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LongText Report for: 5DTJ-pdb

Name Class
5DTJ-pdb
HEADER    HYDROLASE/HYDROLASE INHIBITOR           18-SEP-15   5DTJ              
TITLE     CRYSTAL STRUCTURE OF DFP-INHIBITED MOUSE ACETYLCHOLINESTERASE IN      
TITLE    2 COMPLEX WITH THE REACTIVATOR SP-134                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 32-573;                                       
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: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: ACHE;                                                          
SOURCE   6 EXPRESSION_SYSTEM: MUS MUSCULUS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10090;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELL: HI-5 INSECT CELLS BY C-PERL                  
KEYWDS    HYDROLASE-HYDROLASE INHIBITOR COMPLEX                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.H.TRAN,L.TONG                                                       
REVDAT   1   21-OCT-15 5DTJ    0                                                
JRNL        AUTH   F.S.KATZ,S.PECIC,T.H.TRAN,I.TRAKHT,L.SCHNEIDER,Z.ZHU,        
JRNL        AUTH 2 L.TON-THAT,M.LUZAC,V.ZLATANIC,S.DAMERA,J.MACDONALD,          
JRNL        AUTH 3 D.W.LANDRY,L.TONG,M.N.STOJANOVIC                             
JRNL        TITL   DISCOVERY OF NEW CLASSES OF COMPOUNDS THAT REACTIVATE        
JRNL        TITL 2 ACETYLCHOLINESTERASE INHIBITED BY ORGANOPHOSPHATES.          
JRNL        REF    CHEMBIOCHEM                   V.  16  2205 2015              
JRNL        REFN                   ESSN 1439-7633                               
JRNL        PMID   26350723                                                     
JRNL        DOI    10.1002/CBIC.201500348                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.71 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1685                                      
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) : 2.71                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.20                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 56292                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.550                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1996                            
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 46.2091 -  6.5244    0.99     4133   154  0.1632 0.1834        
REMARK   3     2  6.5244 -  5.1808    1.00     3976   145  0.1586 0.1934        
REMARK   3     3  5.1808 -  4.5266    1.00     3937   145  0.1354 0.1731        
REMARK   3     4  4.5266 -  4.1130    1.00     3932   144  0.1377 0.1619        
REMARK   3     5  4.1130 -  3.8183    1.00     3881   143  0.1563 0.1995        
REMARK   3     6  3.8183 -  3.5933    1.00     3880   143  0.1719 0.2126        
REMARK   3     7  3.5933 -  3.4134    1.00     3881   143  0.1923 0.2402        
REMARK   3     8  3.4134 -  3.2649    1.00     3876   143  0.2286 0.2941        
REMARK   3     9  3.2649 -  3.1392    1.00     3835   140  0.2381 0.2883        
REMARK   3    10  3.1392 -  3.0309    1.00     3854   140  0.2391 0.3503        
REMARK   3    11  3.0309 -  2.9361    1.00     3812   139  0.2312 0.3482        
REMARK   3    12  2.9361 -  2.8522    1.00     3855   143  0.2370 0.2894        
REMARK   3    13  2.8522 -  2.7772    1.00     3838   141  0.2548 0.3034        
REMARK   3    14  2.7772 -  2.7100    0.94     3606   133  0.2555 0.2964        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.460           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           8697                                  
REMARK   3   ANGLE     :  1.272          11871                                  
REMARK   3   CHIRALITY :  0.055           1268                                  
REMARK   3   PLANARITY :  0.007           1558                                  
REMARK   3   DIHEDRAL  : 16.113           3135                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  21.3254  -8.4797 -11.2197              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3451 T22:   0.3402                                     
REMARK   3      T33:   0.3902 T12:  -0.0363                                     
REMARK   3      T13:  -0.0149 T23:  -0.0054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2390 L22:   0.1357                                     
REMARK   3      L33:   1.2366 L12:  -0.0773                                     
REMARK   3      L13:  -0.4856 L23:  -0.1176                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0125 S12:   0.0187 S13:   0.0451                       
REMARK   3      S21:   0.0134 S22:  -0.0389 S23:  -0.0357                       
REMARK   3      S31:  -0.1648 S32:   0.0409 S33:   0.0324                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5DTJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-SEP-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000213790.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-MAR-14                          
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               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.075                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56474                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 16.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP, MOLREP                                        
REMARK 200 STARTING MODEL: PDB ENTRY 2HA2                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% V/V PEG 600, 0.1 M SODIUM CITRATE,   
REMARK 280  PH 6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 274K             
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       39.74350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.55850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.68350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      113.55850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.74350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.68350            
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: 1780 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38590 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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   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     SER A   541                                                      
REMARK 465     ALA A   542                                                      
REMARK 465     ASP B    -2                                                      
REMARK 465     PRO B    -1                                                      
REMARK 465     MET B     0                                                      
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 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   OD2  ASP A     5     OH   TYR A   105              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      -12.52     72.26                                   
REMARK 500    THR A  75       11.58   -140.59                                   
REMARK 500    ALA A 167       71.84   -155.43                                   
REMARK 500    ASN A 170       13.83     55.40                                   
REMARK 500    ALA A 189        0.35    -60.22                                   
REMARK 500    MIS A 203     -120.50     66.50                                   
REMARK 500    GLN A 291       36.98    -77.77                                   
REMARK 500    SER A 293       42.51    -74.85                                   
REMARK 500    ASP A 306      -79.97   -114.54                                   
REMARK 500    ASP A 333       69.45   -116.69                                   
REMARK 500    VAL A 367       77.02   -114.67                                   
REMARK 500    VAL A 407      -63.35   -132.19                                   
REMARK 500    PRO A 537       66.00    -68.28                                   
REMARK 500    LYS A 538      -63.03   -139.98                                   
REMARK 500    PRO B  41       46.46    -81.46                                   
REMARK 500    PHE B  47       -2.33     69.67                                   
REMARK 500    ALA B  62       55.76   -119.28                                   
REMARK 500    GLN B  66     -168.17    -77.39                                   
REMARK 500    CYS B  96       -2.84   -149.93                                   
REMARK 500    ALA B 167       62.18   -156.34                                   
REMARK 500    MIS B 203     -117.46     62.19                                   
REMARK 500    GLN B 291       21.15    -74.09                                   
REMARK 500    SER B 293       43.03    -88.20                                   
REMARK 500    PHE B 295       48.03    -91.48                                   
REMARK 500    ASP B 306      -78.94   -120.52                                   
REMARK 500    LEU B 353       96.06    -69.10                                   
REMARK 500    VAL B 407      -68.00   -127.13                                   
REMARK 500    LYS B 538        4.12    -64.35                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     5G8 A  601                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5G8 A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5G8 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5G8 B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5G8 B 602                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5DTG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5DTI   RELATED DB: PDB                                   
DBREF  5DTJ A    1   542  UNP    P21836   ACES_MOUSE      32    573             
DBREF  5DTJ B    1   542  UNP    P21836   ACES_MOUSE      32    573             
SEQADV 5DTJ ASP A   -2  UNP  P21836              EXPRESSION TAG                 
SEQADV 5DTJ PRO A   -1  UNP  P21836              EXPRESSION TAG                 
SEQADV 5DTJ MET A    0  UNP  P21836              EXPRESSION TAG                 
SEQADV 5DTJ ASP B   -2  UNP  P21836              EXPRESSION TAG                 
SEQADV 5DTJ PRO B   -1  UNP  P21836              EXPRESSION TAG                 
SEQADV 5DTJ MET B    0  UNP  P21836              EXPRESSION TAG                 
SEQRES   1 A  545  ASP PRO MET GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL          
SEQRES   2 A  545  ARG VAL ARG GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS          
SEQRES   3 A  545  ALA PRO GLY GLY PRO VAL SER ALA PHE LEU GLY ILE PRO          
SEQRES   4 A  545  PHE ALA GLU PRO PRO VAL GLY SER ARG ARG PHE MET PRO          
SEQRES   5 A  545  PRO GLU PRO LYS ARG PRO TRP SER GLY VAL LEU ASP ALA          
SEQRES   6 A  545  THR THR PHE GLN ASN VAL CYS TYR GLN TYR VAL ASP THR          
SEQRES   7 A  545  LEU TYR PRO GLY PHE GLU GLY THR GLU MET TRP ASN PRO          
SEQRES   8 A  545  ASN ARG GLU LEU SER GLU ASP CYS LEU TYR LEU ASN VAL          
SEQRES   9 A  545  TRP THR PRO TYR PRO ARG PRO ALA SER PRO THR PRO VAL          
SEQRES  10 A  545  LEU ILE TRP ILE TYR GLY GLY GLY PHE TYR SER GLY ALA          
SEQRES  11 A  545  ALA SER LEU ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN          
SEQRES  12 A  545  VAL GLU GLY ALA VAL LEU VAL SER MET ASN TYR ARG VAL          
SEQRES  13 A  545  GLY THR PHE GLY PHE LEU ALA LEU PRO GLY SER ARG GLU          
SEQRES  14 A  545  ALA PRO GLY ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA          
SEQRES  15 A  545  LEU GLN TRP VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY          
SEQRES  16 A  545  ASP PRO MET SER VAL THR LEU PHE GLY GLU MIS ALA GLY          
SEQRES  17 A  545  ALA ALA SER VAL GLY MET HIS ILE LEU SER LEU PRO SER          
SEQRES  18 A  545  ARG SER LEU PHE HIS ARG ALA VAL LEU GLN SER GLY THR          
SEQRES  19 A  545  PRO ASN GLY PRO TRP ALA THR VAL SER ALA GLY GLU ALA          
SEQRES  20 A  545  ARG ARG ARG ALA THR LEU LEU ALA ARG LEU VAL GLY CYS          
SEQRES  21 A  545  PRO PRO GLY GLY ALA GLY GLY ASN ASP THR GLU LEU ILE          
SEQRES  22 A  545  ALA CYS LEU ARG THR ARG PRO ALA GLN ASP LEU VAL ASP          
SEQRES  23 A  545  HIS GLU TRP HIS VAL LEU PRO GLN GLU SER ILE PHE ARG          
SEQRES  24 A  545  PHE SER PHE VAL PRO VAL VAL ASP GLY ASP PHE LEU SER          
SEQRES  25 A  545  ASP THR PRO GLU ALA LEU ILE ASN THR GLY ASP PHE GLN          
SEQRES  26 A  545  ASP LEU GLN VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY          
SEQRES  27 A  545  SER TYR PHE LEU VAL TYR GLY VAL PRO GLY PHE SER LYS          
SEQRES  28 A  545  ASP ASN GLU SER LEU ILE SER ARG ALA GLN PHE LEU ALA          
SEQRES  29 A  545  GLY VAL ARG ILE GLY VAL PRO GLN ALA SER ASP LEU ALA          
SEQRES  30 A  545  ALA GLU ALA VAL VAL LEU HIS TYR THR ASP TRP LEU HIS          
SEQRES  31 A  545  PRO GLU ASP PRO THR HIS LEU ARG ASP ALA MET SER ALA          
SEQRES  32 A  545  VAL VAL GLY ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN          
SEQRES  33 A  545  LEU ALA GLY ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR          
SEQRES  34 A  545  ALA TYR ILE PHE GLU HIS ARG ALA SER THR LEU THR TRP          
SEQRES  35 A  545  PRO LEU TRP MET GLY VAL PRO HIS GLY TYR GLU ILE GLU          
SEQRES  36 A  545  PHE ILE PHE GLY LEU PRO LEU ASP PRO SER LEU ASN TYR          
SEQRES  37 A  545  THR THR GLU GLU ARG ILE PHE ALA GLN ARG LEU MET LYS          
SEQRES  38 A  545  TYR TRP THR ASN PHE ALA ARG THR GLY ASP PRO ASN ASP          
SEQRES  39 A  545  PRO ARG ASP SER LYS SER PRO GLN TRP PRO PRO TYR THR          
SEQRES  40 A  545  THR ALA ALA GLN GLN TYR VAL SER LEU ASN LEU LYS PRO          
SEQRES  41 A  545  LEU GLU VAL ARG ARG GLY LEU ARG ALA GLN THR CYS ALA          
SEQRES  42 A  545  PHE TRP ASN ARG PHE LEU PRO LYS LEU LEU SER ALA              
SEQRES   1 B  545  ASP PRO MET GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL          
SEQRES   2 B  545  ARG VAL ARG GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS          
SEQRES   3 B  545  ALA PRO GLY GLY PRO VAL SER ALA PHE LEU GLY ILE PRO          
SEQRES   4 B  545  PHE ALA GLU PRO PRO VAL GLY SER ARG ARG PHE MET PRO          
SEQRES   5 B  545  PRO GLU PRO LYS ARG PRO TRP SER GLY VAL LEU ASP ALA          
SEQRES   6 B  545  THR THR PHE GLN ASN VAL CYS TYR GLN TYR VAL ASP THR          
SEQRES   7 B  545  LEU TYR PRO GLY PHE GLU GLY THR GLU MET TRP ASN PRO          
SEQRES   8 B  545  ASN ARG GLU LEU SER GLU ASP CYS LEU TYR LEU ASN VAL          
SEQRES   9 B  545  TRP THR PRO TYR PRO ARG PRO ALA SER PRO THR PRO VAL          
SEQRES  10 B  545  LEU ILE TRP ILE TYR GLY GLY GLY PHE TYR SER GLY ALA          
SEQRES  11 B  545  ALA SER LEU ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN          
SEQRES  12 B  545  VAL GLU GLY ALA VAL LEU VAL SER MET ASN TYR ARG VAL          
SEQRES  13 B  545  GLY THR PHE GLY PHE LEU ALA LEU PRO GLY SER ARG GLU          
SEQRES  14 B  545  ALA PRO GLY ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA          
SEQRES  15 B  545  LEU GLN TRP VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY          
SEQRES  16 B  545  ASP PRO MET SER VAL THR LEU PHE GLY GLU MIS ALA GLY          
SEQRES  17 B  545  ALA ALA SER VAL GLY MET HIS ILE LEU SER LEU PRO SER          
SEQRES  18 B  545  ARG SER LEU PHE HIS ARG ALA VAL LEU GLN SER GLY THR          
SEQRES  19 B  545  PRO ASN GLY PRO TRP ALA THR VAL SER ALA GLY GLU ALA          
SEQRES  20 B  545  ARG ARG ARG ALA THR LEU LEU ALA ARG LEU VAL GLY CYS          
SEQRES  21 B  545  PRO PRO GLY GLY ALA GLY GLY ASN ASP THR GLU LEU ILE          
SEQRES  22 B  545  ALA CYS LEU ARG THR ARG PRO ALA GLN ASP LEU VAL ASP          
SEQRES  23 B  545  HIS GLU TRP HIS VAL LEU PRO GLN GLU SER ILE PHE ARG          
SEQRES  24 B  545  PHE SER PHE VAL PRO VAL VAL ASP GLY ASP PHE LEU SER          
SEQRES  25 B  545  ASP THR PRO GLU ALA LEU ILE ASN THR GLY ASP PHE GLN          
SEQRES  26 B  545  ASP LEU GLN VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY          
SEQRES  27 B  545  SER TYR PHE LEU VAL TYR GLY VAL PRO GLY PHE SER LYS          
SEQRES  28 B  545  ASP ASN GLU SER LEU ILE SER ARG ALA GLN PHE LEU ALA          
SEQRES  29 B  545  GLY VAL ARG ILE GLY VAL PRO GLN ALA SER ASP LEU ALA          
SEQRES  30 B  545  ALA GLU ALA VAL VAL LEU HIS TYR THR ASP TRP LEU HIS          
SEQRES  31 B  545  PRO GLU ASP PRO THR HIS LEU ARG ASP ALA MET SER ALA          
SEQRES  32 B  545  VAL VAL GLY ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN          
SEQRES  33 B  545  LEU ALA GLY ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR          
SEQRES  34 B  545  ALA TYR ILE PHE GLU HIS ARG ALA SER THR LEU THR TRP          
SEQRES  35 B  545  PRO LEU TRP MET GLY VAL PRO HIS GLY TYR GLU ILE GLU          
SEQRES  36 B  545  PHE ILE PHE GLY LEU PRO LEU ASP PRO SER LEU ASN TYR          
SEQRES  37 B  545  THR THR GLU GLU ARG ILE PHE ALA GLN ARG LEU MET LYS          
SEQRES  38 B  545  TYR TRP THR ASN PHE ALA ARG THR GLY ASP PRO ASN ASP          
SEQRES  39 B  545  PRO ARG ASP SER LYS SER PRO GLN TRP PRO PRO TYR THR          
SEQRES  40 B  545  THR ALA ALA GLN GLN TYR VAL SER LEU ASN LEU LYS PRO          
SEQRES  41 B  545  LEU GLU VAL ARG ARG GLY LEU ARG ALA GLN THR CYS ALA          
SEQRES  42 B  545  PHE TRP ASN ARG PHE LEU PRO LYS LEU LEU SER ALA              
MODRES 5DTJ MIS A  203  SER  MODIFIED RESIDUE                                   
MODRES 5DTJ MIS B  203  SER  MODIFIED RESIDUE                                   
HET    MIS  A 203      13                                                       
HET    MIS  B 203      13                                                       
HET    5G8  A 601       9                                                       
HET    5G8  A 602      19                                                       
HET    5G8  B 601      19                                                       
HET    5G8  B 602      19                                                       
HETNAM     MIS MONOISOPROPYLPHOSPHORYLSERINE                                    
HETNAM     5G8 1-[5-(2,4-DICHLOROPHENOXY)PENTYL]-1H-IMIDAZOLE                   
FORMUL   1  MIS    2(C6 H14 N O6 P)                                             
FORMUL   3  5G8    4(C14 H16 CL2 N2 O)                                          
HELIX    1 AA1 MET A    0  GLU A    4  5                                   5    
HELIX    2 AA2 ASP A    5  GLN A    7  5                                   3    
HELIX    3 AA3 VAL A   42  ARG A   46  5                                   5    
HELIX    4 AA4 PHE A   80  MET A   85  1                                   6    
HELIX    5 AA5 LEU A  130  ASP A  134  5                                   5    
HELIX    6 AA6 GLY A  135  GLY A  143  1                                   9    
HELIX    7 AA7 VAL A  153  LEU A  159  1                                   7    
HELIX    8 AA8 ASN A  170  ILE A  187  1                                  18    
HELIX    9 AA9 ALA A  188  PHE A  190  5                                   3    
HELIX   10 AB1 MIS A  203  LEU A  214  1                                  12    
HELIX   11 AB2 SER A  215  SER A  220  1                                   6    
HELIX   12 AB3 ALA A  241  VAL A  255  1                                  15    
HELIX   13 AB4 ASP A  266  ARG A  274  1                                   9    
HELIX   14 AB5 PRO A  277  TRP A  286  1                                  10    
HELIX   15 AB6 HIS A  287  LEU A  289  5                                   3    
HELIX   16 AB7 THR A  311  GLY A  319  1                                   9    
HELIX   17 AB8 GLY A  335  VAL A  343  1                                   9    
HELIX   18 AB9 SER A  355  VAL A  367  1                                  13    
HELIX   19 AC1 SER A  371  THR A  383  1                                  13    
HELIX   20 AC2 ASP A  390  VAL A  407  1                                  18    
HELIX   21 AC3 VAL A  407  GLN A  421  1                                  15    
HELIX   22 AC4 PRO A  440  GLY A  444  5                                   5    
HELIX   23 AC5 GLU A  450  GLY A  456  1                                   7    
HELIX   24 AC6 LEU A  457  ASN A  464  5                                   8    
HELIX   25 AC7 THR A  466  GLY A  487  1                                  22    
HELIX   26 AC8 ARG A  525  ARG A  534  1                                  10    
HELIX   27 AC9 ASP B    5  GLN B    7  5                                   3    
HELIX   28 AD1 VAL B   42  ARG B   46  5                                   5    
HELIX   29 AD2 PHE B   80  MET B   85  1                                   6    
HELIX   30 AD3 LEU B  130  ASP B  134  5                                   5    
HELIX   31 AD4 GLY B  135  GLY B  143  1                                   9    
HELIX   32 AD5 VAL B  153  LEU B  159  1                                   7    
HELIX   33 AD6 ASN B  170  ILE B  187  1                                  18    
HELIX   34 AD7 ALA B  188  PHE B  190  5                                   3    
HELIX   35 AD8 MIS B  203  LEU B  214  1                                  12    
HELIX   36 AD9 SER B  215  SER B  220  1                                   6    
HELIX   37 AE1 ALA B  241  VAL B  255  1                                  15    
HELIX   38 AE2 ASP B  266  THR B  275  1                                  10    
HELIX   39 AE3 PRO B  277  GLU B  285  1                                   9    
HELIX   40 AE4 GLU B  292  ARG B  296  5                                   5    
HELIX   41 AE5 THR B  311  GLY B  319  1                                   9    
HELIX   42 AE6 GLY B  335  VAL B  343  1                                   9    
HELIX   43 AE7 SER B  355  VAL B  367  1                                  13    
HELIX   44 AE8 SER B  371  THR B  383  1                                  13    
HELIX   45 AE9 ASP B  390  VAL B  407  1                                  18    
HELIX   46 AF1 VAL B  407  GLN B  421  1                                  15    
HELIX   47 AF2 PRO B  440  GLY B  444  5                                   5    
HELIX   48 AF3 GLU B  450  GLY B  456  1                                   7    
HELIX   49 AF4 LEU B  457  ASN B  464  5                                   8    
HELIX   50 AF5 THR B  466  GLY B  487  1                                  22    
HELIX   51 AF6 ARG B  525  PHE B  535  1                                  11    
HELIX   52 AF7 LEU B  536  LEU B  540  5                                   5    
SHEET    1 AA1 3 LEU A   9  VAL A  12  0                                        
SHEET    2 AA1 3 GLY A  15  ARG A  18 -1  O  GLY A  15   N  VAL A  12           
SHEET    3 AA1 3 VAL A  59  ASP A  61  1  O  LEU A  60   N  GLN A  16           
SHEET    1 AA211 ILE A  20  ALA A  24  0                                        
SHEET    2 AA211 GLY A  27  PRO A  36 -1  O  VAL A  29   N  LEU A  22           
SHEET    3 AA211 TYR A  98  PRO A 104 -1  O  THR A 103   N  SER A  30           
SHEET    4 AA211 VAL A 145  MET A 149 -1  O  SER A 148   N  ASN A 100           
SHEET    5 AA211 THR A 112  ILE A 118  1  N  TRP A 117   O  VAL A 147           
SHEET    6 AA211 GLY A 192  GLU A 202  1  O  THR A 198   N  VAL A 114           
SHEET    7 AA211 ARG A 224  GLN A 228  1  O  GLN A 228   N  GLY A 201           
SHEET    8 AA211 GLN A 325  VAL A 331  1  O  LEU A 327   N  LEU A 227           
SHEET    9 AA211 ARG A 424  PHE A 430  1  O  TYR A 426   N  VAL A 328           
SHEET   10 AA211 GLN A 509  LEU A 513  1  O  LEU A 513   N  ILE A 429           
SHEET   11 AA211 GLU A 519  ARG A 522 -1  O  ARG A 521   N  TYR A 510           
SHEET    1 AA3 2 VAL A  68  CYS A  69  0                                        
SHEET    2 AA3 2 LEU A  92  SER A  93  1  O  SER A  93   N  VAL A  68           
SHEET    1 AA4 2 VAL A 239  SER A 240  0                                        
SHEET    2 AA4 2 VAL A 302  VAL A 303  1  O  VAL A 303   N  VAL A 239           
SHEET    1 AA5 3 LEU B   9  VAL B  12  0                                        
SHEET    2 AA5 3 GLY B  15  ARG B  18 -1  O  LEU B  17   N  VAL B  10           
SHEET    3 AA5 3 VAL B  59  ASP B  61  1  O  LEU B  60   N  GLN B  16           
SHEET    1 AA611 ILE B  20  ALA B  24  0                                        
SHEET    2 AA611 GLY B  27  PRO B  36 -1  O  GLY B  27   N  ALA B  24           
SHEET    3 AA611 TYR B  98  PRO B 104 -1  O  VAL B 101   N  PHE B  32           
SHEET    4 AA611 VAL B 145  MET B 149 -1  O  SER B 148   N  ASN B 100           
SHEET    5 AA611 THR B 112  ILE B 118  1  N  TRP B 117   O  VAL B 147           
SHEET    6 AA611 GLY B 192  GLU B 202  1  O  THR B 198   N  VAL B 114           
SHEET    7 AA611 ARG B 224  GLN B 228  1  O  ARG B 224   N  LEU B 199           
SHEET    8 AA611 GLN B 325  VAL B 331  1  O  LEU B 327   N  LEU B 227           
SHEET    9 AA611 ARG B 424  PHE B 430  1  O  PHE B 430   N  VAL B 330           
SHEET   10 AA611 GLN B 509  LEU B 513  1  O  VAL B 511   N  ALA B 427           
SHEET   11 AA611 GLU B 519  ARG B 522 -1  O  ARG B 521   N  TYR B 510           
SHEET    1 AA7 2 VAL B  68  CYS B  69  0                                        
SHEET    2 AA7 2 LEU B  92  SER B  93  1  O  SER B  93   N  VAL B  68           
SHEET    1 AA8 2 VAL B 239  SER B 240  0                                        
SHEET    2 AA8 2 VAL B 302  VAL B 303  1  O  VAL B 303   N  VAL B 239           
SSBOND   1 CYS A   69    CYS A   96                          1555   1555  2.03  
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  2.05  
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.07  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.04  
LINK         C   GLU A 202                 N   MIS A 203     1555   1555  1.33  
LINK         C   MIS A 203                 N   ALA A 204     1555   1555  1.33  
LINK         C   GLU B 202                 N   MIS B 203     1555   1555  1.33  
LINK         C   MIS B 203                 N   ALA B 204     1555   1555  1.34  
CISPEP   1 TYR A  105    PRO A  106          0         6.18                     
CISPEP   2 TYR B  105    PRO B  106          0         5.46                     
CISPEP   3 CYS B  257    PRO B  258          0         2.60                     
SITE     1 AC1  4 ASP A  74  TYR A 124  TYR A 341  5G8 A 602                    
SITE     1 AC2 10 TYR A  72  TYR A 124  GLU A 285  TRP A 286                    
SITE     2 AC2 10 ILE A 294  PHE A 295  PHE A 297  PHE A 338                    
SITE     3 AC2 10 ASN A 406  5G8 A 601                                          
SITE     1 AC3 10 TYR B  72  TYR B 124  GLU B 285  TRP B 286                    
SITE     2 AC3 10 PHE B 295  ARG B 296  PHE B 297  PHE B 338                    
SITE     3 AC3 10 ASN B 406  5G8 B 602                                          
SITE     1 AC4 10 ASP B  74  GLY B 121  TYR B 124  GLU B 202                    
SITE     2 AC4 10 MIS B 203  TRP B 286  TYR B 337  PHE B 338                    
SITE     3 AC4 10 TYR B 341  5G8 B 601                                          
CRYST1   79.487  113.367  227.117  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      0.012581  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008821  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004403        0.00000                         
TER    4208      LEU A 540                                                      
TER    8375      SER B 541                                                      
MASTER      331    0    6   52   36    0   10    6 8439    2  108   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:
ESTHER Home Page and ACEDB Home Page
AcePerl Lincoln Stein Home Page
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