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LongText Report for: 5nau-pdb

Name Class
5nau-pdb
HEADER    HYDROLASE                               28-FEB-17   5NAU              
TITLE     TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX WITH A NON-CHIRAL 
TITLE    2 DONEPEZIL-LIKE COMPOUND 20                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ACHE;                                                       
COMPND   5 EC: 3.1.1.7                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: TETRONARCE CALIFORNICA;                         
SOURCE   3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;                               
SOURCE   4 ORGANISM_TAXID: 7787                                                 
KEYWDS    ALZHEIMER'S DISEASE, ACETYLCHOLINESTERASE, DONEPEZIL ANALOGUES, GREEN 
KEYWDS   2 CHEMISTRY, HYDROLASE                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.CALIANDRO,A.PESARESI,D.LAMBA                                        
REVDAT   1   02-MAY-18 5NAU    0                                                
JRNL        AUTH   R.CALIANDRO,A.PESARESI,L.CARIATI,A.PROCOPIO,M.OLIVERIO,      
JRNL        AUTH 2 D.LAMBA                                                      
JRNL        TITL   KINETIC AND STRUCTURAL STUDIES ON THE INTERACTIONS OF        
JRNL        TITL 2 TORPEDO CALIFORNICA ACETYLCHOLINESTERASE WITH TWO            
JRNL        TITL 3 DONEPEZIL-LIKE RIGID ANALOGUES.                              
JRNL        REF    J ENZYME INHIB MED CHEM       V.  33   794 2018              
JRNL        REFN                   ESSN 1475-6374                               
JRNL        PMID   29651884                                                     
JRNL        DOI    10.1080/14756366.2018.1458030                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.33                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 44654                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2369                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.31                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3308                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.09                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2690                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 173                          
REMARK   3   BIN FREE R VALUE                    : 0.3190                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4205                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 150                                     
REMARK   3   SOLVENT ATOMS            : 279                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.09                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.41000                                              
REMARK   3    B22 (A**2) : 1.41000                                              
REMARK   3    B33 (A**2) : -4.56000                                             
REMARK   3    B12 (A**2) : 1.41000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.181         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.169         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.122         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.036         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.936                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4517 ; 0.020 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4120 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6158 ; 1.949 ; 1.983       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9453 ; 1.006 ; 3.004       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   535 ; 7.042 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   204 ;32.761 ;23.922       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   692 ;15.113 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;18.553 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   675 ; 0.123 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5034 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1071 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2131 ; 3.277 ; 3.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2130 ; 3.272 ; 3.498       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2663 ; 4.763 ; 5.235       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2664 ; 4.763 ; 5.237       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2386 ; 4.549 ; 4.131       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2387 ; 4.548 ; 4.132       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3494 ; 6.624 ; 6.058       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  5436 ; 7.842 ;29.802       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  5385 ; 7.830 ;29.710       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3    POSITIONS                                                         
REMARK   4                                                                      
REMARK   4 5NAU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003795.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-JUL-16                          
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               : ELETTRA                            
REMARK 200  BEAMLINE                       : 5.2R                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM 7.0.7                       
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.2.1                      
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47111                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.330                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : 0.19600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 4.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.37                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.86000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.3.0                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MES PH 6.2, 100 MM PEG 200, 30%, VAPOR   
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277.15K                        
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       45.57000            
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       91.14000            
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       91.14000            
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       45.57000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5360 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 41570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 42.0 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 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      193.33151            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      364.56000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 817  LIES ON A SPECIAL POSITION.                          
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     ASP A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     ALA A   536                                                      
REMARK 465     CYS A   537                                                      
REMARK 465     ASP A   538                                                      
REMARK 465     GLY A   539                                                      
REMARK 465     GLU A   540                                                      
REMARK 465     LEU A   541                                                      
REMARK 465     SER A   542                                                      
REMARK 465     SER A   543                                                      
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     ASN A  42    OD1  ND2                                            
REMARK 470     LYS A  52    CE   NZ                                             
REMARK 470     GLU A  89    CD   OE1  OE2                                       
REMARK 470     GLU A 260    CD   OE1  OE2                                       
REMARK 470     GLU A 268    CD   OE1  OE2                                       
REMARK 470     GLU A 299    CD   OE1  OE2                                       
REMARK 470     HIS A 362    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 454    CG   CD   CE   NZ                                   
REMARK 470     HIS A 486    CG   ND1  CD2  CE1  NE2                             
REMARK 470     SER A 487    OG                                                  
REMARK 470     GLN A 488    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 491    CE   NZ                                             
REMARK 470     LYS A 498    CE   NZ                                             
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   O    HOH A   914     O    HOH A   960              1.85            
REMARK 500   O    HOH A   927     O    HOH A   931              2.11            
REMARK 500   O    HOH A   889     O    HOH A   975              2.16            
REMARK 500   O    HOH A   954     O    HOH A   965              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    PRO A  38   CD    PRO A  38   N      -0.136                       
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    VAL A  22      118.98   -160.62                                   
REMARK 500    SER A  24       37.08     74.94                                   
REMARK 500    SER A  25     -164.82   -165.75                                   
REMARK 500    PHE A  45      -11.00     77.29                                   
REMARK 500    PRO A 102      161.12    -49.14                                   
REMARK 500    SER A 108       84.05   -155.39                                   
REMARK 500    LEU A 158       79.81   -117.22                                   
REMARK 500    ASN A 167       14.79     59.18                                   
REMARK 500    SER A 200     -117.52     58.38                                   
REMARK 500    GLU A 299      -74.77   -113.58                                   
REMARK 500    THR A 317     -163.16   -165.94                                   
REMARK 500    ARG A 349      -37.83    -37.19                                   
REMARK 500    HIS A 362       21.19    -79.62                                   
REMARK 500    ASP A 380       84.08   -165.88                                   
REMARK 500    VAL A 400      -61.66   -130.60                                   
REMARK 500    ASN A 424       36.95   -141.18                                   
REMARK 500    ASN A 506     -169.53   -162.03                                   
REMARK 500    MET A 510      130.43    -36.92                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 979        DISTANCE =  7.18 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DZ0 A 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
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 59                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  603 through MAN A 606 bound to ASN A 416                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  607 through MAN A 610 bound to ASN A 457                            
DBREF  5NAU A    1   543  UNP    P04058   ACES_TETCF      22    564             
SEQRES   1 A  543  ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY          
SEQRES   2 A  543  LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS          
SEQRES   3 A  543  ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO          
SEQRES   4 A  543  VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS          
SEQRES   5 A  543  PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN          
SEQRES   6 A  543  ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE          
SEQRES   7 A  543  SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER          
SEQRES   8 A  543  GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO          
SEQRES   9 A  543  ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY          
SEQRES  10 A  543  GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR          
SEQRES  11 A  543  ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU          
SEQRES  12 A  543  VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU          
SEQRES  13 A  543  ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY          
SEQRES  14 A  543  LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP          
SEQRES  15 A  543  ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR          
SEQRES  16 A  543  ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET          
SEQRES  17 A  543  HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG          
SEQRES  18 A  543  ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA          
SEQRES  19 A  543  SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU          
SEQRES  20 A  543  LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU          
SEQRES  21 A  543  GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU          
SEQRES  22 A  543  LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER          
SEQRES  23 A  543  ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU          
SEQRES  24 A  543  PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY          
SEQRES  25 A  543  ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS          
SEQRES  26 A  543  ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY          
SEQRES  27 A  543  PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP          
SEQRES  28 A  543  PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN          
SEQRES  29 A  543  ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP          
SEQRES  30 A  543  TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY          
SEQRES  31 A  543  LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO          
SEQRES  32 A  543  LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN          
SEQRES  33 A  543  GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN          
SEQRES  34 A  543  LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR          
SEQRES  35 A  543  GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU          
SEQRES  36 A  543  LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG          
SEQRES  37 A  543  ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN          
SEQRES  38 A  543  PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU          
SEQRES  39 A  543  PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR          
SEQRES  40 A  543  GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET          
SEQRES  41 A  543  CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN          
SEQRES  42 A  543  ALA THR ALA CYS ASP GLY GLU LEU SER SER                      
MODRES 5NAU NAG A  601  NAG  -D                                                 
MODRES 5NAU FUC A  602  FUC  -L                                                 
MODRES 5NAU NAG A  603  NAG  -D                                                 
MODRES 5NAU NAG A  604  NAG  -D                                                 
MODRES 5NAU MAN A  606  MAN  -D                                                 
MODRES 5NAU NAG A  607  NAG  -D                                                 
MODRES 5NAU NAG A  608  NAG  -D                                                 
MODRES 5NAU MAN A  610  MAN  -D                                                 
HET    NAG  A 601      14                                                       
HET    FUC  A 602      10                                                       
HET    NAG  A 603      14                                                       
HET    NAG  A 604      14                                                       
HET    BMA  A 605      11                                                       
HET    MAN  A 606      11                                                       
HET    NAG  A 607      14                                                       
HET    NAG  A 608      14                                                       
HET    BMA  A 609      11                                                       
HET    MAN  A 610      11                                                       
HET    DZ0  A 611      26                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     DZ0 (2~{E})-5-METHOXY-2-[[1-(PHENYLMETHYL)PIPERIDIN-4-               
HETNAM   2 DZ0  YL]METHYLIDENE]-3~{H}-INDEN-1-ONE                               
FORMUL   2  NAG    5(C8 H15 N O6)                                               
FORMUL   2  FUC    C6 H12 O5                                                    
FORMUL   3  BMA    2(C6 H12 O6)                                                 
FORMUL   3  MAN    2(C6 H12 O6)                                                 
FORMUL   5  DZ0    C23 H25 N O2                                                 
FORMUL   6  HOH   *279(H2 O)                                                    
HELIX    1 AA1 VAL A   40  ARG A   44  5                                   5    
HELIX    2 AA2 PHE A   78  MET A   83  1                                   6    
HELIX    3 AA3 LEU A  127  ASN A  131  5                                   5    
HELIX    4 AA4 GLY A  132  GLU A  140  1                                   9    
HELIX    5 AA5 VAL A  150  LEU A  156  1                                   7    
HELIX    6 AA6 ASN A  167  ILE A  184  1                                  18    
HELIX    7 AA7 GLN A  185  PHE A  187  5                                   3    
HELIX    8 AA8 SER A  200  SER A  212  1                                  13    
HELIX    9 AA9 SER A  215  PHE A  219  5                                   5    
HELIX   10 AB1 SER A  237  ASN A  251  1                                  15    
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  GLY A  312  1                                   9    
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  ASN A  457  5                                   9    
HELIX   23 AC5 THR A  459  GLY A  480  1                                  22    
HELIX   24 AC6 ARG A  517  GLN A  526  1                                  10    
HELIX   25 AC7 GLN A  526  THR A  535  1                                  10    
SHEET    1 AA1 3 LEU A   7  THR A  10  0                                        
SHEET    2 AA1 3 GLY A  13  MET A  16 -1  O  VAL A  15   N  VAL A   8           
SHEET    3 AA1 3 VAL A  57  ASN A  59  1  O  TRP A  58   N  MET A  16           
SHEET    1 AA211 THR A  18  PRO A  21  0                                        
SHEET    2 AA211 HIS A  26  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  MET A 112   O  VAL A 144           
SHEET    6 AA211 GLY A 189  GLU A 199  1  O  ASP A 190   N  THR A 109           
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  PHE A 423   N  VAL A 323           
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   67    CYS A   94                          1555   1555  2.09  
SSBOND   2 CYS A  254    CYS A  265                          1555   1555  2.08  
SSBOND   3 CYS A  402    CYS A  521                          1555   1555  2.09  
LINK         ND2 ASN A  59                 C1  NAG A 601     1555   1555  1.47  
LINK         ND2 ASN A 416                 C1  NAG A 603     1555   1555  1.57  
LINK         ND2 ASN A 457                 C1  NAG A 607     1555   1555  1.47  
LINK         O6  NAG A 601                 C1  FUC A 602     1555   1555  1.45  
LINK         O4  NAG A 603                 C1  NAG A 604     1555   1555  1.44  
LINK         O4  NAG A 604                 C1  BMA A 605     1555   1555  1.44  
LINK         O3  BMA A 605                 C1  MAN A 606     1555   1555  1.44  
LINK         O4  NAG A 607                 C1  NAG A 608     1555   1555  1.45  
LINK         O4  NAG A 608                 C1  BMA A 609     1555   1555  1.46  
LINK         O3  BMA A 609                 C1  MAN A 610     1555   1555  1.44  
CISPEP   1 SER A  103    PRO A  104          0         6.16                     
SITE     1 AC1  6 TYR A 121  GLU A 199  TRP A 279  PHE A 330                    
SITE     2 AC1  6 PHE A 331  HOH A 750                                          
SITE     1 AC2  3 ASN A  59  SER A  61  HOH A 702                               
SITE     1 AC3  4 ASN A 416  HOH A 796  HOH A 835  HOH A 855                    
SITE     1 AC4  5 GLU A 455  ASN A 457  HOH A 705  HOH A 851                    
SITE     2 AC4  5 HOH A 877                                                     
CRYST1  111.620  111.620  136.710  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      0.008959  0.005172  0.000000        0.00000                         
SCALE2      0.000000  0.010345  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007315        0.00000                         
TER    4206      THR A 535                                                      
MASTER      395    0   11   25   14    0    6    6 4634    1  159   42          
END                                                                             

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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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