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LongText Report for: 5DTG-pdb

Name Class
5DTG-pdb
HEADER    HYDROLASE                               18-SEP-15   5DTG              
TITLE     CRYSTAL STRUCTURE OF MOUSE ACETYLCHOINESTERASE INHIBITED BY DFP       
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                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.H.TRAN,L.TONG                                                       
REVDAT   1   21-OCT-15 5DTG    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.    2.40 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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.23                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 79243                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.520                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1995                            
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 46.2387 -  5.7821    0.94     5558   144  0.2035 0.2284        
REMARK   3     2  5.7821 -  4.5908    0.97     5560   144  0.1763 0.1995        
REMARK   3     3  4.5908 -  4.0108    0.98     5565   143  0.1753 0.2117        
REMARK   3     4  4.0108 -  3.6443    0.99     5573   143  0.1933 0.1849        
REMARK   3     5  3.6443 -  3.3832    0.99     5548   145  0.2165 0.2472        
REMARK   3     6  3.3832 -  3.1837    0.99     5570   144  0.2457 0.2645        
REMARK   3     7  3.1837 -  3.0243    0.99     5520   142  0.2486 0.2711        
REMARK   3     8  3.0243 -  2.8927    0.99     5554   144  0.2377 0.2956        
REMARK   3     9  2.8927 -  2.7814    0.99     5536   144  0.2337 0.2689        
REMARK   3    10  2.7814 -  2.6854    0.99     5525   143  0.2365 0.2578        
REMARK   3    11  2.6854 -  2.6014    0.99     5488   142  0.2363 0.2820        
REMARK   3    12  2.6014 -  2.5271    0.99     5441   140  0.2484 0.2931        
REMARK   3    13  2.5271 -  2.4606    0.99     5471   138  0.2657 0.3055        
REMARK   3    14  2.4606 -  2.4000    0.96     5339   139  0.2941 0.3342        
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)     : 0.260            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.250           
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      :  0.003           8606                                  
REMARK   3   ANGLE     :  1.102          11754                                  
REMARK   3   CHIRALITY :  0.037           1265                                  
REMARK   3   PLANARITY :  0.005           1547                                  
REMARK   3   DIHEDRAL  : 14.188           3104                                  
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):  20.8968  -8.5946 -11.0339              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4448 T22:   0.3850                                     
REMARK   3      T33:   0.4042 T12:  -0.0502                                     
REMARK   3      T13:  -0.0113 T23:  -0.0064                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2630 L22:   0.1297                                     
REMARK   3      L33:   1.1759 L12:  -0.0938                                     
REMARK   3      L13:  -0.4902 L23:  -0.1001                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0047 S12:   0.0179 S13:   0.0769                       
REMARK   3      S21:   0.0266 S22:  -0.0321 S23:  -0.0637                       
REMARK   3      S31:  -0.1681 S32:   0.0491 S33:   0.0276                       
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 5DTG 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_1000213783.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-NOV-13                          
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   : 79533                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
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     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 21.4000                            
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: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2HA2                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.94                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.23                     
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       39.28750            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.30850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.17300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      113.30850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.28750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.17300            
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: 39070 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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     SER B   495                                                      
REMARK 465     LYS B   496                                                      
REMARK 465     SER B   541                                                      
REMARK 465     ALA B   542                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG B  356   NE   CZ                                             
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   494     OG   SER A   497              1.44            
REMARK 500   NH2  ARG B   485     O    HOH B   601              1.60            
REMARK 500   OE1  GLN B   508     O    HOH B   602              1.92            
REMARK 500   NE2  GLN B   181     O    HOH B   603              2.05            
REMARK 500   OE1  GLN A   413     O    HOH A   601              2.05            
REMARK 500   OE2  GLU B   142     O    HOH B   604              2.11            
REMARK 500   NH2  ARG A   525     O    HOH A   602              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU B 289   CA  -  CB  -  CG  ANGL. DEV. =  15.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A  47       -5.22     68.39                                   
REMARK 500    ALA A  62       50.73   -116.89                                   
REMARK 500    ALA A 167       71.44   -152.88                                   
REMARK 500    MIS A 203     -116.56     58.56                                   
REMARK 500    ASP A 306      -80.67   -127.30                                   
REMARK 500    TYR A 341       55.88   -104.71                                   
REMARK 500    ASN A 350     -168.03   -108.88                                   
REMARK 500    VAL A 407      -61.56   -127.34                                   
REMARK 500    SER A 495      -37.65   -130.78                                   
REMARK 500    PHE B  47       -5.98     69.03                                   
REMARK 500    ALA B  62       52.09   -116.78                                   
REMARK 500    ALA B 167       70.63   -151.27                                   
REMARK 500    MIS B 203     -112.14     56.64                                   
REMARK 500    ASP B 306      -80.76   -127.59                                   
REMARK 500    TYR B 341       55.11   -105.49                                   
REMARK 500    ASN B 350     -168.32   -111.41                                   
REMARK 500    VAL B 407      -61.69   -127.47                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5DTI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5DTJ   RELATED DB: PDB                                   
DBREF  5DTG A    1   542  UNP    P21836   ACES_MOUSE      32    573             
DBREF  5DTG B    1   542  UNP    P21836   ACES_MOUSE      32    573             
SEQADV 5DTG ASP A   -2  UNP  P21836              EXPRESSION TAG                 
SEQADV 5DTG PRO A   -1  UNP  P21836              EXPRESSION TAG                 
SEQADV 5DTG MET A    0  UNP  P21836              EXPRESSION TAG                 
SEQADV 5DTG ASP B   -2  UNP  P21836              EXPRESSION TAG                 
SEQADV 5DTG PRO B   -1  UNP  P21836              EXPRESSION TAG                 
SEQADV 5DTG 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 5DTG MIS A  203  SER  MODIFIED RESIDUE                                   
MODRES 5DTG MIS B  203  SER  MODIFIED RESIDUE                                   
HET    MIS  A 203      13                                                       
HET    MIS  B 203      13                                                       
HETNAM     MIS MONOISOPROPYLPHOSPHORYLSERINE                                    
FORMUL   1  MIS    2(C6 H14 N O6 P)                                             
FORMUL   3  HOH   *147(H2 O)                                                    
HELIX    1 AA1 MET A    0  GLU A    4  5                                   5    
HELIX    2 AA2 VAL A   42  ARG A   46  5                                   5    
HELIX    3 AA3 PHE A   80  MET A   85  1                                   6    
HELIX    4 AA4 LEU A  130  ASP A  134  5                                   5    
HELIX    5 AA5 GLY A  135  GLY A  143  1                                   9    
HELIX    6 AA6 VAL A  153  LEU A  159  1                                   7    
HELIX    7 AA7 ASN A  170  ILE A  187  1                                  18    
HELIX    8 AA8 ALA A  188  PHE A  190  5                                   3    
HELIX    9 AA9 MIS A  203  LEU A  214  1                                  12    
HELIX   10 AB1 SER A  215  SER A  220  1                                   6    
HELIX   11 AB2 SER A  240  VAL A  255  1                                  16    
HELIX   12 AB3 ASP A  266  THR A  275  1                                  10    
HELIX   13 AB4 PRO A  277  GLU A  285  1                                   9    
HELIX   14 AB5 TRP A  286  LEU A  289  5                                   4    
HELIX   15 AB6 THR A  311  GLY A  319  1                                   9    
HELIX   16 AB7 GLY A  335  VAL A  340  1                                   6    
HELIX   17 AB8 SER A  355  VAL A  367  1                                  13    
HELIX   18 AB9 SER A  371  THR A  383  1                                  13    
HELIX   19 AC1 ASP A  390  VAL A  407  1                                  18    
HELIX   20 AC2 VAL A  407  GLN A  421  1                                  15    
HELIX   21 AC3 PRO A  440  GLY A  444  5                                   5    
HELIX   22 AC4 GLU A  450  PHE A  455  1                                   6    
HELIX   23 AC5 GLY A  456  ASN A  464  5                                   9    
HELIX   24 AC6 THR A  466  GLY A  487  1                                  22    
HELIX   25 AC7 ARG A  525  PHE A  535  1                                  11    
HELIX   26 AC8 LEU A  536  LEU A  540  5                                   5    
HELIX   27 AC9 VAL B   42  ARG B   46  5                                   5    
HELIX   28 AD1 PHE B   80  MET B   85  1                                   6    
HELIX   29 AD2 LEU B  130  ASP B  134  5                                   5    
HELIX   30 AD3 GLY B  135  GLY B  143  1                                   9    
HELIX   31 AD4 VAL B  153  LEU B  159  1                                   7    
HELIX   32 AD5 ASN B  170  ILE B  187  1                                  18    
HELIX   33 AD6 ALA B  188  PHE B  190  5                                   3    
HELIX   34 AD7 MIS B  203  LEU B  214  1                                  12    
HELIX   35 AD8 SER B  215  SER B  220  1                                   6    
HELIX   36 AD9 SER B  240  VAL B  255  1                                  16    
HELIX   37 AE1 ASP B  266  THR B  275  1                                  10    
HELIX   38 AE2 PRO B  277  GLU B  285  1                                   9    
HELIX   39 AE3 TRP B  286  VAL B  288  5                                   3    
HELIX   40 AE4 THR B  311  GLY B  319  1                                   9    
HELIX   41 AE5 GLY B  335  VAL B  340  1                                   6    
HELIX   42 AE6 SER B  355  VAL B  367  1                                  13    
HELIX   43 AE7 SER B  371  THR B  383  1                                  13    
HELIX   44 AE8 ASP B  390  VAL B  407  1                                  18    
HELIX   45 AE9 VAL B  407  GLN B  421  1                                  15    
HELIX   46 AF1 PRO B  440  GLY B  444  5                                   5    
HELIX   47 AF2 GLU B  450  PHE B  455  1                                   6    
HELIX   48 AF3 GLY B  456  ASN B  464  5                                   9    
HELIX   49 AF4 THR B  466  GLY B  487  1                                  22    
HELIX   50 AF5 ARG B  525  PHE B  535  1                                  11    
HELIX   51 AF6 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  ALA A  31   N  ILE A  20           
SHEET    3 AA211 TYR A  98  PRO A 104 -1  O  LEU A  99   N  ILE A  35           
SHEET    4 AA211 VAL A 145  MET A 149 -1  O  LEU A 146   N  TRP A 102           
SHEET    5 AA211 THR A 112  ILE A 118  1  N  LEU A 115   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  ARG A 224   N  LEU A 199           
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  PHE A 430   N  VAL A 330           
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 3 LEU B   9  VAL B  12  0                                        
SHEET    2 AA4 3 GLY B  15  ARG B  18 -1  O  GLY B  15   N  VAL B  12           
SHEET    3 AA4 3 VAL B  59  ASP B  61  1  O  LEU B  60   N  GLN B  16           
SHEET    1 AA511 ILE B  20  ALA B  24  0                                        
SHEET    2 AA511 GLY B  27  PRO B  36 -1  O  ALA B  31   N  ILE B  20           
SHEET    3 AA511 TYR B  98  PRO B 104 -1  O  LEU B  99   N  ILE B  35           
SHEET    4 AA511 VAL B 145  MET B 149 -1  O  LEU B 146   N  TRP B 102           
SHEET    5 AA511 THR B 112  ILE B 118  1  N  LEU B 115   O  VAL B 147           
SHEET    6 AA511 GLY B 192  GLU B 202  1  O  THR B 198   N  VAL B 114           
SHEET    7 AA511 ARG B 224  GLN B 228  1  O  GLN B 228   N  GLY B 201           
SHEET    8 AA511 GLN B 325  VAL B 331  1  O  LEU B 327   N  LEU B 227           
SHEET    9 AA511 ARG B 424  PHE B 430  1  O  PHE B 430   N  VAL B 330           
SHEET   10 AA511 GLN B 509  LEU B 513  1  O  LEU B 513   N  ILE B 429           
SHEET   11 AA511 GLU B 519  ARG B 522 -1  O  ARG B 521   N  TYR B 510           
SHEET    1 AA6 2 VAL B  68  CYS B  69  0                                        
SHEET    2 AA6 2 LEU B  92  SER B  93  1  O  SER B  93   N  VAL B  68           
SSBOND   1 CYS A   69    CYS A   96                          1555   1555  2.03  
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.03  
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.03  
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.03  
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.03  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.03  
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  1.33  
CISPEP   1 TYR A  105    PRO A  106          0         0.94                     
CISPEP   2 TYR B  105    PRO B  106          0         3.71                     
CISPEP   3 CYS B  257    PRO B  258          0        -1.50                     
CRYST1   78.575  114.346  226.617  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      0.012727  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008745  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004413        0.00000                         
TER    4208      LEU A 540                                                      
TER    8354      LEU B 540                                                      
MASTER      332    0    2   51   32    0    0    6 8499    2   42   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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