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LongText Report for: 6eyf-pdb

Name Class
6eyf-pdb
HEADER    HYDROLASE                               12-NOV-17   6EYF              
TITLE     BUTYRYLCOLINESTERASE EXPRESSED IN CHO CELLS CO-CRYSTALLISED WITH A    
TITLE    2 RIVASTIGMINE ANALOGUE                                                
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                                                      
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, ALZHEIMER DISEASE, ORGANOPHOSPHATE,            
KEYWDS   2 CARBAMYLATED, RIVASTIGMINE ANALOGUE, RATIONAL DESIGN, HYDROLASE      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.BRAZZOLOTTO,E.DE LA MORA,S.DIGHE,B.ROSS                             
REVDAT   1   21-NOV-18 6EYF    0                                                
SPRSDE     21-NOV-18 6EYF      6EUL                                             
JRNL        AUTH   S.DIGHE,E.DE LA MORA,S.CHAN,S.KANTHAM,G.MCCOLL,S.K.VELIYATH, 
JRNL        AUTH 2 J.A.MILES,Z.Y.NESSAR,R.MCGEARY,I.SILMAN,I.WEIK,M.O.PARAT,    
JRNL        AUTH 3 X.BRAZZOLOTTO,B.ROSS                                         
JRNL        TITL   ANALOGUES OF RIVASTIGMINE AND NAP FOR THE CNS DELIVERY OF    
JRNL        TITL 2 POLYPHENOLS WITH PUTATIVE ALZHEIMER DISEASE-MODIFYING        
JRNL        TITL 3 PROPERTIES                                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.55                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 23889                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.184                           
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.850                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1158                            
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 38.5500 -  5.1963    0.99     2971   155  0.1886 0.2229        
REMARK   3     2  5.1963 -  4.1260    1.00     2864   155  0.1503 0.1723        
REMARK   3     3  4.1260 -  3.6049    1.00     2827   141  0.1559 0.2064        
REMARK   3     4  3.6049 -  3.2755    1.00     2843   147  0.1754 0.2261        
REMARK   3     5  3.2755 -  3.0408    1.00     2805   147  0.1992 0.2505        
REMARK   3     6  3.0408 -  2.8616    1.00     2788   151  0.2125 0.3035        
REMARK   3     7  2.8616 -  2.7183    1.00     2806   146  0.2314 0.2869        
REMARK   3     8  2.7183 -  2.6000    1.00     2827   116  0.2603 0.4021        
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)     : 0.380            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.340           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 52.49                          
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      :  0.031           4461                                  
REMARK   3   ANGLE     :  1.655           6066                                  
REMARK   3   CHIRALITY :  0.093            647                                  
REMARK   3   PLANARITY :  0.014            779                                  
REMARK   3   DIHEDRAL  : 19.240           1625                                  
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 6EYF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-NOV-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200007461.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-OCT-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-2                             
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                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23889                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.550                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 2.000                              
REMARK 200  R MERGE                    (I) : 0.02830                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 19.1600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.72                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.28070                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.470                              
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: 4AQD                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.68                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.21                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS PH 8.5, 2.15 M AMMONIUM      
REMARK 280  SULFATE., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K           
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       77.09150            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       77.09150            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       63.87600            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       77.09150            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       77.09150            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       63.87600            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       77.09150            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       77.09150            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       63.87600            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       77.09150            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       77.09150            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       63.87600            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       77.09150            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       77.09150            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       63.87600            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       77.09150            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       77.09150            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       63.87600            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       77.09150            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       77.09150            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       63.87600            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       77.09150            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       77.09150            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       63.87600            
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: 2080 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 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 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     TYR A 237    CG   CD1  CD2  CE1  CE2  CZ   OH                    
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   ND2  ASN A   485     C1   NAG A   604              1.14            
REMARK 500   ND2  ASN A   485     O5   NAG A   604              1.52            
REMARK 500   ND2  ASN A   485     C2   NAG A   604              1.78            
REMARK 500   CG   ASN A   485     C1   NAG A   604              1.98            
REMARK 500   ND2  ASN A   341     O7   NAG A   603              2.16            
REMARK 500   NH2  ARG A   381     OD1  ASN A   384              2.18            
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    PHE A 195   N   -  CA  -  C   ANGL. DEV. =  26.2 DEGREES          
REMARK 500    PHE A 195   N   -  CA  -  C   ANGL. DEV. =  34.0 DEGREES          
REMARK 500    PHE A 195   CA  -  C   -  O   ANGL. DEV. = -33.9 DEGREES          
REMARK 500    PHE A 195   CA  -  C   -  O   ANGL. DEV. = -38.9 DEGREES          
REMARK 500    PHE A 195   CA  -  C   -  N   ANGL. DEV. =  27.2 DEGREES          
REMARK 500    PHE A 195   CA  -  C   -  N   ANGL. DEV. =  34.7 DEGREES          
REMARK 500    GLY A 196   N   -  CA  -  C   ANGL. DEV. = -15.4 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  43       -4.26     75.14                                   
REMARK 500    ASP A  54     -167.44    -74.39                                   
REMARK 500    ALA A  58       66.38   -107.68                                   
REMARK 500    PHE A 153       10.86   -143.69                                   
REMARK 500    ALA A 162       76.70   -152.32                                   
REMARK 500    BXT A 198     -121.30     56.97                                   
REMARK 500    GLU A 255      -81.56    -96.20                                   
REMARK 500    ASN A 256      100.35    -46.99                                   
REMARK 500    ASP A 297      -74.98   -124.36                                   
REMARK 500    PHE A 398      -59.81   -138.85                                   
REMARK 500    ARG A 453        7.52    -64.48                                   
REMARK 500    PRO A 480       47.73    -87.98                                   
REMARK 500    GLN A 484      -60.00    -92.10                                   
REMARK 500    ASN A 485       30.30    -68.87                                   
REMARK 500    ASN A 486       71.18     52.02                                   
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 PHE A  195     GLY A  196                 -141.86                    
REMARK 500 PHE A  195     GLY A  196                 -146.84                    
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    PHE A 195         24.88                                           
REMARK 500    PHE A 195         23.69                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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     NAG A  604                                                       
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 NAG A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BY2 A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 601 bound   
REMARK 800  to ASN A 57                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 602 bound   
REMARK 800  to ASN A 106                                                        
DBREF  6EYF A    3   529  UNP    P06276   CHLE_HUMAN      31    557             
SEQRES   1 A  527  ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL ARG GLY          
SEQRES   2 A  527  MET ASN LEU THR VAL PHE GLY GLY THR VAL THR ALA PHE          
SEQRES   3 A  527  LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY ARG LEU          
SEQRES   4 A  527  ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP SER ASP          
SEQRES   5 A  527  ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS CYS GLN          
SEQRES   6 A  527  ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY SER GLU          
SEQRES   7 A  527  MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP CYS LEU          
SEQRES   8 A  527  TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO LYS ASN          
SEQRES   9 A  527  ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY PHE GLN          
SEQRES  10 A  527  THR GLY THR SER SER LEU HIS VAL TYR ASP GLY LYS PHE          
SEQRES  11 A  527  LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER MET ASN          
SEQRES  12 A  527  TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU PRO GLY          
SEQRES  13 A  527  ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE ASP GLN          
SEQRES  14 A  527  GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE ALA ALA          
SEQRES  15 A  527  PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE GLY GLU          
SEQRES  16 A  527  BXT ALA GLY ALA ALA SER VAL SER LEU HIS LEU LEU SER          
SEQRES  17 A  527  PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE LEU GLN          
SEQRES  18 A  527  SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR SER LEU          
SEQRES  19 A  527  TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA LYS LEU          
SEQRES  20 A  527  THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE ILE LYS          
SEQRES  21 A  527  CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU LEU ASN          
SEQRES  22 A  527  GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU SER VAL          
SEQRES  23 A  527  ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU THR ASP          
SEQRES  24 A  527  MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE LYS LYS          
SEQRES  25 A  527  THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU GLY THR          
SEQRES  26 A  527  ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER LYS ASP          
SEQRES  27 A  527  ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN GLU GLY          
SEQRES  28 A  527  LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE GLY LYS          
SEQRES  29 A  527  GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL ASP ASP          
SEQRES  30 A  527  GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY ASP VAL          
SEQRES  31 A  527  VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU GLU PHE          
SEQRES  32 A  527  THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA PHE PHE          
SEQRES  33 A  527  TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO TRP PRO          
SEQRES  34 A  527  GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE GLU PHE          
SEQRES  35 A  527  VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN TYR THR          
SEQRES  36 A  527  LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL LYS ARG          
SEQRES  37 A  527  TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN GLU THR          
SEQRES  38 A  527  GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS SER THR          
SEQRES  39 A  527  GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER THR ARG          
SEQRES  40 A  527  ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG PHE TRP          
SEQRES  41 A  527  THR SER PHE PHE PRO LYS VAL                                  
MODRES 6EYF BXT A  198  SER  MODIFIED RESIDUE                                   
HET    BXT  A 198      12                                                       
HET    NAG  A 601      14                                                       
HET    NAG  A 602      14                                                       
HET    NAG  A 603      14                                                       
HET    NAG  A 604      14                                                       
HET    BY2  A 605      19                                                       
HET    GOL  A 606       6                                                       
HET    GOL  A 607       6                                                       
HET    GOL  A 608       6                                                       
HET    GOL  A 609       6                                                       
HET    SO4  A 610       5                                                       
HETNAM     BXT (2~{S})-2-AZANYL-3-[ETHYL(METHYL)CARBAMOYL]OXY-                  
HETNAM   2 BXT  PROPANOIC ACID                                                  
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BY2 [3-[(1~{R})-1-(DIMETHYLAMINO)ETHYL]-4-OXIDANYL-PHENYL]           
HETNAM   2 BY2  ~{N}-ETHYL-~{N}-METHYL-CARBAMATE                                
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  BXT    C7 H14 N2 O4                                                 
FORMUL   2  NAG    4(C8 H15 N O6)                                               
FORMUL   6  BY2    C14 H22 N2 O3                                                
FORMUL   7  GOL    4(C3 H8 O3)                                                  
FORMUL  11  SO4    O4 S 2-                                                      
FORMUL  12  HOH   *80(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 BXT A  198  SER A  210  1                                  13    
HELIX    8 AA8 PRO A  211  PHE A  217  5                                   7    
HELIX    9 AA9 SER A  235  THR A  250  1                                  16    
HELIX   10 AB1 ASN A  256  ARG A  265  1                                  10    
HELIX   11 AB2 ASP A  268  ALA A  277  1                                  10    
HELIX   12 AB3 MET A  302  LEU A  309  1                                   8    
HELIX   13 AB4 GLY A  326  VAL A  331  1                                   6    
HELIX   14 AB5 THR A  346  PHE A  358  1                                  13    
HELIX   15 AB6 SER A  362  THR A  374  1                                  13    
HELIX   16 AB7 GLU A  383  PHE A  398  1                                  16    
HELIX   17 AB8 PHE A  398  GLU A  411  1                                  14    
HELIX   18 AB9 PRO A  431  GLY A  435  5                                   5    
HELIX   19 AC1 GLU A  441  PHE A  446  1                                   6    
HELIX   20 AC2 GLY A  447  ASN A  455  5                                   9    
HELIX   21 AC3 THR A  457  GLY A  478  1                                  22    
HELIX   22 AC4 ARG A  515  SER A  524  1                                  10    
HELIX   23 AC5 PHE A  525  VAL A  529  5                                   5    
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  LYS A  12           
SHEET    1 AA211 MET A  16  VAL A  20  0                                        
SHEET    2 AA211 GLY A  23  PRO A  32 -1  O  VAL A  25   N  LEU A  18           
SHEET    3 AA211 TYR A  94  ALA A 101 -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  TRP A 112   O  VAL A 142           
SHEET    6 AA211 GLY A 187  GLY A 196  1  O  THR A 193   N  VAL A 109           
SHEET    7 AA211 ARG A 219  GLN A 223  1  O  ARG A 219   N  LEU A 194           
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 421   N  VAL A 321           
SHEET   10 AA211 LYS A 499  LEU A 503  1  O  LEU A 501   N  PHE A 418           
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  2.04  
SSBOND   2 CYS A  252    CYS A  263                          1555   1555  2.05  
SSBOND   3 CYS A  400    CYS A  519                          1555   1555  2.06  
LINK         ND2 ASN A  57                 C1  NAG A 601     1555   1555  1.44  
LINK         ND2 ASN A 106                 C1  NAG A 602     1555   1555  1.45  
LINK         C   GLU A 197                 N   BXT A 198     1555   1555  1.33  
LINK         C   BXT A 198                 N   ALA A 199     1555   1555  1.34  
CISPEP   1 ALA A  101    PRO A  102          0         6.95                     
SITE     1 AC1  2 ASN A 341  HOH A 717                                          
SITE     1 AC2  3 ARG A 465  GLU A 482  ASN A 485                               
SITE     1 AC3 11 ASN A  68  ILE A  69  ASP A  70  TRP A  82                    
SITE     2 AC3 11 GLN A 119  THR A 120  PHE A 329  TYR A 332                    
SITE     3 AC3 11 GOL A 606  HOH A 750  HOH A 752                               
SITE     1 AC4  8 TRP A  82  GLU A 197  BXT A 198  GLY A 439                    
SITE     2 AC4  8 BY2 A 605  HOH A 720  HOH A 732  HOH A 750                    
SITE     1 AC5  5 LEU A  18  TYR A  61  TRP A  98  ASP A 129                    
SITE     2 AC5  5 LYS A 131                                                     
SITE     1 AC6  2 ASP A 340  PRO A 429                                          
SITE     1 AC7  4 LYS A 323  TYR A 420  ARG A 509  ARG A 515                    
SITE     1 AC8  4 GLN A 316  GLY A 413  ASN A 414  ASN A 415                    
SITE     1 AC9  1 ASN A  57                                                     
SITE     1 AD1  2 ASN A 106  LYS A 190                                          
CRYST1  154.183  154.183  127.752  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      0.006486  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006486  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007828        0.00000                         
TER    4230      VAL A 529                                                      
MASTER      405    0   11   23   16    0   14    6 4381    1  126   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.
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