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LongText Report for: 4BC0-pdb

Name Class
4BC0-pdb
HEADER    HYDROLASE                               30-SEP-12   4BC0              
TITLE     STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY CBDP (           
TITLE    2 12-H SOAK): CRESYL-PHOSPHOSERINE ADDUCT                              
CAVEAT     4BC0    NAG A 702   C1 IS PLANAR                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 3.1.1.7;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 OTHER_DETAILS: CRESYL-PHOSPHATE ADDUCT ON S203                       
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
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, BUTYRYLCHOLINESTERASE, NERVE         
KEYWDS   2 TRANSMISSION, INHIBITION, 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 4BC0    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.    3.35 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) : 3.35                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.615                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.36                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.66                          
REMARK   3   NUMBER OF REFLECTIONS             : 75467                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.1631                          
REMARK   3   R VALUE            (WORKING SET) : 0.1618                          
REMARK   3   FREE R VALUE                     : 0.2076                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 2265                            
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 48.6198 -  8.4277    0.92     4606   143  0.1725 0.1997        
REMARK   3     2  8.4277 -  6.6949    0.94     4523   140  0.1525 0.2013        
REMARK   3     3  6.6949 -  5.8502    0.95     4547   141  0.1481 0.2121        
REMARK   3     4  5.8502 -  5.3161    0.96     4574   141  0.1284 0.1845        
REMARK   3     5  5.3161 -  4.9354    0.96     4555   141  0.1199 0.1512        
REMARK   3     6  4.9354 -  4.6447    0.96     4565   142  0.1146 0.1708        
REMARK   3     7  4.6447 -  4.4122    0.97     4553   140  0.1188 0.1639        
REMARK   3     8  4.4122 -  4.2203    0.97     4605   143  0.1311 0.1661        
REMARK   3     9  4.2203 -  4.0579    0.98     4556   141  0.1478 0.1801        
REMARK   3    10  4.0579 -  3.9179    0.98     4611   142  0.1588 0.2154        
REMARK   3    11  3.9179 -  3.7955    0.98     4575   142  0.1796 0.2341        
REMARK   3    12  3.7955 -  3.6870    0.98     4575   141  0.1967 0.2294        
REMARK   3    13  3.6870 -  3.5900    0.98     4591   142  0.2201 0.2878        
REMARK   3    14  3.5900 -  3.5024    0.98     4602   143  0.2434 0.3231        
REMARK   3    15  3.5024 -  3.4228    0.98     4587   142  0.2724 0.3306        
REMARK   3    16  3.4228 -  3.3500    0.98     4577   141  0.3099 0.3324        
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)     : 0.37             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.06            
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      :  0.009          17527                                  
REMARK   3   ANGLE     :  1.482          23960                                  
REMARK   3   CHIRALITY :  0.108           2568                                  
REMARK   3   PLANARITY :  0.008           3140                                  
REMARK   3   DIHEDRAL  : 17.136           6287                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.0300 -28.8538  26.5797              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1486 T22:   0.1647                                     
REMARK   3      T33:   0.2848 T12:   0.0417                                     
REMARK   3      T13:   0.0116 T23:   0.0264                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9249 L22:   1.5694                                     
REMARK   3      L33:   1.0605 L12:  -0.1518                                     
REMARK   3      L13:  -0.1280 L23:   0.1825                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0406 S12:   0.0347 S13:   0.0352                       
REMARK   3      S21:  -0.2593 S22:   0.0125 S23:   0.0472                       
REMARK   3      S31:  -0.1423 S32:  -0.0599 S33:   0.0452                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   8.4933  27.5493  46.2152              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6839 T22:   0.3580                                     
REMARK   3      T33:   0.4524 T12:  -0.4454                                     
REMARK   3      T13:   0.2660 T23:  -0.0120                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9423 L22:   0.7201                                     
REMARK   3      L33:   0.5802 L12:   0.3483                                     
REMARK   3      L13:   0.1452 L23:   0.3100                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0427 S12:   0.2708 S13:   0.0568                       
REMARK   3      S21:  -0.4125 S22:   0.1964 S23:  -0.3699                       
REMARK   3      S31:  -0.5503 S32:   0.5101 S33:   0.1944                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN C                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -24.9244  12.4072  87.1263              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1829 T22:   0.1936                                     
REMARK   3      T33:   0.1287 T12:  -0.0329                                     
REMARK   3      T13:   0.1094 T23:  -0.0422                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8522 L22:   0.8534                                     
REMARK   3      L33:   1.3462 L12:  -0.0523                                     
REMARK   3      L13:  -0.0856 L23:   0.0812                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1288 S12:  -0.0125 S13:  -0.0132                       
REMARK   3      S21:  -0.0175 S22:  -0.0054 S23:   0.0822                       
REMARK   3      S31:  -0.0824 S32:  -0.2288 S33:  -0.2848                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN D                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -47.7610   5.0806  30.9194              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2236 T22:   0.3784                                     
REMARK   3      T33:   0.2353 T12:   0.0370                                     
REMARK   3      T13:  -0.0831 T23:  -0.1480                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8959 L22:   0.9504                                     
REMARK   3      L33:   1.9068 L12:   0.1479                                     
REMARK   3      L13:   0.5628 L23:   0.2230                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1006 S12:  -0.1985 S13:   0.0207                       
REMARK   3      S21:   0.0994 S22:  -0.1283 S23:   0.2801                       
REMARK   3      S31:   0.1435 S32:  -0.3213 S33:  -0.0236                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 203 OR RESSEQ 600)      
REMARK   3     SELECTION          : CHAIN B AND (RESSEQ 203 OR RESSEQ 600)      
REMARK   3     ATOM PAIRS NUMBER  : 17                                          
REMARK   3     RMSD               : 0.033                                       
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 203 OR RESSEQ 600)      
REMARK   3     SELECTION          : CHAIN C AND (RESSEQ 203 OR RESSEQ 600)      
REMARK   3     ATOM PAIRS NUMBER  : 17                                          
REMARK   3     RMSD               : 0.042                                       
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: CHAIN A AND (RESSEQ 203 OR RESSEQ 600)      
REMARK   3     SELECTION          : CHAIN D AND (RESSEQ 203 OR RESSEQ 600)      
REMARK   3     ATOM PAIRS NUMBER  : 17                                          
REMARK   3     RMSD               : 0.036                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4BC0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-SEP-12.                  
REMARK 100 THE PDBE ID CODE IS EBI-54256.                                       
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                             : 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                       : 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   : 75488                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.35                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.60                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.0                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : 3.5                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 16.20                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.35                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.4                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.58                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.80                               
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 4A16                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 78                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS HCL BUFFER PH 7.4,            
REMARK 280  1.6 M AMMONIUM SULFATE                                              
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       68.47000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      112.81000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       87.02000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      112.81000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       68.47000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       87.02000            
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                                                    
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4220 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -106.5 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4630 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 39140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -124.6 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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     GLU B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     GLU C     1                                                      
REMARK 465     GLY C     2                                                      
REMARK 465     ARG C     3                                                      
REMARK 465     GLU D     1                                                      
REMARK 465     GLY D     2                                                      
REMARK 465     ARG D     3                                                      
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   OE2  GLU A   202     O    HOH A  2060              2.13            
REMARK 500   OE1  GLU A   334     O    HOH A  2088              2.10            
REMARK 500   O    ASN B   265     O    HOH B  2044              2.17            
REMARK 500   ND2  ASN C   265     C1   NAG C   701              1.45            
REMARK 500   NE1  TRP C   286     O    HOH C  2077              2.19            
REMARK 500   O    HOH D  2003     O    HOH D  2010              2.10            
REMARK 500   O    HOH D  2009     O    HOH D  2010              2.09            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO C 258   C   -  N   -  CA  ANGL. DEV. = -15.0 DEGREES          
REMARK 500    PRO C 259   C   -  N   -  CA  ANGL. DEV. =  10.0 DEGREES          
REMARK 500    CYS D 257   CA  -  CB  -  SG  ANGL. DEV. =  -7.5 DEGREES          
REMARK 500    SER D 497   N   -  CA  -  C   ANGL. DEV. = -18.8 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    ARG A   3      -18.14     72.69                                   
REMARK 500    SER A 203     -123.38     60.93                                   
REMARK 500    ALA A 262     -155.64    -86.79                                   
REMARK 500    ASP A 306      -74.82   -117.17                                   
REMARK 500    VAL A 367       73.80   -115.27                                   
REMARK 500    LEU A 373      -23.51     72.08                                   
REMARK 500    VAL A 407      -64.57   -130.43                                   
REMARK 500    PRO A 440     -177.98    -61.13                                   
REMARK 500    LYS A 496      177.70    178.15                                   
REMARK 500    ALA A 506      -70.78    -55.43                                   
REMARK 500    LEU A 539      -72.38    -82.22                                   
REMARK 500    SER A 541       35.90    -92.43                                   
REMARK 500    ALA A 542        5.35    117.39                                   
REMARK 500    VAL B  12       97.06     59.48                                   
REMARK 500    ARG B  13      -19.81    -34.74                                   
REMARK 500    ARG B 107     -173.98    -63.07                                   
REMARK 500    ALA B 109      -76.99    -88.61                                   
REMARK 500    PHE B 123       -9.62     68.87                                   
REMARK 500    ALA B 127      156.04    178.26                                   
REMARK 500    SER B 203     -121.22     57.73                                   
REMARK 500    HIS B 223      -57.81   -130.01                                   
REMARK 500    ILE B 294      -63.74   -108.96                                   
REMARK 500    PHE B 295     -155.36    -80.12                                   
REMARK 500    ARG B 296       80.62     68.77                                   
REMARK 500    ASP B 306      -75.91   -120.71                                   
REMARK 500    ASP B 349      -72.19    -87.04                                   
REMARK 500    VAL B 445       79.06   -114.76                                   
REMARK 500    ASP B 488      129.43   -176.63                                   
REMARK 500    ARG B 493      -60.86   -109.50                                   
REMARK 500    LYS B 496     -155.16     55.05                                   
REMARK 500    ARG B 525      -97.12     55.79                                   
REMARK 500    ALA B 526     -103.38     71.36                                   
REMARK 500    THR B 528      -28.93     80.93                                   
REMARK 500    ALA B 542       -5.32     73.02                                   
REMARK 500    PRO C  41       49.00    -78.70                                   
REMARK 500    SER C 110      140.29     69.46                                   
REMARK 500    PHE C 123       -5.76     67.43                                   
REMARK 500    SER C 125     -175.99   -170.33                                   
REMARK 500    SER C 203     -120.05     52.92                                   
REMARK 500    THR C 231      142.62   -175.16                                   
REMARK 500    ASP C 306      -76.10   -108.41                                   
REMARK 500    VAL C 367       73.38   -118.28                                   
REMARK 500    VAL C 407      -65.07   -121.19                                   
REMARK 500    LYS C 496      -76.27    -74.46                                   
REMARK 500    SER C 497       65.59     22.22                                   
REMARK 500    ALA C 506      -70.31    -58.85                                   
REMARK 500    ARG C 525       65.20     36.15                                   
REMARK 500    ASP D   5      127.77   -177.03                                   
REMARK 500    PHE D  47       -2.46     77.16                                   
REMARK 500    PRO D 111       80.24    -62.84                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      60 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 CYS A  257     PRO A  258                  149.41                    
REMARK 500 ASP A  323     LEU A  324                 -146.18                    
REMARK 500 SER A  497     PRO A  498                  -59.06                    
REMARK 500 SER A  541     ALA A  542                 -134.94                    
REMARK 500 LYS B  496     SER B  497                  -35.28                    
REMARK 500 PRO C  258     PRO C  259                  -34.24                    
REMARK 500 GLY C  342     VAL C  343                  147.16                    
REMARK 500 LYS C  496     SER C  497                  121.82                    
REMARK 500 CYS D  257     PRO D  258                 -113.50                    
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    PHE A 158        22.4      L          L   OUTSIDE RANGE           
REMARK 500    PHE A 321        24.5      L          L   OUTSIDE RANGE           
REMARK 500    SER A 541        24.4      L          L   OUTSIDE RANGE           
REMARK 500    ARG B  11        24.5      L          L   OUTSIDE RANGE           
REMARK 500    VAL B  12        21.7      L          L   OUTSIDE RANGE           
REMARK 500    CYS B  96        24.4      L          L   OUTSIDE RANGE           
REMARK 500    PHE B 158        23.2      L          L   OUTSIDE RANGE           
REMARK 500    PHE B 321        24.6      L          L   OUTSIDE RANGE           
REMARK 500    PHE C 158        23.2      L          L   OUTSIDE RANGE           
REMARK 500    ARG C 493        21.0      L          L   OUTSIDE RANGE           
REMARK 500    PHE D 158        22.7      L          L   OUTSIDE RANGE           
REMARK 500    TYR D 449        25.0      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH C2034        DISTANCE =  5.07 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4OJ A 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4OJ B 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4OJ C 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG C 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 4OJ D 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL C3000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL C3001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL C1544                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL D3001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL D3002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL C1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1544                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1544                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D1544                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1546                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1546                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C1547                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1547                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D1545                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B1546                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A1548                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D1546                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG A 701 BOUND TO ASN A 265                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG B 701 BOUND TO ASN B 265                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG B 702 BOUND TO ASN B 350                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG D 701 BOUND TO ASN D 265                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG D 702 BOUND TO ASN D 350                                       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR MONO-SACCHARIDE                   
REMARK 800   NAG D 703 BOUND TO ASN D 464                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1C2B   RELATED DB: PDB                                   
REMARK 900  ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE                       
REMARK 900 RELATED ID: 1C2O   RELATED DB: PDB                                   
REMARK 900  ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE                       
REMARK 900 RELATED ID: 1J06   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN THE              
REMARK 900  APOFORM                                                             
REMARK 900 RELATED ID: 1J07   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-                
REMARK 900  DECIDIUM COMPLEX                                                    
REMARK 900 RELATED ID: 1KU6   RELATED DB: PDB                                   
REMARK 900  FASCICULIN 2-MOUSE ACETYLCHOLINESTERASE COMPLEX                     
REMARK 900 RELATED ID: 1MAA   RELATED DB: PDB                                   
REMARK 900  MOUSE ACETYLCHOLINESTERASE CATALYTIC DOMAIN,                        
REMARK 900  GLYCOSYLATEDPROTEIN                                                 
REMARK 900 RELATED ID: 1MAH   RELATED DB: PDB                                   
REMARK 900  FASCICULIN2 - MOUSE ACETYLCHOLINESTERASE COMPLEX                    
REMARK 900 RELATED ID: 1N5M   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-                
REMARK 900  GALLAMINE COMPLEX                                                   
REMARK 900 RELATED ID: 1N5R   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-                
REMARK 900  PROPIDIUM COMPLEX                                                   
REMARK 900 RELATED ID: 1Q83   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-                
REMARK 900  TZ2PA6SYN COMPLEX                                                   
REMARK 900 RELATED ID: 1Q84   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-                
REMARK 900  TZ2PA6ANTI COMPLEX                                                  
REMARK 900 RELATED ID: 2C0P   RELATED DB: PDB                                   
REMARK 900  AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY                
REMARK 900  TABUN                                                               
REMARK 900 RELATED ID: 2C0Q   RELATED DB: PDB                                   
REMARK 900  NON-AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY            
REMARK 900   TABUN                                                              
REMARK 900 RELATED ID: 2H9Y   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900  COMPLEXEDWITH M-(N,N,N-TRIMETHYLAMMONIO)                            
REMARK 900  TRIFLUOROACETOPHENONE                                               
REMARK 900 RELATED ID: 2HA0   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900  COMPLEXEDWITH 4-KETOAMYLTRIMETHYLAMMONIUM                           
REMARK 900 RELATED ID: 2HA2   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900  COMPLEXEDWITH SUCCINYLCHOLINE                                       
REMARK 900 RELATED ID: 2HA3   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900  COMPLEXEDWITH CHOLINE                                               
REMARK 900 RELATED ID: 2HA4   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MUTANT S203A OF                                
REMARK 900  MOUSEACETYLCHOLINESTERASE COMPLEXED WITH ACETYLCHOLINE              
REMARK 900 RELATED ID: 2HA5   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MUTANT S203A OF                                
REMARK 900  ACETYLCHOLINESTERASECOMPLEXED WITH ACETYLTHIOCHOLINE                
REMARK 900 RELATED ID: 2HA6   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MUTANT S203A OF                                
REMARK 900  MOUSEACETYLCHOLINESTERASE COMPLEXED WITH SUCCINYLCHOLINE            
REMARK 900 RELATED ID: 2HA7   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MUTANT S203A OF                                
REMARK 900  MOUSEACETYLCHOLINESTERASE COMPLEXED WITH BUTYRYLTHIOCHOLINE         
REMARK 900 RELATED ID: 2JEY   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH HLO-7             
REMARK 900 RELATED ID: 2JEZ   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH TABUN             
REMARK 900  AND HLO-7                                                           
REMARK 900 RELATED ID: 2JF0   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH TABUN             
REMARK 900  AND ORTHO-7                                                         
REMARK 900 RELATED ID: 2JGE   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY NON-AGED METHAMIDOPHOS                                           
REMARK 900 RELATED ID: 2JGF   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY NON-AGED FENAMIPHOS                                              
REMARK 900 RELATED ID: 2JGG   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY NON-AGED SARIN                                                   
REMARK 900 RELATED ID: 2JGH   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY NON-AGED VX                                                      
REMARK 900 RELATED ID: 2JGI   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY NON-AGED DIISOPROPYL FLUOROPHOSPHATE (DFP)                       
REMARK 900 RELATED ID: 2JGJ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY AGED METHAMIDOPHOS                                               
REMARK 900 RELATED ID: 2JGK   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY AGED FENAMIPHOS                                                  
REMARK 900 RELATED ID: 2JGL   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY AGED VX AND SARIN                                                
REMARK 900 RELATED ID: 2JGM   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED           
REMARK 900  BY AGED DIISOPROPYL FLUOROPHOSPHATE (DFP)                           
REMARK 900 RELATED ID: 2WHP   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE, PHOSPHONYLATED BY        
REMARK 900   SARIN AND IN COMPLEX WITH HI-6                                     
REMARK 900 RELATED ID: 2WHQ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE, PHOSPHONYLATED BY        
REMARK 900   SARIN (AGED) IN COMPLEX WITH HI-6                                  
REMARK 900 RELATED ID: 2WHR   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE IN COMPLEX WITH           
REMARK 900   K027                                                               
REMARK 900 RELATED ID: 2WLS   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MUS MUSCULUS ACETYLCHOLINESTERASE IN           
REMARK 900   COMPLEX WITH AMTS13                                                
REMARK 900 RELATED ID: 2WU3   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN COMPLEX          
REMARK 900   WITH FENAMIPHOS AND HI-6                                           
REMARK 900 RELATED ID: 2WU4   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN COMPLEX          
REMARK 900   WITH FENAMIPHOS AND ORTHO-7                                        
REMARK 900 RELATED ID: 2XUD   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE Y337A MUTANT OF MOUSE                      
REMARK 900  ACETYLCHOLINESTERASE                                                
REMARK 900 RELATED ID: 2XUF   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (              
REMARK 900  1 MTH)                                                              
REMARK 900 RELATED ID: 2XUG   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (              
REMARK 900  1 WK)                                                               
REMARK 900 RELATED ID: 2XUH   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (              
REMARK 900  10 MTH)                                                             
REMARK 900 RELATED ID: 2XUI   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (1              
REMARK 900   WK)                                                                
REMARK 900 RELATED ID: 2XUJ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (1              
REMARK 900   MTH)                                                               
REMARK 900 RELATED ID: 2XUK   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (               
REMARK 900  10 MTH)                                                             
REMARK 900 RELATED ID: 2XUO   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A MUTANT IN COMPLEX                  
REMARK 900  WITH SOAKED TZ2PA6 ANTI INHIBITOR                                   
REMARK 900 RELATED ID: 2XUP   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MACHE-Y337A MUTANT IN COMPLEX              
REMARK 900   WITH SOAKED TZ2PA6 SYN INHIBITOR                                   
REMARK 900 RELATED ID: 2XUQ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MACHE-Y337A MUTANT IN COMPLEX              
REMARK 900   WITH SOAKED TZ2PA6 ANTI-SYN INHIBITORS                             
REMARK 900 RELATED ID: 4A16   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF MOUSE ACETYLCHOLINESTERASE COMPLEX WITH                
REMARK 900  HUPRINE DERIVATIVE                                                  
REMARK 900 RELATED ID: 4A23   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH RACEMIC           
REMARK 900   C5685                                                              
REMARK 900 RELATED ID: 4ARA   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH (R)-              
REMARK 900  C5685 AT 2.5 A RESOLUTION.                                          
REMARK 900 RELATED ID: 4ARB   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH (S)-              
REMARK 900  C5685 AT 2.25 A RESOLUTION.                                         
REMARK 900 RELATED ID: 4B7Z   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-             
REMARK 900  DIETHYLAMINO-ETHYL)-1-(4-METHYLPHENYL)-METHANESULFONAMIDE           
REMARK 900 RELATED ID: 4B80   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-             
REMARK 900  DIETHYLAMINO-ETHYL)-1-(4-FLUORO-PHENYL)-METHANESULFONAMIDE          
REMARK 900 RELATED ID: 4B81   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH 1-(4-             
REMARK 900  CHLORO-PHENYL)-N-(2-DIETHYLAMINO-ETHYL)-METHANESULFONAMIDE          
REMARK 900 RELATED ID: 4B82   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-             
REMARK 900  DIETHYLAMINO-ETHYL)-2-FLUORANYL-BENZENESULFONAMIDE                  
REMARK 900 RELATED ID: 4B83   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-             
REMARK 900  DIETHYLAMINO-ETHYL)-3-METHOXY-BENZENESULFONAMIDE                    
REMARK 900 RELATED ID: 4B84   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-             
REMARK 900  DIETHYLAMINO-ETHYL)-3-TRIFLUOROMETHYL-BENZENESULFONAMIDE            
REMARK 900 RELATED ID: 4B85   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH 4-                
REMARK 900  CHLORANYL-N-(2-DIETHYLAMINO-ETHYL)-BENZENESULFONAMIDE               
REMARK 900 RELATED ID: 4BBZ   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE INHIBITED BY CBDP          
REMARK 900   (2-MIN 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  4BC0 A    1   543  UNP    P21836   ACES_MOUSE      32    574             
DBREF  4BC0 B    1   543  UNP    P21836   ACES_MOUSE      32    574             
DBREF  4BC0 C    1   543  UNP    P21836   ACES_MOUSE      32    574             
DBREF  4BC0 D    1   543  UNP    P21836   ACES_MOUSE      32    574             
SEQRES   1 A  543  GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG          
SEQRES   2 A  543  GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY          
SEQRES   3 A  543  GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU          
SEQRES   4 A  543  PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO          
SEQRES   5 A  543  LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE          
SEQRES   6 A  543  GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO          
SEQRES   7 A  543  GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU          
SEQRES   8 A  543  LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO          
SEQRES   9 A  543  TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP          
SEQRES  10 A  543  ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU          
SEQRES  11 A  543  ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY          
SEQRES  12 A  543  ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE          
SEQRES  13 A  543  GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY          
SEQRES  14 A  543  ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP          
SEQRES  15 A  543  VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET          
SEQRES  16 A  543  SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER          
SEQRES  17 A  543  VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU          
SEQRES  18 A  543  PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY          
SEQRES  19 A  543  PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG          
SEQRES  20 A  543  ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY          
SEQRES  21 A  543  GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU          
SEQRES  22 A  543  ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP          
SEQRES  23 A  543  HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE          
SEQRES  24 A  543  VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO          
SEQRES  25 A  543  GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN          
SEQRES  26 A  543  VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE          
SEQRES  27 A  543  LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU          
SEQRES  28 A  543  SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG          
SEQRES  29 A  543  ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA          
SEQRES  30 A  543  VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP          
SEQRES  31 A  543  PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY          
SEQRES  32 A  543  ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY          
SEQRES  33 A  543  ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE          
SEQRES  34 A  543  PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP          
SEQRES  35 A  543  MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE          
SEQRES  36 A  543  GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU          
SEQRES  37 A  543  GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR          
SEQRES  38 A  543  ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP          
SEQRES  39 A  543  SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA          
SEQRES  40 A  543  GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL          
SEQRES  41 A  543  ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN          
SEQRES  42 A  543  ARG PHE LEU PRO LYS LEU LEU SER ALA THR                      
SEQRES   1 B  543  GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG          
SEQRES   2 B  543  GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY          
SEQRES   3 B  543  GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU          
SEQRES   4 B  543  PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO          
SEQRES   5 B  543  LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE          
SEQRES   6 B  543  GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO          
SEQRES   7 B  543  GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU          
SEQRES   8 B  543  LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO          
SEQRES   9 B  543  TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP          
SEQRES  10 B  543  ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU          
SEQRES  11 B  543  ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY          
SEQRES  12 B  543  ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE          
SEQRES  13 B  543  GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY          
SEQRES  14 B  543  ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP          
SEQRES  15 B  543  VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET          
SEQRES  16 B  543  SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER          
SEQRES  17 B  543  VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU          
SEQRES  18 B  543  PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY          
SEQRES  19 B  543  PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG          
SEQRES  20 B  543  ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY          
SEQRES  21 B  543  GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU          
SEQRES  22 B  543  ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP          
SEQRES  23 B  543  HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE          
SEQRES  24 B  543  VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO          
SEQRES  25 B  543  GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN          
SEQRES  26 B  543  VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE          
SEQRES  27 B  543  LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU          
SEQRES  28 B  543  SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG          
SEQRES  29 B  543  ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA          
SEQRES  30 B  543  VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP          
SEQRES  31 B  543  PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY          
SEQRES  32 B  543  ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY          
SEQRES  33 B  543  ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE          
SEQRES  34 B  543  PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP          
SEQRES  35 B  543  MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE          
SEQRES  36 B  543  GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU          
SEQRES  37 B  543  GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR          
SEQRES  38 B  543  ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP          
SEQRES  39 B  543  SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA          
SEQRES  40 B  543  GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL          
SEQRES  41 B  543  ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN          
SEQRES  42 B  543  ARG PHE LEU PRO LYS LEU LEU SER ALA THR                      
SEQRES   1 C  543  GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG          
SEQRES   2 C  543  GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY          
SEQRES   3 C  543  GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU          
SEQRES   4 C  543  PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO          
SEQRES   5 C  543  LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE          
SEQRES   6 C  543  GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO          
SEQRES   7 C  543  GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU          
SEQRES   8 C  543  LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO          
SEQRES   9 C  543  TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP          
SEQRES  10 C  543  ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU          
SEQRES  11 C  543  ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY          
SEQRES  12 C  543  ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE          
SEQRES  13 C  543  GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY          
SEQRES  14 C  543  ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP          
SEQRES  15 C  543  VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET          
SEQRES  16 C  543  SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER          
SEQRES  17 C  543  VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU          
SEQRES  18 C  543  PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY          
SEQRES  19 C  543  PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG          
SEQRES  20 C  543  ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY          
SEQRES  21 C  543  GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU          
SEQRES  22 C  543  ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP          
SEQRES  23 C  543  HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE          
SEQRES  24 C  543  VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO          
SEQRES  25 C  543  GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN          
SEQRES  26 C  543  VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE          
SEQRES  27 C  543  LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU          
SEQRES  28 C  543  SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG          
SEQRES  29 C  543  ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA          
SEQRES  30 C  543  VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP          
SEQRES  31 C  543  PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY          
SEQRES  32 C  543  ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY          
SEQRES  33 C  543  ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE          
SEQRES  34 C  543  PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP          
SEQRES  35 C  543  MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE          
SEQRES  36 C  543  GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU          
SEQRES  37 C  543  GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR          
SEQRES  38 C  543  ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP          
SEQRES  39 C  543  SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA          
SEQRES  40 C  543  GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL          
SEQRES  41 C  543  ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN          
SEQRES  42 C  543  ARG PHE LEU PRO LYS LEU LEU SER ALA THR                      
SEQRES   1 D  543  GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG          
SEQRES   2 D  543  GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY          
SEQRES   3 D  543  GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU          
SEQRES   4 D  543  PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO          
SEQRES   5 D  543  LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE          
SEQRES   6 D  543  GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO          
SEQRES   7 D  543  GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU          
SEQRES   8 D  543  LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO          
SEQRES   9 D  543  TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP          
SEQRES  10 D  543  ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU          
SEQRES  11 D  543  ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY          
SEQRES  12 D  543  ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE          
SEQRES  13 D  543  GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY          
SEQRES  14 D  543  ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP          
SEQRES  15 D  543  VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET          
SEQRES  16 D  543  SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER          
SEQRES  17 D  543  VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU          
SEQRES  18 D  543  PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY          
SEQRES  19 D  543  PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG          
SEQRES  20 D  543  ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY          
SEQRES  21 D  543  GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU          
SEQRES  22 D  543  ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP          
SEQRES  23 D  543  HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE          
SEQRES  24 D  543  VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO          
SEQRES  25 D  543  GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN          
SEQRES  26 D  543  VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE          
SEQRES  27 D  543  LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU          
SEQRES  28 D  543  SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG          
SEQRES  29 D  543  ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA          
SEQRES  30 D  543  VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP          
SEQRES  31 D  543  PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY          
SEQRES  32 D  543  ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY          
SEQRES  33 D  543  ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE          
SEQRES  34 D  543  PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP          
SEQRES  35 D  543  MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE          
SEQRES  36 D  543  GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU          
SEQRES  37 D  543  GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR          
SEQRES  38 D  543  ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP          
SEQRES  39 D  543  SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA          
SEQRES  40 D  543  GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL          
SEQRES  41 D  543  ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN          
SEQRES  42 D  543  ARG PHE LEU PRO LYS LEU LEU SER ALA THR                      
HET    4OJ  A 600      11                                                       
HET    NAG  A 701      14                                                       
HET    4OJ  B 600      11                                                       
HET    NAG  B 701      14                                                       
HET    NAG  B 702      14                                                       
HET    4OJ  C 600      11                                                       
HET    NAG  C 701      14                                                       
HET    4OJ  D 600      11                                                       
HET    NAG  D 701      14                                                       
HET    NAG  D 702      14                                                       
HET    NAG  D 703      14                                                       
HET     CL  C3000       1                                                       
HET     CL  C3001       1                                                       
HET     CL  C1544       1                                                       
HET     CL  C3002       1                                                       
HET     CL  D3000       1                                                       
HET     CL  D3001       1                                                       
HET     CL  D3002       1                                                       
HET     CL  C1545       1                                                       
HET    SO4  B1544       5                                                       
HET    SO4  A1544       5                                                       
HET    SO4  A1545       5                                                       
HET    SO4  D1544       5                                                       
HET    SO4  C1546       5                                                       
HET    SO4  A1546       5                                                       
HET    SO4  B1545       5                                                       
HET    SO4  C1547       5                                                       
HET    SO4  A1547       5                                                       
HET    SO4  D1545       5                                                       
HET    SO4  B1546       5                                                       
HET    SO4  A1548       5                                                       
HET    SO4  D1546       5                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM      CL CHLORIDE ION                                                     
HETNAM     4OJ (2-METHYLPHENYL) DIHYDROGEN PHOSPHATE                            
HETNAM     SO4 SULFATE ION                                                      
HETSYN     4OJ O-CRESYL-PHOSPHATE                                               
FORMUL   6  NAG    7(C8 H15 N O6)                                               
FORMUL   7   CL    8(CL 1-)                                                     
FORMUL   8  4OJ    4(C7 H9 O4 P)                                                
FORMUL   9  SO4    13(O4 S 2-)                                                  
FORMUL  10  HOH   *411(H2 O)                                                    
HELIX    1   1 VAL A   42  ARG A   46  5                                   5    
HELIX    2   2 PHE A   80  MET A   85  1                                   6    
HELIX    3   3 LEU A  130  ASP A  134  5                                   5    
HELIX    4   4 GLY A  135  GLY A  143  1                                   9    
HELIX    5   5 VAL A  153  LEU A  159  1                                   7    
HELIX    6   6 ASN A  170  ILE A  187  1                                  18    
HELIX    7   7 ALA A  188  GLY A  191  5                                   4    
HELIX    8   8 SER A  203  SER A  215  1                                  13    
HELIX    9   9 SER A  215  SER A  220  1                                   6    
HELIX   10  10 SER A  240  VAL A  255  1                                  16    
HELIX   11  11 ASN A  265  ARG A  274  1                                  10    
HELIX   12  12 PRO A  277  GLU A  285  1                                   9    
HELIX   13  13 THR A  311  GLY A  319  1                                   9    
HELIX   14  14 GLY A  335  VAL A  340  1                                   6    
HELIX   15  15 SER A  355  VAL A  367  1                                  13    
HELIX   16  16 ALA A  374  THR A  383  1                                  10    
HELIX   17  17 ASP A  390  VAL A  407  1                                  18    
HELIX   18  18 VAL A  407  GLN A  421  1                                  15    
HELIX   19  19 PRO A  440  GLY A  444  5                                   5    
HELIX   20  20 GLU A  450  PHE A  455  1                                   6    
HELIX   21  21 GLY A  456  ASP A  460  5                                   5    
HELIX   22  22 ASP A  460  ASN A  464  5                                   5    
HELIX   23  23 THR A  466  GLY A  487  1                                  22    
HELIX   24  24 ARG A  525  ARG A  534  1                                  10    
HELIX   25  25 ARG A  534  SER A  541  1                                   8    
HELIX   26  26 VAL B   42  ARG B   46  5                                   5    
HELIX   27  27 PHE B   80  MET B   85  1                                   6    
HELIX   28  28 GLY B  135  GLY B  143  1                                   9    
HELIX   29  29 VAL B  153  LEU B  159  1                                   7    
HELIX   30  30 ASN B  170  ILE B  187  1                                  18    
HELIX   31  31 ALA B  188  PHE B  190  5                                   3    
HELIX   32  32 SER B  203  SER B  215  1                                  13    
HELIX   33  33 LEU B  216  PHE B  222  5                                   7    
HELIX   34  34 ALA B  241  VAL B  255  1                                  15    
HELIX   35  35 PRO B  258  ALA B  262  5                                   5    
HELIX   36  36 ASN B  265  ARG B  274  1                                  10    
HELIX   37  37 PRO B  277  GLU B  285  1                                   9    
HELIX   38  38 TRP B  286  VAL B  288  5                                   3    
HELIX   39  39 THR B  311  GLY B  319  1                                   9    
HELIX   40  40 GLY B  335  VAL B  340  1                                   6    
HELIX   41  41 SER B  355  VAL B  367  1                                  13    
HELIX   42  42 SER B  371  THR B  383  1                                  13    
HELIX   43  43 ASP B  390  VAL B  407  1                                  18    
HELIX   44  44 VAL B  407  GLN B  421  1                                  15    
HELIX   45  45 PRO B  440  GLY B  444  5                                   5    
HELIX   46  46 GLU B  450  PHE B  455  1                                   6    
HELIX   47  47 GLY B  456  ASP B  460  5                                   5    
HELIX   48  48 ASP B  460  ASN B  464  5                                   5    
HELIX   49  49 THR B  466  GLY B  487  1                                  22    
HELIX   50  50 THR B  528  ARG B  534  1                                   7    
HELIX   51  51 ARG B  534  SER B  541  1                                   8    
HELIX   52  52 VAL C   42  ARG C   46  5                                   5    
HELIX   53  53 PHE C   80  MET C   85  1                                   6    
HELIX   54  54 LEU C  130  ASP C  134  5                                   5    
HELIX   55  55 GLY C  135  GLU C  142  1                                   8    
HELIX   56  56 GLY C  154  LEU C  159  1                                   6    
HELIX   57  57 ASN C  170  ILE C  187  1                                  18    
HELIX   58  58 ALA C  188  PHE C  190  5                                   3    
HELIX   59  59 SER C  203  SER C  215  1                                  13    
HELIX   60  60 SER C  215  SER C  220  1                                   6    
HELIX   61  61 ALA C  241  VAL C  255  1                                  15    
HELIX   62  62 ASN C  265  ARG C  274  1                                  10    
HELIX   63  63 PRO C  277  TRP C  286  1                                  10    
HELIX   64  64 HIS C  287  LEU C  289  5                                   3    
HELIX   65  65 THR C  311  GLY C  319  1                                   9    
HELIX   66  66 GLY C  335  VAL C  340  1                                   6    
HELIX   67  67 SER C  355  VAL C  367  1                                  13    
HELIX   68  68 SER C  371  THR C  383  1                                  13    
HELIX   69  69 ASP C  390  VAL C  407  1                                  18    
HELIX   70  70 VAL C  407  GLN C  421  1                                  15    
HELIX   71  71 PRO C  440  GLY C  444  5                                   5    
HELIX   72  72 GLU C  450  PHE C  455  1                                   6    
HELIX   73  73 GLY C  456  ASP C  460  5                                   5    
HELIX   74  74 ASP C  460  ASN C  464  5                                   5    
HELIX   75  75 THR C  466  GLY C  487  1                                  22    
HELIX   76  76 ARG C  525  ARG C  534  1                                  10    
HELIX   77  77 ARG C  534  SER C  541  1                                   8    
HELIX   78  78 VAL D   42  ARG D   46  5                                   5    
HELIX   79  79 PHE D   80  MET D   85  1                                   6    
HELIX   80  80 LEU D  130  ASP D  134  5                                   5    
HELIX   81  81 GLY D  135  GLY D  143  1                                   9    
HELIX   82  82 VAL D  153  LEU D  159  1                                   7    
HELIX   83  83 ASN D  170  ILE D  187  1                                  18    
HELIX   84  84 ALA D  188  PHE D  190  5                                   3    
HELIX   85  85 SER D  203  LEU D  214  1                                  12    
HELIX   86  86 SER D  215  PHE D  222  5                                   8    
HELIX   87  87 SER D  240  VAL D  255  1                                  16    
HELIX   88  88 ASN D  265  ARG D  274  1                                  10    
HELIX   89  89 PRO D  277  TRP D  286  1                                  10    
HELIX   90  90 THR D  311  THR D  318  1                                   8    
HELIX   91  91 GLY D  335  VAL D  340  1                                   6    
HELIX   92  92 SER D  355  VAL D  367  1                                  13    
HELIX   93  93 SER D  371  THR D  383  1                                  13    
HELIX   94  94 ASP D  390  VAL D  407  1                                  18    
HELIX   95  95 VAL D  407  GLN D  421  1                                  15    
HELIX   96  96 PRO D  440  GLY D  444  5                                   5    
HELIX   97  97 GLU D  450  GLY D  456  1                                   7    
HELIX   98  98 LEU D  457  ASN D  464  5                                   8    
HELIX   99  99 THR D  466  GLY D  487  1                                  22    
HELIX  100 100 ARG D  525  ARG D  534  1                                  10    
HELIX  101 101 ARG D  534  THR D  543  1                                  10    
SHEET    1  AA 3 LEU A   9  VAL A  12  0                                        
SHEET    2  AA 3 GLY A  15  ARG A  18 -1  O  GLY A  15   N  VAL A  12           
SHEET    3  AA 3 VAL A  59  ASP A  61  1  O  LEU A  60   N  ARG A  18           
SHEET    1  AB11 ILE A  20  LYS A  23  0                                        
SHEET    2  AB11 PRO A  28  PRO A  36 -1  O  VAL A  29   N  LEU A  22           
SHEET    3  AB11 TYR A  98  PRO A 104 -1  O  LEU A  99   N  ILE A  35           
SHEET    4  AB11 VAL A 145  MET A 149 -1  O  LEU A 146   N  TRP A 102           
SHEET    5  AB11 VAL A 114  ILE A 118  1  O  LEU A 115   N  VAL A 147           
SHEET    6  AB11 VAL A 197  GLU A 202  1  O  THR A 198   N  ILE A 116           
SHEET    7  AB11 ARG A 224  GLN A 228  1  O  ARG A 224   N  LEU A 199           
SHEET    8  AB11 GLN A 325  VAL A 331  1  O  GLN A 325   N  ALA A 225           
SHEET    9  AB11 ARG A 424  PHE A 430  1  O  ARG A 424   N  VAL A 326           
SHEET   10  AB11 GLN A 509  LEU A 513  1  O  VAL A 511   N  ILE A 429           
SHEET   11  AB11 VAL A 520  ARG A 522 -1  O  ARG A 521   N  TYR A 510           
SHEET    1  AC 2 VAL A  68  CYS A  69  0                                        
SHEET    2  AC 2 LEU A  92  SER A  93  1  N  SER A  93   O  VAL A  68           
SHEET    1  BA 3 LEU B   9  VAL B  10  0                                        
SHEET    2  BA 3 LEU B  17  ARG B  18 -1  O  LEU B  17   N  VAL B  10           
SHEET    3  BA 3 LEU B  60  ASP B  61  1  O  LEU B  60   N  ARG B  18           
SHEET    1  BB11 ILE B  20  ALA B  24  0                                        
SHEET    2  BB11 GLY B  27  PRO B  36 -1  O  GLY B  27   N  ALA B  24           
SHEET    3  BB11 TYR B  98  PRO B 104 -1  O  LEU B  99   N  GLY B  34           
SHEET    4  BB11 VAL B 145  MET B 149 -1  O  LEU B 146   N  TRP B 102           
SHEET    5  BB11 THR B 112  ILE B 118  1  O  PRO B 113   N  VAL B 145           
SHEET    6  BB11 GLY B 192  GLU B 202  1  N  ASP B 193   O  THR B 112           
SHEET    7  BB11 ARG B 224  GLN B 228  1  O  ARG B 224   N  LEU B 199           
SHEET    8  BB11 GLN B 325  VAL B 331  1  O  GLN B 325   N  ALA B 225           
SHEET    9  BB11 ARG B 424  PHE B 430  1  O  ARG B 424   N  VAL B 326           
SHEET   10  BB11 GLN B 509  LEU B 513  1  O  VAL B 511   N  ILE B 429           
SHEET   11  BB11 GLU B 519  ARG B 522 -1  O  GLU B 519   N  SER B 512           
SHEET    1  BC 2 VAL B  68  CYS B  69  0                                        
SHEET    2  BC 2 LEU B  92  SER B  93  1  N  SER B  93   O  VAL B  68           
SHEET    1  BD 2 VAL B 239  SER B 240  0                                        
SHEET    2  BD 2 VAL B 302  VAL B 303  1  N  VAL B 303   O  VAL B 239           
SHEET    1  CA 3 LEU C   9  VAL C  12  0                                        
SHEET    2  CA 3 GLY C  15  ARG C  18 -1  O  GLY C  15   N  VAL C  12           
SHEET    3  CA 3 VAL C  59  ASP C  61  1  O  LEU C  60   N  ARG C  18           
SHEET    1  CB11 ILE C  20  ALA C  24  0                                        
SHEET    2  CB11 GLY C  27  PRO C  36 -1  O  GLY C  27   N  ALA C  24           
SHEET    3  CB11 TYR C  98  PRO C 104 -1  O  LEU C  99   N  ILE C  35           
SHEET    4  CB11 VAL C 145  MET C 149 -1  O  LEU C 146   N  TRP C 102           
SHEET    5  CB11 THR C 112  ILE C 118  1  O  PRO C 113   N  VAL C 145           
SHEET    6  CB11 GLY C 192  GLU C 202  1  N  ASP C 193   O  THR C 112           
SHEET    7  CB11 ARG C 224  GLN C 228  1  O  ARG C 224   N  LEU C 199           
SHEET    8  CB11 GLN C 325  VAL C 331  1  O  GLN C 325   N  ALA C 225           
SHEET    9  CB11 ARG C 424  PHE C 430  1  O  ARG C 424   N  VAL C 326           
SHEET   10  CB11 GLN C 509  LEU C 513  1  O  VAL C 511   N  ILE C 429           
SHEET   11  CB11 VAL C 520  ARG C 522 -1  O  ARG C 521   N  TYR C 510           
SHEET    1  CC 2 VAL C  68  CYS C  69  0                                        
SHEET    2  CC 2 LEU C  92  SER C  93  1  N  SER C  93   O  VAL C  68           
SHEET    1  CD 2 VAL C 239  SER C 240  0                                        
SHEET    2  CD 2 VAL C 302  VAL C 303  1  N  VAL C 303   O  VAL C 239           
SHEET    1  DA 3 LEU D   9  VAL D  12  0                                        
SHEET    2  DA 3 GLY D  15  ARG D  18 -1  O  GLY D  15   N  VAL D  12           
SHEET    3  DA 3 VAL D  59  ASP D  61  1  O  LEU D  60   N  ARG D  18           
SHEET    1  DB11 ILE D  20  ALA D  24  0                                        
SHEET    2  DB11 GLY D  27  PRO D  36 -1  O  GLY D  27   N  ALA D  24           
SHEET    3  DB11 TYR D  98  PRO D 104 -1  O  LEU D  99   N  ILE D  35           
SHEET    4  DB11 VAL D 145  MET D 149 -1  O  LEU D 146   N  TRP D 102           
SHEET    5  DB11 THR D 112  ILE D 118  1  O  PRO D 113   N  VAL D 145           
SHEET    6  DB11 GLY D 192  GLU D 202  1  N  ASP D 193   O  THR D 112           
SHEET    7  DB11 ARG D 224  GLN D 228  1  O  ARG D 224   N  LEU D 199           
SHEET    8  DB11 GLN D 325  VAL D 331  1  O  GLN D 325   N  ALA D 225           
SHEET    9  DB11 ARG D 424  PHE D 430  1  O  ARG D 424   N  VAL D 326           
SHEET   10  DB11 GLN D 509  LEU D 513  1  O  VAL D 511   N  ILE D 429           
SHEET   11  DB11 GLU D 519  ARG D 522 -1  O  GLU D 519   N  SER D 512           
SHEET    1  DC 2 VAL D  68  CYS D  69  0                                        
SHEET    2  DC 2 LEU D  92  SER D  93  1  N  SER D  93   O  VAL D  68           
SSBOND   1 CYS A   69    CYS A   96                          1555   1555  2.05  
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.05  
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.04  
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.04  
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.05  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.04  
SSBOND   7 CYS C   69    CYS C   96                          1555   1555  2.04  
SSBOND   8 CYS C  257    CYS C  272                          1555   1555  2.06  
SSBOND   9 CYS C  409    CYS C  529                          1555   1555  2.04  
SSBOND  10 CYS D   69    CYS D   96                          1555   1555  2.04  
SSBOND  11 CYS D  257    CYS D  272                          1555   1555  2.05  
SSBOND  12 CYS D  409    CYS D  529                          1555   1555  2.05  
LINK         ND2 ASN A 265                 C1  NAG A 701     1555   1555  1.46  
LINK         P13 4OJ A 600                 OG  SER A 203     1555   1555  1.58  
LINK         ND2 ASN B 265                 C1  NAG B 701     1555   1555  1.45  
LINK         ND2 ASN B 350                 C1  NAG B 702     1555   1555  1.46  
LINK         P13 4OJ B 600                 OG  SER B 203     1555   1555  1.56  
LINK         P13 4OJ C 600                 OG  SER C 203     1555   1555  1.59  
LINK         ND2 ASN D 265                 C1  NAG D 701     1555   1555  1.44  
LINK         ND2 ASN D 350                 C1  NAG D 702     1555   1555  1.47  
LINK         ND2 ASN D 464                 C1  NAG D 703     1555   1555  1.45  
LINK         P13 4OJ D 600                 OG  SER D 203     1555   1555  1.58  
CISPEP   1 TYR A  105    PRO A  106          0         0.86                     
CISPEP   2 PRO A  258    PRO A  259          0       -13.89                     
CISPEP   3 TYR B  105    PRO B  106          0        12.49                     
CISPEP   4 CYS B  257    PRO B  258          0        -6.88                     
CISPEP   5 SER B  495    LYS B  496          0        -8.68                     
CISPEP   6 SER B  497    PRO B  498          0        -0.35                     
CISPEP   7 TYR C  105    PRO C  106          0        -1.65                     
CISPEP   8 TYR D  105    PRO D  106          0         6.20                     
SITE     1 AC1  8 TRP A  86  GLY A 121  GLY A 122  GLU A 202                    
SITE     2 AC1  8 SER A 203  ALA A 204  HOH A2042  HOH A2101                    
SITE     1 AC2  8 TRP B  86  GLY B 121  GLY B 122  TYR B 124                    
SITE     2 AC2  8 GLU B 202  SER B 203  ALA B 204  HIS B 447                    
SITE     1 AC3  8 GLY C 121  GLY C 122  GLU C 202  SER C 203                    
SITE     2 AC3  8 ALA C 204  HIS C 447  HOH C2048  HOH C2100                    
SITE     1 AC4  1 ASN C 265                                                     
SITE     1 AC5  9 GLY D 121  GLY D 122  GLU D 202  SER D 203                    
SITE     2 AC5  9 ALA D 204  PHE D 295  PHE D 297  HIS D 447                    
SITE     3 AC5  9 HOH D2088                                                     
SITE     1 AC6  2 ARG C  11  HOH C2005                                          
SITE     1 AC7  1 ARG C 136                                                     
SITE     1 AC8  1 ARG C 356                                                     
SITE     1 AC9  1 ARG D 136                                                     
SITE     1 BC1  1 ARG D  90                                                     
SITE     1 BC2  2 GLN C 413  ARG C 417                                          
SITE     1 BC3  3 ARG B 525  GLN B 527  THR B 528                               
SITE     1 BC4  4 ARG A 525  ALA A 526  GLN A 527  THR A 528                    
SITE     1 BC5  4 GLN A 413  ARG A 417  HOH A2113  HOH A2115                    
SITE     1 BC6  4 ARG D 525  ALA D 526  GLN D 527  THR D 528                    
SITE     1 BC7  4 ARG C 525  ALA C 526  GLN C 527  THR C 528                    
SITE     1 BC8  1 ARG A 356                                                     
SITE     1 BC9  3 GLN B 413  ARG B 417  HOH B2082                               
SITE     1 CC1  5 LEU C 380  HIS C 381  PHE C 531  LEU D 380                    
SITE     2 CC1  5 HIS D 381                                                     
SITE     1 CC2  4 LEU A 380  HIS A 381  LEU B 380  HIS B 381                    
SITE     1 CC3  3 HOH C2115  ARG D 356  LEU D 360                               
SITE     1 CC4  2 ARG B 356  LEU B 360                                          
SITE     1 CC5  1 ARG A 136                                                     
SITE     1 CC6  2 GLN D 413  ARG D 417                                          
SITE     1 CC7  1 ASN A 265                                                     
SITE     1 CC8  3 ASN B 265  THR B 267  GLU B 268                               
SITE     1 CC9  2 SER B 347  ASN B 350                                          
SITE     1 DC1  1 ASN D 265                                                     
SITE     1 DC2  3 SER D 347  ASN D 350  GLN D 358                               
SITE     1 DC3  2 SER D 462  ASN D 464                                          
CRYST1  136.940  174.040  225.620  90.00  90.00  90.00 P 21 21 21   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      0.007302  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005746  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004432        0.00000                         
TER    4216      THR A 543                                                      
TER    8408      THR B 543                                                      
TER   12609      THR C 543                                                      
TER   16810      THR D 543                                                      
MASTER      792    0   32  101   68    0   36    617432    4  242  168          
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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