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LongText Report for: 2XUQ-pdb

Name Class
2XUQ-pdb
HEADER    HYDROLASE                               20-OCT-10   2XUQ              
TITLE     CRYSTAL STRUCTURE OF THE MACHE-Y337A MUTANT IN COMPLEX WITH           
TITLE    2 SOAKED TZ2PA6 ANTI-SYN INHIBITORS                                    
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;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 STRAIN: BLACK6CBA CROSS F1;                                          
SOURCE   6 ORGAN: BRAIN (CDNA);                                                 
SOURCE   7 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   8 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  10 EXPRESSION_SYSTEM_CELL_LINE: HEK293;                                 
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: LAMBDA-ZAP                                
KEYWDS    HYDROLASE, HYDROLASE FOLD, CLICK CHEMISTRY                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.BOURNE,Z.RADIC,P.TAYLOR,P.MARCHOT                                   
REVDAT   1   08-DEC-10 2XUQ    0                                                
JRNL        AUTH   Y.BOURNE,Z.RADIC,P.TAYLOR,P.MARCHOT                          
JRNL        TITL   CONFORMATIONAL REMODELING OF FEMTOMOLAR INHIBITOR-           
JRNL        TITL 2 ACETYLCHOLINESTERASE COMPLEXES IN THE CRYSTALLINE STATE      
JRNL        REF    J.AM.CHEM.SOC.                             2010              
JRNL        REFN                   ESSN 1520-5126                               
JRNL        PMID   21090615                                                     
JRNL        DOI    10.1021/JA106820E                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.62                          
REMARK   3   NUMBER OF REFLECTIONS             : 53502                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.20215                         
REMARK   3   R VALUE            (WORKING SET) : 0.20127                         
REMARK   3   FREE R VALUE                     : 0.24460                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1117                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.700                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.769                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3792                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.33                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.326                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 73                           
REMARK   3   BIN FREE R VALUE                    : 0.345                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8354                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 119                                     
REMARK   3   SOLVENT ATOMS            : 58                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 68.9                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 58.051                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.87                                                 
REMARK   3    B22 (A**2) : 4.03                                                 
REMARK   3    B33 (A**2) : -7.90                                                
REMARK   3    B12 (A**2) : -0.00                                                
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : -0.00                                                
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.364         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.266         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.223         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 24.582        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.926                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8743 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11954 ; 1.333 ; 1.972       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1068 ; 5.927 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   397 ;33.290 ;22.872       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1260 ;17.197 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    73 ;18.414 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1267 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6897 ; 0.007 ; 0.022       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5340 ; 0.527 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8612 ; 1.027 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3403 ; 1.430 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3340 ; 2.537 ; 4.500       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 5                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     16       A      56      5                      
REMARK   3           1     B     16       B      56      5                      
REMARK   3           2     A     60       A      74      5                      
REMARK   3           2     B     60       B      74      5                      
REMARK   3           3     A     80       A     255      5                      
REMARK   3           3     B     80       B     255      5                      
REMARK   3           4     A    266       A     490      5                      
REMARK   3           4     B    266       B     490      5                      
REMARK   3           5     A    508       A     539      5                      
REMARK   3           5     B    508       B     539      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1954 ;  0.12 ;  0.50           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):   1954 ;  0.12 ;  0.50           
REMARK   3   LOOSE POSITIONAL   1    A    (A):   1847 ;  0.39 ;  5.00           
REMARK   3   LOOSE POSITIONAL   1    B    (A):   1847 ;  0.39 ;  5.00           
REMARK   3   MEDIUM THERMAL     1    A (A**2):   1954 ;  0.51 ;  2.00           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1954 ;  0.51 ;  2.00           
REMARK   3   LOOSE THERMAL      1    A (A**2):   1847 ;  0.69 ; 10.00           
REMARK   3   LOOSE THERMAL      1    B (A**2):   1847 ;  0.69 ; 10.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   541                          
REMARK   3    RESIDUE RANGE :   B     4        B   541                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.8130   8.1815 -12.0503              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0817 T22:   0.0217                                     
REMARK   3      T33:   0.0956 T12:  -0.0262                                     
REMARK   3      T13:   0.0074 T23:  -0.0075                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5551 L22:   0.1373                                     
REMARK   3      L33:   2.2162 L12:  -0.0846                                     
REMARK   3      L13:   0.8399 L23:   0.1626                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0421 S12:   0.0262 S13:  -0.1196                       
REMARK   3      S21:   0.0129 S22:  -0.0420 S23:   0.0575                       
REMARK   3      S31:   0.2235 S32:  -0.0622 S33:  -0.0001                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   4                                                                      
REMARK   4 2XUQ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-OCT-10.                  
REMARK 100 THE PDBE ID CODE IS EBI-45843.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-MAR-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.931                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 54760                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.70                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 5.0                                
REMARK 200  R MERGE                    (I) : 0.08                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 17.30                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.7                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.56                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.40                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: REFMAC5                                               
REMARK 200 STARTING MODEL: PDB ENTRY 1J06                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.6                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN WAS CRYSTALLIZED FROM            
REMARK 280  PEG-600 25-35% (V/V) IN 50-100 MM HEPES, PH 6.0-7.0, OR             
REMARK 280  WITH PEG-550 MME 30% (V/V) IN 50 MM NA ACETATE, PH 7.5              
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       39.30000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.96950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.85000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      113.96950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.30000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.85000            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, TYR 368 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, TYR 368 TO ALA                        
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     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     ALA A   542                                                      
REMARK 465     THR A   543                                                      
REMARK 465     GLU B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
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     ALA B   542                                                      
REMARK 465     THR B   543                                                      
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 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    PRO A  41       48.13    -78.64                                   
REMARK 500    PHE A  47       -9.73     72.42                                   
REMARK 500    PHE A 158       -3.08   -142.13                                   
REMARK 500    ALA A 167       67.60   -152.59                                   
REMARK 500    ASN A 170       15.84     53.49                                   
REMARK 500    SER A 203     -128.28     52.06                                   
REMARK 500    ASP A 306      -83.92   -134.03                                   
REMARK 500    TYR A 341       52.08   -100.80                                   
REMARK 500    PRO A 388        3.10    -62.39                                   
REMARK 500    VAL A 407      -64.19   -126.22                                   
REMARK 500    LYS A 496       83.43     29.98                                   
REMARK 500    SER A 497       87.71     30.78                                   
REMARK 500    LEU A 540       37.38    -98.67                                   
REMARK 500    ALA B  62       58.82   -117.88                                   
REMARK 500    ARG B 107      126.67    -26.34                                   
REMARK 500    PRO B 111      115.44    -38.57                                   
REMARK 500    PHE B 123        9.56     59.51                                   
REMARK 500    ARG B 136      -67.48    -10.74                                   
REMARK 500    SER B 203     -121.29     51.72                                   
REMARK 500    ASP B 306      -84.76   -110.10                                   
REMARK 500    ASP B 323       64.68   -100.58                                   
REMARK 500    TYR B 341       47.61    -99.75                                   
REMARK 500    PRO B 458       -6.30    -59.90                                   
REMARK 500    THR B 486      -11.97   -141.40                                   
REMARK 500    SER B 495     -153.77   -111.78                                   
REMARK 500    LYS B 496      -71.54     49.63                                   
REMARK 500    SER B 497      -91.85     71.50                                   
REMARK 500    PHE B 535      -67.35    -91.04                                   
REMARK 500    LEU B 539      -71.02    -71.83                                   
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    TYR A 449        24.7      L          L   OUTSIDE RANGE           
REMARK 500    SER B 497        22.2      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G A1542                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TZ4 A1543                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TZ4 B1542                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2JGH   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   INHIBITED BY NON-AGED VX                                           
REMARK 900 RELATED ID: 2WHQ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE,                          
REMARK 900  PHOSPHONYLATED BY SARIN (AGED) IN COMPLEX                           
REMARK 900  WITH HI-6                                                           
REMARK 900 RELATED ID: 1MAH   RELATED DB: PDB                                   
REMARK 900  FASCICULIN2 - MOUSE ACETYLCHOLINESTERASE COMPLEX                    
REMARK 900 RELATED ID: 1MAA   RELATED DB: PDB                                   
REMARK 900  MOUSE ACETYLCHOLINESTERASE CATALYTIC DOMAIN,                        
REMARK 900  GLYCOSYLATEDPROTEIN                                                 
REMARK 900 RELATED ID: 2HA6   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MUTANT S203A OF                                
REMARK 900  MOUSEACETYLCHOLINESTERASE COMPLEXED WITH                            
REMARK 900  SUCCINYLCHOLINE                                                     
REMARK 900 RELATED ID: 2JGG   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   INHIBITED BY NON-AGED SARIN                                        
REMARK 900 RELATED ID: 2C0Q   RELATED DB: PDB                                   
REMARK 900  NON-AGED FORM OF MOUSE ACETYLCHOLINESTERASE                         
REMARK 900  INHIBITED BY TABUN                                                  
REMARK 900 RELATED ID: 2JGL   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   INHIBITED BY AGED VX AND SARIN                                     
REMARK 900 RELATED ID: 1Q84   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE                                      
REMARK 900  ACETYLCHOLINESTERASE-TZ2PA6ANTI COMPLEX                             
REMARK 900 RELATED ID: 2WHR   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE IN                        
REMARK 900  COMPLEX WITH K027                                                   
REMARK 900 RELATED ID: 2JGM   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   INHIBITED BY AGED DIISOPROPYL FLUOROPHOSPHATE                      
REMARK 900   (DFP)                                                              
REMARK 900 RELATED ID: 1Q83   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE                                      
REMARK 900  ACETYLCHOLINESTERASE-TZ2PA6SYN COMPLEX                              
REMARK 900 RELATED ID: 2JGE   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900 RELATED ID: 2WLS   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MUS MUSCULUS                                   
REMARK 900  ACETYLCHOLINESTERASE IN COMPLEX WITH AMTS13                         
REMARK 900 RELATED ID: 2HA3   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   COMPLEXEDWITH CHOLINE                                              
REMARK 900 RELATED ID: 1C2B   RELATED DB: PDB                                   
REMARK 900  ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE                       
REMARK 900 RELATED ID: 2HA0   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   COMPLEXEDWITH 4-KETOAMYLTRIMETHYLAMMONIUM                          
REMARK 900 RELATED ID: 2WU3   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   IN COMPLEX WITH FENAMIPHOS AND HI-6                                
REMARK 900 RELATED ID: 2JEY   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX                        
REMARK 900  WITH HLO-7                                                          
REMARK 900 RELATED ID: 2JGI   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   INHIBITED BY NON-AGED DIISOPROPYL                                  
REMARK 900  FLUOROPHOSPHATE (DFP)                                               
REMARK 900 RELATED ID: 1N5R   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE                                      
REMARK 900  ACETYLCHOLINESTERASE-PROPIDIUM COMPLEX                              
REMARK 900 RELATED ID: 2JGJ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   INHIBITED BY AGED METHAMIDOPHOS                                    
REMARK 900 RELATED ID: 1J06   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   IN THE APOFORM                                                     
REMARK 900 RELATED ID: 2C0P   RELATED DB: PDB                                   
REMARK 900  AGED FORM OF MOUSE ACETYLCHOLINESTERASE                             
REMARK 900  INHIBITED BY TABUN                                                  
REMARK 900 RELATED ID: 2JF0   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX                        
REMARK 900  WITH TABUN AND ORTHO-7                                              
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: 1N5M   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE                                      
REMARK 900  ACETYLCHOLINESTERASE-GALLAMINE COMPLEX                              
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: 2HA2   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   COMPLEXEDWITH SUCCINYLCHOLINE                                      
REMARK 900 RELATED ID: 2WHP   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE,                          
REMARK 900  PHOSPHONYLATED BY SARIN AND IN COMPLEX WITH                         
REMARK 900   HI-6                                                               
REMARK 900 RELATED ID: 2JEZ   RELATED DB: PDB                                   
REMARK 900  MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX                        
REMARK 900  WITH TABUN AND HLO-7                                                
REMARK 900 RELATED ID: 2JGK   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   INHIBITED BY AGED FENAMIPHOS                                       
REMARK 900 RELATED ID: 1KU6   RELATED DB: PDB                                   
REMARK 900  FASCICULIN 2-MOUSE ACETYLCHOLINESTERASE COMPLEX                     
REMARK 900 RELATED ID: 2HA4   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MUTANT S203A OF                                
REMARK 900  MOUSEACETYLCHOLINESTERASE COMPLEXED WITH                            
REMARK 900  ACETYLCHOLINE                                                       
REMARK 900 RELATED ID: 1J07   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MOUSE                                      
REMARK 900  ACETYLCHOLINESTERASE-DECIDIUM COMPLEX                               
REMARK 900 RELATED ID: 2HA7   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MUTANT S203A OF                                
REMARK 900  MOUSEACETYLCHOLINESTERASE COMPLEXED WITH                            
REMARK 900  BUTYRYLTHIOCHOLINE                                                  
REMARK 900 RELATED ID: 2JGF   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   INHIBITED BY NON-AGED FENAMIPHOS                                   
REMARK 900 RELATED ID: 2WU4   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE                     
REMARK 900   IN COMPLEX WITH FENAMIPHOS AND ORTHO-7                             
REMARK 900 RELATED ID: 1C2O   RELATED DB: PDB                                   
REMARK 900  ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE                       
REMARK 900 RELATED ID: 2XUD   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE Y337A MUTANT OF                            
REMARK 900  MOUSE ACETYLCHOLINESTERASE                                          
REMARK 900   INHIBITED BY NON-AGED METHAMIDOPHOS                                
REMARK 900 RELATED ID: 2XUF   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI                        
REMARK 900   COMPLEX (1 MTH)                                                    
REMARK 900 RELATED ID: 2XUG   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI                        
REMARK 900   COMPLEX (1 WK)                                                     
REMARK 900 RELATED ID: 2XUP   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE MACHE-Y337A MUTANT                         
REMARK 900   IN COMPLEX WITH SOAKED TZ2PA6 SYN                                  
REMARK 900  INHIBITOR                                                           
REMARK 900 RELATED ID: 2XUI   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN                         
REMARK 900   COMPLEX (1 WK)                                                     
REMARK 900 RELATED ID: 2XUK   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN                         
REMARK 900   COMPLEX (10 MTH)                                                   
REMARK 900 RELATED ID: 2XUO   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A MUTANT IN                          
REMARK 900  COMPLEX WITH SOAKED TZ2PA6 ANTI INHIBITOR                           
REMARK 900 RELATED ID: 2XUJ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 SYN                         
REMARK 900   COMPLEX (1 MTH)                                                    
REMARK 900 RELATED ID: 2XUH   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MACHE-Y337A-TZ2PA6 ANTI                        
REMARK 900   COMPLEX (10 MTH)                                                   
DBREF  2XUQ A    1   543  UNP    P21836   ACES_MOUSE      32    574             
DBREF  2XUQ B    1   543  UNP    P21836   ACES_MOUSE      32    574             
SEQADV 2XUQ ALA A  337  UNP  P21836    TYR   368 ENGINEERED MUTATION            
SEQADV 2XUQ ALA B  337  UNP  P21836    TYR   368 ENGINEERED MUTATION            
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 ALA 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 ALA 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                      
HET    P6G  A1542      19                                                       
HET    TZ4  A1543      50                                                       
HET    TZ4  B1542      50                                                       
HETNAM     P6G HEXAETHYLENE GLYCOL                                              
HETNAM     TZ4 3,8-DIAMINO-6-PHENYL-5-[6-[1-[2-[(1,2,3,4-TETRAHYDRO-9-          
HETNAM   2 TZ4  ACRIDINYL)AMINO]ETHYL]-1H-1,2,3-TRIAZOL-4-YL]HEXYL]-            
HETNAM   3 TZ4  PHENANTHRIDINIUM                                                
HETSYN     P6G POLYETHYLENE GLYCOL PEG400                                       
FORMUL   3  P6G    C12 H26 O7                                                   
FORMUL   4  TZ4    2(C42 H45 N8 1+)                                             
FORMUL   5  HOH   *58(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  PHE A  190  5                                   3    
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 TRP A  286  LEU A  289  5                                   4    
HELIX   14  14 THR A  311  THR A  318  1                                   8    
HELIX   15  15 GLY A  335  TYR A  341  5                                   7    
HELIX   16  16 SER A  355  VAL A  367  1                                  13    
HELIX   17  17 SER A  371  THR A  383  1                                  13    
HELIX   18  18 ASP A  390  VAL A  407  1                                  18    
HELIX   19  19 VAL A  407  GLN A  421  1                                  15    
HELIX   20  20 PRO A  440  GLY A  444  5                                   5    
HELIX   21  21 GLU A  450  PHE A  455  1                                   6    
HELIX   22  22 GLY A  456  ASP A  460  5                                   5    
HELIX   23  23 ASP A  460  ASN A  464  5                                   5    
HELIX   24  24 THR A  466  GLY A  487  1                                  22    
HELIX   25  25 ARG A  525  LEU A  540  1                                  16    
HELIX   26  26 ASP B    5  GLN B    7  5                                   3    
HELIX   27  27 VAL B   42  ARG B   46  5                                   5    
HELIX   28  28 PHE B   80  MET B   85  1                                   6    
HELIX   29  29 LEU B  130  ASP B  134  5                                   5    
HELIX   30  30 GLY B  135  VAL B  141  1                                   7    
HELIX   31  31 VAL B  153  LEU B  159  1                                   7    
HELIX   32  32 ASN B  170  ILE B  187  1                                  18    
HELIX   33  33 ALA B  188  PHE B  190  5                                   3    
HELIX   34  34 SER B  203  LEU B  214  1                                  12    
HELIX   35  35 SER B  215  PHE B  222  5                                   8    
HELIX   36  36 ALA B  241  VAL B  255  1                                  15    
HELIX   37  37 ASN B  265  THR B  275  1                                  11    
HELIX   38  38 PRO B  277  HIS B  284  1                                   8    
HELIX   39  39 GLU B  285  LEU B  289  5                                   5    
HELIX   40  40 THR B  311  GLY B  319  1                                   9    
HELIX   41  41 GLY B  335  VAL B  340  1                                   6    
HELIX   42  42 SER B  355  VAL B  367  1                                  13    
HELIX   43  43 SER B  371  THR B  383  1                                  13    
HELIX   44  44 ASP B  390  VAL B  407  1                                  18    
HELIX   45  45 VAL B  407  GLN B  421  1                                  15    
HELIX   46  46 PRO B  440  GLY B  444  5                                   5    
HELIX   47  47 GLU B  450  GLY B  456  1                                   7    
HELIX   48  48 LEU B  457  ASN B  464  5                                   8    
HELIX   49  49 THR B  466  GLY B  487  1                                  22    
HELIX   50  50 ARG B  525  PHE B  535  1                                  11    
HELIX   51  51 PHE B  535  LEU B  540  1                                   6    
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  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           
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           
SSBOND   1 CYS A   69    CYS A   96                          1555   1555  2.05  
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.11  
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.07  
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.05  
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.08  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.07  
CISPEP   1 TYR A  105    PRO A  106          0        -2.60                     
CISPEP   2 LYS A  496    SER A  497          0         3.25                     
CISPEP   3 TYR B  105    PRO B  106          0         9.06                     
CISPEP   4 SER B  497    PRO B  498          0       -15.14                     
SITE     1 AC1  7 LEU A 380  HIS A 381  GLN A 527  PHE A 535                    
SITE     2 AC1  7 HIS B 381  GLN B 527  PHE B 535                               
SITE     1 AC2 12 TYR A  72  ASP A  74  TRP A  86  TYR A 124                    
SITE     2 AC2 12 GLU A 202  GLU A 285  TRP A 286  ALA A 337                    
SITE     3 AC2 12 PHE A 338  TYR A 341  HIS A 447  HOH A2010                    
SITE     1 AC3 10 TYR B  72  ASP B  74  TRP B  86  GLY B 121                    
SITE     2 AC3 10 GLU B 202  GLU B 285  TRP B 286  ALA B 337                    
SITE     3 AC3 10 TYR B 341  HIS B 447                                          
CRYST1   78.600  109.700  227.939  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      0.012723  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009116  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004387        0.00000                         
MTRIX1   1  0.732300 -0.403800 -0.548300        0.94600    1                    
MTRIX2   1 -0.405100 -0.905600  0.125800       24.23000    1                    
MTRIX3   1 -0.547300  0.130000 -0.826800      -13.73000    1                    
MTRIX1   2  0.732300 -0.403800 -0.548300        0.94600    1                    
MTRIX2   2 -0.405100 -0.905600  0.125800       24.23000    1                    
MTRIX3   2 -0.547300  0.130000 -0.826800      -13.73000    1                    
MTRIX1   3  0.732300 -0.403800 -0.548300        0.94600    1                    
MTRIX2   3 -0.405100 -0.905600  0.125800       24.23000    1                    
MTRIX3   3 -0.547300  0.130000 -0.826800      -13.73000    1                    
MTRIX1   4  0.732300 -0.403800 -0.548300        0.94600    1                    
MTRIX2   4 -0.405100 -0.905600  0.125800       24.23000    1                    
MTRIX3   4 -0.547300  0.130000 -0.826800      -13.73000    1                    
TER    4199      SER A 541                                                      
TER    8356      SER B 541                                                      
MASTER      549    0    3   51   32    0    8   18 8531    2  131   84          
END                                                                             

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