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LongText Report for: 5ei5-pdb

Name Class
5ei5-pdb
HEADER    HYDROLASE                               29-OCT-15   5EI5              
TITLE     CRYSTAL STRUCTURE OF MSF-AGED TORPEDO CALIFORNICA ACETYLCHOLINESTERASE
TITLE    2 IN COMPLEX WITH ALKYLENE-LINKED BIS-TACRINE DIMER (7 CARBON LINKER)  
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: TORPEDO CALIFORNICA;                            
SOURCE   3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;                               
SOURCE   4 ORGANISM_TAXID: 7787                                                 
KEYWDS    ALPHA BETA HYDROLASE, IRREVERSIBLE INHIBITOR, HYDROLASE               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.PESARESI,D.LAMBA                                                    
REVDAT   1   09-NOV-16 5EI5    0                                                
JRNL        AUTH   A.PESARESI,D.LAMBA                                           
JRNL        TITL   MSF-AGED TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN COMPLEX 
JRNL        TITL 2 WITH BISTACRINE                                              
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.23                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 54256                          
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) : 0.175                           
REMARK   3   R VALUE            (WORKING SET) : 0.173                           
REMARK   3   FREE R VALUE                     : 0.206                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2898                            
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.16                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3940                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.52                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2010                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 218                          
REMARK   3   BIN FREE R VALUE                    : 0.2380                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4263                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 97                                      
REMARK   3   SOLVENT ATOMS            : 364                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.83                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.87000                                              
REMARK   3    B22 (A**2) : 0.87000                                              
REMARK   3    B33 (A**2) : -2.81000                                             
REMARK   3    B12 (A**2) : 0.87000                                              
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): 0.136         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.131         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.081         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.956         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4497 ; 0.020 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4136 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6113 ; 2.053 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9504 ; 1.077 ; 3.005       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   533 ; 6.647 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   213 ;32.895 ;24.038       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   708 ;15.105 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;19.117 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   640 ; 0.154 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5085 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1087 ; 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):  2135 ; 2.447 ; 2.552       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2134 ; 2.429 ; 2.549       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2667 ; 3.205 ; 3.809       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2668 ; 3.207 ; 3.812       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2362 ; 3.818 ; 3.031       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2363 ; 3.817 ; 3.031       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3447 ; 5.710 ; 4.392       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  5605 ; 8.673 ;22.452       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  5448 ; 8.289 ;22.086       
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 5EI5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-OCT-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000214952.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-FEB-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
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                                  
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   : 54256                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.230                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.21700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 5.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.400                              
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: 1EA5                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MES 100 MM, PH 6.2 PEG 200 30%, VAPOR    
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
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       45.58000            
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       91.16000            
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       91.16000            
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       45.58000            
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: 1770 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21250 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 9.0 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 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    TRP A  58   C     ASN A  59   N      -0.185                       
REMARK 500    ASN A  59   C     ALA A  60   N      -0.141                       
REMARK 500    SER A 228   CB    SER A 228   OG     -0.092                       
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    VAL A 129   CB  -  CA  -  C   ANGL. DEV. = -14.6 DEGREES          
REMARK 500    LEU A 494   CA  -  CB  -  CG  ANGL. DEV. =  15.1 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    HIS A   3      -69.37   -146.25                                   
REMARK 500    SER A  24        1.08     82.35                                   
REMARK 500    SER A  25     -157.49   -132.76                                   
REMARK 500    PHE A  45      -12.67     81.03                                   
REMARK 500    SER A 108       72.50   -158.58                                   
REMARK 500    SER A 200     -116.38     55.14                                   
REMARK 500    GLU A 299      -72.72   -125.43                                   
REMARK 500    ASP A 380       56.01   -159.23                                   
REMARK 500    VAL A 400      -66.47   -131.03                                   
REMARK 500    ASN A 457       32.35     77.37                                   
REMARK 500    ARG A 515       66.78     61.60                                   
REMARK 500    GLN A 526      -52.67   -121.46                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 03S A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue AA7 A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 601 bound   
REMARK 800  to ASN A 59                                                         
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  602 through NAG A 603 bound to ASN A 416                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 604 bound   
REMARK 800  to ASN A 457                                                        
DBREF  5EI5 A    2   535  UNP    P04058   ACES_TORCA      23    556             
SEQRES   1 A  534  ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY LYS          
SEQRES   2 A  534  VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS ILE          
SEQRES   3 A  534  SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO VAL          
SEQRES   4 A  534  GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS PRO          
SEQRES   5 A  534  TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN ASN          
SEQRES   6 A  534  CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE SER          
SEQRES   7 A  534  GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER GLU          
SEQRES   8 A  534  ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO ARG          
SEQRES   9 A  534  PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY GLY          
SEQRES  10 A  534  GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR ASN          
SEQRES  11 A  534  GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU VAL          
SEQRES  12 A  534  SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU ALA          
SEQRES  13 A  534  LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY LEU          
SEQRES  14 A  534  LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP ASN          
SEQRES  15 A  534  ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR ILE          
SEQRES  16 A  534  PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET HIS          
SEQRES  17 A  534  ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG ALA          
SEQRES  18 A  534  ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA SER          
SEQRES  19 A  534  VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU LEU          
SEQRES  20 A  534  GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU GLU          
SEQRES  21 A  534  LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU LEU          
SEQRES  22 A  534  ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER ILE          
SEQRES  23 A  534  PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU PHE          
SEQRES  24 A  534  PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY ASN          
SEQRES  25 A  534  PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS ASP          
SEQRES  26 A  534  GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY PHE          
SEQRES  27 A  534  SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP PHE          
SEQRES  28 A  534  MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN ASP          
SEQRES  29 A  534  LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP TRP          
SEQRES  30 A  534  MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY LEU          
SEQRES  31 A  534  ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO LEU          
SEQRES  32 A  534  MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN GLY          
SEQRES  33 A  534  THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN LEU          
SEQRES  34 A  534  VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR GLU          
SEQRES  35 A  534  ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU LEU          
SEQRES  36 A  534  ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG ILE          
SEQRES  37 A  534  MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN PRO          
SEQRES  38 A  534  ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU PHE          
SEQRES  39 A  534  THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR GLU          
SEQRES  40 A  534  PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET CYS          
SEQRES  41 A  534  VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN ALA          
SEQRES  42 A  534  THR                                                          
MODRES 5EI5 NAG A  604  NAG  -D                                                 
HET    NAG  A 601      14                                                       
HET    NAG  A 602      14                                                       
HET    NAG  A 603      14                                                       
HET    NAG  A 604      14                                                       
HET    03S  A 605       4                                                       
HET    AA7  A 606      37                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     03S METHANESULFONIC ACID                                             
HETNAM     AA7 N,N'-DI-1,2,3,4-TETRAHYDROACRIDIN-9-YLHEPTANE-1,7-               
HETNAM   2 AA7  DIAMINE                                                         
FORMUL   2  NAG    4(C8 H15 N O6)                                               
FORMUL   5  03S    C H4 O3 S                                                    
FORMUL   6  AA7    C33 H40 N4                                                   
FORMUL   7  HOH   *364(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 VAL A  238  LEU A  252  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  VAL A  22  0                                        
SHEET    2 AA211 SER A  25  PRO A  34 -1  O  ILE A  27   N  VAL A  20           
SHEET    3 AA211 TYR A  96  VAL A 101 -1  O  ILE A  99   N  PHE A  30           
SHEET    4 AA211 VAL A 142  SER A 145 -1  O  LEU A 143   N  TRP A 100           
SHEET    5 AA211 THR A 109  ILE A 115  1  N  MET A 112   O  VAL A 144           
SHEET    6 AA211 GLY A 189  GLU A 199  1  O  THR A 195   N  VAL A 113           
SHEET    7 AA211 ARG A 221  GLN A 225  1  O  GLN A 225   N  GLY A 198           
SHEET    8 AA211 GLN A 318  ASN A 324  1  O  LEU A 320   N  ALA A 222           
SHEET    9 AA211 GLY A 417  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           
SHEET    1 AA3 2 VAL A 236  SER A 237  0                                        
SHEET    2 AA3 2 VAL A 295  ILE A 296  1  O  ILE A 296   N  VAL A 236           
SSBOND   1 CYS A   67    CYS A   94                          1555   1555  2.13  
SSBOND   2 CYS A  254    CYS A  265                          1555   1555  2.10  
SSBOND   3 CYS A  402    CYS A  521                          1555   1555  2.08  
LINK         ND2 ASN A  59                 C1  NAG A 601     1555   1555  1.45  
LINK         OG  SER A 200                 S10 03S A 605     1555   1555  1.59  
LINK         ND2 ASN A 416                 C1  NAG A 602     1555   1555  1.46  
LINK         ND2 ASN A 457                 C1  NAG A 604     1555   1555  1.49  
LINK         O4  NAG A 602                 C1  NAG A 603     1555   1555  1.44  
CISPEP   1 SER A  103    PRO A  104          0         7.37                     
SITE     1 AC1  7 GLY A 118  GLY A 119  SER A 200  ALA A 201                    
SITE     2 AC1  7 TRP A 233  PHE A 290  HIS A 440                               
SITE     1 AC2 13 TYR A  70  TRP A  84  GLY A 118  TYR A 121                    
SITE     2 AC2 13 PRO A 191  GLU A 199  ILE A 275  GLU A 278                    
SITE     3 AC2 13 TRP A 279  PHE A 330  TRP A 432  HIS A 440                    
SITE     4 AC2 13 HOH A 746                                                     
SITE     1 AC3  1 ASN A  59                                                     
SITE     1 AC4  3 ASN A 416  HOH A 706  HOH A 849                               
SITE     1 AC5  2 GLU A 455  ASN A 457                                          
CRYST1  111.280  111.280  136.740  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      0.008986  0.005188  0.000000        0.00000                         
SCALE2      0.000000  0.010377  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007313        0.00000                         
TER    4264      THR A 535                                                      
MASTER      340    0    6   25   16    0    9    6 4724    1  107   42          
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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