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LongText Report for: 6ewk-pdb

Name Class
6ewk-pdb
HEADER    HYDROLASE                               04-NOV-17   6EWK              
TITLE     T. CALIFORNICA ACHE IN COMPLEX WITH A 3-HYDROXY-2-PYRIDINE ALDOXIME.  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ACHE;                                                       
COMPND   5 EC: 3.1.1.7                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: TETRONARCE CALIFORNICA;                         
SOURCE   3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;                               
SOURCE   4 ORGANISM_TAXID: 7787                                                 
KEYWDS    ACETYLCHOLINESTERASE, REACTIVATOR, ALDEHYDE OXIME, ORGANOPHOSPHATE    
KEYWDS   2 POISONING, HYDROLASE                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.DE LA MORA,M.WEIK,A.BRAIKI,R.MOUGEOT,L.JEAN,P.I.RENARD              
REVDAT   1   14-NOV-18 6EWK    0                                                
JRNL        AUTH   T.ZORBAZ,A.BRAIKI,M.KATALINIC,J.RENOU,E.DE LA MORA,G.MERCEY, 
JRNL        AUTH 2 C.GOMEZ,R.MOUGEOT,N.M.HRVAT,N.MARAKOVIC,B.PEREZ,M.WEIK,      
JRNL        AUTH 3 L.JEAN,Z.KOVARIK,P.Y.RENARD                                  
JRNL        TITL   REACTIVATION POTENCY AND BLOOD-BRAIN BARRIER PENETRATION OF  
JRNL        TITL 2 3-HYDROXY-2-PYRIDINE ALDOXIMES IN ORGANOPHOSPHATE POISONING  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.22 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575: ???)                            
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) : 2.22                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.12                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 48625                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.179                           
REMARK   3   R VALUE            (WORKING SET) : 0.177                           
REMARK   3   FREE R VALUE                     : 0.220                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.140                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2014                            
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 29.1244 -  5.3403    0.95     3381   144  0.1681 0.2010        
REMARK   3     2  5.3403 -  4.2429    0.99     3376   149  0.1353 0.1634        
REMARK   3     3  4.2429 -  3.7078    0.99     3348   148  0.1418 0.1825        
REMARK   3     4  3.7078 -  3.3694    1.00     3354   147  0.1534 0.1914        
REMARK   3     5  3.3694 -  3.1282    1.00     3355   147  0.1818 0.2241        
REMARK   3     6  3.1282 -  2.9439    1.00     3311   142  0.1823 0.2395        
REMARK   3     7  2.9439 -  2.7966    1.00     3324   146  0.1852 0.2433        
REMARK   3     8  2.7966 -  2.6749    1.00     3336   143  0.1900 0.2674        
REMARK   3     9  2.6749 -  2.5720    1.00     3294   136  0.2015 0.2719        
REMARK   3    10  2.5720 -  2.4833    1.00     3295   140  0.2114 0.2776        
REMARK   3    11  2.4833 -  2.4057    1.00     3351   143  0.2269 0.2708        
REMARK   3    12  2.4057 -  2.3370    1.00     3277   142  0.2409 0.3141        
REMARK   3    13  2.3370 -  2.2755    0.99     3279   143  0.2577 0.2834        
REMARK   3    14  2.2755 -  2.2200    0.99     3330   144  0.2663 0.2760        
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)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.920           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.19                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.010           4498                                  
REMARK   3   ANGLE     :  1.185           6104                                  
REMARK   3   CHIRALITY :  0.077            639                                  
REMARK   3   PLANARITY :  0.007            790                                  
REMARK   3   DIHEDRAL  : 16.790           1666                                  
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 : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6EWK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-NOV-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200007370.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-SEP-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM30A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48656                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.220                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.120                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.10600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 9.1400                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.22                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.56830                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.100                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.84                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: POLYETHYLEN GLYCOL 200 36 % MES 100 MM   
REMARK 280  PH 5.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 299K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.54667            
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       91.09333            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       91.09333            
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       45.54667            
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 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 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      386.31661            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      364.37333            
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   OD1  ASN A    42     O    HOH A   701              1.91            
REMARK 500   O    HOH A   754     O    HOH A   953              1.98            
REMARK 500   OE2  GLU A   268     O    HOH A   702              2.12            
REMARK 500   O    HOH A   754     O    HOH A   883              2.14            
REMARK 500   OD1  ASP A   128     O    HOH A   703              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  19   O   -  C   -  N   ANGL. DEV. = -10.4 DEGREES          
REMARK 500    ARG A  88   C   -  N   -  CA  ANGL. DEV. =  27.8 DEGREES          
REMARK 500    ARG A  88   C   -  N   -  CA  ANGL. DEV. =  25.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A  45       -7.55     78.09                                   
REMARK 500    ALA A  60       41.68   -109.11                                   
REMARK 500    SER A 108       82.06   -156.35                                   
REMARK 500    LEU A 158       79.54   -114.93                                   
REMARK 500    SER A 200     -121.75     60.20                                   
REMARK 500    GLU A 299      -73.51   -123.78                                   
REMARK 500    GLU A 299      -73.71   -123.66                                   
REMARK 500    THR A 317     -163.81   -164.19                                   
REMARK 500    VAL A 360       68.25   -116.81                                   
REMARK 500    ASP A 380       58.01   -155.57                                   
REMARK 500    VAL A 400      -62.09   -131.92                                   
REMARK 500    HIS A 440      118.21    -38.65                                   
REMARK 500    ASN A 457       35.55     70.54                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ARG A  19         11.38                                           
REMARK 500    ARG A  19         11.64                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1107        DISTANCE =  7.58 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NAG A  603                                                       
REMARK 610     1PE A  605                                                       
REMARK 610     1PE A  606                                                       
REMARK 610     1PE A  607                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue RM0 A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 602 bound   
REMARK 800  to ASN A 59                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 601 bound   
REMARK 800  to ASN A 416                                                        
DBREF  6EWK A    4   535  UNP    P04058   ACES_TETCF      25    556             
SEQRES   1 A  532  SER GLU LEU LEU VAL ASN THR LYS SER GLY LYS VAL MET          
SEQRES   2 A  532  GLY THR ARG VAL PRO VAL LEU SER SER HIS ILE SER ALA          
SEQRES   3 A  532  PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO VAL GLY ASN          
SEQRES   4 A  532  MET ARG PHE ARG ARG PRO GLU PRO LYS LYS PRO TRP SER          
SEQRES   5 A  532  GLY VAL TRP ASN ALA SER THR TYR PRO ASN ASN CYS GLN          
SEQRES   6 A  532  GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE SER GLY SER          
SEQRES   7 A  532  GLU MET TRP ASN PRO ASN ARG GLU MET SER GLU ASP CYS          
SEQRES   8 A  532  LEU TYR LEU ASN ILE TRP VAL PRO SER PRO ARG PRO LYS          
SEQRES   9 A  532  SER THR THR VAL MET VAL TRP ILE TYR GLY GLY GLY PHE          
SEQRES  10 A  532  TYR SER GLY SER SER THR LEU ASP VAL TYR ASN GLY LYS          
SEQRES  11 A  532  TYR LEU ALA TYR THR GLU GLU VAL VAL LEU VAL SER LEU          
SEQRES  12 A  532  SER TYR ARG VAL GLY ALA PHE GLY PHE LEU ALA LEU HIS          
SEQRES  13 A  532  GLY SER GLN GLU ALA PRO GLY ASN VAL GLY LEU LEU ASP          
SEQRES  14 A  532  GLN ARG MET ALA LEU GLN TRP VAL HIS ASP ASN ILE GLN          
SEQRES  15 A  532  PHE PHE GLY GLY ASP PRO LYS THR VAL THR ILE PHE GLY          
SEQRES  16 A  532  GLU SER ALA GLY GLY ALA SER VAL GLY MET HIS ILE LEU          
SEQRES  17 A  532  SER PRO GLY SER ARG ASP LEU PHE ARG ARG ALA ILE LEU          
SEQRES  18 A  532  GLN SER GLY SER PRO ASN CYS PRO TRP ALA SER VAL SER          
SEQRES  19 A  532  VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU LEU GLY ARG          
SEQRES  20 A  532  ASN LEU ASN CYS ASN LEU ASN SER ASP GLU GLU LEU ILE          
SEQRES  21 A  532  HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU LEU ILE ASP          
SEQRES  22 A  532  VAL GLU TRP ASN VAL LEU PRO PHE ASP SER ILE PHE ARG          
SEQRES  23 A  532  PHE SER PHE VAL PRO VAL ILE ASP GLY GLU PHE PHE PRO          
SEQRES  24 A  532  THR SER LEU GLU SER MET LEU ASN SER GLY ASN PHE LYS          
SEQRES  25 A  532  LYS THR GLN ILE LEU LEU GLY VAL ASN LYS ASP GLU GLY          
SEQRES  26 A  532  SER PHE PHE LEU LEU TYR GLY ALA PRO GLY PHE SER LYS          
SEQRES  27 A  532  ASP SER GLU SER LYS ILE SER ARG GLU ASP PHE MET SER          
SEQRES  28 A  532  GLY VAL LYS LEU SER VAL PRO HIS ALA ASN ASP LEU GLY          
SEQRES  29 A  532  LEU ASP ALA VAL THR LEU GLN TYR THR ASP TRP MET ASP          
SEQRES  30 A  532  ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY LEU ASP ASP          
SEQRES  31 A  532  ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO LEU MET HIS          
SEQRES  32 A  532  PHE VAL ASN LYS TYR THR LYS PHE GLY ASN GLY THR TYR          
SEQRES  33 A  532  LEU TYR PHE PHE ASN HIS ARG ALA SER ASN LEU VAL TRP          
SEQRES  34 A  532  PRO GLU TRP MET GLY VAL ILE HIS GLY TYR GLU ILE GLU          
SEQRES  35 A  532  PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU LEU ASN TYR          
SEQRES  36 A  532  THR ALA GLU GLU GLU ALA LEU SER ARG ARG ILE MET HIS          
SEQRES  37 A  532  TYR TRP ALA THR PHE ALA LYS THR GLY ASN PRO ASN GLU          
SEQRES  38 A  532  PRO HIS SER GLN GLU SER LYS TRP PRO LEU PHE THR THR          
SEQRES  39 A  532  LYS GLU GLN LYS PHE ILE ASP LEU ASN THR GLU PRO MET          
SEQRES  40 A  532  LYS VAL HIS GLN ARG LEU ARG VAL GLN MET CYS VAL PHE          
SEQRES  41 A  532  TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN ALA THR              
HET    NAG  A 601      14                                                       
HET    NAG  A 602      14                                                       
HET    NAG  A 603      14                                                       
HET    RM0  A 604      21                                                       
HET    1PE  A 605      10                                                       
HET    1PE  A 606      10                                                       
HET    1PE  A 607       7                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     RM0 2-[(~{E})-HYDROXYIMINOMETHYL]-6-(5-MORPHOLIN-4-                  
HETNAM   2 RM0  YLPENTYL)PYRIDIN-3-OL                                           
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETSYN     1PE PEG400                                                           
FORMUL   2  NAG    3(C8 H15 N O6)                                               
FORMUL   5  RM0    C15 H23 N3 O3                                                
FORMUL   6  1PE    3(C10 H22 O6)                                                
FORMUL   9  HOH   *407(H2 O)                                                    
HELIX    1 AA1 VAL A   40  ARG A   44  5                                   5    
HELIX    2 AA2 PHE A   78  MET A   83  1                                   6    
HELIX    3 AA3 LEU A  127  ASN A  131  5                                   5    
HELIX    4 AA4 GLY A  132  GLU A  140  1                                   9    
HELIX    5 AA5 VAL A  150  LEU A  156  1                                   7    
HELIX    6 AA6 ASN A  167  ILE A  184  1                                  18    
HELIX    7 AA7 GLN A  185  PHE A  187  5                                   3    
HELIX    8 AA8 SER A  200  SER A  212  1                                  13    
HELIX    9 AA9 SER A  215  PHE A  219  5                                   5    
HELIX   10 AB1 SER A  237  LEU A  252  1                                  16    
HELIX   11 AB2 SER A  258  LYS A  269  1                                  12    
HELIX   12 AB3 LYS A  270  GLU A  278  1                                   9    
HELIX   13 AB4 TRP A  279  LEU A  282  5                                   4    
HELIX   14 AB5 SER A  304  SER A  311  1                                   8    
HELIX   15 AB6 GLY A  328  ALA A  336  1                                   9    
HELIX   16 AB7 SER A  348  VAL A  360  1                                  13    
HELIX   17 AB8 ASN A  364  THR A  376  1                                  13    
HELIX   18 AB9 ASN A  383  VAL A  400  1                                  18    
HELIX   19 AC1 VAL A  400  GLY A  415  1                                  16    
HELIX   20 AC2 PRO A  433  GLY A  437  5                                   5    
HELIX   21 AC3 GLU A  443  PHE A  448  1                                   6    
HELIX   22 AC4 GLY A  449  ASN A  457  5                                   9    
HELIX   23 AC5 THR A  459  GLY A  480  1                                  22    
HELIX   24 AC6 ARG A  517  GLN A  526  1                                  10    
HELIX   25 AC7 GLN A  526  THR A  535  1                                  10    
SHEET    1 AA1 3 LEU A   7  THR A  10  0                                        
SHEET    2 AA1 3 GLY A  13  MET A  16 -1  O  VAL A  15   N  VAL A   8           
SHEET    3 AA1 3 VAL A  57  ASN A  59  1  O  TRP A  58   N  MET A  16           
SHEET    1 AA211 THR A  18  VAL A  22  0                                        
SHEET    2 AA211 SER A  25  PRO A  34 -1  O  ILE A  27   N  VAL A  20           
SHEET    3 AA211 TYR A  96  VAL A 101 -1  O  ILE A  99   N  PHE A  30           
SHEET    4 AA211 VAL A 142  SER A 145 -1  O  LEU A 143   N  TRP A 100           
SHEET    5 AA211 THR A 109  ILE A 115  1  N  TRP A 114   O  VAL A 144           
SHEET    6 AA211 GLY A 189  GLU A 199  1  O  THR A 195   N  VAL A 113           
SHEET    7 AA211 ARG A 221  GLN A 225  1  O  GLN A 225   N  GLY A 198           
SHEET    8 AA211 ILE A 319  ASN A 324  1  O  LEU A 320   N  LEU A 224           
SHEET    9 AA211 THR A 418  PHE A 423  1  O  PHE A 423   N  VAL A 323           
SHEET   10 AA211 LYS A 501  LEU A 505  1  O  ILE A 503   N  PHE A 422           
SHEET   11 AA211 VAL A 512  GLN A 514 -1  O  HIS A 513   N  PHE A 502           
SSBOND   1 CYS A   67    CYS A   94                          1555   1555  2.03  
SSBOND   2 CYS A  254    CYS A  265                          1555   1555  2.03  
SSBOND   3 CYS A  402    CYS A  521                          1555   1555  2.04  
LINK         ND2 ASN A  59                 C1  NAG A 602     1555   1555  1.45  
LINK         ND2 ASN A 416                 C1  NAG A 601     1555   1555  1.45  
CISPEP   1 SER A  103    PRO A  104          0         2.18                     
SITE     1 AC1  3 GLU A 455  ASN A 457  HOH A 742                               
SITE     1 AC2 11 TYR A  70  GLY A 118  TYR A 121  SER A 200                    
SITE     2 AC2 11 TRP A 279  PHE A 330  PHE A 331  1PE A 605                    
SITE     3 AC2 11 HOH A 709  HOH A 755  HOH A 985                               
SITE     1 AC3  9 ASP A  72  TRP A  84  SER A 122  PHE A 330                    
SITE     2 AC3  9 RM0 A 604  HOH A 754  HOH A 767  HOH A 792                    
SITE     3 AC3  9 HOH A1014                                                     
SITE     1 AC4  4 GLU A 247  ARG A 250  ASN A 251  ASN A 253                    
SITE     1 AC5  5 ARG A 105  PRO A 106  LYS A 107  GLN A 185                    
SITE     2 AC5  5 PHE A 186                                                     
SITE     1 AC6  3 ASN A  59  SER A  61  HOH A 706                               
SITE     1 AC7  4 ASN A 416  HOH A 778  HOH A 827  HOH A 970                    
CRYST1  111.520  111.520  136.640  90.00  90.00 120.00 P 31 2 1      6          
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      0.008967  0.005177  0.000000        0.00000                         
SCALE2      0.000000  0.010354  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007319        0.00000                         
TER    4278      THR A 535                                                      
MASTER      346    0    7   25   14    0   12    6 4741    1   98   41          
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:
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