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LongText Report for: 7e3i-pdb

Name Class
7e3i-pdb
HEADER    HYDROLASE                               08-FEB-21   7E3I              
TITLE     STRUCTURE OF HUMAN ACETYLCHOLINESTERASE IN COMPLEX WITH TACRINE       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ACHE;                                                       
COMPND   5 EC: 3.1.1.7;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ACHE;                                                          
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HEK293                                  
KEYWDS    HUMAN ACETYLCHOLINESTERASE, HACHE, ALZHEIMER'S DISEASE, HYDROLASE     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.V.DILEEP,K.IHARA,C.MISHIMA-TSUMAGARI,M.KUKIMOTO-NIINO,M.YONEMOCHI,  
AUTHOR   2 K.HANADA,M.SHIROUZU,K.Y.J.ZHANG                                      
REVDAT   1   16-FEB-22 7E3I    0                                                
JRNL        AUTH   K.V.DILEEP,K.IHARA,C.MISHIMA-TSUMAGARI,M.KUKIMOTO-NIINO,     
JRNL        AUTH 2 M.YONEMOCHI,K.HANADA,M.SHIROUZU,K.Y.J.ZHANG                  
JRNL        TITL   STRUCTURE OF HUMAN ACETYLCHOLINESTERASE IN COMPLEX WITH      
JRNL        TITL 2 TACRINE                                                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.17.1_3660                                   
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) : 2.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.22                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 48480                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2419                            
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 47.0200 -  7.3200    0.99     2968   135  0.2008 0.2184        
REMARK   3     2  7.3200 -  5.8100    1.00     2794   144  0.2043 0.2408        
REMARK   3     3  5.8100 -  5.0800    1.00     2786   146  0.1764 0.2011        
REMARK   3     4  5.0800 -  4.6200    0.96     2621   143  0.1541 0.2182        
REMARK   3     5  4.6100 -  4.2900    0.99     2715   128  0.1555 0.1954        
REMARK   3     6  4.2800 -  4.0300    0.98     2654   152  0.1637 0.1910        
REMARK   3     7  4.0300 -  3.8300    0.99     2687   164  0.1694 0.2345        
REMARK   3     8  3.8300 -  3.6600    1.00     2738   131  0.1864 0.2001        
REMARK   3     9  3.6600 -  3.5200    1.00     2689   145  0.1962 0.2438        
REMARK   3    10  3.5200 -  3.4000    1.00     2671   150  0.1981 0.2776        
REMARK   3    11  3.4000 -  3.2900    1.00     2698   127  0.1988 0.2424        
REMARK   3    12  3.2900 -  3.2000    1.00     2736   122  0.2137 0.2794        
REMARK   3    13  3.2000 -  3.1200    1.00     2653   170  0.2282 0.3138        
REMARK   3    14  3.1200 -  3.0400    1.00     2637   164  0.2316 0.3043        
REMARK   3    15  3.0400 -  2.9700    1.00     2644   145  0.2354 0.2828        
REMARK   3    16  2.9700 -  2.9100    1.00     2694   133  0.2459 0.3183        
REMARK   3    17  2.9100 -  2.8500    1.00     2676   120  0.2560 0.3576        
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)     : 0.370            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.500           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.11                          
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN A AND ((RESID 4 AND (NAME N OR       
REMARK   3                          NAME CA OR NAME C OR NAME O OR NAME CB ))   
REMARK   3                          OR RESID 5 THROUGH 53 OR RESID 55 THROUGH   
REMARK   3                          60 OR (RESID 61 THROUGH 62 AND (NAME N OR   
REMARK   3                          NAME CA OR NAME C OR NAME O OR NAME CB ))   
REMARK   3                          OR RESID 63 THROUGH 90 OR (RESID 91 AND     
REMARK   3                          (NAME N OR NAME CA OR NAME C OR NAME O OR   
REMARK   3                          NAME CB )) OR RESID 92 THROUGH 249 OR       
REMARK   3                          RESID 251 THROUGH 290 OR (RESID 291 AND     
REMARK   3                          (NAME N OR NAME CA OR NAME C OR NAME O OR   
REMARK   3                          NAME CB )) OR RESID 292 THROUGH 380 OR      
REMARK   3                          RESID 382 THROUGH 515 OR (RESID 516 AND     
REMARK   3                          (NAME N OR NAME CA OR NAME C OR NAME O OR   
REMARK   3                          NAME CB )) OR RESID 517 THROUGH 524 OR      
REMARK   3                          RESID 526 THROUGH 542))                     
REMARK   3     SELECTION          : (CHAIN B AND (RESID 4 THROUGH 53 OR RESID   
REMARK   3                          55 THROUGH 249 OR RESID 251 THROUGH 380     
REMARK   3                          OR RESID 382 THROUGH 490 OR RESID 498       
REMARK   3                          THROUGH 524 OR RESID 526 THROUGH 542))      
REMARK   3     ATOM PAIRS NUMBER  : 4857                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 7E3I COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-FEB-21.                  
REMARK 100 THE DEPOSITION ID IS D_1300018935.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-SEP-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0 - 9.0                          
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.7                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER2 X 16M               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48576                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.020                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.15000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.94                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.56600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.600                              
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: 4EY4                                                 
REMARK 200                                                                      
REMARK 200 REMARK: CLUSTERED HEXAGONAL ROD SHAPED CRYSTALS OF SIZE ~ 10 X 10    
REMARK 200  X 300 UM                                                            
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.38                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS HCL BUFFER PH 9.0, 20 %      
REMARK 280  PEG 3350, 200 MM KNO3, VAPOR DIFFUSION, HANGING DROP,               
REMARK 280  TEMPERATURE 293.15K                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      107.50033            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      215.00067            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      215.00067            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      107.50033            
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: 4520 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 37820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 11.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     THR A   262                                                      
REMARK 465     GLY A   263                                                      
REMARK 465     GLY A   264                                                      
REMARK 465     GLU A   491                                                      
REMARK 465     PRO A   492                                                      
REMARK 465     ARG A   493                                                      
REMARK 465     ASP A   494                                                      
REMARK 465     PRO A   495                                                      
REMARK 465     LYS A   496                                                      
REMARK 465     ALA A   497                                                      
REMARK 465     THR A   543                                                      
REMARK 465     PRO B   259                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     GLY B   261                                                      
REMARK 465     THR B   262                                                      
REMARK 465     GLY B   263                                                      
REMARK 465     GLY B   264                                                      
REMARK 465     ARG B   493                                                      
REMARK 465     ASP B   494                                                      
REMARK 465     PRO B   495                                                      
REMARK 465     LYS B   496                                                      
REMARK 465     ALA B   497                                                      
REMARK 465     THR B   543                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU B   4    CG   CD   OE1  OE2                                  
REMARK 470     ASP B  61    CG   OD1  OD2                                       
REMARK 470     GLU B  91    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 291    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 516    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 258   C   -  N   -  CA  ANGL. DEV. =   9.0 DEGREES          
REMARK 500    PRO B 492   C   -  N   -  CA  ANGL. DEV. =   9.1 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       -3.45     78.04                                   
REMARK 500    ALA A  62       70.10   -102.14                                   
REMARK 500    SER A 203     -121.62     44.49                                   
REMARK 500    ASP A 306      -90.14    -85.41                                   
REMARK 500    VAL A 367       75.31   -117.79                                   
REMARK 500    HIS A 387       59.29   -140.83                                   
REMARK 500    VAL A 407      -64.82   -129.53                                   
REMARK 500    ASN A 464       56.77    -99.90                                   
REMARK 500    PHE B  47       -4.05     79.50                                   
REMARK 500    ALA B  62       68.32   -100.03                                   
REMARK 500    SER B 203     -121.18     44.80                                   
REMARK 500    ASP B 306      -91.89    -84.48                                   
REMARK 500    VAL B 367       72.43   -119.62                                   
REMARK 500    VAL B 407      -62.61   -128.71                                   
REMARK 500    ASN B 464       56.05   -103.29                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  7E3I A    4   543  UNP    P22303   ACES_HUMAN      35    574             
DBREF  7E3I B    4   543  UNP    P22303   ACES_HUMAN      35    574             
SEQRES   1 A  540  GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY GLY ARG          
SEQRES   2 A  540  LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY PRO VAL          
SEQRES   3 A  540  SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO MET          
SEQRES   4 A  540  GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS GLN PRO          
SEQRES   5 A  540  TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN SER VAL          
SEQRES   6 A  540  CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY PHE GLU          
SEQRES   7 A  540  GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU SER GLU          
SEQRES   8 A  540  ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR PRO ARG          
SEQRES   9 A  540  PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE TYR GLY          
SEQRES  10 A  540  GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP VAL TYR          
SEQRES  11 A  540  ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR VAL LEU          
SEQRES  12 A  540  VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY PHE LEU          
SEQRES  13 A  540  ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN VAL GLY          
SEQRES  14 A  540  LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL GLN GLU          
SEQRES  15 A  540  ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER VAL THR          
SEQRES  16 A  540  LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL GLY MET          
SEQRES  17 A  540  HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE HIS ARG          
SEQRES  18 A  540  ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO TRP ALA          
SEQRES  19 A  540  THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA THR GLN          
SEQRES  20 A  540  LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY THR GLY          
SEQRES  21 A  540  GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG THR ARG          
SEQRES  22 A  540  PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS VAL LEU          
SEQRES  23 A  540  PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL PRO VAL          
SEQRES  24 A  540  VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU ALA LEU          
SEQRES  25 A  540  ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL LEU VAL          
SEQRES  26 A  540  GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU VAL TYR          
SEQRES  27 A  540  GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER LEU ILE          
SEQRES  28 A  540  SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL GLY VAL          
SEQRES  29 A  540  PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL VAL LEU          
SEQRES  30 A  540  HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO ALA ARG          
SEQRES  31 A  540  LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP HIS ASN          
SEQRES  32 A  540  VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG LEU ALA          
SEQRES  33 A  540  ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE GLU HIS          
SEQRES  34 A  540  ARG ALA SER THR LEU SER TRP PRO LEU TRP MET GLY VAL          
SEQRES  35 A  540  PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY ILE PRO          
SEQRES  36 A  540  LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU LYS ILE          
SEQRES  37 A  540  PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN PHE ALA          
SEQRES  38 A  540  ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO LYS ALA          
SEQRES  39 A  540  PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN GLN TYR          
SEQRES  40 A  540  VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG ARG GLY          
SEQRES  41 A  540  LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG PHE LEU          
SEQRES  42 A  540  PRO LYS LEU LEU SER ALA THR                                  
SEQRES   1 B  540  GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY GLY ARG          
SEQRES   2 B  540  LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY PRO VAL          
SEQRES   3 B  540  SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO MET          
SEQRES   4 B  540  GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS GLN PRO          
SEQRES   5 B  540  TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN SER VAL          
SEQRES   6 B  540  CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY PHE GLU          
SEQRES   7 B  540  GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU SER GLU          
SEQRES   8 B  540  ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR PRO ARG          
SEQRES   9 B  540  PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE TYR GLY          
SEQRES  10 B  540  GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP VAL TYR          
SEQRES  11 B  540  ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR VAL LEU          
SEQRES  12 B  540  VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY PHE LEU          
SEQRES  13 B  540  ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN VAL GLY          
SEQRES  14 B  540  LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL GLN GLU          
SEQRES  15 B  540  ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER VAL THR          
SEQRES  16 B  540  LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL GLY MET          
SEQRES  17 B  540  HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE HIS ARG          
SEQRES  18 B  540  ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO TRP ALA          
SEQRES  19 B  540  THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA THR GLN          
SEQRES  20 B  540  LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY THR GLY          
SEQRES  21 B  540  GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG THR ARG          
SEQRES  22 B  540  PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS VAL LEU          
SEQRES  23 B  540  PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL PRO VAL          
SEQRES  24 B  540  VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU ALA LEU          
SEQRES  25 B  540  ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL LEU VAL          
SEQRES  26 B  540  GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU VAL TYR          
SEQRES  27 B  540  GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER LEU ILE          
SEQRES  28 B  540  SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL GLY VAL          
SEQRES  29 B  540  PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL VAL LEU          
SEQRES  30 B  540  HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO ALA ARG          
SEQRES  31 B  540  LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP HIS ASN          
SEQRES  32 B  540  VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG LEU ALA          
SEQRES  33 B  540  ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE GLU HIS          
SEQRES  34 B  540  ARG ALA SER THR LEU SER TRP PRO LEU TRP MET GLY VAL          
SEQRES  35 B  540  PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY ILE PRO          
SEQRES  36 B  540  LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU LYS ILE          
SEQRES  37 B  540  PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN PHE ALA          
SEQRES  38 B  540  ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO LYS ALA          
SEQRES  39 B  540  PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN GLN TYR          
SEQRES  40 B  540  VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG ARG GLY          
SEQRES  41 B  540  LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG PHE LEU          
SEQRES  42 B  540  PRO LYS LEU LEU SER ALA THR                                  
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    FUC  C   3      10                                                       
HET    NAG  D   1      14                                                       
HET    FUC  D   2      10                                                       
HET    THA  A 601      15                                                       
HET    PE8  A 602      25                                                       
HET    THA  B 601      15                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     FUC ALPHA-L-FUCOPYRANOSE                                             
HETNAM     THA TACRINE                                                          
HETNAM     PE8 3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL                    
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
HETSYN     FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-              
HETSYN   2 FUC  FUCOSE; FUCOSE                                                  
FORMUL   3  NAG    3(C8 H15 N O6)                                               
FORMUL   3  FUC    2(C6 H12 O5)                                                 
FORMUL   5  THA    2(C13 H14 N2)                                                
FORMUL   6  PE8    C16 H34 O9                                                   
FORMUL   8  HOH   *31(H2 O)                                                     
HELIX    1 AA1 ASP A    5  GLU A    7  5                                   3    
HELIX    2 AA2 MET 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  ARG A  143  1                                   9    
HELIX    6 AA6 GLY A  154  LEU A  159  1                                   6    
HELIX    7 AA7 ASN A  170  VAL A  187  1                                  18    
HELIX    8 AA8 ALA A  188  PHE A  190  5                                   3    
HELIX    9 AA9 SER A  203  LEU A  214  1                                  12    
HELIX   10 AB1 SER A  215  GLY A  220  1                                   6    
HELIX   11 AB2 MET A  241  VAL A  255  1                                  15    
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  ALA A  318  1                                   8    
HELIX   16 AB7 GLY A  335  GLY A  342  5                                   8    
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  ASP A  460  5                                   5    
HELIX   24 AC6 THR A  466  GLY A  487  1                                  22    
HELIX   25 AC7 ARG A  525  ARG A  534  1                                  10    
HELIX   26 AC8 ARG A  534  SER A  541  1                                   8    
HELIX   27 AC9 ASP B    5  GLU B    7  5                                   3    
HELIX   28 AD1 MET 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  ARG B  143  1                                   9    
HELIX   32 AD5 VAL B  153  LEU B  159  1                                   7    
HELIX   33 AD6 ASN B  170  VAL B  187  1                                  18    
HELIX   34 AD7 ALA B  188  PHE B  190  5                                   3    
HELIX   35 AD8 SER B  203  LEU B  214  1                                  12    
HELIX   36 AD9 SER B  215  GLY B  220  1                                   6    
HELIX   37 AE1 MET B  241  VAL B  255  1                                  15    
HELIX   38 AE2 ASP B  266  THR B  275  1                                  10    
HELIX   39 AE3 PRO B  277  HIS B  284  1                                   8    
HELIX   40 AE4 GLU B  285  LEU B  289  5                                   5    
HELIX   41 AE5 THR B  311  ALA B  318  1                                   8    
HELIX   42 AE6 SER B  336  GLY B  342  5                                   7    
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  PHE B  455  1                                   6    
HELIX   49 AF4 GLY B  456  ASP B  460  5                                   5    
HELIX   50 AF5 THR B  466  GLY B  487  1                                  22    
HELIX   51 AF6 ARG B  525  ARG B  534  1                                  10    
HELIX   52 AF7 ARG B  534  SER B  541  1                                   8    
SHEET    1 AA1 3 LEU A   9  VAL A  12  0                                        
SHEET    2 AA1 3 GLY A  15  ARG A  18 -1  O  LEU A  17   N  VAL A  10           
SHEET    3 AA1 3 VAL A  59  ASP A  61  1  O  VAL A  60   N  ARG A  18           
SHEET    1 AA211 ILE A  20  THR 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  LEU A  99   N  ILE A  35           
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  VAL A 226   N  LEU A 199           
SHEET    8 AA211 GLN A 325  VAL A 331  1  O  LEU A 327   N  ALA A 225           
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  VAL 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 239  GLY A 240  0                                        
SHEET    2 AA3 2 VAL A 302  VAL A 303  1  O  VAL A 303   N  VAL A 239           
SHEET    1 AA4 3 LEU B   9  VAL B  12  0                                        
SHEET    2 AA4 3 GLY B  15  ARG B  18 -1  O  LEU B  17   N  VAL B  10           
SHEET    3 AA4 3 VAL B  59  ASP B  61  1  O  VAL B  60   N  ARG B  16           
SHEET    1 AA511 ILE B  20  LEU B  22  0                                        
SHEET    2 AA511 VAL B  29  PRO B  36 -1  O  VAL B  29   N  LEU B  22           
SHEET    3 AA511 TYR B  98  PRO B 104 -1  O  VAL B 101   N  PHE B  32           
SHEET    4 AA511 VAL B 145  MET B 149 -1  O  SER B 148   N  ASN B 100           
SHEET    5 AA511 THR B 112  ILE B 118  1  N  TRP B 117   O  VAL B 147           
SHEET    6 AA511 GLY B 192  GLU B 202  1  O  THR B 198   N  VAL B 116           
SHEET    7 AA511 ARG B 224  GLN B 228  1  O  VAL B 226   N  LEU B 199           
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  VAL B 511   N  VAL 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 239  GLY B 240  0                                        
SHEET    2 AA6 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  2.04  
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.08  
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.03  
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.04  
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.07  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.03  
LINK         ND2 ASN A 350                 C1  NAG C   1     1555   1555  1.44  
LINK         ND2 ASN B 350                 C1  NAG D   1     1555   1555  1.46  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.46  
LINK         O6  NAG C   1                 C1  FUC C   3     1555   1555  1.44  
LINK         O6  NAG D   1                 C1  FUC D   2     1555   1555  1.43  
CISPEP   1 TYR A  105    PRO A  106          0        -3.15                     
CISPEP   2 TYR B  105    PRO B  106          0        -3.29                     
CISPEP   3 CYS B  257    PRO B  258          0         7.29                     
CRYST1  104.578  104.578  322.501  90.00  90.00 120.00 P 31 2 1     12          
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      0.009562  0.005521  0.000000        0.00000                         
SCALE2      0.000000  0.011042  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003101        0.00000                         
TER    4125      ALA A 542                                                      
TER    8246      ALA B 542                                                      
MASTER      337    0    8   52   32    0    0    6 8333    2  131   84          
END                                                                             

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