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LongText Report for: 6qab-pdb

Name Class
6qab-pdb
HEADER    HYDROLASE                               19-DEC-18   6QAB              
TITLE     HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH (S)-N-(1-((2-             
TITLE    2 CYCLOHEPTYLETHYL)AMINO)-3-(1H-INDOL-3-YL)-1-OXOPROPAN-2-YL)-N,N-     
TITLE    3 DIMETHYLBUTAN-1-AMINIUM                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLINESTERASE;                                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ACYLCHOLINE ACYLHYDROLASE,BUTYRYLCHOLINE ESTERASE,CHOLINE   
COMPND   5 ESTERASE II,PSEUDOCHOLINESTERASE;                                    
COMPND   6 EC: 3.1.1.8;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 OTHER_DETAILS: RESIDUES 1-20 ARE SIGNAL PEPTIDENAG AND FUC ARE       
COMPND  10 GLYCOSYLATIONSDMS IS DMSOGOL IS GLYCEROLMES IS MES BUFFER266 IS THE  
COMPND  11 LIGAND                                                               
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: BCHE, CHE1;                                                    
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029                                       
KEYWDS    BUTYRYLCHOLINESTERASE, INHIBITOR, COMPLEX, HYDROLASE                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.BRAZZOLOTTO,F.NACHON,M.HARST,D.KNEZ,S.GOBEC                         
REVDAT   1   27-MAR-19 6QAB    0                                                
JRNL        AUTH   A.MEDEN,D.KNEZ,M.JUKIC,X.BRAZZOLOTTO,M.GRSIC,A.PISLAR,       
JRNL        AUTH 2 A.ZAHIROVIC,J.KOS,F.NACHON,J.SVETE,S.GOBEC,U.GROSELJ         
JRNL        TITL   TRYPTOPHAN-DERIVED BUTYRYLCHOLINESTERASE INHIBITORS AS       
JRNL        TITL 2 PROMISING LEADS AGAINST ALZHEIMER'S DISEASE.                 
JRNL        REF    CHEM.COMMUN.(CAMB.)                        2019              
JRNL        REFN                   ESSN 1364-548X                               
JRNL        PMID   30864579                                                     
JRNL        DOI    10.1039/C9CC01330J                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.49 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.14_3260: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.49                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.58                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 27177                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.890                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1328                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 47.5852 -  5.1775    0.99     3043   139  0.1822 0.2064        
REMARK   3     2  5.1775 -  4.1103    1.00     2904   150  0.1580 0.1870        
REMARK   3     3  4.1103 -  3.5909    1.00     2851   168  0.1743 0.2659        
REMARK   3     4  3.5909 -  3.2627    1.00     2885   136  0.2051 0.2410        
REMARK   3     5  3.2627 -  3.0289    1.00     2815   161  0.2187 0.2585        
REMARK   3     6  3.0289 -  2.8503    1.00     2839   149  0.2231 0.3046        
REMARK   3     7  2.8503 -  2.7076    1.00     2830   150  0.2454 0.2985        
REMARK   3     8  2.7076 -  2.5897    1.00     2835   150  0.2654 0.3073        
REMARK   3     9  2.5897 -  2.4900    1.00     2847   125  0.2645 0.2962        
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)     : 0.290            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.240           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 62.46                          
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      :  0.006           4599                                  
REMARK   3   ANGLE     :  0.815           6269                                  
REMARK   3   CHIRALITY :  0.051            685                                  
REMARK   3   PLANARITY :  0.004            785                                  
REMARK   3   DIHEDRAL  :  9.549           3636                                  
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 6QAB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-DEC-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200013532.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-SEP-18                          
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               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27181                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.490                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.580                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 8.100                              
REMARK 200  R MERGE                    (I) : 0.11940                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 13.3300                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.49                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.44500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.170                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 1P0I                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE MES PH 6.5, VAPOR       
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z                                                 
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      11555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290      12555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290      13555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      14555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      15555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290      16555   -Y+1/2,-X+1/2,-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        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  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        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
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        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       76.81600            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       76.81600            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       64.29450            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       76.81600            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       76.81600            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       64.29450            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       76.81600            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       76.81600            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       64.29450            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       76.81600            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       76.81600            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       64.29450            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       76.81600            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       76.81600            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       64.29450            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       76.81600            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       76.81600            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       64.29450            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       76.81600            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       76.81600            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       64.29450            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       76.81600            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       76.81600            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       64.29450            
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: 5050 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21170 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 3.0 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 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     MET A   -27                                                      
REMARK 465     ASP A   -26                                                      
REMARK 465     SER A   -25                                                      
REMARK 465     LYS A   -24                                                      
REMARK 465     VAL A   -23                                                      
REMARK 465     THR A   -22                                                      
REMARK 465     ILE A   -21                                                      
REMARK 465     ILE A   -20                                                      
REMARK 465     CYS A   -19                                                      
REMARK 465     ILE A   -18                                                      
REMARK 465     ARG A   -17                                                      
REMARK 465     PHE A   -16                                                      
REMARK 465     LEU A   -15                                                      
REMARK 465     PHE A   -14                                                      
REMARK 465     TRP A   -13                                                      
REMARK 465     PHE A   -12                                                      
REMARK 465     LEU A   -11                                                      
REMARK 465     LEU A   -10                                                      
REMARK 465     LEU A    -9                                                      
REMARK 465     CYS A    -8                                                      
REMARK 465     MET A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     ILE A    -5                                                      
REMARK 465     GLY A    -4                                                      
REMARK 465     LYS A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     THR A     0                                                      
REMARK 465     GLU A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     ASP A     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     GLN A 486    CG   CD   OE1  NE2                                  
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   NE2  HIS A   372     O1   SO4 A   622              2.12            
REMARK 500   OG   SER A   198     O    HOH A   701              2.15            
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  43       -6.70     77.11                                   
REMARK 500    ALA A  58       63.68   -105.58                                   
REMARK 500    LYS A 103      126.62    -37.08                                   
REMARK 500    ALA A 162       71.77   -161.26                                   
REMARK 500    SER A 198     -118.05     58.73                                   
REMARK 500    ASP A 297      -73.18   -111.14                                   
REMARK 500    SER A 362      152.73    -43.54                                   
REMARK 500    PHE A 398      -53.47   -137.98                                   
REMARK 500    PRO A 480       47.54    -80.78                                   
REMARK 500    GLU A 506      -75.31    -78.81                                   
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 DMS A 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MES A 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HUQ A 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  601 through FUC A 602 bound to ASN A 57                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 603 bound   
REMARK 800  to ASN A 106                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  607 through FUC A 609 bound to ASN A 241                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 610 bound   
REMARK 800  to ASN A 256                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  604 through FUC A 606 bound to ASN A 341                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 611 bound   
REMARK 800  to ASN A 485                                                        
DBREF  6QAB A  -27   529  UNP    P06276   CHLE_HUMAN       1    557             
SEQADV 6QAB ASP A  -26  UNP  P06276    HIS     2 CONFLICT                       
SEQADV 6QAB GLN A   17  UNP  P06276    ASN    45 ENGINEERED MUTATION            
SEQADV 6QAB GLN A  455  UNP  P06276    ASN   483 ENGINEERED MUTATION            
SEQADV 6QAB GLN A  481  UNP  P06276    ASN   509 ENGINEERED MUTATION            
SEQADV 6QAB GLN A  486  UNP  P06276    ASN   514 ENGINEERED MUTATION            
SEQRES   1 A  557  MET ASP SER LYS VAL THR ILE ILE CYS ILE ARG PHE LEU          
SEQRES   2 A  557  PHE TRP PHE LEU LEU LEU CYS MET LEU ILE GLY LYS SER          
SEQRES   3 A  557  HIS THR GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY          
SEQRES   4 A  557  LYS VAL ARG GLY MET GLN LEU THR VAL PHE GLY GLY THR          
SEQRES   5 A  557  VAL THR ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO          
SEQRES   6 A  557  LEU GLY ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR          
SEQRES   7 A  557  LYS TRP SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN          
SEQRES   8 A  557  SER CYS CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE          
SEQRES   9 A  557  HIS GLY SER GLU MET TRP ASN PRO ASN THR ASP LEU SER          
SEQRES  10 A  557  GLU ASP CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO          
SEQRES  11 A  557  LYS PRO LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY          
SEQRES  12 A  557  GLY GLY PHE GLN THR GLY THR SER SER LEU HIS VAL TYR          
SEQRES  13 A  557  ASP GLY LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL          
SEQRES  14 A  557  VAL SER MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU          
SEQRES  15 A  557  ALA LEU PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY          
SEQRES  16 A  557  LEU PHE ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS          
SEQRES  17 A  557  ASN ILE ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR          
SEQRES  18 A  557  LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU          
SEQRES  19 A  557  HIS LEU LEU SER PRO GLY SER HIS SER LEU PHE THR ARG          
SEQRES  20 A  557  ALA ILE LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA          
SEQRES  21 A  557  VAL THR SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN          
SEQRES  22 A  557  LEU ALA LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR          
SEQRES  23 A  557  GLU ILE ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU          
SEQRES  24 A  557  ILE LEU LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR          
SEQRES  25 A  557  PRO LEU SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP          
SEQRES  26 A  557  PHE LEU THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY          
SEQRES  27 A  557  GLN PHE LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS          
SEQRES  28 A  557  ASP GLU GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY          
SEQRES  29 A  557  PHE SER LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU          
SEQRES  30 A  557  PHE GLN GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER          
SEQRES  31 A  557  GLU PHE GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP          
SEQRES  32 A  557  TRP VAL ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA          
SEQRES  33 A  557  LEU GLY ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO          
SEQRES  34 A  557  ALA LEU GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN          
SEQRES  35 A  557  ASN ALA PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS          
SEQRES  36 A  557  LEU PRO TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR          
SEQRES  37 A  557  GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG          
SEQRES  38 A  557  ASP GLN TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER          
SEQRES  39 A  557  ILE VAL LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN          
SEQRES  40 A  557  PRO GLN GLU THR GLN ASN GLN SER THR SER TRP PRO VAL          
SEQRES  41 A  557  PHE LYS SER THR GLU GLN LYS TYR LEU THR LEU ASN THR          
SEQRES  42 A  557  GLU SER THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN          
SEQRES  43 A  557  CYS ARG PHE TRP THR SER PHE PHE PRO LYS VAL                  
HET    NAG  A 601      14                                                       
HET    FUC  A 602      10                                                       
HET    NAG  A 603      14                                                       
HET    NAG  A 604      14                                                       
HET    NAG  A 605      14                                                       
HET    FUC  A 606      10                                                       
HET    NAG  A 607      14                                                       
HET    NAG  A 608      14                                                       
HET    FUC  A 609      10                                                       
HET    NAG  A 610      14                                                       
HET    NAG  A 611      14                                                       
HET    DMS  A 612       4                                                       
HET    GOL  A 613       6                                                       
HET    GOL  A 614       6                                                       
HET    GOL  A 615       6                                                       
HET    GOL  A 616       6                                                       
HET    MES  A 617      12                                                       
HET    HUQ  A 618      30                                                       
HET    SO4  A 619       5                                                       
HET    SO4  A 620       5                                                       
HET    SO4  A 621       5                                                       
HET    SO4  A 622       5                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     GOL GLYCEROL                                                         
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETNAM     HUQ BUTYL-[(2~{S})-1-(2-CYCLOHEPTYLETHYLAMINO)-3-(1~{H}-             
HETNAM   2 HUQ  INDOL-3-YL)-1-OXIDANYLIDENE-PROPAN-2-YL]-DIMETHYL-              
HETNAM   3 HUQ  AZANIUM                                                         
HETNAM     SO4 SULFATE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  NAG    8(C8 H15 N O6)                                               
FORMUL   2  FUC    3(C6 H12 O5)                                                 
FORMUL   8  DMS    C2 H6 O S                                                    
FORMUL   9  GOL    4(C3 H8 O3)                                                  
FORMUL  13  MES    C6 H13 N O4 S                                                
FORMUL  14  HUQ    C26 H42 N3 O 1+                                              
FORMUL  15  SO4    4(O4 S 2-)                                                   
FORMUL  19  HOH   *68(H2 O)                                                     
HELIX    1 AA1 LEU A   38  ARG A   42  5                                   5    
HELIX    2 AA2 PHE A   76  MET A   81  1                                   6    
HELIX    3 AA3 LEU A  125  ASP A  129  5                                   5    
HELIX    4 AA4 GLY A  130  ARG A  138  1                                   9    
HELIX    5 AA5 VAL A  148  LEU A  154  1                                   7    
HELIX    6 AA6 ASN A  165  ILE A  182  1                                  18    
HELIX    7 AA7 ALA A  183  PHE A  185  5                                   3    
HELIX    8 AA8 SER A  198  SER A  210  1                                  13    
HELIX    9 AA9 PRO A  211  PHE A  217  5                                   7    
HELIX   10 AB1 SER A  235  THR A  250  1                                  16    
HELIX   11 AB2 ASN A  256  ASN A  266  1                                  11    
HELIX   12 AB3 ASP A  268  GLU A  276  1                                   9    
HELIX   13 AB4 ALA A  277  VAL A  279  5                                   3    
HELIX   14 AB5 MET A  302  LEU A  309  1                                   8    
HELIX   15 AB6 GLY A  326  VAL A  331  1                                   6    
HELIX   16 AB7 THR A  346  PHE A  358  1                                  13    
HELIX   17 AB8 SER A  362  THR A  374  1                                  13    
HELIX   18 AB9 GLU A  383  PHE A  398  1                                  16    
HELIX   19 AC1 PHE A  398  GLU A  411  1                                  14    
HELIX   20 AC2 PRO A  431  GLY A  435  5                                   5    
HELIX   21 AC3 GLU A  441  PHE A  446  1                                   6    
HELIX   22 AC4 GLY A  447  GLU A  451  5                                   5    
HELIX   23 AC5 THR A  457  GLY A  478  1                                  22    
HELIX   24 AC6 ARG A  515  SER A  524  1                                  10    
SHEET    1 AA1 3 ILE A   5  THR A   8  0                                        
SHEET    2 AA1 3 GLY A  11  ARG A  14 -1  O  VAL A  13   N  ILE A   6           
SHEET    3 AA1 3 ILE A  55  ASN A  57  1  O  TRP A  56   N  ARG A  14           
SHEET    1 AA211 MET A  16  VAL A  20  0                                        
SHEET    2 AA211 GLY A  23  PRO A  32 -1  O  ALA A  27   N  MET A  16           
SHEET    3 AA211 TYR A  94  PRO A 100 -1  O  LEU A  95   N  ILE A  31           
SHEET    4 AA211 ILE A 140  MET A 144 -1  O  SER A 143   N  ASN A  96           
SHEET    5 AA211 ALA A 107  ILE A 113  1  N  LEU A 110   O  ILE A 140           
SHEET    6 AA211 GLY A 187  GLU A 197  1  O  ASN A 188   N  ALA A 107           
SHEET    7 AA211 ARG A 219  GLN A 223  1  O  GLN A 223   N  GLY A 196           
SHEET    8 AA211 ILE A 317  ASN A 322  1  O  LEU A 318   N  LEU A 222           
SHEET    9 AA211 ALA A 416  PHE A 421  1  O  PHE A 417   N  VAL A 319           
SHEET   10 AA211 LYS A 499  LEU A 503  1  O  LEU A 501   N  TYR A 420           
SHEET   11 AA211 ILE A 510  THR A 512 -1  O  MET A 511   N  TYR A 500           
SHEET    1 AA3 2 SER A  64  CYS A  65  0                                        
SHEET    2 AA3 2 LEU A  88  SER A  89  1  O  SER A  89   N  SER A  64           
SSBOND   1 CYS A   65    CYS A   92                          1555   1555  2.03  
SSBOND   2 CYS A  252    CYS A  263                          1555   1555  2.04  
SSBOND   3 CYS A  400    CYS A  519                          1555   1555  2.02  
LINK         ND2 ASN A  57                 C1  NAG A 601     1555   1555  1.45  
LINK         ND2 ASN A 106                 C1  NAG A 603     1555   1555  1.44  
LINK         ND2 ASN A 241                 C1  NAG A 607     1555   1555  1.45  
LINK         ND2 ASN A 256                 C1  NAG A 610     1555   1555  1.45  
LINK         ND2 ASN A 341                 C1  NAG A 605     1555   1555  1.45  
LINK         ND2 ASN A 485                 C1  NAG A 611     1555   1555  1.44  
LINK         O6  NAG A 601                 C1  FUC A 602     1555   1555  1.44  
LINK         C1  NAG A 604                 O4  NAG A 605     1555   1555  1.44  
LINK         O6  NAG A 605                 C1  FUC A 606     1555   1555  1.44  
LINK         O4  NAG A 607                 C1  NAG A 608     1555   1555  1.45  
LINK         O6  NAG A 607                 C1  FUC A 609     1555   1555  1.45  
CISPEP   1 ALA A  101    PRO A  102          0         0.03                     
SITE     1 AC1  4 GLY A 115  GLY A 116  TYR A 128  HUQ A 618                    
SITE     1 AC2  7 HIS A  77  MET A  81  SER A 425  LYS A 427                    
SITE     2 AC2  7 TYR A 440  GLU A 443  HOH A 762                               
SITE     1 AC3  7 MET A  16  LEU A  18  LEU A  29  TYR A  61                    
SITE     2 AC3  7 TRP A  98  ASP A 129  LYS A 131                               
SITE     1 AC4  5 TRP A 231  ARG A 242  LEU A 286  SER A 287                    
SITE     2 AC4  5 VAL A 288                                                     
SITE     1 AC5  2 VAL A 492  LYS A 499                                          
SITE     1 AC6  7 LYS A 323  TYR A 420  ARG A 509  LEU A 514                    
SITE     2 AC6  7 ARG A 515  GLN A 518  HOH A 702                               
SITE     1 AC7 11 TRP A  82  GLY A 117  GLN A 119  PRO A 285                    
SITE     2 AC7 11 LEU A 286  SER A 287  PHE A 329  TYR A 332                    
SITE     3 AC7 11 TRP A 430  HIS A 438  DMS A 612                               
SITE     1 AC8  4 GLN A 316  GLY A 413  ASN A 414  ASN A 415                    
SITE     1 AC9  4 SER A 487  THR A 488  THR A 508  HOH A 703                    
SITE     1 AD1  3 ARG A 347  LYS A 348  GLN A 351                               
SITE     1 AD2  4 HIS A 372  PHE A 521  PHE A 525  LYS A 528                    
SITE     1 AD3  2 ARG A  14  ASN A  57                                          
SITE     1 AD4  2 ASN A 106  ASN A 188                                          
SITE     1 AD5  5 TYR A 237  ASN A 241  ASN A 245  LEU A 249                    
SITE     2 AD5  5 PHE A 278                                                     
SITE     1 AD6  2 ASN A 256  GLU A 259                                          
SITE     1 AD7  4 GLY A 336  SER A 338  ASN A 341  ASN A 342                    
SITE     1 AD8  3 ARG A 465  LYS A 469  ASN A 485                               
CRYST1  153.632  153.632  128.589  90.00  90.00  90.00 I 4 2 2      16          
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      0.006509  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006509  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007777        0.00000                         
TER    4234      VAL A 529                                                      
MASTER      406    0   22   24   16    0   24    6 4491    1  244   43          
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.
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