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LongText Report for: 6tt0-pdb

Name Class
6tt0-pdb
HEADER    HYDROLASE                               22-DEC-19   6TT0              
TITLE     CRYSTAL STRUCTURE OF A POTENT AND REVERSIBLE DUAL BINDING SITE        
TITLE    2 ACETYLCHOLINESTERASE CHIRAL INHIBITOR                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ACHE;                                                       
COMPND   5 EC: 3.1.1.7;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: T. CALIFORNICA ACETYLCHOLINESTERASE                   
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: TETRONARCE CALIFORNICA;                         
SOURCE   3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;                               
SOURCE   4 ORGANISM_TAXID: 7787;                                                
SOURCE   5 GENE: ACHE;                                                          
SOURCE   6 EXPRESSION_SYSTEM: TETRONARCE CALIFORNICA;                           
SOURCE   7 EXPRESSION_SYSTEM_COMMON: PACIFIC ELECTRIC RAY;                      
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7787                                        
KEYWDS    DUAL BINDING SITE INHIBITOR, CHIRAL SEPARATION, ACETYLCHOLINESTERASE, 
KEYWDS   2 ALZHEIMER'S DISEASE, HYDROLASE                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.DE LA MORA,G.F.MANGIATORDI,B.D.BELVISO,R.CALIANDRO,J.P.COLLETIER,   
AUTHOR   2 M.CATTO                                                              
REVDAT   1   10-JUN-20 6TT0    0                                                
JRNL        AUTH   M.CATTO,L.PISANI,E.DE LA MORA,B.D.BELVISO,G.F.MANGIATORDI,   
JRNL        AUTH 2 A.PINTO,A.PALMA,N.DENORA,R.CALIANDRO,J.P.COLLETIER,I.SILMAN, 
JRNL        AUTH 3 O.NICOLOTTI,C.D.ALTOMARE                                     
JRNL        TITL   CHIRAL SEPARATION, X-RAY STRUCTURE, AND BIOLOGICAL           
JRNL        TITL 2 EVALUATION OF A POTENT AND REVERSIBLE DUAL BINDING SITE ACHE 
JRNL        TITL 3 INHIBITOR.                                                   
JRNL        REF    ACS MED.CHEM.LETT.            V.  11   869 2020              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   32435398                                                     
JRNL        DOI    10.1021/ACSMEDCHEMLETT.9B00656                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.48                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.349                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 24321                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.191                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.889                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1189                            
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 39.4798 -  5.5954    0.95     2942   172  0.1771 0.2134        
REMARK   3     2  5.5954 -  4.4432    0.98     2890   163  0.1534 0.2025        
REMARK   3     3  4.4432 -  3.8821    0.98     2912   142  0.1631 0.2342        
REMARK   3     4  3.8821 -  3.5274    0.99     2903   132  0.1737 0.2153        
REMARK   3     5  3.5274 -  3.2747    0.98     2867   138  0.2164 0.2556        
REMARK   3     6  3.2747 -  3.0817    0.99     2891   145  0.2407 0.3200        
REMARK   3     7  3.0817 -  2.9274    0.99     2857   145  0.2814 0.3272        
REMARK   3     8  2.9274 -  2.8000    0.99     2870   152  0.3208 0.3564        
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)     : 0.396            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.377           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 67.68                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 69.95                          
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           4435                                  
REMARK   3   ANGLE     :  1.363           6027                                  
REMARK   3   CHIRALITY :  0.070            632                                  
REMARK   3   PLANARITY :  0.007            781                                  
REMARK   3   DIHEDRAL  : 18.649           1614                                  
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 6TT0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-DEC-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292106018.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-AUG-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
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) : 1.074                              
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   : 24409                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.480                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.500                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 1.800                              
REMARK 200  R MERGE                    (I) : 0.04067                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 10.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37680                            
REMARK 200  R SYM FOR SHELL            (I) : 0.53280                            
REMARK 200   FOR SHELL         : 1.570                              
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: 2VT7                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 32% PEG 200 100 MM MES PH 5.5, VAPOR     
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.79000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       91.58000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       91.58000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       45.79000            
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: 410 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 20650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 6.0 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     GLU A   536                                                      
REMARK 465     THR A   537                                                      
REMARK 465     ILE A   538                                                      
REMARK 465     ASP A   539                                                      
REMARK 465     GLU A   540                                                      
REMARK 465     ALA A   541                                                      
REMARK 465     GLU A   542                                                      
REMARK 465     ARG A   543                                                      
REMARK 465     GLN A   544                                                      
REMARK 465     TRP A   545                                                      
REMARK 465     LYS A   546                                                      
REMARK 465     THR A   547                                                      
REMARK 465     GLU A   548                                                      
REMARK 465     PHE A   549                                                      
REMARK 465     HIS A   550                                                      
REMARK 465     ARG A   551                                                      
REMARK 465     TRP A   552                                                      
REMARK 465     SER A   553                                                      
REMARK 465     SER A   554                                                      
REMARK 465     TYR A   555                                                      
REMARK 465     MET A   556                                                      
REMARK 465     MET A   557                                                      
REMARK 465     HIS A   558                                                      
REMARK 465     TRP A   559                                                      
REMARK 465     LYS A   560                                                      
REMARK 465     ASN A   561                                                      
REMARK 465     GLN A   562                                                      
REMARK 465     PHE A   563                                                      
REMARK 465     ASP A   564                                                      
REMARK 465     HIS A   565                                                      
REMARK 465     TYR A   566                                                      
REMARK 465     SER A   567                                                      
REMARK 465     ARG A   568                                                      
REMARK 465     HIS A   569                                                      
REMARK 465     GLU A   570                                                      
REMARK 465     SER A   571                                                      
REMARK 465     CYS A   572                                                      
REMARK 465     ALA A   573                                                      
REMARK 465     GLU A   574                                                      
REMARK 465     LEU A   575                                                      
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   416     C1   NAG A   603              1.00            
REMARK 500   SG   CYS A    67     CB   CYS A    94              1.74            
REMARK 500   CG   ASN A   416     C1   NAG A   603              1.88            
REMARK 500   ND2  ASN A   416     O5   NAG A   603              1.89            
REMARK 500   CB   CYS A    67     SG   CYS A    94              1.93            
REMARK 500   ND2  ASN A   416     C2   NAG A   603              2.09            
REMARK 500   OE1  GLU A     5     OG   SER A   103              2.10            
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    CYS A  94   CA  -  CB  -  SG  ANGL. DEV. =  10.3 DEGREES          
REMARK 500    PRO A 104   C   -  N   -  CD  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    SER A  24       12.82     59.16                                   
REMARK 500    SER A  25     -165.58   -129.28                                   
REMARK 500    PHE A  45       -3.84     81.07                                   
REMARK 500    ALA A  60       52.07    -93.36                                   
REMARK 500    LEU A  95       80.92    -64.70                                   
REMARK 500    SER A 108       76.38   -153.77                                   
REMARK 500    PHE A 120       -3.11     71.81                                   
REMARK 500    PHE A 155       19.89   -143.06                                   
REMARK 500    THR A 193       59.18   -152.20                                   
REMARK 500    SER A 200     -128.95     51.82                                   
REMARK 500    GLU A 299      -67.92   -106.36                                   
REMARK 500    THR A 317     -155.73   -159.27                                   
REMARK 500    VAL A 360       66.83   -118.44                                   
REMARK 500    ASP A 380       59.21   -152.19                                   
REMARK 500    ASN A 382       40.92   -100.51                                   
REMARK 500    VAL A 400      -70.47   -136.21                                   
REMARK 500    GLU A 455       13.98   -145.76                                   
REMARK 500    ASN A 457       74.51     60.46                                   
REMARK 500    HIS A 486       75.04     51.70                                   
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 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue N9T A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 602 bound   
REMARK 800  to ASN A 59                                                         
DBREF  6TT0 A    4   575  UNP    P04058   ACES_TETCF      25    596             
SEQRES   1 A  572  SER GLU LEU LEU VAL ASN THR LYS SER GLY LYS VAL MET          
SEQRES   2 A  572  GLY THR ARG VAL PRO VAL LEU SER SER HIS ILE SER ALA          
SEQRES   3 A  572  PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO VAL GLY ASN          
SEQRES   4 A  572  MET ARG PHE ARG ARG PRO GLU PRO LYS LYS PRO TRP SER          
SEQRES   5 A  572  GLY VAL TRP ASN ALA SER THR TYR PRO ASN ASN CYS GLN          
SEQRES   6 A  572  GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE SER GLY SER          
SEQRES   7 A  572  GLU MET TRP ASN PRO ASN ARG GLU MET SER GLU ASP CYS          
SEQRES   8 A  572  LEU TYR LEU ASN ILE TRP VAL PRO SER PRO ARG PRO LYS          
SEQRES   9 A  572  SER THR THR VAL MET VAL TRP ILE TYR GLY GLY GLY PHE          
SEQRES  10 A  572  TYR SER GLY SER SER THR LEU ASP VAL TYR ASN GLY LYS          
SEQRES  11 A  572  TYR LEU ALA TYR THR GLU GLU VAL VAL LEU VAL SER LEU          
SEQRES  12 A  572  SER TYR ARG VAL GLY ALA PHE GLY PHE LEU ALA LEU HIS          
SEQRES  13 A  572  GLY SER GLN GLU ALA PRO GLY ASN VAL GLY LEU LEU ASP          
SEQRES  14 A  572  GLN ARG MET ALA LEU GLN TRP VAL HIS ASP ASN ILE GLN          
SEQRES  15 A  572  PHE PHE GLY GLY ASP PRO LYS THR VAL THR ILE PHE GLY          
SEQRES  16 A  572  GLU SER ALA GLY GLY ALA SER VAL GLY MET HIS ILE LEU          
SEQRES  17 A  572  SER PRO GLY SER ARG ASP LEU PHE ARG ARG ALA ILE LEU          
SEQRES  18 A  572  GLN SER GLY SER PRO ASN CYS PRO TRP ALA SER VAL SER          
SEQRES  19 A  572  VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU LEU GLY ARG          
SEQRES  20 A  572  ASN LEU ASN CYS ASN LEU ASN SER ASP GLU GLU LEU ILE          
SEQRES  21 A  572  HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU LEU ILE ASP          
SEQRES  22 A  572  VAL GLU TRP ASN VAL LEU PRO PHE ASP SER ILE PHE ARG          
SEQRES  23 A  572  PHE SER PHE VAL PRO VAL ILE ASP GLY GLU PHE PHE PRO          
SEQRES  24 A  572  THR SER LEU GLU SER MET LEU ASN SER GLY ASN PHE LYS          
SEQRES  25 A  572  LYS THR GLN ILE LEU LEU GLY VAL ASN LYS ASP GLU GLY          
SEQRES  26 A  572  SER PHE PHE LEU LEU TYR GLY ALA PRO GLY PHE SER LYS          
SEQRES  27 A  572  ASP SER GLU SER LYS ILE SER ARG GLU ASP PHE MET SER          
SEQRES  28 A  572  GLY VAL LYS LEU SER VAL PRO HIS ALA ASN ASP LEU GLY          
SEQRES  29 A  572  LEU ASP ALA VAL THR LEU GLN TYR THR ASP TRP MET ASP          
SEQRES  30 A  572  ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY LEU ASP ASP          
SEQRES  31 A  572  ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO LEU MET HIS          
SEQRES  32 A  572  PHE VAL ASN LYS TYR THR LYS PHE GLY ASN GLY THR TYR          
SEQRES  33 A  572  LEU TYR PHE PHE ASN HIS ARG ALA SER ASN LEU VAL TRP          
SEQRES  34 A  572  PRO GLU TRP MET GLY VAL ILE HIS GLY TYR GLU ILE GLU          
SEQRES  35 A  572  PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU LEU ASN TYR          
SEQRES  36 A  572  THR ALA GLU GLU GLU ALA LEU SER ARG ARG ILE MET HIS          
SEQRES  37 A  572  TYR TRP ALA THR PHE ALA LYS THR GLY ASN PRO ASN GLU          
SEQRES  38 A  572  PRO HIS SER GLN GLU SER LYS TRP PRO LEU PHE THR THR          
SEQRES  39 A  572  LYS GLU GLN LYS PHE ILE ASP LEU ASN THR GLU PRO MET          
SEQRES  40 A  572  LYS VAL HIS GLN ARG LEU ARG VAL GLN MET CYS VAL PHE          
SEQRES  41 A  572  TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN ALA THR GLU          
SEQRES  42 A  572  THR ILE ASP GLU ALA GLU ARG GLN TRP LYS THR GLU PHE          
SEQRES  43 A  572  HIS ARG TRP SER SER TYR MET MET HIS TRP LYS ASN GLN          
SEQRES  44 A  572  PHE ASP HIS TYR SER ARG HIS GLU SER CYS ALA GLU LEU          
HET    N9T  A 601      32                                                       
HET    NAG  A 602      14                                                       
HET    NAG  A 603      14                                                       
HETNAM     N9T (1~{R},3~{S})-~{N}-(6,7-DIMETHOXY-2-OXIDANYLIDENE-               
HETNAM   2 N9T  CHROMEN-3-YL)-3-[(PHENYLMETHYL)AMINO]CYCLOHEXANE-1-             
HETNAM   3 N9T  CARBOXAMIDE                                                     
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
FORMUL   2  N9T    C25 H28 N2 O5                                                
FORMUL   3  NAG    2(C8 H15 N O6)                                               
FORMUL   5  HOH   *88(H2 O)                                                     
HELIX    1 AA1 VAL A   40  ARG A   44  5                                   5    
HELIX    2 AA2 PHE A   78  MET A   83  1                                   6    
HELIX    3 AA3 LEU A  127  TYR A  130  5                                   4    
HELIX    4 AA4 ASN A  131  GLU A  140  1                                  10    
HELIX    5 AA5 GLY A  151  LEU A  156  1                                   6    
HELIX    6 AA6 ASN A  167  ILE A  184  1                                  18    
HELIX    7 AA7 GLN A  185  PHE A  187  5                                   3    
HELIX    8 AA8 SER A  200  SER A  212  1                                  13    
HELIX    9 AA9 SER A  212  ASP A  217  1                                   6    
HELIX   10 AB1 SER A  237  LEU A  252  1                                  16    
HELIX   11 AB2 SER A  258  LYS A  269  1                                  12    
HELIX   12 AB3 LYS A  270  GLU A  278  1                                   9    
HELIX   13 AB4 TRP A  279  LEU A  282  5                                   4    
HELIX   14 AB5 SER A  304  SER A  311  1                                   8    
HELIX   15 AB6 GLY A  328  ALA A  336  1                                   9    
HELIX   16 AB7 SER A  348  VAL A  360  1                                  13    
HELIX   17 AB8 ASN A  364  THR A  376  1                                  13    
HELIX   18 AB9 ASN A  383  VAL A  400  1                                  18    
HELIX   19 AC1 VAL A  400  LYS A  413  1                                  14    
HELIX   20 AC2 PRO A  433  GLY A  437  5                                   5    
HELIX   21 AC3 GLU A  443  PHE A  448  1                                   6    
HELIX   22 AC4 GLY A  449  VAL A  453  5                                   5    
HELIX   23 AC5 THR A  459  GLY A  480  1                                  22    
HELIX   24 AC6 ARG A  517  GLN A  526  1                                  10    
HELIX   25 AC7 GLN A  526  ALA A  534  1                                   9    
SHEET    1 AA1 3 LEU A   7  THR A  10  0                                        
SHEET    2 AA1 3 GLY A  13  MET A  16 -1  O  VAL A  15   N  VAL A   8           
SHEET    3 AA1 3 VAL A  57  ASN A  59  1  O  TRP A  58   N  MET A  16           
SHEET    1 AA211 THR A  18  VAL A  22  0                                        
SHEET    2 AA211 SER A  25  PRO A  34 -1  O  ILE A  27   N  VAL A  20           
SHEET    3 AA211 TYR A  96  VAL A 101 -1  O  ILE A  99   N  PHE A  30           
SHEET    4 AA211 VAL A 142  LEU A 146 -1  O  LEU A 143   N  TRP A 100           
SHEET    5 AA211 THR A 109  ILE A 115  1  N  TRP A 114   O  VAL A 144           
SHEET    6 AA211 GLY A 189  GLU A 199  1  O  PHE A 197   N  VAL A 113           
SHEET    7 AA211 ARG A 221  GLN A 225  1  O  GLN A 225   N  GLY A 198           
SHEET    8 AA211 ILE A 319  ASN A 324  1  O  LEU A 320   N  ALA A 222           
SHEET    9 AA211 THR A 418  PHE A 423  1  O  TYR A 419   N  LEU A 321           
SHEET   10 AA211 LYS A 501  LEU A 505  1  O  LEU A 505   N  PHE A 422           
SHEET   11 AA211 VAL A 512  GLN A 514 -1  O  HIS A 513   N  PHE A 502           
SSBOND   1 CYS A  254    CYS A  265                          1555   1555  2.04  
SSBOND   2 CYS A  402    CYS A  521                          1555   1555  2.05  
LINK         ND2 ASN A  59                 C1  NAG A 602     1555   1555  1.47  
CISPEP   1 SER A  103    PRO A  104          0         2.75                     
SITE     1 AC1 10 TYR A  70  ASP A  72  TYR A 121  GLN A 185                    
SITE     2 AC1 10 GLU A 199  TRP A 279  PHE A 330  PHE A 331                    
SITE     3 AC1 10 HIS A 440  HOH A 749                                          
SITE     1 AC2  1 ASN A 416                                                     
SITE     1 AC3  2 ASN A  59  HOH A 715                                          
CRYST1  111.420  111.420  137.370  90.00  90.00 120.00 P 31 2 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008975  0.005182  0.000000        0.00000                         
SCALE2      0.000000  0.010363  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007280        0.00000                         
TER    4245      THR A 535                                                      
MASTER      347    0    3   25   14    0    5    6 4392    1   65   44          
END                                                                             

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
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