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LongText Report for: 7aix-pdb

Name Class
7aix-pdb
HEADER    HYDROLASE                               28-SEP-20   7AIX              
TITLE     CRYSTAL STRUCTURE OF TORPEDO CALIFORNICA ACETYLCHOLINESTERASE IN      
TITLE    2 COMPLEX WITH 2-{1-[4-(12-AMINO-3-CHLORO-6,7,10,11-TETRAHYDRO-7,11-   
TITLE    3 METHANOCYCLOOCTA[B]QUINOLIN-9-YL)BUTYL]-1H-1,2,3-TRIAZOL-4-YL}-N-[4- 
TITLE    4 HYDROXY-3-METHOXYBENZYL]ACETAMIDE                                    
CAVEAT     7AIX    8U2 A 601 HAS WRONG CHIRALITY AT ATOM CAR                    
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    TORPEDO CALIFORNICA ACETYLCHOLINESTERASE, AD, ALZHEIMER DISEASE,      
KEYWDS   2 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.COQUELLE,J.P.COLLETIER                                              
REVDAT   1   06-OCT-21 7AIX    0                                                
JRNL        AUTH   E.VIENNA,N.COQUELLE,M.CIESLIKIEWICZ-BOUTET,M.BARTOLINI,      
JRNL        AUTH 2 A.DE SIMONE,M.RICCHINI,M.RENDINA,O.FIRUZI,B.PEREZ,L.SASO,    
JRNL        AUTH 3 V.ANDRISANO,F.NACHON,X.BRAZZOLOTTO,L.JEAN,J.P.COLLETIER,     
JRNL        AUTH 4 P.Y.RENARD,D.MUNOZ-TORERO                                    
JRNL        TITL   OVERCOMING THE ACHE OVER BCHE SELECTIVITY OF HUPRINE         
JRNL        TITL 2 DERIVATIVES IN A NOVEL CLASS OF MULTI TARGET ANTI-ALZHEIMER  
JRNL        TITL 3 COMPOUNDS                                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.86 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.10.1_2155                                   
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.86                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.01                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 83177                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.178                           
REMARK   3   R VALUE            (WORKING SET) : 0.177                           
REMARK   3   FREE R VALUE                     : 0.197                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4158                            
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 46.0120 -  5.7758    0.97     2810   139  0.1855 0.1824        
REMARK   3     2  5.7758 -  4.5858    0.97     2667   154  0.1436 0.1554        
REMARK   3     3  4.5858 -  4.0065    0.97     2635   136  0.1396 0.1519        
REMARK   3     4  4.0065 -  3.6403    0.96     2629   136  0.1442 0.1804        
REMARK   3     5  3.6403 -  3.3795    0.98     2641   152  0.1625 0.1674        
REMARK   3     6  3.3795 -  3.1803    0.98     2621   146  0.1724 0.2015        
REMARK   3     7  3.1803 -  3.0211    0.98     2660   124  0.1799 0.2071        
REMARK   3     8  3.0211 -  2.8896    0.98     2650   145  0.1785 0.2084        
REMARK   3     9  2.8896 -  2.7783    0.99     2637   141  0.1789 0.2217        
REMARK   3    10  2.7783 -  2.6825    0.98     2614   134  0.1845 0.2252        
REMARK   3    11  2.6825 -  2.5986    0.99     2678   140  0.1859 0.2174        
REMARK   3    12  2.5986 -  2.5243    0.99     2627   149  0.1849 0.2014        
REMARK   3    13  2.5243 -  2.4579    0.99     2618   146  0.1851 0.2153        
REMARK   3    14  2.4579 -  2.3979    0.99     2625   135  0.1796 0.2197        
REMARK   3    15  2.3979 -  2.3434    0.99     2666   149  0.1858 0.2105        
REMARK   3    16  2.3434 -  2.2935    0.99     2639   134  0.1935 0.2262        
REMARK   3    17  2.2935 -  2.2477    0.99     2616   136  0.1914 0.2063        
REMARK   3    18  2.2477 -  2.2053    0.99     2649   155  0.2000 0.2260        
REMARK   3    19  2.2053 -  2.1659    0.99     2592   148  0.2087 0.2111        
REMARK   3    20  2.1659 -  2.1292    0.99     2630   133  0.2186 0.2352        
REMARK   3    21  2.1292 -  2.0948    0.98     2677   111  0.2195 0.2558        
REMARK   3    22  2.0948 -  2.0626    0.98     2609   113  0.2220 0.2216        
REMARK   3    23  2.0626 -  2.0322    0.98     2635   141  0.2220 0.2266        
REMARK   3    24  2.0322 -  2.0036    0.97     2551   127  0.2358 0.2736        
REMARK   3    25  2.0036 -  1.9765    0.98     2599   133  0.2482 0.2775        
REMARK   3    26  1.9765 -  1.9509    0.98     2583   149  0.2672 0.2813        
REMARK   3    27  1.9509 -  1.9265    0.99     2615   152  0.2675 0.2994        
REMARK   3    28  1.9265 -  1.9033    0.98     2626   144  0.2769 0.2837        
REMARK   3    29  1.9033 -  1.8811    0.97     2575   123  0.3062 0.3631        
REMARK   3    30  1.8811 -  1.8600    0.98     2645   133  0.3342 0.3305        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.140           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 43.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.16                          
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      :  0.008           4506                                  
REMARK   3   ANGLE     :  0.853           6133                                  
REMARK   3   CHIRALITY :  0.052            635                                  
REMARK   3   PLANARITY :  0.005            798                                  
REMARK   3   DIHEDRAL  : 14.748           2693                                  
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 7AIX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-SEP-20.                  
REMARK 100 THE DEPOSITION ID IS D_1292111161.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-FEB-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.8-6.2                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : MASSIF-3                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9679                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 2M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 83186                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.860                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.012                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.03900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 13.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.93                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.76600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.700                              
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: 2XI4                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.81                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM MES 28-32% PEG 200, 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       45.58833            
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       91.17667            
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       91.17667            
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       45.58833            
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: 2640 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 39140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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        0.00000            
REMARK 350   BIOMT2   2 -0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -91.17667            
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 A1078  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1093  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     MET A   -20                                                      
REMARK 465     ASN A   -19                                                      
REMARK 465     LEU A   -18                                                      
REMARK 465     LEU A   -17                                                      
REMARK 465     VAL A   -16                                                      
REMARK 465     THR A   -15                                                      
REMARK 465     SER A   -14                                                      
REMARK 465     SER A   -13                                                      
REMARK 465     LEU A   -12                                                      
REMARK 465     GLY A   -11                                                      
REMARK 465     VAL A   -10                                                      
REMARK 465     LEU A    -9                                                      
REMARK 465     LEU A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     VAL A    -4                                                      
REMARK 465     LEU A    -3                                                      
REMARK 465     CYS A    -2                                                      
REMARK 465     GLN A    -1                                                      
REMARK 465     ALA A     0                                                      
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 465     SER A   544                                                      
REMARK 465     GLY A   545                                                      
REMARK 465     THR A   546                                                      
REMARK 465     SER A   547                                                      
REMARK 465     SER A   548                                                      
REMARK 465     SER A   549                                                      
REMARK 465     LYS A   550                                                      
REMARK 465     GLY A   551                                                      
REMARK 465     ILE A   552                                                      
REMARK 465     ILE A   553                                                      
REMARK 465     PHE A   554                                                      
REMARK 465     TYR A   555                                                      
REMARK 465     VAL A   556                                                      
REMARK 465     LEU A   557                                                      
REMARK 465     PHE A   558                                                      
REMARK 465     SER A   559                                                      
REMARK 465     ILE A   560                                                      
REMARK 465     LEU A   561                                                      
REMARK 465     TYR A   562                                                      
REMARK 465     LEU A   563                                                      
REMARK 465     ILE A   564                                                      
REMARK 465     PHE A   565                                                      
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     LYS A 454    CE   NZ                                             
REMARK 470     LYS A 511    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   706     O    HOH A  1045              1.87            
REMARK 500   O    HOH A   701     O    HOH A   982              1.88            
REMARK 500   O    HOH A   804     O    HOH A   830              1.93            
REMARK 500   O    HOH A  1068     O    HOH A  1085              1.95            
REMARK 500   O    HOH A  1068     O    HOH A  1101              1.96            
REMARK 500   O    HOH A   751     O    HOH A  1021              1.98            
REMARK 500   O    HOH A   835     O    HOH A   944              2.00            
REMARK 500   O    HOH A   864     O    HOH A  1046              2.03            
REMARK 500   OD1  ASN A    65     O    HOH A   701              2.03            
REMARK 500   O    HOH A   760     O    HOH A  1106              2.08            
REMARK 500   O    HOH A   840     O    HOH A  1104              2.09            
REMARK 500   O    HOH A  1012     O    HOH A  1081              2.12            
REMARK 500   O    HOH A   749     O    HOH A   817              2.12            
REMARK 500   O    HOH A   702     O    HOH A  1090              2.13            
REMARK 500   O    HOH A  1085     O    HOH A  1089              2.13            
REMARK 500   O    HOH A  1045     O    HOH A  1102              2.14            
REMARK 500   ND2  ASN A    59     O    HOH A   702              2.15            
REMARK 500   OE1  GLN A   526     O    HOH A   703              2.17            
REMARK 500   OD1  ASP A   381     O    HOH A   704              2.18            
REMARK 500   O    HOH A   896     O    HOH A   971              2.18            
REMARK 500   O    HOH A   758     O    HOH A  1086              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  1064     O    HOH A  1092     2565     1.92            
REMARK 500   O    HOH A   723     O    HOH A   741     2565     2.18            
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    LEU A  23     -113.78     52.13                                   
REMARK 500    SER A  25     -157.81   -137.27                                   
REMARK 500    PHE A  45       -7.17     77.86                                   
REMARK 500    ALA A  60       44.09   -106.86                                   
REMARK 500    SER A 108       79.19   -157.32                                   
REMARK 500    SER A 200     -120.87     62.31                                   
REMARK 500    ASP A 380       49.66   -157.54                                   
REMARK 500    VAL A 400      -60.42   -128.53                                   
REMARK 500    ASN A 457       31.25     73.51                                   
REMARK 500    HIS A 486       -0.32     65.85                                   
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 A1124        DISTANCE =  5.90 ANGSTROMS                       
REMARK 525    HOH A1125        DISTANCE =  6.23 ANGSTROMS                       
REMARK 525    HOH A1126        DISTANCE =  6.24 ANGSTROMS                       
REMARK 525    HOH A1127        DISTANCE =  6.44 ANGSTROMS                       
REMARK 525    HOH A1128        DISTANCE =  7.05 ANGSTROMS                       
REMARK 525    HOH A1129        DISTANCE =  7.07 ANGSTROMS                       
REMARK 525    HOH A1130        DISTANCE =  8.69 ANGSTROMS                       
DBREF  7AIX A  -20   565  UNP    P04058   ACES_TETCF       1    586             
SEQRES   1 A  586  MET ASN LEU LEU VAL THR SER SER LEU GLY VAL LEU LEU          
SEQRES   2 A  586  HIS LEU VAL VAL LEU CYS GLN ALA ASP ASP HIS SER GLU          
SEQRES   3 A  586  LEU LEU VAL ASN THR LYS SER GLY LYS VAL MET GLY THR          
SEQRES   4 A  586  ARG VAL PRO VAL LEU SER SER HIS ILE SER ALA PHE LEU          
SEQRES   5 A  586  GLY ILE PRO PHE ALA GLU PRO PRO VAL GLY ASN MET ARG          
SEQRES   6 A  586  PHE ARG ARG PRO GLU PRO LYS LYS PRO TRP SER GLY VAL          
SEQRES   7 A  586  TRP ASN ALA SER THR TYR PRO ASN ASN CYS GLN GLN TYR          
SEQRES   8 A  586  VAL ASP GLU GLN PHE PRO GLY PHE SER GLY SER GLU MET          
SEQRES   9 A  586  TRP ASN PRO ASN ARG GLU MET SER GLU ASP CYS LEU TYR          
SEQRES  10 A  586  LEU ASN ILE TRP VAL PRO SER PRO ARG PRO LYS SER THR          
SEQRES  11 A  586  THR VAL MET VAL TRP ILE TYR GLY GLY GLY PHE TYR SER          
SEQRES  12 A  586  GLY SER SER THR LEU ASP VAL TYR ASN GLY LYS TYR LEU          
SEQRES  13 A  586  ALA TYR THR GLU GLU VAL VAL LEU VAL SER LEU SER TYR          
SEQRES  14 A  586  ARG VAL GLY ALA PHE GLY PHE LEU ALA LEU HIS GLY SER          
SEQRES  15 A  586  GLN GLU ALA PRO GLY ASN VAL GLY LEU LEU ASP GLN ARG          
SEQRES  16 A  586  MET ALA LEU GLN TRP VAL HIS ASP ASN ILE GLN PHE PHE          
SEQRES  17 A  586  GLY GLY ASP PRO LYS THR VAL THR ILE PHE GLY GLU SER          
SEQRES  18 A  586  ALA GLY GLY ALA SER VAL GLY MET HIS ILE LEU SER PRO          
SEQRES  19 A  586  GLY SER ARG ASP LEU PHE ARG ARG ALA ILE LEU GLN SER          
SEQRES  20 A  586  GLY SER PRO ASN CYS PRO TRP ALA SER VAL SER VAL ALA          
SEQRES  21 A  586  GLU GLY ARG ARG ARG ALA VAL GLU LEU GLY ARG ASN LEU          
SEQRES  22 A  586  ASN CYS ASN LEU ASN SER ASP GLU GLU LEU ILE HIS CYS          
SEQRES  23 A  586  LEU ARG GLU LYS LYS PRO GLN GLU LEU ILE ASP VAL GLU          
SEQRES  24 A  586  TRP ASN VAL LEU PRO PHE ASP SER ILE PHE ARG PHE SER          
SEQRES  25 A  586  PHE VAL PRO VAL ILE ASP GLY GLU PHE PHE PRO THR SER          
SEQRES  26 A  586  LEU GLU SER MET LEU ASN SER GLY ASN PHE LYS LYS THR          
SEQRES  27 A  586  GLN ILE LEU LEU GLY VAL ASN LYS ASP GLU GLY SER PHE          
SEQRES  28 A  586  PHE LEU LEU TYR GLY ALA PRO GLY PHE SER LYS ASP SER          
SEQRES  29 A  586  GLU SER LYS ILE SER ARG GLU ASP PHE MET SER GLY VAL          
SEQRES  30 A  586  LYS LEU SER VAL PRO HIS ALA ASN ASP LEU GLY LEU ASP          
SEQRES  31 A  586  ALA VAL THR LEU GLN TYR THR ASP TRP MET ASP ASP ASN          
SEQRES  32 A  586  ASN GLY ILE LYS ASN ARG ASP GLY LEU ASP ASP ILE VAL          
SEQRES  33 A  586  GLY ASP HIS ASN VAL ILE CYS PRO LEU MET HIS PHE VAL          
SEQRES  34 A  586  ASN LYS TYR THR LYS PHE GLY ASN GLY THR TYR LEU TYR          
SEQRES  35 A  586  PHE PHE ASN HIS ARG ALA SER ASN LEU VAL TRP PRO GLU          
SEQRES  36 A  586  TRP MET GLY VAL ILE HIS GLY TYR GLU ILE GLU PHE VAL          
SEQRES  37 A  586  PHE GLY LEU PRO LEU VAL LYS GLU LEU ASN TYR THR ALA          
SEQRES  38 A  586  GLU GLU GLU ALA LEU SER ARG ARG ILE MET HIS TYR TRP          
SEQRES  39 A  586  ALA THR PHE ALA LYS THR GLY ASN PRO ASN GLU PRO HIS          
SEQRES  40 A  586  SER GLN GLU SER LYS TRP PRO LEU PHE THR THR LYS GLU          
SEQRES  41 A  586  GLN LYS PHE ILE ASP LEU ASN THR GLU PRO MET LYS VAL          
SEQRES  42 A  586  HIS GLN ARG LEU ARG VAL GLN MET CYS VAL PHE TRP ASN          
SEQRES  43 A  586  GLN PHE LEU PRO LYS LEU LEU ASN ALA THR ALA CYS ASP          
SEQRES  44 A  586  GLY GLU LEU SER SER SER GLY THR SER SER SER LYS GLY          
SEQRES  45 A  586  ILE ILE PHE TYR VAL LEU PHE SER ILE LEU TYR LEU ILE          
SEQRES  46 A  586  PHE                                                          
HET    8U2  A 601      42                                                       
HET    PEG  A 602       7                                                       
HET    PEG  A 603       7                                                       
HET     CL  A 604       1                                                       
HETNAM     8U2 2-{1-[4-(12-AMINO-3-CHLORO-6,7,10,11-TETRAHYDRO-7,11-            
HETNAM   2 8U2  METHANOCYCLOOCTA[B]QUINOLIN-9-YL)BUTYL]-1H-1,2,3-               
HETNAM   3 8U2  TRIAZOL-4-YL}-N-[4-HYDROXY-3-METHOXYBENZYL]ACETAMIDE            
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM      CL CHLORIDE ION                                                     
FORMUL   2  8U2    C32 H37 CL N6 O3                                             
FORMUL   3  PEG    2(C4 H10 O3)                                                 
FORMUL   5   CL    CL 1-                                                        
FORMUL   6  HOH   *430(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  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  LEU A  97   N  ILE A  33           
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           
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  2.05  
SSBOND   2 CYS A  254    CYS A  265                          1555   1555  2.05  
SSBOND   3 CYS A  402    CYS A  521                          1555   1555  2.06  
CISPEP   1 SER A  103    PRO A  104          0         5.43                     
CRYST1  112.838  112.838  136.765  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      0.008862  0.005117  0.000000        0.00000                         
SCALE2      0.000000  0.010233  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007312        0.00000                         
TER    4310      THR A 535                                                      
MASTER      406    0    4   25   16    0    0    6 4727    1   62   46          
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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