 RESIDUES  631 TO  633                                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO         
REMARK 800   ASN B 256 RESIDUES  641 TO  643                                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG B 651 BOUND TO ASN B 341                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN B OF SUGAR BOUND TO         
REMARK 800   ASN B 455 RESIDUES  661 TO  663                                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG B 671 BOUND TO ASN B 481                                       
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                                   
DBREF  4AQD A   -1   529  UNP    P06276   CHLE_HUMAN      27    557             
DBREF  4AQD B   -1   529  UNP    P06276   CHLE_HUMAN      27    557             
SEQRES   1 A  531  ARG SER GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY          
SEQRES   2 A  531  LYS VAL ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR          
SEQRES   3 A  531  VAL THR ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO          
SEQRES   4 A  531  LEU GLY ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR          
SEQRES   5 A  531  LYS TRP SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN          
SEQRES   6 A  531  SER CYS CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE          
SEQRES   7 A  531  HIS GLY SER GLU MET TRP ASN PRO ASN THR ASP LEU SER          
SEQRES   8 A  531  GLU ASP CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO          
SEQRES   9 A  531  LYS PRO LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY          
SEQRES  10 A  531  GLY GLY PHE GLN THR GLY THR SER SER LEU HIS VAL TYR          
SEQRES  11 A  531  ASP GLY LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL          
SEQRES  12 A  531  VAL SER MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU          
SEQRES  13 A  531  ALA LEU PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY          
SEQRES  14 A  531  LEU PHE ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS          
SEQRES  15 A  531  ASN ILE ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR          
SEQRES  16 A  531  LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU          
SEQRES  17 A  531  HIS LEU LEU SER PRO GLY SER HIS SER LEU PHE THR ARG          
SEQRES  18 A  531  ALA ILE LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA          
SEQRES  19 A  531  VAL THR SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN          
SEQRES  20 A  531  LEU ALA LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR          
SEQRES  21 A  531  GLU ILE ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU          
SEQRES  22 A  531  ILE LEU LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR          
SEQRES  23 A  531  PRO LEU SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP          
SEQRES  24 A  531  PHE LEU THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY          
SEQRES  25 A  531  GLN PHE LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS          
SEQRES  26 A  531  ASP GLU GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY          
SEQRES  27 A  531  PHE SER LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU          
SEQRES  28 A  531  PHE GLN GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER          
SEQRES  29 A  531  GLU PHE GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP          
SEQRES  30 A  531  TRP VAL ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA          
SEQRES  31 A  531  LEU GLY ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO          
SEQRES  32 A  531  ALA LEU GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN          
SEQRES  33 A  531  ASN ALA PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS          
SEQRES  34 A  531  LEU PRO TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR          
SEQRES  35 A  531  GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG          
SEQRES  36 A  531  ASP ASN TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER          
SEQRES  37 A  531  ILE VAL LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN          
SEQRES  38 A  531  PRO ASN GLU THR GLN ASN ASN SER THR SER TRP PRO VAL          
SEQRES  39 A  531  PHE LYS SER THR GLU GLN LYS TYR LEU THR LEU ASN THR          
SEQRES  40 A  531  GLU SER THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN          
SEQRES  41 A  531  CYS ARG PHE TRP THR SER PHE PHE PRO LYS VAL                  
SEQRES   1 B  531  ARG SER GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY          
SEQRES   2 B  531  LYS VAL ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR          
SEQRES   3 B  531  VAL THR ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO          
SEQRES   4 B  531  LEU GLY ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR          
SEQRES   5 B  531  LYS TRP SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN          
SEQRES   6 B  531  SER CYS CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE          
SEQRES   7 B  531  HIS GLY SER GLU MET TRP ASN PRO ASN THR ASP LEU SER          
SEQRES   8 B  531  GLU ASP CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO          
SEQRES   9 B  531  LYS PRO LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY          
SEQRES  10 B  531  GLY GLY PHE GLN THR GLY THR SER SER LEU HIS VAL TYR          
SEQRES  11 B  531  ASP GLY LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL          
SEQRES  12 B  531  VAL SER MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU          
SEQRES  13 B  531  ALA LEU PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY          
SEQRES  14 B  531  LEU PHE ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS          
SEQRES  15 B  531  ASN ILE ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR          
SEQRES  16 B  531  LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU          
SEQRES  17 B  531  HIS LEU LEU SER PRO GLY SER HIS SER LEU PHE THR ARG          
SEQRES  18 B  531  ALA ILE LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA          
SEQRES  19 B  531  VAL THR SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN          
SEQRES  20 B  531  LEU ALA LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR          
SEQRES  21 B  531  GLU ILE ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU          
SEQRES  22 B  531  ILE LEU LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR          
SEQRES  23 B  531  PRO LEU SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP          
SEQRES  24 B  531  PHE LEU THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY          
SEQRES  25 B  531  GLN PHE LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS          
SEQRES  26 B  531  ASP GLU GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY          
SEQRES  27 B  531  PHE SER LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU          
SEQRES  28 B  531  PHE GLN GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER          
SEQRES  29 B  531  GLU PHE GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP          
SEQRES  30 B  531  TRP VAL ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA          
SEQRES  31 B  531  LEU GLY ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO          
SEQRES  32 B  531  ALA LEU GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN          
SEQRES  33 B  531  ASN ALA PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS          
SEQRES  34 B  531  LEU PRO TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR          
SEQRES  35 B  531  GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG          
SEQRES  36 B  531  ASP ASN TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER          
SEQRES  37 B  531  ILE VAL LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN          
SEQRES  38 B  531  PRO ASN GLU THR GLN ASN ASN SER THR SER TRP PRO VAL          
SEQRES  39 B  531  PHE LYS SER THR GLU GLN LYS TYR LEU THR LEU ASN THR          
SEQRES  40 B  531  GLU SER THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN          
SEQRES  41 B  531  CYS ARG PHE TRP THR SER PHE PHE PRO LYS VAL                  
HET    BAL  A 550       6                                                       
HET    NAG  A 601      14                                                       
HET    NAG  A 602      14                                                       
HET    NAG  A 611      14                                                       
HET    NAG  A 612      14                                                       
HET    FUL  A 613      10                                                       
HET    NAG  A 621      14                                                       
HET    NAG  A 622      14                                                       
HET    NAG  A 631      14                                                       
HET    NAG  A 632      14                                                       
HET    FUL  A 633      10                                                       
HET    NAG  A 651      14                                                       
HET    NAG  A 671      14                                                       
HET    NAG  A 672      14                                                       
HET    MAN  A 673      11                                                       
HET    NAG  A 681      14                                                       
HET    NAG  A 682      14                                                       
HET    FUL  A 683      10                                                       
HET    PG4  A1530      13                                                       
HET    PG4  A1531      13                                                       
HET    EDO  A1532       4                                                       
HET    EDO  A1533       4                                                       
HET    EDO  A1534       4                                                       
HET    EDO  A1535       4                                                       
HET    EDO  A1536       4                                                       
HET    EDO  A1537       4                                                       
HET    EDO  A1538       4                                                       
HET    EDO  A1539       4                                                       
HET    EDO  A1540       4                                                       
HET     CL  A1545       1                                                       
HET     CL  A1546       1                                                       
HET     CL  A1547       1                                                       
HET    GLY  A1643       5                                                       
HET    BAL  B 550       6                                                       
HET    NAG  B 601      14                                                       
HET    NAG  B 611      14                                                       
HET    NAG  B 621      14                                                       
HET    NAG  B 631      14                                                       
HET    NAG  B 632      14                                                       
HET    FUL  B 633      10                                                       
HET    NAG  B 641      14                                                       
HET    NAG  B 642      14                                                       
HET    FUL  B 643      10                                                       
HET    NAG  B 651      14                                                       
HET    NAG  B 661      14                                                       
HET    NAG  B 662      14                                                       
HET    FUL  B 663      10                                                       
HET    NAG  B 671      14                                                       
HET    PEG  B1530       7                                                       
HET    PEG  B1531       7                                                       
HET    EDO  B1532       4                                                       
HET    EDO  B1533       4                                                       
HET    EDO  B1534       4                                                       
HET    EDO  B1535       4                                                       
HET    EDO  B1536       4                                                       
HET    EDO  B1537       4                                                       
HET    EDO  B1538       4                                                       
HET    EDO  B1539       4                                                       
HET    EDO  B1540       4                                                       
HET    EDO  B1541       4                                                       
HET     CL  B1546       1                                                       
HET     CL  B1547       1                                                       
HET     CL  B1549       1                                                       
HET     CL  B1550       1                                                       
HET    GLY  B1642       5                                                       
HET    UNX  A1541                                                               
HET    UNX  A1542                                                               
HET    UNX  A1543                                                               
HET    UNX  A1544                                                               
HET    UNX  A1548                                                               
HET    UNX  B1542                                                               
HET    UNX  B1543                                                               
HET    UNX  B1544                                                               
HET    UNX  B1545                                                               
HET    UNX  B1548                                                               
HETNAM     BAL BETA-ALANINE                                                     
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUL BETA-L-FUCOSE                                                    
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     UNX UNKNOWN ATOM OR ION                                              
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GLY GLYCINE                                                          
HETSYN     FUL 6-DEOXY-BETA-L-GALACTOSE                                         
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  BAL    2(C3 H7 N O2)                                                
FORMUL   3  NAG    24(C8 H15 N O6)                                              
FORMUL   4  FUL    6(C6 H12 O5)                                                 
FORMUL   5  MAN    C6 H12 O6                                                    
FORMUL   6  PG4    2(C8 H18 O5)                                                 
FORMUL   7  EDO    19(C2 H6 O2)                                                 
FORMUL   9   CL    7(CL 1-)                                                     
FORMUL  10  PEG    2(C4 H10 O3)                                                 
FORMUL  11  UNX    10(X)                                                        
FORMUL  12  GLY    2(C2 H5 N O2)                                                
FORMUL  13  HOH   *278(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  SER A  210  1                                  13    
HELIX    9   9 SER A  235  THR A  250  1                                  16    
HELIX   10  10 ASN A  256  ARG A  265  1                                  10    
HELIX   11  11 ASP A  268  LEU A  274  1                                   7    
HELIX   12  12 ASN A  275  VAL A  279  5                                   5    
HELIX   13  13 MET A  302  LEU A  309  1                                   8    
HELIX   14  14 GLY A  326  VAL A  331  1                                   6    
HELIX   15  15 THR A  346  PHE A  358  1                                  13    
HELIX   16  16 SER A  362  TYR A  373  1                                  12    
HELIX   17  17 GLU A  383  PHE A  398  1                                  16    
HELIX   18  18 PHE A  398  GLU A  411  1                                  14    
HELIX   19  19 PRO A  431  GLY A  435  5                                   5    
HELIX   20  20 GLU A  441  PHE A  446  1                                   6    
HELIX   21  21 GLY A  447  GLU A  451  5                                   5    
HELIX   22  22 GLU A  451  ASN A  455  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    
HELIX   26  26 LEU B   38  ARG B   42  5                                   5    
HELIX   27  27 PHE B   76  MET B   81  1                                   6    
HELIX   28  28 LEU B  125  ASP B  129  5                                   5    
HELIX   29  29 GLY B  130  ARG B  138  1                                   9    
HELIX   30  30 VAL B  148  LEU B  154  1                                   7    
HELIX   31  31 ASN B  165  ILE B  182  1                                  18    
HELIX   32  32 ALA B  183  PHE B  185  5                                   3    
HELIX   33  33 SER B  198  LEU B  208  1                                  11    
HELIX   34  34 SER B  210  PHE B  217  5                                   8    
HELIX   35  35 SER B  235  THR B  250  1                                  16    
HELIX   36  36 ASN B  256  LYS B  267  1                                  12    
HELIX   37  37 ASP B  268  LEU B  274  1                                   7    
HELIX   38  38 ASN B  275  VAL B  279  5                                   5    
HELIX   39  39 MET B  302  GLY B  310  1                                   9    
HELIX   40  40 GLY B  326  VAL B  331  1                                   6    
HELIX   41  41 THR B  346  PHE B  358  1                                  13    
HELIX   42  42 SER B  362  TYR B  373  1                                  12    
HELIX   43  43 GLU B  383  PHE B  398  1                                  16    
HELIX   44  44 PHE B  398  GLU B  411  1                                  14    
HELIX   45  45 PRO B  431  GLY B  435  5                                   5    
HELIX   46  46 GLU B  441  PHE B  446  1                                   6    
HELIX   47  47 GLY B  447  GLU B  451  5                                   5    
HELIX   48  48 THR B  457  GLY B  478  1                                  22    
HELIX   49  49 ARG B  515  PHE B  525  1                                  11    
HELIX   50  50 PHE B  526  VAL B  529  5                                   4    
SHEET    1  AA 3 ILE A   5  THR A   8  0                                        
SHEET    2  AA 3 GLY A  11  ARG A  14 -1  O  GLY A  11   N  THR A   8           
SHEET    3  AA 3 TRP A  56  ASN A  57  1  O  TRP A  56   N  ARG A  14           
SHEET    1  AB11 MET A  16  VAL A  20  0                                        
SHEET    2  AB11 GLY A  23  PRO A  32 -1  O  GLY A  23   N  VAL A  20           
SHEET    3  AB11 TYR A  94  PRO A 100 -1  O  LEU A  95   N  ILE A  31           
SHEET    4  AB11 ILE A 140  MET A 144 -1  O  VAL A 141   N  TRP A  98           
SHEET    5  AB11 ALA A 107  ILE A 113  1  O  THR A 108   N  ILE A 140           
SHEET    6  AB11 GLY A 187  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           
SHEET    1  BA 3 ILE B   5  ALA B   7  0                                        
SHEET    2  BA 3 LYS B  12  ARG B  14 -1  O  VAL B  13   N  ILE B   6           
SHEET    3  BA 3 TRP B  56  ASN B  57  1  O  TRP B  56   N  ARG B  14           
SHEET    1  BB11 MET B  16  VAL B  20  0                                        
SHEET    2  BB11 GLY B  23  PRO B  32 -1  O  GLY B  23   N  VAL B  20           
SHEET    3  BB11 TYR B  94  PRO B 100 -1  O  LEU B  95   N  ILE B  31           
SHEET    4  BB11 ILE B 140  MET B 144 -1  O  VAL B 141   N  TRP B  98           
SHEET    5  BB11 ALA B 107  ILE B 113  1  O  THR B 108   N  ILE B 140           
SHEET    6  BB11 GLY B 187  GLU B 197  1  N  ASN B 188   O  ALA B 107           
SHEET    7  BB11 ARG B 219  GLN B 223  1  O  ARG B 219   N  LEU B 194           
SHEET    8  BB11 ILE B 317  ASN B 322  1  O  LEU B 318   N  LEU B 222           
SHEET    9  BB11 ALA B 416  PHE B 421  1  O  PHE B 417   N  VAL B 319           
SHEET   10  BB11 LYS B 499  LEU B 503  1  O  LEU B 501   N  TYR B 420           
SHEET   11  BB11 ILE B 510  THR B 512 -1  O  MET B 511   N  TYR B 500           
SHEET    1  BC 2 SER B  64  CYS B  65  0                                        
SHEET    2  BC 2 LEU B  88  SER B  89  1  N  SER B  89   O  SER B  64           
SSBOND   1 CYS A   65    CYS A   92                          1555   1555  2.04  
SSBOND   2 CYS A  252    CYS A  263                          1555   1555  2.06  
SSBOND   3 CYS A  400    CYS A  519                          1555   1555  2.07  
SSBOND   4 CYS B   65    CYS B   92                          1555   1555  2.05  
SSBOND   5 CYS B  252    CYS B  263                          1555   1555  2.06  
SSBOND   6 CYS B  400    CYS B  519                          1555   1555  2.06  
LINK         ND2 ASN A  17                 C1  NAG A 601     1555   1555  1.45  
LINK         ND2 ASN A  57                 C1  NAG A 611     1555   1555  1.45  
LINK         ND2 ASN A 106                 C1  NAG A 621     1555   1555  1.44  
LINK         ND2 ASN A 241                 C1  NAG A 631     1555   1555  1.44  
LINK         ND2 ASN A 341                 C1  NAG A 651     1555   1555  1.44  
LINK         ND2 ASN A 481                 C1  NAG A 671     1555   1555  1.45  
LINK         ND2 ASN A 486                 C1  NAG A 681     1555   1555  1.44  
LINK         O4  NAG A 601                 C1  NAG A 602     1555   1555  1.45  
LINK         O6  NAG A 611                 C1  FUL A 613     1555   1555  1.44  
LINK         O4  NAG A 611                 C1  NAG A 612     1555   1555  1.45  
LINK         O4  NAG A 621                 C1  NAG A 622     1555   1555  1.46  
LINK         O6  NAG A 631                 C1  FUL A 633     1555   1555  1.45  
LINK         O4  NAG A 631                 C1  NAG A 632     1555   1555  1.45  
LINK         O4  NAG A 671                 C1  NAG A 672     1555   1555  1.44  
LINK         O4  NAG A 672                 C1  MAN A 673     1555   1555  1.45  
LINK         O6  NAG A 681                 C1  FUL A 683     1555   1555  1.44  
LINK         O4  NAG A 681                 C1  NAG A 682     1555   1555  1.45  
LINK         ND2 ASN B  17                 C1  NAG B 601     1555   1555  1.45  
LINK         ND2 ASN B  57                 C1  NAG B 611     1555   1555  1.44  
LINK         ND2 ASN B 106                 C1  NAG B 621     1555   1555  1.45  
LINK         ND2 ASN B 241                 C1  NAG B 631     1555   1555  1.45  
LINK         ND2 ASN B 256                 C1  NAG B 641     1555   1555  1.45  
LINK         ND2 ASN B 341                 C1  NAG B 651     1555   1555  1.46  
LINK         ND2 ASN B 455                 C1  NAG B 661     1555   1555  1.47  
LINK         ND2 ASN B 481                 C1  NAG B 671     1555   1555  1.45  
LINK         O6  NAG B 631                 C1  FUL B 633     1555   1555  1.45  
LINK         O4  NAG B 631                 C1  NAG B 632     1555   1555  1.44  
LINK         O6  NAG B 641                 C1  FUL B 643     1555   1555  1.43  
LINK         O4  NAG B 641                 C1  NAG B 642     1555   1555  1.44  
LINK         O6  NAG B 661                 C1  FUL B 663     1555   1555  1.46  
LINK         O4  NAG B 661                 C1  NAG B 662     1555   1555  1.45  
CISPEP   1 ALA A  101    PRO A  102          0        -0.57                     
CISPEP   2 ASP A  379    GLN A  380          0        -3.65                     
CISPEP   3 ALA B  101    PRO B  102          0        -0.70                     
SITE     1 AC1  6 GLY A 116  GLY A 117  SER A 198  ALA A 199                    
SITE     2 AC1  6 HIS A 438  HOH A2156                                          
SITE     1 AC2  2 ASN A 455  NAG A 602                                          
SITE     1 AC3  7 LEU A 307  GLU A 308  LYS A 408  GLU A 411                    
SITE     2 AC3  7 TRP A 412  LYS B 248  GLY B 251                               
SITE     1 AC4  3 CYS A 400  PRO A 401  THR A 523                               
SITE     1 AC5  4 PHE A  21  LEU A 450  GLU A 451  ARG A 452                    
SITE     1 AC6  3 HIS A  77  LYS A 427  GLU A 443                               
SITE     1 AC7  2 LYS A 494  THR A 496                                          
SITE     1 AC8  4 HIS A 423  ASN A 504  THR A 505  HOH A2123                    
SITE     1 AC9  4 ASN A 479  TRP A 490  HOH A2137  GLN B  71                    
SITE     1 BC1  7 LEU A  29  GLY A  30  TRP A  56  ASN A  57                    
SITE     2 BC1  7 LYS A  60  ALA A  62  HOH A2021                               
SITE     1 BC2  3 GLY A 116  THR A 120  HOH A2156                               
SITE     1 BC3  4 TYR A  33  SER A  48  LEU A  49  LYS A 180                    
SITE     1 BC4  1 ARG A 465                                                     
SITE     1 BC5  4 ARG A 470  ASN A 481  SER A 489  TRP A 490                    
SITE     1 BC6  1 ARG A 386                                                     
SITE     1 BC7  5 LEU A  18  TYR A  61  TRP A  98  ASP A 129                    
SITE     2 BC7  5 LYS A 131                                                     
SITE     1 BC8  6 GLY B 116  GLY B 117  SER B 198  ALA B 199                    
SITE     2 BC8  6 HIS B 438  HOH B2070                                          
SITE     1 BC9  7 HIS B 207  LEU B 208  LEU B 209  SER B 210                    
SITE     2 BC9  7 HIS B 214  GLN B 311  LYS B 313                               
SITE     1 CC1  8 HIS B  77  MET B  81  SER B 425  LYS B 427                    
SITE     2 CC1  8 LEU B 428  PRO B 429  GLU B 443  HOH B2114                    
SITE     1 CC2  4 SER A 368  PHE A 371  HIS A 372  PHE B 525                    
SITE     1 CC3  3 TYR B  33  LEU B  49  LYS B 180                               
SITE     1 CC4  6 PRO B 449  GLU B 451  ARG B 452  ASN B 455                    
SITE     2 CC4  6 TYR B 456  GLU B 461                                          
SITE     1 CC5  3 ASP B 295  GLU B 497  LYS B 499                               
SITE     1 CC6  1 PRO B 285                                                     
SITE     1 CC7  4 ARG B 265  ASN B 266  LYS B 267  ASP B 268                    
SITE     1 CC8  5 THR B 284  PHE B 357  TYR B 396  ASN B 397                    
SITE     2 CC8  5 HOH B2116                                                     
SITE     1 CC9  8 GLN B  35  PRO B  37  LEU B  41  LYS B  44                    
SITE     2 CC9  8 LYS B  45  PRO B  46  GLN B  47  ARG B 147                    
SITE     1 DC1  4 ASN B  68  ASP B  70  THR B 120  HOH B2117                    
SITE     1 DC2  5 LYS B  60  TYR B  61  ASN B  63  THR B  86                    
SITE     2 DC2  5 ASP B  87                                                     
SITE     1 DC3  2 TRP B 231  VAL B 288                                          
SITE     1 DC4  2 LYS B 458  ILE B 462                                          
SITE     1 DC5  3 LEU B  18  ASP B 129  LYS B 131                               
SITE     1 DC6  3 ILE A   4  ASN A  17  PG4 A1530                               
SITE     1 DC7  4 ARG A  14  ILE A  55  ASN A  57  LYS B  12                    
SITE     1 DC8  3 ASN A 106  ASN A 188  LYS A 190                               
SITE     1 DC9  7 ASN A 241  ASN A 245  LYS A 248  PHE A 278                    
SITE     2 DC9  7 PRO A 281  NAG B 661  FUL B 663                               
SITE     1 EC1  3 SER A 338  ASN A 341  HOH A2158                               
SITE     1 EC2 10 TYR A 477  ASN A 479  ASN A 481  GLU A 482                    
SITE     2 EC2 10 THR A 483  GLN A 484  HOH A2159  ASP B  87                    
SITE     3 EC2 10 LEU B  88  GLN B 270                                          
SITE     1 EC3  6 ASN A 486  SER A 487  THR A 488  GLU A 506                    
SITE     2 EC3  6 THR A 508  GLY B  75                                          
SITE     1 EC4  2 ASN B  17  THR B  24                                          
SITE     1 EC5  2 ARG B  14  ASN B  57                                          
SITE     1 EC6  3 ASN B 106  ASN B 188  LYS B 190                               
SITE     1 EC7  7 TYR B 237  ASN B 241  ASN B 245  LYS B 248                    
SITE     2 EC7  7 LEU B 249  PHE B 278  TYR B 282                               
SITE     1 EC8  4 GLU B 255  ASN B 256  GLU B 259  GLU B 411                    
SITE     1 EC9  3 SER B 338  ASN B 341  ASN B 342                               
SITE     1 FC1  6 TYR A 237  LEU A 244  NAG A 631  LYS B 427                    
SITE     2 FC1  6 ASP B 454  ASN B 455                                          
SITE     1 FC2  2 TYR B 477  ASN B 481                                          
CRYST1   72.750   79.260  227.200  90.00  90.00  90.00 P 21 21 21    8          
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      0.013746  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012617  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004401        0.00000                         
TER    4223      VAL A 529                                                      
TER    8415      VAL B 529                                                      
MASTER      679    0   75   50   32    0   64    6 9253    2  572   82          
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
AcePerl Lincoln Stein Home Page
webmaster

Acknowledgements and disclaimer