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LongText Report for: 6eue-pdb

Name Class
6eue-pdb
HEADER    HYDROLASE                               30-OCT-17   6EUE              
TITLE     RIVASTIGMINE ANALOGUE BOUND TO TC ACHE.                               
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 OTHER_DETAILS: TC ACHE WITH CARBAMYLATED SER200                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: TETRONARCE CALIFORNICA;                         
SOURCE   3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;                               
SOURCE   4 ORGANISM_TAXID: 7787                                                 
KEYWDS    CHOLINESTERASE, ALZHEIMER DISEASE, ORGANOPHOSPHATE, CARBAMYLATED,     
KEYWDS   2 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.DE LA MORA,X.BRAZZOLOTTO,S.N.DIGHE,I.SILMAN,M.WEIK,B.ROSS           
REVDAT   1   14-NOV-18 6EUE    0                                                
JRNL        AUTH   S.N.DIGHE,E.DE LA MORA,S.CHAN,S.KANTHAM,G.MCCOLL,            
JRNL        AUTH 2 S.K.VELIYAT,J.A.MILES,R.P.MCGEARY,I.SILMAN,M.WEIK,M.P.PARAT, 
JRNL        AUTH 3 X.BRAZZOLOTTO,B.ROSS                                         
JRNL        TITL   ANALOGUES OF RIVASTIGMINE AND NAP FOR THE CNS DELIVERY OF    
JRNL        TITL 2 POLYPHENOLS WITH PUTATIVE ALZHEIMER DISEASE-MODIFYING        
JRNL        TITL 3 PROPERTIES                                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.60                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 67375                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.197                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.210                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3508                            
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 39.5900 -  5.8420    1.00     2746   137  0.1843 0.1928        
REMARK   3     2  5.8420 -  4.6393    1.00     2620   154  0.1504 0.1675        
REMARK   3     3  4.6393 -  4.0535    1.00     2618   133  0.1375 0.1530        
REMARK   3     4  4.0535 -  3.6832    1.00     2607   126  0.1489 0.1766        
REMARK   3     5  3.6832 -  3.4194    1.00     2559   156  0.1656 0.1901        
REMARK   3     6  3.4194 -  3.2179    1.00     2583   132  0.1813 0.2250        
REMARK   3     7  3.2179 -  3.0568    1.00     2546   142  0.1999 0.2615        
REMARK   3     8  3.0568 -  2.9237    1.00     2556   154  0.1953 0.2153        
REMARK   3     9  2.9237 -  2.8112    1.00     2545   143  0.1849 0.2262        
REMARK   3    10  2.8112 -  2.7142    1.00     2563   163  0.1933 0.2432        
REMARK   3    11  2.7142 -  2.6294    1.00     2511   154  0.2048 0.2734        
REMARK   3    12  2.6294 -  2.5542    1.00     2533   133  0.2115 0.2622        
REMARK   3    13  2.5542 -  2.4870    1.00     2541   149  0.2266 0.3000        
REMARK   3    14  2.4870 -  2.4263    1.00     2509   179  0.2382 0.2901        
REMARK   3    15  2.4263 -  2.3712    1.00     2575   113  0.2377 0.2599        
REMARK   3    16  2.3712 -  2.3207    1.00     2497   161  0.2594 0.2753        
REMARK   3    17  2.3207 -  2.2743    0.99     2546   128  0.2629 0.2648        
REMARK   3    18  2.2743 -  2.2314    0.99     2548   123  0.2728 0.3520        
REMARK   3    19  2.2314 -  2.1916    1.00     2533   125  0.2939 0.3299        
REMARK   3    20  2.1916 -  2.1544    0.99     2527   119  0.3140 0.3320        
REMARK   3    21  2.1544 -  2.1197    0.99     2523   156  0.3143 0.3618        
REMARK   3    22  2.1197 -  2.0871    1.00     2512   128  0.3383 0.3384        
REMARK   3    23  2.0871 -  2.0564    0.99     2543   149  0.3568 0.3714        
REMARK   3    24  2.0564 -  2.0274    0.99     2474   134  0.3802 0.3684        
REMARK   3    25  2.0274 -  2.0000    1.00     2552   117  0.3700 0.3700        
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)     : 0.260            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.170           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 37.82                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.011           4547                                  
REMARK   3   ANGLE     :  1.971           6177                                  
REMARK   3   CHIRALITY :  0.120            645                                  
REMARK   3   PLANARITY :  0.008            803                                  
REMARK   3   DIHEDRAL  : 19.094           1696                                  
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 6EUE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-OCT-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200007036.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-OCT-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 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                       : ID23-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 67469                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 39.600                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.900                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 13.5200                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.66000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.890                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.21                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MES 100 MM PH 5.5 PEG 200 32%, VAPOR     
REMARK 280  DIFFUSION, TEMPERATURE 295K                                         
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       45.71667            
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       91.43333            
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       91.43333            
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       45.71667            
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: 5420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 39310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 8.0 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 -0.500000 -0.866025  0.000000      168.00000            
REMARK 350   BIOMT2   2 -0.866025  0.500000  0.000000       96.99485            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      320.01667            
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     HIS A     3                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASN A  42    CG   OD1  ND2                                       
REMARK 470     LYS A 491    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   CE2  PHE A   330     O    HOH A   808              1.54            
REMARK 500   OE1  GLU A   344     NZ   LYS A   346              1.65            
REMARK 500   CZ   PHE A   330     O    HOH A   808              1.93            
REMARK 500   O    ASN A   457     O    HOH A   802              1.94            
REMARK 500   OE1  GLU A   327     ND1  HIS A   440              2.03            
REMARK 500   O    HOH A  1057     O    HOH A  1145              2.16            
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    GLU A 350   N     GLU A 350   CA      0.127                       
REMARK 500    MET A 379   CA    MET A 379   C       0.176                       
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    MET A  43   N   -  CA  -  C   ANGL. DEV. =  18.1 DEGREES          
REMARK 500    ARG A  88   N   -  CA  -  C   ANGL. DEV. =  23.0 DEGREES          
REMARK 500    ARG A  88   CA  -  C   -  O   ANGL. DEV. = -13.5 DEGREES          
REMARK 500    ARG A  88   CA  -  C   -  O   ANGL. DEV. = -17.8 DEGREES          
REMARK 500    ARG A  88   CA  -  C   -  N   ANGL. DEV. =  17.5 DEGREES          
REMARK 500    GLU A 140   N   -  CA  -  C   ANGL. DEV. =  16.9 DEGREES          
REMARK 500    GLU A 140   CA  -  C   -  O   ANGL. DEV. =  17.4 DEGREES          
REMARK 500    GLU A 140   CA  -  C   -  N   ANGL. DEV. = -17.6 DEGREES          
REMARK 500    LYS A 192   CA  -  C   -  O   ANGL. DEV. =  16.1 DEGREES          
REMARK 500    LYS A 192   CA  -  C   -  N   ANGL. DEV. = -13.4 DEGREES          
REMARK 500    PHE A 330   CA  -  C   -  O   ANGL. DEV. =  17.7 DEGREES          
REMARK 500    PHE A 330   CA  -  C   -  O   ANGL. DEV. =  15.2 DEGREES          
REMARK 500    PHE A 330   CA  -  C   -  N   ANGL. DEV. = -14.8 DEGREES          
REMARK 500    GLU A 350   C   -  N   -  CA  ANGL. DEV. = -15.3 DEGREES          
REMARK 500    GLU A 350   N   -  CA  -  C   ANGL. DEV. =  16.8 DEGREES          
REMARK 500    MET A 379   CA  -  C   -  N   ANGL. DEV. = -15.8 DEGREES          
REMARK 500    HIS A 440   CB  -  CA  -  C   ANGL. DEV. =  14.9 DEGREES          
REMARK 500    LEU A 456   CA  -  C   -  N   ANGL. DEV. =  14.4 DEGREES          
REMARK 500    LEU A 456   O   -  C   -  N   ANGL. DEV. = -18.5 DEGREES          
REMARK 500    ASN A 457   CB  -  CA  -  C   ANGL. DEV. =  35.1 DEGREES          
REMARK 500    ASN A 457   N   -  CA  -  C   ANGL. DEV. = -22.5 DEGREES          
REMARK 500    TYR A 458   C   -  N   -  CA  ANGL. DEV. =  41.5 DEGREES          
REMARK 500    TYR A 458   N   -  CA  -  CB  ANGL. DEV. =  26.4 DEGREES          
REMARK 500    GLU A 489   CB  -  CA  -  C   ANGL. DEV. = -13.9 DEGREES          
REMARK 500    GLU A 489   N   -  CA  -  C   ANGL. DEV. =  19.3 DEGREES          
REMARK 500    GLU A 489   N   -  CA  -  C   ANGL. DEV. =  23.5 DEGREES          
REMARK 500    GLU A 489   CA  -  C   -  O   ANGL. DEV. = -26.5 DEGREES          
REMARK 500    GLU A 489   CA  -  C   -  O   ANGL. DEV. = -26.2 DEGREES          
REMARK 500    GLU A 489   CA  -  C   -  N   ANGL. DEV. =  25.6 DEGREES          
REMARK 500    GLU A 489   CA  -  C   -  N   ANGL. DEV. =  23.3 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  25     -157.80   -120.81                                   
REMARK 500    PHE A  45      -10.36     79.27                                   
REMARK 500    ALA A  60       41.63   -106.86                                   
REMARK 500    CYS A  94       10.72   -145.67                                   
REMARK 500    SER A 108       77.70   -159.05                                   
REMARK 500    ASN A 131      106.19    -58.30                                   
REMARK 500    GLU A 140       65.96     32.60                                   
REMARK 500    PHE A 155       10.34   -140.30                                   
REMARK 500    BXT A 200     -122.42     67.01                                   
REMARK 500    GLU A 299      -74.00   -113.94                                   
REMARK 500    ASP A 380       55.61   -142.61                                   
REMARK 500    VAL A 400      -60.07   -129.89                                   
REMARK 500    HIS A 440      110.78    -16.66                                   
REMARK 500    HIS A 440      112.21    -16.72                                   
REMARK 500    ASN A 457     -145.24     96.19                                   
REMARK 500    ASN A 457       38.71    109.65                                   
REMARK 500    TYR A 458      123.64     91.90                                   
REMARK 500    ARG A 515       62.14     61.78                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASN A   87     ARG A   88                  148.87                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    GLU A 350        -10.25                                           
REMARK 500    LEU A 456         14.15                                           
REMARK 500    GLU A 489         13.71                                           
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     1PE A  701                                                       
REMARK 610     1PE A  702                                                       
REMARK 610     1PE A  703                                                       
REMARK 610     1PE A  704                                                       
REMARK 610     1PE A  705                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 706 bound   
REMARK 800  to ASN A 59                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 707 bound   
REMARK 800  to ASN A 416                                                        
DBREF  6EUE A    3   535  UNP    P04058   ACES_TETCF      24    556             
SEQRES   1 A  533  HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY LYS VAL          
SEQRES   2 A  533  MET GLY THR ARG VAL PRO VAL LEU SER SER HIS ILE SER          
SEQRES   3 A  533  ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO VAL GLY          
SEQRES   4 A  533  ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS PRO TRP          
SEQRES   5 A  533  SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN ASN CYS          
SEQRES   6 A  533  GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE SER GLY          
SEQRES   7 A  533  SER GLU MET TRP ASN PRO ASN ARG GLU MET SER GLU ASP          
SEQRES   8 A  533  CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO ARG PRO          
SEQRES   9 A  533  LYS SER THR THR VAL MET VAL TRP ILE TYR GLY GLY GLY          
SEQRES  10 A  533  PHE TYR SER GLY SER SER THR LEU ASP VAL TYR ASN GLY          
SEQRES  11 A  533  LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU VAL SER          
SEQRES  12 A  533  LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU ALA LEU          
SEQRES  13 A  533  HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY LEU LEU          
SEQRES  14 A  533  ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP ASN ILE          
SEQRES  15 A  533  GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR ILE PHE          
SEQRES  16 A  533  GLY GLU BXT ALA GLY GLY ALA SER VAL GLY MET HIS ILE          
SEQRES  17 A  533  LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG ALA ILE          
SEQRES  18 A  533  LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA SER VAL          
SEQRES  19 A  533  SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU LEU GLY          
SEQRES  20 A  533  ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU GLU LEU          
SEQRES  21 A  533  ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU LEU ILE          
SEQRES  22 A  533  ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER ILE PHE          
SEQRES  23 A  533  ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU PHE PHE          
SEQRES  24 A  533  PRO THR SER LEU GLU SER MET LEU ASN SER GLY ASN PHE          
SEQRES  25 A  533  LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS ASP GLU          
SEQRES  26 A  533  GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY PHE SER          
SEQRES  27 A  533  LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP PHE MET          
SEQRES  28 A  533  SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN ASP LEU          
SEQRES  29 A  533  GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP TRP MET          
SEQRES  30 A  533  ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY LEU ASP          
SEQRES  31 A  533  ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO LEU MET          
SEQRES  32 A  533  HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN GLY THR          
SEQRES  33 A  533  TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN LEU VAL          
SEQRES  34 A  533  TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR GLU ILE          
SEQRES  35 A  533  GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU LEU ASN          
SEQRES  36 A  533  TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG ILE MET          
SEQRES  37 A  533  HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN PRO ASN          
SEQRES  38 A  533  GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU PHE THR          
SEQRES  39 A  533  THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR GLU PRO          
SEQRES  40 A  533  MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET CYS VAL          
SEQRES  41 A  533  PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN ALA THR          
MODRES 6EUE BXT A  200  SER  MODIFIED RESIDUE                                   
HET    BXT  A 200      12                                                       
HET    1PE  A 701      14                                                       
HET    1PE  A 702      10                                                       
HET    1PE  A 703       7                                                       
HET    1PE  A 704       7                                                       
HET    1PE  A 705       7                                                       
HET    NAG  A 706      14                                                       
HET    NAG  A 707      14                                                       
HETNAM     BXT (2~{S})-2-AZANYL-3-[ETHYL(METHYL)CARBAMOYL]OXY-                  
HETNAM   2 BXT  PROPANOIC ACID                                                  
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETSYN     1PE PEG400                                                           
FORMUL   1  BXT    C7 H14 N2 O4                                                 
FORMUL   2  1PE    5(C10 H22 O6)                                                
FORMUL   7  NAG    2(C8 H15 N O6)                                               
FORMUL   9  HOH   *389(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 BXT A  200  SER A  212  1                                  13    
HELIX    9 AA9 SER A  215  PHE A  219  5                                   5    
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  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  GLY A  415  1                                  16    
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  TRP A 114   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 ILE A 319  ASN A 324  1  O  LEU A 320   N  LEU A 224           
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  2.05  
SSBOND   2 CYS A  254    CYS A  265                          1555   1555  2.04  
SSBOND   3 CYS A  402    CYS A  521                          1555   1555  2.05  
LINK         ND2 ASN A  59                 C1  NAG A 706     1555   1555  1.46  
LINK         C   GLU A 199                 N   BXT A 200     1555   1555  1.33  
LINK         C   BXT A 200                 N   ALA A 201     1555   1555  1.33  
LINK         ND2 ASN A 416                 C1  NAG A 707     1555   1555  1.45  
CISPEP   1 SER A  103    PRO A  104          0         3.08                     
SITE     1 AC1 11 TRP A  84  GLY A 117  GLY A 118  GLU A 199                    
SITE     2 AC1 11 BXT A 200  PHE A 330  HIS A 440  HOH A 801                    
SITE     3 AC1 11 HOH A 808  HOH A 817  HOH A 868                               
SITE     1 AC2  5 TYR A 121  PHE A 330  HOH A 808  HOH A1102                    
SITE     2 AC2  5 HOH A1124                                                     
SITE     1 AC3  2 ARG A 250  ASN A 253                                          
SITE     1 AC4  3 ILE A 296  SER A 304  HOH A1009                               
SITE     1 AC5  4 GLN A 374  THR A 376  ASP A 377  HOH A1035                    
SITE     1 AC6  2 ASN A  59  SER A  61                                          
SITE     1 AC7  2 ASN A 416  HOH A 811                                          
CRYST1  112.000  112.000  137.150  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      0.008929  0.005155  0.000000        0.00000                         
SCALE2      0.000000  0.010310  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007291        0.00000                         
TER    4337      THR A 535                                                      
MASTER      431    0    8   25   14    0   10    6 4700    1   95   41          
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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