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Database: PDB
Entry: 4B7Z
LinkDB: 4B7Z
Original site: 4B7Z 
HEADER    HYDROLASE                               24-AUG-12   4B7Z              
TITLE     MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH N-(2-DIETHYLAMINO-  
TITLE    2 ETHYL)-1-(4-METHYLPHENYL)-METHANESULFONAMIDE                         
CAVEAT     4B7Z    NAG A 1548 HAS WRONG CHIRALITY AT ATOM C1                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 32-574;                         
COMPND   5 SYNONYM: ACHE;                                                       
COMPND   6 EC: 3.1.1.7;                                                         
COMPND   7 ENGINEERED: YES                                                      
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: HOMO SAPIENS;                                     
SOURCE   6 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HEK 293F;                               
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1                                  
KEYWDS    HYDROLASE, INHIBITOR                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.D.ANDERSSON,N.FORSGREN,C.AKFUR,A.ALLGARDSSON,L.BERG,W.QIAN,         
AUTHOR   2 F.EKSTROM,A.LINUSSON                                                 
REVDAT   6   20-DEC-23 4B7Z    1       HETSYN                                   
REVDAT   5   29-JUL-20 4B7Z    1       CAVEAT COMPND REMARK HETNAM              
REVDAT   5 2                   1       LINK   SITE                              
REVDAT   4   17-JAN-18 4B7Z    1       REMARK                                   
REVDAT   3   30-OCT-13 4B7Z    1       JRNL                                     
REVDAT   2   11-SEP-13 4B7Z    1       JRNL                                     
REVDAT   1   04-SEP-13 4B7Z    0                                                
JRNL        AUTH   C.D.ANDERSSON,N.FORSGREN,C.AKFUR,A.ALLGARDSSON,L.BERG,       
JRNL        AUTH 2 C.ENGDAHL,W.QIAN,F.J.EKSTROM,A.LINUSSON                      
JRNL        TITL   DIVERGENT STRUCTURE-ACTIVITY RELATIONSHIPS OF STRUCTURALLY   
JRNL        TITL 2 SIMILAR ACETYLCHOLINESTERASE INHIBITORS.                     
JRNL        REF    J.MED.CHEM.                   V.  56  7615 2013              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   23984975                                                     
JRNL        DOI    10.1021/JM400990P                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.3_928)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.80                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 90244                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.201                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1784                            
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 28.7990 -  5.3971    0.99     7113   139  0.1834 0.1890        
REMARK   3     2  5.3971 -  4.2884    1.00     6923   134  0.1379 0.1567        
REMARK   3     3  4.2884 -  3.7476    1.00     6862   135  0.1401 0.1818        
REMARK   3     4  3.7476 -  3.4056    1.00     6813   147  0.1579 0.2123        
REMARK   3     5  3.4056 -  3.1618    1.00     6811   120  0.1714 0.1913        
REMARK   3     6  3.1618 -  2.9756    1.00     6761   150  0.1691 0.1834        
REMARK   3     7  2.9756 -  2.8267    1.00     6765   138  0.1761 0.2097        
REMARK   3     8  2.8267 -  2.7038    1.00     6778   135  0.1974 0.2218        
REMARK   3     9  2.7038 -  2.5997    1.00     6706   149  0.2172 0.2871        
REMARK   3    10  2.5997 -  2.5101    1.00     6744   145  0.2172 0.2796        
REMARK   3    11  2.5101 -  2.4316    1.00     6724   118  0.2183 0.2156        
REMARK   3    12  2.4316 -  2.3622    1.00     6716   130  0.2276 0.2786        
REMARK   3    13  2.3622 -  2.3000    1.00     6744   144  0.2296 0.2554        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.98                                          
REMARK   3   K_SOL              : 0.35                                          
REMARK   3   B_SOL              : 62.03                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.290            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.290           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 42.97                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.61                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.33200                                             
REMARK   3    B22 (A**2) : 3.05820                                              
REMARK   3    B33 (A**2) : -1.72610                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           8784                                  
REMARK   3   ANGLE     :  1.086          11948                                  
REMARK   3   CHIRALITY :  0.077           1277                                  
REMARK   3   PLANARITY :  0.005           1553                                  
REMARK   3   DIHEDRAL  : 17.868           3214                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 11                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 1:228)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  30.7953  11.5420  29.3660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1901 T22:   0.1802                                     
REMARK   3      T33:   0.2103 T12:  -0.0062                                     
REMARK   3      T13:  -0.0112 T23:   0.0396                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5765 L22:   1.0172                                     
REMARK   3      L33:   2.7638 L12:  -0.0988                                     
REMARK   3      L13:  -0.1303 L23:  -0.2103                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0227 S12:  -0.1189 S13:  -0.0107                       
REMARK   3      S21:   0.1219 S22:   0.0154 S23:  -0.0387                       
REMARK   3      S31:   0.1399 S32:   0.0828 S33:   0.0134                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 229:331)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  39.9413   9.8054  10.5020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2603 T22:   0.2375                                     
REMARK   3      T33:   0.2451 T12:   0.0589                                     
REMARK   3      T13:   0.0376 T23:   0.0141                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5045 L22:   1.0650                                     
REMARK   3      L33:   2.3764 L12:   0.8468                                     
REMARK   3      L13:   0.2906 L23:  -0.3523                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0619 S12:   0.1696 S13:  -0.2285                       
REMARK   3      S21:  -0.0796 S22:  -0.0287 S23:  -0.2235                       
REMARK   3      S31:   0.3030 S32:   0.3927 S33:   0.0745                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 332:486)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  18.3198  17.6387   6.6510              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1499 T22:   0.2283                                     
REMARK   3      T33:   0.2458 T12:  -0.0274                                     
REMARK   3      T13:  -0.0261 T23:   0.0153                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1271 L22:   1.2134                                     
REMARK   3      L33:   3.1770 L12:   0.0642                                     
REMARK   3      L13:   0.1004 L23:  -0.4578                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0290 S12:   0.0774 S13:   0.0006                       
REMARK   3      S21:  -0.0926 S22:   0.0274 S23:   0.1607                       
REMARK   3      S31:   0.0393 S32:  -0.3399 S33:  -0.0067                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 487:513)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   6.3052   1.6734  14.7315              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3242 T22:   0.5971                                     
REMARK   3      T33:   0.4400 T12:  -0.2027                                     
REMARK   3      T13:  -0.0207 T23:   0.0487                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3860 L22:   8.4780                                     
REMARK   3      L33:   3.0491 L12:   0.0188                                     
REMARK   3      L13:   1.3876 L23:  -3.0132                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0011 S12:  -0.1832 S13:  -0.3506                       
REMARK   3      S21:   0.4039 S22:   0.1323 S23:   0.8798                       
REMARK   3      S31:   0.5221 S32:  -1.3913 S33:  -0.0476                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN A AND (RESSEQ 514:542)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  17.0961   6.6215  -0.7443              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2341 T22:   0.2995                                     
REMARK   3      T33:   0.2214 T12:  -0.0897                                     
REMARK   3      T13:  -0.1003 T23:  -0.0088                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5603 L22:   2.2088                                     
REMARK   3      L33:   4.9592 L12:  -0.9867                                     
REMARK   3      L13:  -2.1768 L23:   0.9395                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0192 S12:   0.1009 S13:  -0.1719                       
REMARK   3      S21:  -0.1237 S22:  -0.1484 S23:   0.2718                       
REMARK   3      S31:   0.5139 S32:  -0.2847 S33:   0.0900                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 4:45)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.8034   5.9812 -61.6916              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2667 T22:   0.2695                                     
REMARK   3      T33:   0.2672 T12:   0.0416                                     
REMARK   3      T13:  -0.1173 T23:  -0.1077                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5521 L22:   2.5365                                     
REMARK   3      L33:   4.6284 L12:  -0.9053                                     
REMARK   3      L13:  -0.9867 L23:   0.3309                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0424 S12:   0.5762 S13:   0.1250                       
REMARK   3      S21:  -0.4695 S22:  -0.1078 S23:   0.4213                       
REMARK   3      S31:  -0.2929 S32:  -0.6604 S33:  -0.0057                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 46:158)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   2.2447   1.1306 -51.2632              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2852 T22:   0.3123                                     
REMARK   3      T33:   0.3072 T12:  -0.0282                                     
REMARK   3      T13:  -0.0607 T23:  -0.0927                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9556 L22:   1.0202                                     
REMARK   3      L33:   2.4713 L12:  -0.0017                                     
REMARK   3      L13:  -0.1277 L23:   0.5180                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0822 S12:   0.1910 S13:  -0.1725                       
REMARK   3      S21:  -0.1562 S22:  -0.0473 S23:   0.1773                       
REMARK   3      S31:   0.2938 S32:  -0.2141 S33:  -0.0378                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 159:331)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  17.0992   5.3621 -45.8510              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1713 T22:   0.2740                                     
REMARK   3      T33:   0.2236 T12:  -0.0199                                     
REMARK   3      T13:  -0.0271 T23:  -0.0437                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4414 L22:   2.2228                                     
REMARK   3      L33:   2.4788 L12:  -0.6325                                     
REMARK   3      L13:   0.0151 L23:   0.7504                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0757 S12:   0.1870 S13:   0.0274                       
REMARK   3      S21:  -0.0072 S22:   0.0217 S23:  -0.2365                       
REMARK   3      S31:   0.0896 S32:   0.4016 S33:  -0.0966                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 332:486)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   4.3296   2.1532 -26.6972              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3665 T22:   0.2459                                     
REMARK   3      T33:   0.3083 T12:  -0.0502                                     
REMARK   3      T13:   0.0124 T23:  -0.0537                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4315 L22:   1.6101                                     
REMARK   3      L33:   2.7191 L12:  -0.1963                                     
REMARK   3      L13:   0.6532 L23:  -0.0928                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1605 S12:  -0.1360 S13:  -0.1579                       
REMARK   3      S21:   0.2645 S22:  -0.0904 S23:   0.1347                       
REMARK   3      S31:   0.4062 S32:  -0.1922 S33:  -0.0883                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 487:513)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.7116  22.3636 -28.5929              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3582 T22:   0.2444                                     
REMARK   3      T33:   0.4185 T12:   0.0370                                     
REMARK   3      T13:   0.0485 T23:  -0.0530                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8504 L22:   4.9483                                     
REMARK   3      L33:   9.3840 L12:   0.9271                                     
REMARK   3      L13:   1.3401 L23:  -1.5298                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0069 S12:  -0.2883 S13:   0.7693                       
REMARK   3      S21:   0.2373 S22:   0.1267 S23:   0.7816                       
REMARK   3      S31:  -0.7455 S32:  -0.5105 S33:  -0.0754                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN B AND (RESSEQ 514:543)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  12.7370  11.3756 -21.3522              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3801 T22:   0.2832                                     
REMARK   3      T33:   0.1813 T12:  -0.0398                                     
REMARK   3      T13:   0.0251 T23:  -0.0312                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0129 L22:   2.0649                                     
REMARK   3      L33:   3.9296 L12:   0.0059                                     
REMARK   3      L13:   4.4969 L23:  -0.1946                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2323 S12:   0.2270 S13:  -0.1809                       
REMARK   3      S21:   0.2045 S22:  -0.1174 S23:  -0.0032                       
REMARK   3      S31:   0.0889 S32:   0.3944 S33:  -0.0858                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: DUE TO INSUFFICIENT ELECTRON DENSITY      
REMARK   3  THE FOLLOWING RESIDUES WERE NOT MODELED: CHAIN A 258-264 AND 543-   
REMARK   3  548, CHAIN B 1-3, 258-264 AND 544-548. DUE TO INSUFFICIENT          
REMARK   3  ELECTRON DENSITY THE FOLLOWING RESIDUES WERE MODELED AS ALANINES,   
REMARK   3  CHAIN A 496 AND CHAIN B 493.                                        
REMARK   4                                                                      
REMARK   4 4B7Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-AUG-12.                  
REMARK 100 THE DEPOSITION ID IS D_1290053834.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JAN-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I911-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.039                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 90383                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.120                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 5.900                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1J06                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 27-30% (V/V) PEG750MME, 0.1 M HEPES PH   
REMARK 280  7.0-7.1                                                             
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       39.65350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.36900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.91650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      113.36900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.65350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.91650            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38240 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.6 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 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     PRO A   258                                                      
REMARK 465     PRO A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     ALA A   262                                                      
REMARK 465     GLY A   263                                                      
REMARK 465     GLY A   264                                                      
REMARK 465     THR A   543                                                      
REMARK 465     ALA A   544                                                      
REMARK 465     THR A   545                                                      
REMARK 465     GLU A   546                                                      
REMARK 465     ALA A   547                                                      
REMARK 465     PRO A   548                                                      
REMARK 465     GLU B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     PRO B   258                                                      
REMARK 465     PRO B   259                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     GLY B   261                                                      
REMARK 465     ALA B   262                                                      
REMARK 465     GLY B   263                                                      
REMARK 465     GLY B   264                                                      
REMARK 465     THR B   545                                                      
REMARK 465     GLU B   546                                                      
REMARK 465     ALA B   547                                                      
REMARK 465     PRO B   548                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 496    CG   CD   CE   NZ                                   
REMARK 470     ARG B 493    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ALA B 544    CA   C    O    CB                                   
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   OG   SER A   203     O    HOH A  2151              2.08            
REMARK 500   O    HOH A  2099     O    HOH A  2140              2.09            
REMARK 500   O    HOH A  2098     O    HOH A  2099              2.10            
REMARK 500   O    CYS B   257     O    HOH B  2193              2.10            
REMARK 500   NH1  ARG A    45     OE1  GLU A    51              2.12            
REMARK 500   O    HOH A  2115     O    HOH A  2236              2.12            
REMARK 500   O    HOH A  2042     O    HOH A  2128              2.17            
REMARK 500   O    HOH B  2284     O    HOH B  2288              2.19            
REMARK 500   O    HOH B  2086     O    HOH B  2179              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A  47       -2.46     72.86                                   
REMARK 500    ALA A  62       50.90   -118.74                                   
REMARK 500    SER A 203     -121.31     60.15                                   
REMARK 500    ASP A 306      -87.85   -127.04                                   
REMARK 500    VAL A 407      -61.19   -129.38                                   
REMARK 500    ARG A 493        5.56    -69.42                                   
REMARK 500    SER A 541       35.33    -82.79                                   
REMARK 500    PHE B  47       -6.69     77.43                                   
REMARK 500    PHE B 158       -1.73   -141.12                                   
REMARK 500    ALA B 167       73.90   -154.39                                   
REMARK 500    SER B 203     -120.13     58.92                                   
REMARK 500    ASP B 306      -85.74   -125.31                                   
REMARK 500    VAL B 407      -61.25   -126.72                                   
REMARK 500    SER B 495     -177.42    -67.86                                   
REMARK 500    LYS B 496      114.56    -24.90                                   
REMARK 500    SER B 541       34.72    -74.26                                   
REMARK 500    ALA B 542        4.05   -168.65                                   
REMARK 500    THR B 543      -80.00     54.14                                   
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 A2122        DISTANCE =  7.15 ANGSTROMS                       
REMARK 525    HOH A2154        DISTANCE =  6.05 ANGSTROMS                       
REMARK 525    HOH A2157        DISTANCE =  6.35 ANGSTROMS                       
REMARK 525    HOH A2165        DISTANCE =  7.36 ANGSTROMS                       
REMARK 525    HOH B2335        DISTANCE =  6.93 ANGSTROMS                       
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 APOFORM       
REMARK 900 RELATED ID: 1J07   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE- DECIDIUM        
REMARK 900 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, 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- GALLAMINE       
REMARK 900 COMPLEX                                                              
REMARK 900 RELATED ID: 1N5R   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE- PROPIDIUM       
REMARK 900 COMPLEX                                                              
REMARK 900 RELATED ID: 1Q83   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE- TZ2PA6SYN       
REMARK 900 COMPLEX                                                              
REMARK 900 RELATED ID: 1Q84   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE- TZ2PA6ANTI      
REMARK 900 COMPLEX                                                              
REMARK 900 RELATED ID: 2C0P   RELATED DB: PDB                                   
REMARK 900 AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY TABUN           
REMARK 900 RELATED ID: 2C0Q   RELATED DB: PDB                                   
REMARK 900 NON-AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY TABUN       
REMARK 900 RELATED ID: 2H9Y   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE COMPLEXEDWITH M-(N,  
REMARK 900 N,N-TRIMETHYLAMMONIO) TRIFLUOROACETOPHENONE                          
REMARK 900 RELATED ID: 2HA0   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE COMPLEXEDWITH 4-     
REMARK 900 KETOAMYLTRIMETHYLAMMONIUM                                            
REMARK 900 RELATED ID: 2HA2   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE COMPLEXEDWITH        
REMARK 900 SUCCINYLCHOLINE                                                      
REMARK 900 RELATED ID: 2HA3   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE COMPLEXEDWITH        
REMARK 900 CHOLINE                                                              
REMARK 900 RELATED ID: 2HA4   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF MOUSEACETYLCHOLINESTERASE       
REMARK 900 COMPLEXED WITH ACETYLCHOLINE                                         
REMARK 900 RELATED ID: 2HA5   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF ACETYLCHOLINESTERASECOMPLEXED   
REMARK 900 WITH ACETYLTHIOCHOLINE                                               
REMARK 900 RELATED ID: 2HA6   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF MOUSEACETYLCHOLINESTERASE       
REMARK 900 COMPLEXED WITH SUCCINYLCHOLINE                                       
REMARK 900 RELATED ID: 2HA7   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF MOUSEACETYLCHOLINESTERASE       
REMARK 900 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 AND HLO-7    
REMARK 900 RELATED ID: 2JF0   RELATED DB: PDB                                   
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH TABUN AND ORTHO-7  
REMARK 900 RELATED ID: 2JGE   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY NON-    
REMARK 900 AGED METHAMIDOPHOS                                                   
REMARK 900 RELATED ID: 2JGF   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY NON-    
REMARK 900 AGED FENAMIPHOS                                                      
REMARK 900 RELATED ID: 2JGG   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY NON-    
REMARK 900 AGED SARIN                                                           
REMARK 900 RELATED ID: 2JGH   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY NON-    
REMARK 900 AGED VX                                                              
REMARK 900 RELATED ID: 2JGI   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY NON-    
REMARK 900 AGED DIISOPROPYL FLUOROPHOSPHATE (DFP)                               
REMARK 900 RELATED ID: 2JGJ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY AGED    
REMARK 900 METHAMIDOPHOS                                                        
REMARK 900 RELATED ID: 2JGK   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY AGED    
REMARK 900 FENAMIPHOS                                                           
REMARK 900 RELATED ID: 2JGL   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY AGED    
REMARK 900 VX AND SARIN                                                         
REMARK 900 RELATED ID: 2JGM   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY AGED    
REMARK 900 DIISOPROPYL FLUOROPHOSPHATE (DFP)                                    
REMARK 900 RELATED ID: 2WHP   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE, PHOSPHONYLATED BY SARIN   
REMARK 900 AND IN COMPLEX WITH HI-6                                             
REMARK 900 RELATED ID: 2WHQ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE, PHOSPHONYLATED BY SARIN   
REMARK 900 (AGED) IN COMPLEX WITH HI-6                                          
REMARK 900 RELATED ID: 2WHR   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE IN COMPLEX WITH K027       
REMARK 900 RELATED ID: 2WLS   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX    
REMARK 900 WITH AMTS13                                                          
REMARK 900 RELATED ID: 2WU3   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN COMPLEX WITH      
REMARK 900 FENAMIPHOS AND HI-6                                                  
REMARK 900 RELATED ID: 2WU4   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN COMPLEX WITH      
REMARK 900 FENAMIPHOS AND ORTHO-7                                               
REMARK 900 RELATED ID: 2XUD   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE Y337A MUTANT OF MOUSE ACETYLCHOLINESTERASE  
REMARK 900 RELATED ID: 2XUF   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (1 MTH)         
REMARK 900 RELATED ID: 2XUG   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (1 WK)          
REMARK 900 RELATED ID: 2XUH   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI COMPLEX (10 MTH)        
REMARK 900 RELATED ID: 2XUI   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (1 WK)           
REMARK 900 RELATED ID: 2XUJ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (1 MTH)          
REMARK 900 RELATED ID: 2XUK   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN COMPLEX (10 MTH)         
REMARK 900 RELATED ID: 2XUO   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MACHE-Y337A MUTANT IN COMPLEX WITH SOAKED       
REMARK 900 TZ2PA6 ANTI INHIBITOR                                                
REMARK 900 RELATED ID: 2XUP   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE MACHE-Y337A MUTANT IN COMPLEX WITH SOAKED   
REMARK 900 TZ2PA6 SYN INHIBITOR                                                 
REMARK 900 RELATED ID: 2XUQ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE MACHE-Y337A MUTANT IN COMPLEX WITH SOAKED   
REMARK 900 TZ2PA6 ANTI-SYN INHIBITORS                                           
REMARK 900 RELATED ID: 4A16   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF MOUSE ACETYLCHOLINESTERASE COMPLEX WITH HUPRINE         
REMARK 900 DERIVATIVE                                                           
REMARK 900 RELATED ID: 4A23   RELATED DB: PDB                                   
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH RACEMIC C5685      
REMARK 900 RELATED ID: 4ARA   RELATED DB: PDB                                   
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH (R)- C5685 AT 2.5  
REMARK 900 A RESOLUTION.                                                        
REMARK 900 RELATED ID: 4ARB   RELATED DB: PDB                                   
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH (S)- C5685 AT      
REMARK 900 2.25 A RESOLUTION.                                                   
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 C-(4- CHLORO-      
REMARK 900 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- CHLORANYL-N-(2- 
REMARK 900 DIETHYLAMINO-ETHYL)-BENZENESULFONAMIDE                               
DBREF  4B7Z A    1   545  UNP    P21836   ACES_MOUSE      32    576             
DBREF  4B7Z B    1   545  UNP    P21836   ACES_MOUSE      32    576             
SEQADV 4B7Z GLU A  546  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B7Z ALA A  547  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B7Z PRO A  548  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B7Z GLU B  546  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B7Z ALA B  547  UNP  P21836              EXPRESSION TAG                 
SEQADV 4B7Z PRO B  548  UNP  P21836              EXPRESSION TAG                 
SEQRES   1 A  548  GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG          
SEQRES   2 A  548  GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY          
SEQRES   3 A  548  GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU          
SEQRES   4 A  548  PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO          
SEQRES   5 A  548  LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE          
SEQRES   6 A  548  GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO          
SEQRES   7 A  548  GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU          
SEQRES   8 A  548  LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO          
SEQRES   9 A  548  TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP          
SEQRES  10 A  548  ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU          
SEQRES  11 A  548  ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY          
SEQRES  12 A  548  ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE          
SEQRES  13 A  548  GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY          
SEQRES  14 A  548  ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP          
SEQRES  15 A  548  VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET          
SEQRES  16 A  548  SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER          
SEQRES  17 A  548  VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU          
SEQRES  18 A  548  PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY          
SEQRES  19 A  548  PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG          
SEQRES  20 A  548  ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY          
SEQRES  21 A  548  GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU          
SEQRES  22 A  548  ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP          
SEQRES  23 A  548  HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE          
SEQRES  24 A  548  VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO          
SEQRES  25 A  548  GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN          
SEQRES  26 A  548  VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE          
SEQRES  27 A  548  LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU          
SEQRES  28 A  548  SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG          
SEQRES  29 A  548  ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA          
SEQRES  30 A  548  VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP          
SEQRES  31 A  548  PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY          
SEQRES  32 A  548  ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY          
SEQRES  33 A  548  ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE          
SEQRES  34 A  548  PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP          
SEQRES  35 A  548  MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE          
SEQRES  36 A  548  GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU          
SEQRES  37 A  548  GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR          
SEQRES  38 A  548  ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP          
SEQRES  39 A  548  SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA          
SEQRES  40 A  548  GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL          
SEQRES  41 A  548  ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN          
SEQRES  42 A  548  ARG PHE LEU PRO LYS LEU LEU SER ALA THR ALA THR GLU          
SEQRES  43 A  548  ALA PRO                                                      
SEQRES   1 B  548  GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG          
SEQRES   2 B  548  GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY          
SEQRES   3 B  548  GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU          
SEQRES   4 B  548  PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO          
SEQRES   5 B  548  LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE          
SEQRES   6 B  548  GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO          
SEQRES   7 B  548  GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU          
SEQRES   8 B  548  LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO          
SEQRES   9 B  548  TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP          
SEQRES  10 B  548  ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU          
SEQRES  11 B  548  ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY          
SEQRES  12 B  548  ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE          
SEQRES  13 B  548  GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY          
SEQRES  14 B  548  ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP          
SEQRES  15 B  548  VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET          
SEQRES  16 B  548  SER VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER          
SEQRES  17 B  548  VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU          
SEQRES  18 B  548  PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY          
SEQRES  19 B  548  PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG          
SEQRES  20 B  548  ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY          
SEQRES  21 B  548  GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU          
SEQRES  22 B  548  ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP          
SEQRES  23 B  548  HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE          
SEQRES  24 B  548  VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO          
SEQRES  25 B  548  GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN          
SEQRES  26 B  548  VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE          
SEQRES  27 B  548  LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU          
SEQRES  28 B  548  SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG          
SEQRES  29 B  548  ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA          
SEQRES  30 B  548  VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP          
SEQRES  31 B  548  PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY          
SEQRES  32 B  548  ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY          
SEQRES  33 B  548  ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE          
SEQRES  34 B  548  PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP          
SEQRES  35 B  548  MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE          
SEQRES  36 B  548  GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU          
SEQRES  37 B  548  GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR          
SEQRES  38 B  548  ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP          
SEQRES  39 B  548  SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA          
SEQRES  40 B  548  GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL          
SEQRES  41 B  548  ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN          
SEQRES  42 B  548  ARG PHE LEU PRO LYS LEU LEU SER ALA THR ALA THR GLU          
SEQRES  43 B  548  ALA PRO                                                      
MODRES 4B7Z ASN A  350  ASN  GLYCOSYLATION SITE                                 
MODRES 4B7Z ASN A  464  ASN  GLYCOSYLATION SITE                                 
MODRES 4B7Z ASN B  350  ASN  GLYCOSYLATION SITE                                 
HET    Q4Q  A 600      19                                                       
HET    PEG  A1543       7                                                       
HET    P6G  A1544      19                                                       
HET    PEG  A1545       7                                                       
HET    NAG  A1546      14                                                       
HET    PEG  A1547       7                                                       
HET    NAG  A1548      14                                                       
HET    PEG  A1549       7                                                       
HET    PEG  A1550       7                                                       
HET    PEG  A1551       7                                                       
HET    PEG  A1552       7                                                       
HET    SO4  A1553       5                                                       
HET    Q4Q  B 600      19                                                       
HET    PEG  B1544       7                                                       
HET    PEG  B1545       7                                                       
HET    PEG  B1546       7                                                       
HET    NAG  B1547      14                                                       
HET    PEG  B1548       7                                                       
HET    SO4  B1549       5                                                       
HET    PEG  B1550       7                                                       
HET    PEG  B1551       7                                                       
HETNAM     Q4Q N-[2-(DIETHYLAMINO)ETHYL]-1-(4-METHYLPHENYL)                     
HETNAM   2 Q4Q  METHANESULFONAMIDE                                              
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     P6G HEXAETHYLENE GLYCOL                                              
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     SO4 SULFATE ION                                                      
HETSYN     P6G POLYETHYLENE GLYCOL PEG400                                       
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
FORMUL   3  Q4Q    2(C14 H24 N2 O2 S)                                           
FORMUL   4  PEG    13(C4 H10 O3)                                                
FORMUL   5  P6G    C12 H26 O7                                                   
FORMUL   7  NAG    3(C8 H15 N O6)                                               
FORMUL  14  SO4    2(O4 S 2-)                                                   
FORMUL  24  HOH   *748(H2 O)                                                    
HELIX    1   1 ASP A    5  GLN A    7  5                                   3    
HELIX    2   2 VAL A   42  ARG A   46  5                                   5    
HELIX    3   3 PHE A   80  MET A   85  1                                   6    
HELIX    4   4 LEU A  130  ASP A  134  5                                   5    
HELIX    5   5 GLY A  135  GLY A  143  1                                   9    
HELIX    6   6 VAL A  153  LEU A  159  1                                   7    
HELIX    7   7 ASN A  170  ILE A  187  1                                  18    
HELIX    8   8 ALA A  188  PHE A  190  5                                   3    
HELIX    9   9 SER A  203  SER A  215  1                                  13    
HELIX   10  10 SER A  215  SER A  220  1                                   6    
HELIX   11  11 SER A  240  VAL A  255  1                                  16    
HELIX   12  12 ASN A  265  ARG A  274  1                                  10    
HELIX   13  13 PRO A  277  GLU A  285  1                                   9    
HELIX   14  14 TRP A  286  LEU A  289  5                                   4    
HELIX   15  15 THR A  311  GLY A  319  1                                   9    
HELIX   16  16 GLY A  335  VAL A  340  1                                   6    
HELIX   17  17 SER A  355  VAL A  367  1                                  13    
HELIX   18  18 SER A  371  THR A  383  1                                  13    
HELIX   19  19 ASP A  390  VAL A  407  1                                  18    
HELIX   20  20 VAL A  407  GLN A  421  1                                  15    
HELIX   21  21 PRO A  440  GLY A  444  5                                   5    
HELIX   22  22 GLU A  450  PHE A  455  1                                   6    
HELIX   23  23 GLY A  456  ASP A  460  5                                   5    
HELIX   24  24 ASP A  460  ASN A  464  5                                   5    
HELIX   25  25 THR A  466  GLY A  487  1                                  22    
HELIX   26  26 ARG A  525  ARG A  534  1                                  10    
HELIX   27  27 ARG A  534  SER A  541  1                                   8    
HELIX   28  28 ASP B    5  GLN B    7  5                                   3    
HELIX   29  29 VAL B   42  ARG B   46  5                                   5    
HELIX   30  30 PHE B   80  MET B   85  1                                   6    
HELIX   31  31 LEU B  130  ASP B  134  5                                   5    
HELIX   32  32 GLY B  135  GLY B  143  1                                   9    
HELIX   33  33 VAL B  153  LEU B  159  1                                   7    
HELIX   34  34 ASN B  170  ILE B  187  1                                  18    
HELIX   35  35 ALA B  188  PHE B  190  5                                   3    
HELIX   36  36 SER B  203  SER B  215  1                                  13    
HELIX   37  37 SER B  215  SER B  220  1                                   6    
HELIX   38  38 SER B  240  VAL B  255  1                                  16    
HELIX   39  39 ASN B  265  THR B  275  1                                  11    
HELIX   40  40 PRO B  277  ASP B  283  1                                   7    
HELIX   41  41 HIS B  284  LEU B  289  5                                   6    
HELIX   42  42 THR B  311  GLY B  319  1                                   9    
HELIX   43  43 GLY B  335  VAL B  340  1                                   6    
HELIX   44  44 SER B  355  VAL B  367  1                                  13    
HELIX   45  45 SER B  371  THR B  383  1                                  13    
HELIX   46  46 ASP B  390  VAL B  407  1                                  18    
HELIX   47  47 VAL B  407  GLN B  421  1                                  15    
HELIX   48  48 PRO B  440  GLY B  444  5                                   5    
HELIX   49  49 GLU B  450  PHE B  455  1                                   6    
HELIX   50  50 GLY B  456  ASP B  460  5                                   5    
HELIX   51  51 ASP B  460  ASN B  464  5                                   5    
HELIX   52  52 THR B  466  GLY B  487  1                                  22    
HELIX   53  53 ARG B  525  ARG B  534  1                                  10    
HELIX   54  54 ARG B  534  SER B  541  1                                   8    
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  ALA A  24  0                                        
SHEET    2  AB11 GLY A  27  PRO A  36 -1  O  GLY A  27   N  ALA A  24           
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 THR A 112  ILE A 118  1  O  PRO A 113   N  VAL A 145           
SHEET    6  AB11 GLY A 192  GLU A 202  1  N  ASP A 193   O  THR A 112           
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 GLU A 519  ARG A 522 -1  O  GLU A 519   N  SER A 512           
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  12  0                                        
SHEET    2  BA 3 GLY B  15  ARG B  18 -1  O  GLY B  15   N  VAL B  12           
SHEET    3  BA 3 VAL B  59  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  ILE B  35           
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           
SSBOND   1 CYS A   69    CYS A   96                          1555   1555  2.06  
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.06  
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.05  
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.06  
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.06  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.06  
LINK         ND2 ASN A 350                 C1  NAG A1546     1555   1555  1.46  
LINK         ND2 ASN A 464                 C1  NAG A1548     1555   1555  1.45  
LINK         ND2 ASN B 350                 C1  NAG B1547     1555   1555  1.45  
CISPEP   1 TYR A  105    PRO A  106          0        -1.60                     
CISPEP   2 TYR B  105    PRO B  106          0         0.01                     
CISPEP   3 SER B  497    PRO B  498          0       -10.99                     
CRYST1   79.307  111.833  226.738  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012609  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008942  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004410        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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