Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 6zwe-pdb

Name Class
6zwe-pdb
HEADER    HYDROLASE                               28-JUL-20   6ZWE              
TITLE     CRYSTAL STRUCTURE OF HUMAN ACETYLCHOLINESTERASE IN COMPLEX WITH ((6-  
TITLE    2 ((2E,4E)-5-(BENZO[D][1,3]DIOXOL-5-YL)PENTA-2,4-DIENAMIDO)HEXYL)      
TITLE    3 TRIPHENYLPHOSPHONIUM BROMIDE)                                        
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: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029                                       
KEYWDS    HUMAN ACETYLCHOLINESTERASE, PIPERINE DERIVATIVE, MITOCHONDRIA,        
KEYWDS   2 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    O.DA SILVA,J.DIAS,F.NACHON,X.BRAZZOLOTTO                              
REVDAT   1   09-JUN-21 6ZWE    0                                                
JRNL        AUTH   D.CHAVARRIA,O.DA SILVA,S.BENFEITO,S.BARREIRO,J.GARRIDO,      
JRNL        AUTH 2 F.CAGIDE,P.SOARES,F.REMIAO,X.BRAZZOLOTTO,F.NACHON,           
JRNL        AUTH 3 P.J.OLIVEIRA,J.DIAS,F.BORGES                                 
JRNL        TITL   FINE-TUNING THE BIOLOGICAL PROFILE OF MULTITARGET            
JRNL        TITL 2 MITOCHONDRIOTROPIC ANTIOXIDANTS FOR NEURODEGENERATIVE        
JRNL        TITL 3 DISEASES.                                                    
JRNL        REF    ANTIOXIDANTS (BASEL)          V.  10       2021              
JRNL        REFN                   ISSN 2076-3921                               
JRNL        PMID   33672269                                                     
JRNL        DOI    10.3390/ANTIOX10020329                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 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 : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 78.09                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.390                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 59024                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1180                            
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 78.0900 -  6.0000    1.00     7352   151  0.1722 0.2216        
REMARK   3     2  6.0000 -  4.7600    1.00     7267   148  0.1828 0.2075        
REMARK   3     3  4.7600 -  4.1600    1.00     7235   148  0.1696 0.2227        
REMARK   3     4  4.1600 -  3.7800    1.00     7202   147  0.1932 0.2200        
REMARK   3     5  3.7800 -  3.5100    1.00     7211   147  0.2158 0.2897        
REMARK   3     6  3.5100 -  3.3000    1.00     7167   145  0.2486 0.2680        
REMARK   3     7  3.3000 -  3.1400    1.00     7209   147  0.2840 0.3440        
REMARK   3     8  3.1400 -  3.0000    1.00     7201   147  0.3342 0.3924        
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)     : 0.394            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.973           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 85.22                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 97.42                          
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      :  0.004           8859                                  
REMARK   3   ANGLE     :  0.871          12125                                  
REMARK   3   CHIRALITY :  0.058           1300                                  
REMARK   3   PLANARITY :  0.007           1581                                  
REMARK   3   DIHEDRAL  : 21.592           1268                                  
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 5 THROUGH 363 OR      
REMARK   3                          RESID 365 THROUGH 380 OR RESID 382          
REMARK   3                          THROUGH 543 OR RESID 600 THROUGH 602))      
REMARK   3     SELECTION          : (CHAIN 'B' AND (RESID 5 THROUGH 258 OR      
REMARK   3                          RESID 265 THROUGH 363 OR RESID 365          
REMARK   3                          THROUGH 380 OR RESID 382 THROUGH 492 OR     
REMARK   3                          (RESID 493 AND (NAME N OR NAME CA OR NAME   
REMARK   3                          C OR NAME O OR NAME CB OR NAME CG OR NAME   
REMARK   3                          CD )) OR RESID 494 THROUGH 543 OR RESID     
REMARK   3                          600 THROUGH 602))                           
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6ZWE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-JUL-20.                  
REMARK 100 THE DEPOSITION ID IS D_1292110380.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-APR-19                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 2                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9801                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 9M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 59080                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 78.090                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 39.80                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 20.8100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4EY4                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 80.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M LISO4, 100 MM HEPES PH7, 60 MM     
REMARK 280  MGSO4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
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   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
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       38.63333            
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       77.26667            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       57.95000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       96.58333            
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       19.31667            
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: 9820 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 40140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -340.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E                         
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     GLY A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     GLU A     4                                                      
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     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
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     ARG A 493    NE   CZ   NH1  NH2                                  
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   OG   SER A   203     O    HOH A   701              2.17            
REMARK 500   O    HOH B   705     O    HOH B   729              2.17            
REMARK 500   OG1  THR A   504     O2   SO4 A   606              2.18            
REMARK 500   O    LEU B   221     O    HOH B   701              2.18            
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    ALA A  62       40.73   -107.87                                   
REMARK 500    PRO A 106       95.41    -63.89                                   
REMARK 500    PHE A 123       16.41     59.80                                   
REMARK 500    SER A 203     -124.07     51.76                                   
REMARK 500    PHE A 307      -59.52     71.89                                   
REMARK 500    VAL A 367       71.65   -113.30                                   
REMARK 500    VAL A 407      -61.45   -120.58                                   
REMARK 500    ASN A 464       51.63    -95.66                                   
REMARK 500    ARG A 493       51.10    -91.18                                   
REMARK 500    ASP A 494       77.73   -161.37                                   
REMARK 500    LEU A 518      107.36    -51.38                                   
REMARK 500    ASP B   5     -168.48   -113.83                                   
REMARK 500    PRO B 106       95.19     25.31                                   
REMARK 500    PHE B 158       10.48   -144.61                                   
REMARK 500    SER B 203     -116.58     45.38                                   
REMARK 500    PRO B 217        0.18    -62.11                                   
REMARK 500    ASP B 306      -82.34    -88.71                                   
REMARK 500    ALA B 318       60.65   -113.44                                   
REMARK 500    VAL B 367       72.28   -112.44                                   
REMARK 500    VAL B 407      -52.09   -123.03                                   
REMARK 500    ASN B 464       45.04    -93.53                                   
REMARK 500    ARG B 493       57.40   -158.94                                   
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 TYR B  105     PRO B  106                 -138.36                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6ZWE A    2   543  UNP    P22303   ACES_HUMAN      33    574             
DBREF  6ZWE B    2   543  UNP    P22303   ACES_HUMAN      33    574             
SEQRES   1 A  542  GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY          
SEQRES   2 A  542  GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY          
SEQRES   3 A  542  PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO          
SEQRES   4 A  542  PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS          
SEQRES   5 A  542  GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN          
SEQRES   6 A  542  SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY          
SEQRES   7 A  542  PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU          
SEQRES   8 A  542  SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR          
SEQRES   9 A  542  PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE          
SEQRES  10 A  542  TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP          
SEQRES  11 A  542  VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR          
SEQRES  12 A  542  VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY          
SEQRES  13 A  542  PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN          
SEQRES  14 A  542  VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL          
SEQRES  15 A  542  GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER          
SEQRES  16 A  542  VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL          
SEQRES  17 A  542  GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE          
SEQRES  18 A  542  HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO          
SEQRES  19 A  542  TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA          
SEQRES  20 A  542  THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY          
SEQRES  21 A  542  THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG          
SEQRES  22 A  542  THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS          
SEQRES  23 A  542  VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL          
SEQRES  24 A  542  PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU          
SEQRES  25 A  542  ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL          
SEQRES  26 A  542  LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU          
SEQRES  27 A  542  VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER          
SEQRES  28 A  542  LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL          
SEQRES  29 A  542  GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL          
SEQRES  30 A  542  VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO          
SEQRES  31 A  542  ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP          
SEQRES  32 A  542  HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG          
SEQRES  33 A  542  LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE          
SEQRES  34 A  542  GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP MET          
SEQRES  35 A  542  GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY          
SEQRES  36 A  542  ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU          
SEQRES  37 A  542  LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN          
SEQRES  38 A  542  PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO          
SEQRES  39 A  542  LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN          
SEQRES  40 A  542  GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG          
SEQRES  41 A  542  ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG          
SEQRES  42 A  542  PHE LEU PRO LYS LEU LEU SER ALA THR                          
SEQRES   1 B  542  GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY          
SEQRES   2 B  542  GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY          
SEQRES   3 B  542  PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO          
SEQRES   4 B  542  PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS          
SEQRES   5 B  542  GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN          
SEQRES   6 B  542  SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY          
SEQRES   7 B  542  PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU          
SEQRES   8 B  542  SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR          
SEQRES   9 B  542  PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE          
SEQRES  10 B  542  TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP          
SEQRES  11 B  542  VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR          
SEQRES  12 B  542  VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY          
SEQRES  13 B  542  PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN          
SEQRES  14 B  542  VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL          
SEQRES  15 B  542  GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER          
SEQRES  16 B  542  VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL          
SEQRES  17 B  542  GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE          
SEQRES  18 B  542  HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO          
SEQRES  19 B  542  TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA          
SEQRES  20 B  542  THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY          
SEQRES  21 B  542  THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG          
SEQRES  22 B  542  THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS          
SEQRES  23 B  542  VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL          
SEQRES  24 B  542  PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU          
SEQRES  25 B  542  ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL          
SEQRES  26 B  542  LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU          
SEQRES  27 B  542  VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER          
SEQRES  28 B  542  LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL          
SEQRES  29 B  542  GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL          
SEQRES  30 B  542  VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO          
SEQRES  31 B  542  ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP          
SEQRES  32 B  542  HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG          
SEQRES  33 B  542  LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE          
SEQRES  34 B  542  GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP MET          
SEQRES  35 B  542  GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY          
SEQRES  36 B  542  ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU          
SEQRES  37 B  542  LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN          
SEQRES  38 B  542  PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO          
SEQRES  39 B  542  LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN          
SEQRES  40 B  542  GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG          
SEQRES  41 B  542  ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG          
SEQRES  42 B  542  PHE LEU 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    NAG  D   2      14                                                       
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET    FUC  E   3      10                                                       
HET    NAG  A 601      14                                                       
HET    QRH  A 602      41                                                       
HET    SO4  A 603       5                                                       
HET    SO4  A 604       5                                                       
HET    SO4  A 605       5                                                       
HET    SO4  A 606       5                                                       
HET    SO4  A 607       5                                                       
HET    SO4  A 608       5                                                       
HET    SO4  A 609       5                                                       
HET    SO4  A 610       5                                                       
HET    SO4  A 611       5                                                       
HET    SO4  A 612       5                                                       
HET     BR  A 613       1                                                       
HET     CL  A 614       1                                                       
HET     CL  A 615       1                                                       
HET     CL  A 616       1                                                       
HET     CL  A 617       1                                                       
HET     CL  A 618       1                                                       
HET     CL  A 619       1                                                       
HET     CL  A 620       1                                                       
HET     CL  A 621       1                                                       
HET     CL  A 622       1                                                       
HET     CL  A 623       1                                                       
HET     CL  A 624       1                                                       
HET    SO4  B 601       5                                                       
HET    SO4  B 602       5                                                       
HET    SO4  B 603       5                                                       
HET    SO4  B 604       5                                                       
HET    SO4  B 605       5                                                       
HET    SO4  B 606       5                                                       
HET    SO4  B 607       5                                                       
HET    SO4  B 608       5                                                       
HET     BR  B 609       1                                                       
HET     CL  B 610       1                                                       
HET     CL  B 611       1                                                       
HET     CL  B 612       1                                                       
HET     CL  B 613       1                                                       
HET     CL  B 614       1                                                       
HET     CL  B 615       1                                                       
HET     CL  B 616       1                                                       
HET     CL  B 617       1                                                       
HET     CL  B 618       1                                                       
HET     CL  B 619       1                                                       
HET     CL  B 620       1                                                       
HET     CL  B 621       1                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     FUC ALPHA-L-FUCOPYRANOSE                                             
HETNAM     QRH (2~{E},4~{E})-5-(1,3-BENZODIOXOL-5-YL)-~{N}-[6-                  
HETNAM   2 QRH  (TRIPHENYL-$L^{5}-PHOSPHANYL)HEXYL]PENTA-2,4-DIENAMIDE          
HETNAM     SO4 SULFATE ION                                                      
HETNAM      BR BROMIDE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
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    7(C8 H15 N O6)                                               
FORMUL   3  FUC    2(C6 H12 O5)                                                 
FORMUL   7  QRH    C36 H38 N O3 P                                               
FORMUL   8  SO4    18(O4 S 2-)                                                  
FORMUL  18   BR    2(BR 1-)                                                     
FORMUL  19   CL    23(CL 1-)                                                    
FORMUL  51  HOH   *145(H2 O)                                                    
HELIX    1 AA1 MET A   42  ARG A   46  5                                   5    
HELIX    2 AA2 PHE A   80  MET A   85  1                                   6    
HELIX    3 AA3 LEU A  130  ASP A  134  5                                   5    
HELIX    4 AA4 GLY A  135  ARG A  143  1                                   9    
HELIX    5 AA5 VAL A  153  LEU A  159  1                                   7    
HELIX    6 AA6 ASN A  170  VAL A  187  1                                  18    
HELIX    7 AA7 ALA A  188  PHE A  190  5                                   3    
HELIX    8 AA8 SER A  203  LEU A  214  1                                  12    
HELIX    9 AA9 SER A  215  GLY A  220  1                                   6    
HELIX   10 AB1 MET A  241  VAL A  255  1                                  15    
HELIX   11 AB2 ASP A  266  ARG A  276  1                                  11    
HELIX   12 AB3 PRO A  277  HIS A  284  1                                   8    
HELIX   13 AB4 GLU A  285  LEU A  289  5                                   5    
HELIX   14 AB5 THR A  311  ALA A  318  1                                   8    
HELIX   15 AB6 GLY A  335  VAL A  340  1                                   6    
HELIX   16 AB7 SER A  355  VAL A  367  1                                  13    
HELIX   17 AB8 SER A  371  THR A  383  1                                  13    
HELIX   18 AB9 ASP A  390  VAL A  407  1                                  18    
HELIX   19 AC1 VAL A  407  GLN A  421  1                                  15    
HELIX   20 AC2 PRO A  440  GLY A  444  5                                   5    
HELIX   21 AC3 GLU A  450  PHE A  455  1                                   6    
HELIX   22 AC4 GLY A  456  ASP A  460  5                                   5    
HELIX   23 AC5 THR A  466  GLY A  487  1                                  22    
HELIX   24 AC6 ARG A  525  ARG A  534  1                                  10    
HELIX   25 AC7 ARG A  534  THR A  543  1                                  10    
HELIX   26 AC8 MET B   42  ARG B   46  5                                   5    
HELIX   27 AC9 PHE B   80  MET B   85  1                                   6    
HELIX   28 AD1 LEU B  130  ASP B  134  5                                   5    
HELIX   29 AD2 GLY B  135  ARG B  143  1                                   9    
HELIX   30 AD3 VAL B  153  LEU B  159  1                                   7    
HELIX   31 AD4 ASN B  170  VAL B  187  1                                  18    
HELIX   32 AD5 ALA B  188  PHE B  190  5                                   3    
HELIX   33 AD6 SER B  203  LEU B  213  1                                  11    
HELIX   34 AD7 SER B  215  GLY B  220  1                                   6    
HELIX   35 AD8 MET B  241  VAL B  255  1                                  15    
HELIX   36 AD9 GLY B  264  ARG B  276  1                                  13    
HELIX   37 AE1 PRO B  277  HIS B  284  1                                   8    
HELIX   38 AE2 GLU B  285  LEU B  289  5                                   5    
HELIX   39 AE3 THR B  311  ALA B  318  1                                   8    
HELIX   40 AE4 GLY B  335  VAL B  340  1                                   6    
HELIX   41 AE5 SER B  355  VAL B  367  1                                  13    
HELIX   42 AE6 SER B  371  THR B  383  1                                  13    
HELIX   43 AE7 ASP B  390  VAL B  407  1                                  18    
HELIX   44 AE8 VAL B  407  GLN B  421  1                                  15    
HELIX   45 AE9 PRO B  440  GLY B  444  5                                   5    
HELIX   46 AF1 GLU B  450  PHE B  455  1                                   6    
HELIX   47 AF2 GLY B  456  ASP B  460  5                                   5    
HELIX   48 AF3 THR B  466  GLY B  487  1                                  22    
HELIX   49 AF4 ARG B  525  ARG B  534  1                                  10    
HELIX   50 AF5 ARG B  534  THR B  543  1                                  10    
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  16           
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  LEU A 115   O  VAL A 147           
SHEET    6 AA211 GLY A 192  GLU A 202  1  O  ASP A 193   N  THR A 112           
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  LEU A 227           
SHEET    9 AA211 ARG A 424  PHE A 430  1  O  PHE A 430   N  VAL A 330           
SHEET   10 AA211 GLN A 509  LEU A 513  1  O  LEU A 513   N  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  68  CYS A  69  0                                        
SHEET    2 AA3 2 LEU A  92  SER A  93  1  O  SER A  93   N  VAL A  68           
SHEET    1 AA4 2 VAL A 239  GLY A 240  0                                        
SHEET    2 AA4 2 VAL A 302  VAL A 303  1  O  VAL A 303   N  VAL A 239           
SHEET    1 AA5 3 LEU B   9  VAL B  12  0                                        
SHEET    2 AA5 3 GLY B  15  ARG B  18 -1  O  LEU B  17   N  VAL B  10           
SHEET    3 AA5 3 VAL B  59  ASP B  61  1  O  VAL B  60   N  ARG B  16           
SHEET    1 AA611 ILE B  20  THR B  24  0                                        
SHEET    2 AA611 GLY B  27  PRO B  36 -1  O  VAL B  29   N  LEU B  22           
SHEET    3 AA611 TYR B  98  PRO B 104 -1  O  LEU B  99   N  ILE B  35           
SHEET    4 AA611 VAL B 145  MET B 149 -1  O  LEU B 146   N  TRP B 102           
SHEET    5 AA611 THR B 112  ILE B 118  1  N  LEU B 115   O  VAL B 147           
SHEET    6 AA611 GLY B 192  GLU B 202  1  O  PHE B 200   N  VAL B 116           
SHEET    7 AA611 ARG B 224  GLN B 228  1  O  VAL B 226   N  LEU B 199           
SHEET    8 AA611 GLN B 325  VAL B 331  1  O  LEU B 327   N  LEU B 227           
SHEET    9 AA611 ARG B 424  PHE B 430  1  O  TYR B 426   N  VAL B 328           
SHEET   10 AA611 GLN B 509  LEU B 513  1  O  LEU B 513   N  VAL B 429           
SHEET   11 AA611 GLU B 519  ARG B 522 -1  O  ARG B 521   N  TYR B 510           
SHEET    1 AA7 2 VAL B  68  CYS B  69  0                                        
SHEET    2 AA7 2 LEU B  92  SER B  93  1  O  SER B  93   N  VAL B  68           
SHEET    1 AA8 2 VAL B 239  GLY B 240  0                                        
SHEET    2 AA8 2 VAL B 302  VAL B 303  1  O  VAL B 303   N  VAL B 239           
SSBOND   1 CYS A   69    CYS A   96                          1555   1555  2.03  
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.04  
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  2.03  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.03  
LINK         ND2 ASN A 265                 C1  NAG D   1     1555   1555  1.44  
LINK         ND2 ASN A 350                 C1  NAG C   1     1555   1555  1.43  
LINK         ND2 ASN A 464                 C1  NAG A 601     1555   1555  1.44  
LINK         ND2 ASN B 350                 C1  NAG E   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  1.45  
LINK         O3  NAG D   1                 C1  NAG D   2     1555   1555  1.46  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.46  
LINK         O6  NAG E   1                 C1  FUC E   3     1555   1555  1.47  
CRYST1  211.350  211.350  115.900  90.00  90.00 120.00 P 61         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      0.004731  0.002732  0.000000        0.00000                         
SCALE2      0.000000  0.005463  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008628        0.00000                         
TER    4157      THR A 543                                                      
TER    8365      THR B 543                                                      
MASTER      310    0   53   50   36    0    0    6 8754    2  265   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
webmaster

Acknowledgements and disclaimer