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LongText Report for: 6xys-pdb

Name Class
6xys-pdb
HEADER    HYDROLASE                               31-JAN-20   6XYS              
TITLE     UPDATE OF NATIVE ACETYLCHOLINESTERASE FROM DROSOPHILA MELANOGASTER    
CAVEAT     6XYS    NAG A 602 HAS WRONG CHIRALITY AT ATOM C1 BMA A 604 HAS WRONG 
CAVEAT   2 6XYS    CHIRALITY AT ATOM C1                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ACHE;                                                       
COMPND   5 EC: 3.1.1.7;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DROSOPHILA MELANOGASTER;                        
SOURCE   3 ORGANISM_COMMON: FRUIT FLY;                                          
SOURCE   4 ORGANISM_TAXID: 7227;                                                
SOURCE   5 GENE: ACE, CG17907;                                                  
SOURCE   6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SCHNEIDER LINE 2;                       
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID DNA;                          
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: S2-SEC 1/3                                
KEYWDS    ACETYLCHOLINESTERASE, INSECT, CATALYTIC, INTERMEDIATES, HYDROLASE     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.NACHON,J.L.SUSSMAN                                                  
REVDAT   1   18-MAR-20 6XYS    0                                                
SPRSDE     18-MAR-20 6XYS      1QO9                                             
JRNL        AUTH   F.NACHON,T.L.ROSENBERRY,I.SILMAN,J.L.SUSSMAN                 
JRNL        TITL   A SECOND LOOK AT THE CRYSTAL STRUCTURES OFDROSOPHILA         
JRNL        TITL 2 MELANOGASTERACETYLCHOLINESTERASE IN COMPLEX WITH TACRINE     
JRNL        TITL 3 DERIVATIVES PROVIDES INSIGHTS CONCERNING CATALYTIC           
JRNL        TITL 4 INTERMEDIATES AND THE DESIGN OF SPECIFIC INSECTICIDES.       
JRNL        REF    MOLECULES                     V.  25       2020              
JRNL        REFN                   ESSN 1420-3049                               
JRNL        PMID   32155891                                                     
JRNL        DOI    10.3390/MOLECULES25051198                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.HAREL,G.KRYGER,T.L.ROSENBERRY,W.D.MALLENDER,T.LEWIS,       
REMARK   1  AUTH 2 R.J.FLETCHER,J.M.GUSS,I.SILMAN,J.L.SUSSMAN                   
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURES OF DROSOPHILA MELANOGASTER      
REMARK   1  TITL 2 ACETYLCHOLINESTERASE AND OF ITS COMPLEXES WITH TWO POTENT    
REMARK   1  TITL 3 INHIBITORS.                                                  
REMARK   1  REF    PROTEIN SCI.                  V.   9  1063 2000              
REMARK   1  REFN                   ISSN 0961-8368                               
REMARK   1  PMID   10892800                                                     
REMARK   1  DOI    10.1110/PS.9.6.1063                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.46 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.16_3549                                     
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.46                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.18                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 26738                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.233                           
REMARK   3   R VALUE            (WORKING SET) : 0.229                           
REMARK   3   FREE R VALUE                     : 0.296                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1338                            
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 34.1800 -  5.2800    0.97     2694   142  0.1736 0.1928        
REMARK   3     2  5.2800 -  4.2000    0.99     2588   136  0.1646 0.2317        
REMARK   3     3  4.2000 -  3.6700    0.99     2576   136  0.1971 0.2727        
REMARK   3     4  3.6700 -  3.3300    0.99     2551   134  0.2469 0.3641        
REMARK   3     5  3.3300 -  3.0900    1.00     2547   135  0.2885 0.3737        
REMARK   3     6  3.0900 -  2.9100    1.00     2521   132  0.3123 0.3960        
REMARK   3     7  2.9100 -  2.7600    0.99     2520   134  0.3161 0.3719        
REMARK   3     8  2.7600 -  2.6400    0.99     2496   131  0.3357 0.4093        
REMARK   3     9  2.6400 -  2.5400    0.99     2504   132  0.3526 0.4409        
REMARK   3    10  2.5400 -  2.4600    0.95     2403   126  0.3994 0.5233        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.442            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 38.130           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 51.47                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 79.57                          
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      :  0.008           4427                                  
REMARK   3   ANGLE     :  1.044           6026                                  
REMARK   3   CHIRALITY :  0.056            638                                  
REMARK   3   PLANARITY :  0.007            783                                  
REMARK   3   DIHEDRAL  :  7.681           3561                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 94 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  26.6830  61.2624  -7.5890              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7632 T22:   0.8266                                     
REMARK   3      T33:   0.5430 T12:  -0.2579                                     
REMARK   3      T13:   0.1959 T23:  -0.0706                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6415 L22:   2.3309                                     
REMARK   3      L33:   3.6014 L12:  -0.6662                                     
REMARK   3      L13:  -0.2308 L23:   0.7659                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4753 S12:   0.3436 S13:   0.1676                       
REMARK   3      S21:  -1.0063 S22:  -0.0360 S23:  -0.3271                       
REMARK   3      S31:  -0.7755 S32:   1.3245 S33:  -0.1818                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 95 THROUGH 289 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  17.7086  61.6307   2.9363              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5204 T22:   0.4012                                     
REMARK   3      T33:   0.4651 T12:  -0.1633                                     
REMARK   3      T13:   0.0539 T23:  -0.0885                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0066 L22:   3.1076                                     
REMARK   3      L33:   4.5143 L12:  -1.1492                                     
REMARK   3      L13:  -0.2085 L23:   0.5012                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1669 S12:  -0.0664 S13:   0.1285                       
REMARK   3      S21:  -0.5914 S22:   0.0984 S23:   0.0465                       
REMARK   3      S31:  -0.8202 S32:   0.8442 S33:  -0.1299                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 290 THROUGH 375 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  17.9854  73.0646   8.2711              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0431 T22:   0.4697                                     
REMARK   3      T33:   0.6005 T12:  -0.3067                                     
REMARK   3      T13:   0.1213 T23:  -0.0827                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9121 L22:   1.9024                                     
REMARK   3      L33:   3.2924 L12:  -0.7358                                     
REMARK   3      L13:   0.1496 L23:  -0.0034                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0455 S12:  -0.1075 S13:   0.4771                       
REMARK   3      S21:  -0.3384 S22:   0.1423 S23:  -0.2176                       
REMARK   3      S31:  -1.5201 S32:   0.8372 S33:  -0.0840                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 376 THROUGH 499 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  32.8334  65.2159  22.7449              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6375 T22:   1.1942                                     
REMARK   3      T33:   0.6610 T12:  -0.2145                                     
REMARK   3      T13:   0.0603 T23:  -0.2331                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2650 L22:   1.8506                                     
REMARK   3      L33:   2.1336 L12:  -0.6171                                     
REMARK   3      L13:   0.1477 L23:   0.5357                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1498 S12:  -0.1289 S13:   0.2926                       
REMARK   3      S21:   0.0407 S22:   0.5146 S23:  -0.5664                       
REMARK   3      S31:  -0.6561 S32:   1.1918 S33:  -0.2971                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 500 THROUGH 573 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  25.8591  51.3858  23.6718              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3681 T22:   0.9799                                     
REMARK   3      T33:   0.5214 T12:   0.1549                                     
REMARK   3      T13:   0.0325 T23:  -0.0235                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6718 L22:   1.1280                                     
REMARK   3      L33:   3.7980 L12:   0.1691                                     
REMARK   3      L13:  -0.1107 L23:   0.3134                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2620 S12:  -0.3513 S13:  -0.1927                       
REMARK   3      S21:   0.1224 S22:   0.3462 S23:  -0.2167                       
REMARK   3      S31:   0.3685 S32:   1.1307 S33:  -0.2148                       
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 6XYS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-JAN-20.                  
REMARK 100 THE DEPOSITION ID IS D_1292106538.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-JAN-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ELETTRA                            
REMARK 200  BEAMLINE                       : 5.2R                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26803                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.455                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.180                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : 0.04870                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 20.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.46                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.300                              
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: 1QO9                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.83                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 13% MPEG2000, 0.1 M AMMONIUM SULFATE,    
REMARK 280  0.03 M LEUCINE, 0.1 M ACETATE, PH 4.6, VAPOR DIFFUSION, HANGING     
REMARK 280  DROP, TEMPERATURE 292K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       79.50500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       47.31000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       47.31000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      119.25750            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       47.31000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       47.31000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       39.75250            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       47.31000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       47.31000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      119.25750            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       47.31000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       47.31000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       39.75250            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       79.50500            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1550 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 13.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 CL    CL A 606  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 708  LIES ON A SPECIAL POSITION.                          
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     VAL A     1                                                      
REMARK 465     ILE A     2                                                      
REMARK 465     LYS A   103                                                      
REMARK 465     ALA A   104                                                      
REMARK 465     ARG A   105                                                      
REMARK 465     LEU A   106                                                      
REMARK 465     ARG A   107                                                      
REMARK 465     HIS A   108                                                      
REMARK 465     GLY A   109                                                      
REMARK 465     ARG A   110                                                      
REMARK 465     GLY A   111                                                      
REMARK 465     ALA A   112                                                      
REMARK 465     ASN A   113                                                      
REMARK 465     GLY A   114                                                      
REMARK 465     GLY A   115                                                      
REMARK 465     GLU A   116                                                      
REMARK 465     HIS A   117                                                      
REMARK 465     PRO A   118                                                      
REMARK 465     ASN A   119                                                      
REMARK 465     GLY A   120                                                      
REMARK 465     LYS A   121                                                      
REMARK 465     GLN A   122                                                      
REMARK 465     ALA A   123                                                      
REMARK 465     ASP A   124                                                      
REMARK 465     THR A   125                                                      
REMARK 465     ASP A   126                                                      
REMARK 465     HIS A   127                                                      
REMARK 465     LEU A   128                                                      
REMARK 465     ILE A   129                                                      
REMARK 465     HIS A   130                                                      
REMARK 465     ASN A   131                                                      
REMARK 465     GLY A   132                                                      
REMARK 465     ASN A   133                                                      
REMARK 465     PRO A   134                                                      
REMARK 465     GLN A   135                                                      
REMARK 465     ASN A   136                                                      
REMARK 465     THR A   137                                                      
REMARK 465     THR A   138                                                      
REMARK 465     ALA A   574                                                      
REMARK 465     GLY A   575                                                      
REMARK 465     THR A   576                                                      
REMARK 465     CYS A   577                                                      
REMARK 465     ASP A   578                                                      
REMARK 465     GLY A   579                                                      
REMARK 465     ASP A   580                                                      
REMARK 465     SER A   581                                                      
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   O3   MAN A   603     O5   BMA A   604              1.93            
REMARK 500   OD2  ASP A   482     O    HOH A   701              2.07            
REMARK 500   OH   TYR A   461     O    HOH A   702              2.07            
REMARK 500   O    GLU A    72     O    HOH A   703              2.11            
REMARK 500   OD1  ASP A    92     OH   TYR A    95              2.11            
REMARK 500   NH1  ARG A   254     O    HOH A   704              2.12            
REMARK 500   OD1  ASP A   378     O    HOH A   705              2.13            
REMARK 500   O    PHE A   380     O    HOH A   706              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   N    HIS A   303     NZ   LYS A   547     3554     1.89            
REMARK 500   OD1  ASN A   300     CE   LYS A   547     3554     2.08            
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    GLU A  40     -109.41     57.73                                   
REMARK 500    PHE A  44       -3.65     76.22                                   
REMARK 500    ALA A  59       54.82   -106.02                                   
REMARK 500    GLU A  72       54.16   -141.18                                   
REMARK 500    PHE A  77      105.41    -37.89                                   
REMARK 500    ASP A  92       90.31    -62.54                                   
REMARK 500    CYS A  93       -9.80   -151.05                                   
REMARK 500    MET A 153       -9.21   -150.59                                   
REMARK 500    PHE A 178      143.71   -173.71                                   
REMARK 500    ALA A 202       67.44   -152.27                                   
REMARK 500    TRP A 231       40.83    -86.72                                   
REMARK 500    SER A 238     -126.90     63.33                                   
REMARK 500    ASN A 288      -19.19   -144.18                                   
REMARK 500    ASN A 293      -65.06     80.36                                   
REMARK 500    ALA A 294      -20.04     69.46                                   
REMARK 500    LEU A 297      -13.73    -45.52                                   
REMARK 500    ASN A 300       78.65   -156.90                                   
REMARK 500    PRO A 301      -89.76    -63.91                                   
REMARK 500    ALA A 302        7.64    -55.15                                   
REMARK 500    ALA A 339      -92.05   -139.89                                   
REMARK 500    LEU A 354       34.07    -95.42                                   
REMARK 500    GLU A 367      -69.21    -28.37                                   
REMARK 500    ALA A 387       96.26    -69.98                                   
REMARK 500    PRO A 389     -170.73    -69.62                                   
REMARK 500    LYS A 403        2.21    -66.67                                   
REMARK 500    ASN A 422      109.10    -50.94                                   
REMARK 500    PHE A 440      -68.73   -130.05                                   
REMARK 500    TRP A 529       80.62   -161.41                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASN A  288     ASP A  289                  147.91                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  601 through MAN A 605 bound to ASN A 493                            
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1QO9   RELATED DB: PDB                                   
REMARK 900 EARLIER MODEL                                                        
DBREF  6XYS A    1   581  UNP    P07140   ACES_DROME      39    619             
SEQRES   1 A  581  VAL ILE ASP ARG LEU VAL VAL GLN THR SER SER GLY PRO          
SEQRES   2 A  581  VAL ARG GLY ARG SER VAL THR VAL GLN GLY ARG GLU VAL          
SEQRES   3 A  581  HIS VAL TYR THR GLY ILE PRO TYR ALA LYS PRO PRO VAL          
SEQRES   4 A  581  GLU ASP LEU ARG PHE ARG LYS PRO VAL PRO ALA GLU PRO          
SEQRES   5 A  581  TRP HIS GLY VAL LEU ASP ALA THR GLY LEU SER ALA THR          
SEQRES   6 A  581  CYS VAL GLN GLU ARG TYR GLU TYR PHE PRO GLY PHE SER          
SEQRES   7 A  581  GLY GLU GLU ILE TRP ASN PRO ASN THR ASN VAL SER GLU          
SEQRES   8 A  581  ASP CYS LEU TYR ILE ASN VAL TRP ALA PRO ALA LYS ALA          
SEQRES   9 A  581  ARG LEU ARG HIS GLY ARG GLY ALA ASN GLY GLY GLU HIS          
SEQRES  10 A  581  PRO ASN GLY LYS GLN ALA ASP THR ASP HIS LEU ILE HIS          
SEQRES  11 A  581  ASN GLY ASN PRO GLN ASN THR THR ASN GLY LEU PRO ILE          
SEQRES  12 A  581  LEU ILE TRP ILE TYR GLY GLY GLY PHE MET THR GLY SER          
SEQRES  13 A  581  ALA THR LEU ASP ILE TYR ASN ALA ASP ILE MET ALA ALA          
SEQRES  14 A  581  VAL GLY ASN VAL ILE VAL ALA SER PHE GLN TYR ARG VAL          
SEQRES  15 A  581  GLY ALA PHE GLY PHE LEU HIS LEU ALA PRO GLU MET PRO          
SEQRES  16 A  581  SER GLU PHE ALA GLU GLU ALA PRO GLY ASN VAL GLY LEU          
SEQRES  17 A  581  TRP ASP GLN ALA LEU ALA ILE ARG TRP LEU LYS ASP ASN          
SEQRES  18 A  581  ALA HIS ALA PHE GLY GLY ASN PRO GLU TRP MET THR LEU          
SEQRES  19 A  581  PHE GLY GLU SER ALA GLY SER SER SER VAL ASN ALA GLN          
SEQRES  20 A  581  LEU MET SER PRO VAL THR ARG GLY LEU VAL LYS ARG GLY          
SEQRES  21 A  581  MET MET GLN SER GLY THR MET ASN ALA PRO TRP SER HIS          
SEQRES  22 A  581  MET THR SER GLU LYS ALA VAL GLU ILE GLY LYS ALA LEU          
SEQRES  23 A  581  ILE ASN ASP CYS ASN CYS ASN ALA SER MET LEU LYS THR          
SEQRES  24 A  581  ASN PRO ALA HIS VAL MET SER CYS MET ARG SER VAL ASP          
SEQRES  25 A  581  ALA LYS THR ILE SER VAL GLN GLN TRP ASN SER TYR SER          
SEQRES  26 A  581  GLY ILE LEU SER PHE PRO SER ALA PRO THR ILE ASP GLY          
SEQRES  27 A  581  ALA PHE LEU PRO ALA ASP PRO MET THR LEU MET LYS THR          
SEQRES  28 A  581  ALA ASP LEU LYS ASP TYR ASP ILE LEU MET GLY ASN VAL          
SEQRES  29 A  581  ARG ASP GLU GLY THR TYR PHE LEU LEU TYR ASP PHE ILE          
SEQRES  30 A  581  ASP TYR PHE ASP LYS ASP ASP ALA THR ALA LEU PRO ARG          
SEQRES  31 A  581  ASP LYS TYR LEU GLU ILE MET ASN ASN ILE PHE GLY LYS          
SEQRES  32 A  581  ALA THR GLN ALA GLU ARG GLU ALA ILE ILE PHE GLN TYR          
SEQRES  33 A  581  THR SER TRP GLU GLY ASN PRO GLY TYR GLN ASN GLN GLN          
SEQRES  34 A  581  GLN ILE GLY ARG ALA VAL GLY ASP HIS PHE PHE THR CYS          
SEQRES  35 A  581  PRO THR ASN GLU TYR ALA GLN ALA LEU ALA GLU ARG GLY          
SEQRES  36 A  581  ALA SER VAL HIS TYR TYR TYR PHE THR HIS ARG THR SER          
SEQRES  37 A  581  THR SER LEU TRP GLY GLU TRP MET GLY VAL LEU HIS GLY          
SEQRES  38 A  581  ASP GLU ILE GLU TYR PHE PHE GLY GLN PRO LEU ASN ASN          
SEQRES  39 A  581  SER LEU GLN TYR ARG PRO VAL GLU ARG GLU LEU GLY LYS          
SEQRES  40 A  581  ARG MET LEU SER ALA VAL ILE GLU PHE ALA LYS THR GLY          
SEQRES  41 A  581  ASN PRO ALA GLN ASP GLY GLU GLU TRP PRO ASN PHE SER          
SEQRES  42 A  581  LYS GLU ASP PRO VAL TYR TYR ILE PHE SER THR ASP ASP          
SEQRES  43 A  581  LYS ILE GLU LYS LEU ALA ARG GLY PRO LEU ALA ALA ARG          
SEQRES  44 A  581  CYS SER PHE TRP ASN ASP TYR LEU PRO LYS VAL ARG SER          
SEQRES  45 A  581  TRP ALA GLY THR CYS ASP GLY ASP SER                          
HET    NAG  A 601      14                                                       
HET    NAG  A 602      14                                                       
HET    MAN  A 603      11                                                       
HET    BMA  A 604      11                                                       
HET    MAN  A 605      11                                                       
HET     CL  A 606       1                                                       
HET    ACT  A 607       3                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM      CL CHLORIDE ION                                                     
HETNAM     ACT ACETATE ION                                                      
FORMUL   2  NAG    2(C8 H15 N O6)                                               
FORMUL   2  MAN    2(C6 H12 O6)                                                 
FORMUL   2  BMA    C6 H12 O6                                                    
FORMUL   3   CL    CL 1-                                                        
FORMUL   4  ACT    C2 H3 O2 1-                                                  
FORMUL   5  HOH   *94(H2 O)                                                     
HELIX    1 AA1 VAL A   39  ARG A   43  5                                   5    
HELIX    2 AA2 PHE A   77  ILE A   82  1                                   6    
HELIX    3 AA3 LEU A  159  ASN A  163  5                                   5    
HELIX    4 AA4 ALA A  164  ASN A  172  1                                   9    
HELIX    5 AA5 GLY A  183  LEU A  188  1                                   6    
HELIX    6 AA6 LEU A  190  MET A  194  5                                   5    
HELIX    7 AA7 PRO A  195  ALA A  202  5                                   8    
HELIX    8 AA8 ASN A  205  ASN A  221  1                                  17    
HELIX    9 AA9 ALA A  222  PHE A  225  5                                   4    
HELIX   10 AB1 SER A  238  SER A  250  1                                  13    
HELIX   11 AB2 ALA A  269  HIS A  273  5                                   5    
HELIX   12 AB3 THR A  275  CYS A  290  1                                  16    
HELIX   13 AB4 ALA A  302  SER A  310  1                                   9    
HELIX   14 AB5 ASP A  312  GLN A  320  1                                   9    
HELIX   15 AB6 TRP A  321  TYR A  324  5                                   4    
HELIX   16 AB7 ASP A  344  ALA A  352  1                                   9    
HELIX   17 AB8 GLY A  368  PHE A  376  1                                   9    
HELIX   18 AB9 ARG A  390  PHE A  401  1                                  12    
HELIX   19 AC1 THR A  405  TYR A  416  1                                  12    
HELIX   20 AC2 GLY A  424  PHE A  440  1                                  17    
HELIX   21 AC3 PHE A  440  ARG A  454  1                                  15    
HELIX   22 AC4 GLY A  473  GLY A  477  5                                   5    
HELIX   23 AC5 GLU A  483  PHE A  488  1                                   6    
HELIX   24 AC6 GLY A  489  ASN A  493  5                                   5    
HELIX   25 AC7 ARG A  499  GLY A  520  1                                  22    
HELIX   26 AC8 ARG A  553  ASP A  565  1                                  13    
HELIX   27 AC9 ASP A  565  ARG A  571  1                                   7    
SHEET    1 AA1 3 VAL A   6  THR A   9  0                                        
SHEET    2 AA1 3 GLY A  12  ARG A  15 -1  O  GLY A  12   N  THR A   9           
SHEET    3 AA1 3 LEU A  57  ASP A  58  1  O  LEU A  57   N  ARG A  15           
SHEET    1 AA211 ARG A  17  VAL A  21  0                                        
SHEET    2 AA211 ARG A  24  PRO A  33 -1  O  VAL A  26   N  VAL A  19           
SHEET    3 AA211 TYR A  95  PRO A 101 -1  O  ALA A 100   N  HIS A  27           
SHEET    4 AA211 ILE A 174  PHE A 178 -1  O  VAL A 175   N  TRP A  99           
SHEET    5 AA211 LEU A 141  ILE A 147  1  N  LEU A 144   O  ILE A 174           
SHEET    6 AA211 GLY A 227  GLU A 237  1  O  ASN A 228   N  LEU A 141           
SHEET    7 AA211 ARG A 259  GLN A 263  1  O  GLN A 263   N  GLY A 236           
SHEET    8 AA211 ASP A 358  VAL A 364  1  O  ASP A 358   N  GLY A 260           
SHEET    9 AA211 SER A 457  PHE A 463  1  O  PHE A 463   N  ASN A 363           
SHEET   10 AA211 TYR A 539  PHE A 542  1  O  TYR A 540   N  TYR A 460           
SHEET   11 AA211 LEU A 551  ALA A 552 -1  O  ALA A 552   N  TYR A 539           
SSBOND   1 CYS A   66    CYS A   93                          1555   1555  2.07  
SSBOND   2 CYS A  292    CYS A  307                          1555   1555  2.05  
SSBOND   3 CYS A  442    CYS A  560                          1555   1555  2.01  
LINK         OG  SER A 238                 C   ACT A 607     1555   1555  1.43  
LINK         ND2 ASN A 493                 C1  NAG A 601     1555   1555  1.43  
LINK         O4  NAG A 601                 C1  NAG A 602     1555   1555  1.37  
LINK         O4  NAG A 602                 C1  MAN A 603     1555   1555  1.38  
LINK         O3  MAN A 603                 C1  BMA A 604     1555   1555  1.37  
LINK         O3  BMA A 604                 C1  MAN A 605     1555   1555  1.38  
SITE     1 AC1  5 GLY A 150  GLY A 151  SER A 238  ALA A 239                    
SITE     2 AC1  5 HIS A 480                                                     
SITE     1 AC2  7 ARG A  17  VAL A  21  THR A  60  GLY A  61                    
SITE     2 AC2  7 LEU A  62  ILE A 166  ASN A 493                               
CRYST1   94.620   94.620  159.010  90.00  90.00  90.00 P 43 21 2     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      0.010569  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010569  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006289        0.00000                         
TER    4240      TRP A 573                                                      
MASTER      474    0    7   27   14    0    4    6 4376    1   72   45          
END                                                                             

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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.
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