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LongText Report for: 6h14-pdb

Name Class
6h14-pdb
HEADER    HYDROLASE                               10-JUL-18   6H14              
TITLE     CRYSTAL STRUCTURE OF TCACHE COMPLEXED TO 1-(6-OXO-1,2,3,4,6,10B-      
TITLE    2 HEXAHYDROPYRIDO[2,1-A]ISOINDOL-10-YL)-3-(4-(1-(2-((1,2,3,4-          
TITLE    3 TETRAHYDROACRIDIN-9-YL)AMINO)ETHYL)-1H-1,2,3-TRIAZOL-4-YL)PYRIDIN-2- 
TITLE    4 YL)UREA                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A, B;                                                         
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    COMPLEX, INHIBITOR, ALZHEIMER, ACETYLCHOLINESTERASE, MULTI-TARGET-    
KEYWDS   2 DIRECTED LIGANDS, MTDL, HYDROLASE                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.COQUELLE,J.P.COLLETIER                                              
REVDAT   1   15-MAY-19 6H14    0                                                
JRNL        AUTH   K.OUKOLOFF,N.COQUELLE,M.BARTOLINI,M.NALDI,R.LE GUEVEL,       
JRNL        AUTH 2 S.BACH,B.JOSSELIN,S.RUCHAUD,M.CATTO,L.PISANI,N.DENORA,       
JRNL        AUTH 3 R.M.IACOBAZZI,I.SILMAN,J.L.SUSSMAN,F.BURON,J.P.COLLETIER,    
JRNL        AUTH 4 L.JEAN,S.ROUTIER,P.Y.RENARD                                  
JRNL        TITL   DESIGN, BIOLOGICAL EVALUATION AND X-RAY CRYSTALLOGRAPHY OF   
JRNL        TITL 2 NANOMOLAR MULTIFUNCTIONAL LIGANDS TARGETING SIMULTANEOUSLY   
JRNL        TITL 3 ACETYLCHOLINESTERASE AND GLYCOGEN SYNTHASE KINASE-3.         
JRNL        REF    EUR.J.MED.CHEM.               V. 168    58 2019              
JRNL        REFN                   ISSN 0223-5234                               
JRNL        PMID   30798053                                                     
JRNL        DOI    10.1016/J.EJMECH.2018.12.063                                 
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.86                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.49                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 123607                         
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                     : 0.211                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6202                            
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 46.5081 -  5.7759    0.98     4190   219  0.1932 0.2344        
REMARK   3     2  5.7759 -  4.5858    0.99     4060   225  0.1456 0.1625        
REMARK   3     3  4.5858 -  4.0065    0.99     4021   212  0.1388 0.1666        
REMARK   3     4  4.0065 -  3.6403    1.00     4020   216  0.1516 0.1731        
REMARK   3     5  3.6403 -  3.3795    0.99     3957   217  0.1622 0.1835        
REMARK   3     6  3.3795 -  3.1803    0.98     3910   212  0.1763 0.1857        
REMARK   3     7  3.1803 -  3.0210    0.99     3955   214  0.1810 0.2187        
REMARK   3     8  3.0210 -  2.8896    0.99     3931   202  0.1720 0.2273        
REMARK   3     9  2.8896 -  2.7783    0.99     3954   211  0.1765 0.2017        
REMARK   3    10  2.7783 -  2.6825    0.99     3936   226  0.1761 0.2262        
REMARK   3    11  2.6825 -  2.5986    0.99     3980   199  0.1726 0.1888        
REMARK   3    12  2.5986 -  2.5243    0.99     3920   211  0.1768 0.2387        
REMARK   3    13  2.5243 -  2.4579    0.99     3933   204  0.1762 0.2147        
REMARK   3    14  2.4579 -  2.3979    0.99     3953   199  0.1791 0.2517        
REMARK   3    15  2.3979 -  2.3434    0.99     3889   231  0.1748 0.2232        
REMARK   3    16  2.3434 -  2.2935    0.99     3921   199  0.1758 0.2010        
REMARK   3    17  2.2935 -  2.2477    0.96     3799   198  0.1731 0.2277        
REMARK   3    18  2.2477 -  2.2052    0.98     3905   198  0.1832 0.2376        
REMARK   3    19  2.2052 -  2.1659    0.99     3906   224  0.1927 0.2424        
REMARK   3    20  2.1659 -  2.1291    0.99     3883   204  0.1899 0.2403        
REMARK   3    21  2.1291 -  2.0948    0.99     3900   218  0.2009 0.2531        
REMARK   3    22  2.0948 -  2.0626    0.99     3860   224  0.1988 0.2249        
REMARK   3    23  2.0626 -  2.0322    0.99     3863   210  0.2067 0.2578        
REMARK   3    24  2.0322 -  2.0036    0.99     3894   196  0.2056 0.2474        
REMARK   3    25  2.0036 -  1.9765    0.98     3927   196  0.2213 0.2783        
REMARK   3    26  1.9765 -  1.9509    0.98     3816   208  0.2373 0.2789        
REMARK   3    27  1.9509 -  1.9265    0.97     3902   177  0.2401 0.2701        
REMARK   3    28  1.9265 -  1.9033    0.96     3821   173  0.2543 0.2830        
REMARK   3    29  1.9033 -  1.8811    0.95     3722   195  0.2650 0.3167        
REMARK   3    30  1.8811 -  1.8600    0.94     3677   184  0.2745 0.3141        
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)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.590           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
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      :  0.008           9215                                  
REMARK   3   ANGLE     :  1.006          12520                                  
REMARK   3   CHIRALITY :  0.054           1294                                  
REMARK   3   PLANARITY :  0.006           1599                                  
REMARK   3   DIHEDRAL  : 13.627           5521                                  
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 6H14 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-AUG-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200010883.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-JUL-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : MASSIF-1                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
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   : 123623                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.860                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.490                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 4.600                              
REMARK 200  R MERGE                    (I) : 0.09300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 10.3000                            
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     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.96400                            
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   (%): 56.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.82                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM MES PH 6.0, 30% PEG 2000, VAPOR    
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
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 -1.000000  0.000000  0.000000       45.79550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.34900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       53.96300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       75.34900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       45.79550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       53.96300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: 5200 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 40560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 30.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     GLN A   488                                                      
REMARK 465     GLU A   489                                                      
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 465     ASP B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     GLN B   488                                                      
REMARK 465     GLU B   489                                                      
REMARK 465     ALA B   536                                                      
REMARK 465     CYS B   537                                                      
REMARK 465     ASP B   538                                                      
REMARK 465     GLY B   539                                                      
REMARK 465     GLU B   540                                                      
REMARK 465     LEU B   541                                                      
REMARK 465     SER B   542                                                      
REMARK 465     SER B   543                                                      
REMARK 465     SER B   544                                                      
REMARK 465     GLY B   545                                                      
REMARK 465     THR B   546                                                      
REMARK 465     SER B   547                                                      
REMARK 465     SER B   548                                                      
REMARK 465     SER B   549                                                      
REMARK 465     LYS B   550                                                      
REMARK 465     GLY B   551                                                      
REMARK 465     ILE B   552                                                      
REMARK 465     ILE B   553                                                      
REMARK 465     PHE B   554                                                      
REMARK 465     TYR B   555                                                      
REMARK 465     VAL B   556                                                      
REMARK 465     LEU B   557                                                      
REMARK 465     PHE B   558                                                      
REMARK 465     SER B   559                                                      
REMARK 465     ILE B   560                                                      
REMARK 465     LEU B   561                                                      
REMARK 465     TYR B   562                                                      
REMARK 465     LEU B   563                                                      
REMARK 465     ILE B   564                                                      
REMARK 465     PHE B   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 413    CD   CE   NZ                                        
REMARK 470     LYS A 454    CE   NZ                                             
REMARK 470     HIS A 486    ND1  CD2  CE1  NE2                                  
REMARK 470     LYS A 511    CE   NZ                                             
REMARK 470     LYS B 413    CD   CE   NZ                                        
REMARK 470     LYS B 454    CE   NZ                                             
REMARK 470     HIS B 486    ND1  CD2  CE1  NE2                                  
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   O4   PGE B   611     O    HOH B   701              2.02            
REMARK 500   O    HOH B   701     O    HOH B  1190              2.09            
REMARK 500   OBL  FW8 B   609     O    HOH B   702              2.09            
REMARK 500   OD1  ASN B    65     O    HOH B   703              2.11            
REMARK 500   NE2  GLN B    74     O    HOH B   704              2.12            
REMARK 500   O    HOH A   702     O    HOH A  1060              2.13            
REMARK 500   O    HOH B   736     O    HOH B   956              2.14            
REMARK 500   O    HOH B  1089     O    HOH B  1214              2.14            
REMARK 500   O2   GOL A   607     O    HOH A   701              2.15            
REMARK 500   ND2  ASN A    65     O    HOH A   702              2.17            
REMARK 500   O    HOH B  1257     O    HOH B  1265              2.17            
REMARK 500   O    HOH B  1004     O    HOH B  1234              2.18            
REMARK 500   O    HOH A  1083     O    HOH A  1134              2.18            
REMARK 500   OE1  GLN A   526     O    HOH A   701              2.19            
REMARK 500   OG   SER B     4     O    HOH B   705              2.19            
REMARK 500   O    HOH B  1033     O    HOH B  1144              2.19            
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    PHE A  45       -5.61     77.05                                   
REMARK 500    ALA A  60       44.01   -106.53                                   
REMARK 500    SER A 108       77.36   -154.27                                   
REMARK 500    SER A 200     -121.79     59.06                                   
REMARK 500    GLU A 299      -72.19   -129.39                                   
REMARK 500    ASP A 380       52.96   -161.52                                   
REMARK 500    VAL A 400      -60.27   -129.09                                   
REMARK 500    HIS A 486      131.57     73.33                                   
REMARK 500    SER B  25     -159.66   -131.81                                   
REMARK 500    PHE B  45       -9.50     81.68                                   
REMARK 500    ALA B  60       44.60   -108.20                                   
REMARK 500    SER B 108       73.68   -155.24                                   
REMARK 500    SER B 200     -122.03     54.45                                   
REMARK 500    GLU B 299      -76.33   -123.58                                   
REMARK 500    ASP B 380       46.33   -158.41                                   
REMARK 500    VAL B 400      -59.24   -129.24                                   
REMARK 500    PRO B 485       82.48    -60.05                                   
REMARK 500    HIS B 486      126.03    155.24                                   
REMARK 500    ASN B 506     -169.57   -165.49                                   
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 A1213        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH A1214        DISTANCE =  5.87 ANGSTROMS                       
REMARK 525    HOH A1215        DISTANCE =  6.24 ANGSTROMS                       
REMARK 525    HOH A1216        DISTANCE =  6.45 ANGSTROMS                       
REMARK 525    HOH B1263        DISTANCE =  5.90 ANGSTROMS                       
REMARK 525    HOH B1264        DISTANCE =  6.81 ANGSTROMS                       
REMARK 525    HOH B1265        DISTANCE =  7.40 ANGSTROMS                       
REMARK 525    HOH B1266        DISTANCE =  9.49 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FW8 A 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FW8 B 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 610                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MES B 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 601 bound   
REMARK 800  to ASN A 59                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 602 bound   
REMARK 800  to ASN A 416                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 603 bound   
REMARK 800  to ASN A 457                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  601 through NAG B 602 bound to ASN B 59                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 603 bound   
REMARK 800  to ASN B 416                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 604 bound   
REMARK 800  to ASN B 457                                                        
DBREF  6H14 A    1   565  UNP    P04058   ACES_TETCF      22    586             
DBREF  6H14 B    1   565  UNP    P04058   ACES_TETCF      22    586             
SEQRES   1 A  565  ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY          
SEQRES   2 A  565  LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS          
SEQRES   3 A  565  ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO          
SEQRES   4 A  565  VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS          
SEQRES   5 A  565  PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN          
SEQRES   6 A  565  ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE          
SEQRES   7 A  565  SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER          
SEQRES   8 A  565  GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO          
SEQRES   9 A  565  ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY          
SEQRES  10 A  565  GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR          
SEQRES  11 A  565  ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU          
SEQRES  12 A  565  VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU          
SEQRES  13 A  565  ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY          
SEQRES  14 A  565  LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP          
SEQRES  15 A  565  ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR          
SEQRES  16 A  565  ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET          
SEQRES  17 A  565  HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG          
SEQRES  18 A  565  ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA          
SEQRES  19 A  565  SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU          
SEQRES  20 A  565  LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU          
SEQRES  21 A  565  GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU          
SEQRES  22 A  565  LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER          
SEQRES  23 A  565  ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU          
SEQRES  24 A  565  PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY          
SEQRES  25 A  565  ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS          
SEQRES  26 A  565  ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY          
SEQRES  27 A  565  PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP          
SEQRES  28 A  565  PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN          
SEQRES  29 A  565  ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP          
SEQRES  30 A  565  TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY          
SEQRES  31 A  565  LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO          
SEQRES  32 A  565  LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN          
SEQRES  33 A  565  GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN          
SEQRES  34 A  565  LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR          
SEQRES  35 A  565  GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU          
SEQRES  36 A  565  LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG          
SEQRES  37 A  565  ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN          
SEQRES  38 A  565  PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU          
SEQRES  39 A  565  PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR          
SEQRES  40 A  565  GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET          
SEQRES  41 A  565  CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN          
SEQRES  42 A  565  ALA THR ALA CYS ASP GLY GLU LEU SER SER SER GLY THR          
SEQRES  43 A  565  SER SER SER LYS GLY ILE ILE PHE TYR VAL LEU PHE SER          
SEQRES  44 A  565  ILE LEU TYR LEU ILE PHE                                      
SEQRES   1 B  565  ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY          
SEQRES   2 B  565  LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS          
SEQRES   3 B  565  ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO          
SEQRES   4 B  565  VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS          
SEQRES   5 B  565  PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN          
SEQRES   6 B  565  ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE          
SEQRES   7 B  565  SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER          
SEQRES   8 B  565  GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO          
SEQRES   9 B  565  ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY          
SEQRES  10 B  565  GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR          
SEQRES  11 B  565  ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU          
SEQRES  12 B  565  VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU          
SEQRES  13 B  565  ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY          
SEQRES  14 B  565  LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP          
SEQRES  15 B  565  ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR          
SEQRES  16 B  565  ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET          
SEQRES  17 B  565  HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG          
SEQRES  18 B  565  ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA          
SEQRES  19 B  565  SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU          
SEQRES  20 B  565  LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU          
SEQRES  21 B  565  GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU          
SEQRES  22 B  565  LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER          
SEQRES  23 B  565  ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU          
SEQRES  24 B  565  PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY          
SEQRES  25 B  565  ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS          
SEQRES  26 B  565  ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY          
SEQRES  27 B  565  PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP          
SEQRES  28 B  565  PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN          
SEQRES  29 B  565  ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP          
SEQRES  30 B  565  TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY          
SEQRES  31 B  565  LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO          
SEQRES  32 B  565  LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN          
SEQRES  33 B  565  GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN          
SEQRES  34 B  565  LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR          
SEQRES  35 B  565  GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU          
SEQRES  36 B  565  LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG          
SEQRES  37 B  565  ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN          
SEQRES  38 B  565  PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU          
SEQRES  39 B  565  PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR          
SEQRES  40 B  565  GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET          
SEQRES  41 B  565  CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN          
SEQRES  42 B  565  ALA THR ALA CYS ASP GLY GLU LEU SER SER SER GLY THR          
SEQRES  43 B  565  SER SER SER LYS GLY ILE ILE PHE TYR VAL LEU PHE SER          
SEQRES  44 B  565  ILE LEU TYR LEU ILE PHE                                      
HET    NAG  A 601      14                                                       
HET    NAG  A 602      14                                                       
HET    NAG  A 603      14                                                       
HET    EDO  A 604       4                                                       
HET    EDO  A 605       4                                                       
HET    PEG  A 606       7                                                       
HET    GOL  A 607       6                                                       
HET    EDO  A 608       4                                                       
HET    EDO  A 609       4                                                       
HET    FW8  A 610      92                                                       
HET    PGE  A 611      10                                                       
HET    SO4  A 612       5                                                       
HET    NAG  B 601      14                                                       
HET    NAG  B 602      14                                                       
HET    NAG  B 603      14                                                       
HET    NAG  B 604      14                                                       
HET    EDO  B 605       4                                                       
HET    GOL  B 606       6                                                       
HET    EDO  B 607       4                                                       
HET    EDO  B 608       4                                                       
HET    FW8  B 609      92                                                       
HET     CL  B 610       1                                                       
HET    PGE  B 611      10                                                       
HET    MES  B 612      12                                                       
HET    EDO  B 613       4                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     GOL GLYCEROL                                                         
HETNAM     FW8 1-[(10~{B}~{S})-6-OXIDANYLIDENE-2,3,4,10~{B}-                    
HETNAM   2 FW8  TETRAHYDRO-1~{H}-PYRIDO[2,1-A]ISOINDOL-10-YL]-3-[4-[1-          
HETNAM   3 FW8  [2-(1,2,3,4-TETRAHYDROACRIDIN-9-YLAMINO)ETHYL]-1,2,3-           
HETNAM   4 FW8  TRIAZOL-4-YL]PYRIDIN-2-YL]UREA                                  
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  NAG    7(C8 H15 N O6)                                               
FORMUL   6  EDO    8(C2 H6 O2)                                                  
FORMUL   8  PEG    C4 H10 O3                                                    
FORMUL   9  GOL    2(C3 H8 O3)                                                  
FORMUL  12  FW8    2(C35 H35 N9 O2)                                             
FORMUL  13  PGE    2(C6 H14 O4)                                                 
FORMUL  14  SO4    O4 S 2-                                                      
FORMUL  23   CL    CL 1-                                                        
FORMUL  25  MES    C6 H13 N O4 S                                                
FORMUL  27  HOH   *1082(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 PRO A  213  PHE A  219  5                                   7    
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  VAL A  277  1                                   8    
HELIX   13 AB4 GLU A  278  LEU A  282  5                                   5    
HELIX   14 AB5 SER A  304  GLY A  312  1                                   9    
HELIX   15 AB6 GLY A  328  ALA A  336  1                                   9    
HELIX   16 AB7 SER A  348  VAL A  360  1                                  13    
HELIX   17 AB8 ASN A  364  THR A  376  1                                  13    
HELIX   18 AB9 ASN A  383  VAL A  400  1                                  18    
HELIX   19 AC1 VAL A  400  LYS A  413  1                                  14    
HELIX   20 AC2 PRO A  433  GLY A  437  5                                   5    
HELIX   21 AC3 GLU A  443  PHE A  448  1                                   6    
HELIX   22 AC4 GLY A  449  ASN A  457  5                                   9    
HELIX   23 AC5 THR A  459  GLY A  480  1                                  22    
HELIX   24 AC6 ARG A  517  GLN A  526  1                                  10    
HELIX   25 AC7 GLN A  526  THR A  535  1                                  10    
HELIX   26 AC8 VAL B   40  ARG B   44  5                                   5    
HELIX   27 AC9 PHE B   78  MET B   83  1                                   6    
HELIX   28 AD1 LEU B  127  ASN B  131  5                                   5    
HELIX   29 AD2 GLY B  132  GLU B  140  1                                   9    
HELIX   30 AD3 VAL B  150  LEU B  156  1                                   7    
HELIX   31 AD4 ASN B  167  ILE B  184  1                                  18    
HELIX   32 AD5 GLN B  185  PHE B  187  5                                   3    
HELIX   33 AD6 SER B  200  SER B  212  1                                  13    
HELIX   34 AD7 SER B  212  ASP B  217  1                                   6    
HELIX   35 AD8 VAL B  238  LEU B  252  1                                  15    
HELIX   36 AD9 SER B  258  GLU B  268  1                                  11    
HELIX   37 AE1 LYS B  270  GLU B  278  1                                   9    
HELIX   38 AE2 TRP B  279  LEU B  282  5                                   4    
HELIX   39 AE3 SER B  304  GLY B  312  1                                   9    
HELIX   40 AE4 GLY B  328  ALA B  336  1                                   9    
HELIX   41 AE5 SER B  348  VAL B  360  1                                  13    
HELIX   42 AE6 ASN B  364  THR B  376  1                                  13    
HELIX   43 AE7 ASN B  383  VAL B  400  1                                  18    
HELIX   44 AE8 VAL B  400  LYS B  413  1                                  14    
HELIX   45 AE9 PRO B  433  GLY B  437  5                                   5    
HELIX   46 AF1 GLU B  443  PHE B  448  1                                   6    
HELIX   47 AF2 GLY B  449  ASN B  457  5                                   9    
HELIX   48 AF3 THR B  459  GLY B  480  1                                  22    
HELIX   49 AF4 ARG B  517  GLN B  526  1                                  10    
HELIX   50 AF5 GLN B  526  ASN B  533  1                                   8    
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  LYS A  14           
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           
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           
SHEET    1 AA4 3 LEU B   7  THR B  10  0                                        
SHEET    2 AA4 3 GLY B  13  MET B  16 -1  O  VAL B  15   N  VAL B   8           
SHEET    3 AA4 3 VAL B  57  ASN B  59  1  O  TRP B  58   N  LYS B  14           
SHEET    1 AA511 THR B  18  VAL B  22  0                                        
SHEET    2 AA511 SER B  25  PRO B  34 -1  O  ILE B  27   N  VAL B  20           
SHEET    3 AA511 TYR B  96  VAL B 101 -1  O  ILE B  99   N  PHE B  30           
SHEET    4 AA511 VAL B 142  SER B 145 -1  O  LEU B 143   N  TRP B 100           
SHEET    5 AA511 THR B 109  ILE B 115  1  N  TRP B 114   O  VAL B 144           
SHEET    6 AA511 GLY B 189  GLU B 199  1  O  ASP B 190   N  THR B 109           
SHEET    7 AA511 ARG B 221  GLN B 225  1  O  GLN B 225   N  GLY B 198           
SHEET    8 AA511 ILE B 319  ASN B 324  1  O  LEU B 320   N  LEU B 224           
SHEET    9 AA511 THR B 418  PHE B 423  1  O  PHE B 423   N  VAL B 323           
SHEET   10 AA511 LYS B 501  LEU B 505  1  O  LEU B 505   N  PHE B 422           
SHEET   11 AA511 VAL B 512  GLN B 514 -1  O  HIS B 513   N  PHE B 502           
SHEET    1 AA6 2 VAL B 236  SER B 237  0                                        
SHEET    2 AA6 2 VAL B 295  ILE B 296  1  O  ILE B 296   N  VAL B 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  2.05  
SSBOND   4 CYS B   67    CYS B   94                          1555   1555  2.07  
SSBOND   5 CYS B  254    CYS B  265                          1555   1555  2.03  
SSBOND   6 CYS B  402    CYS B  521                          1555   1555  2.04  
LINK         ND2 ASN A  59                 C1  NAG A 601     1555   1555  1.45  
LINK         ND2 ASN A 416                 C1  NAG A 602     1555   1555  1.52  
LINK         ND2 ASN A 457                 C1  NAG A 603     1555   1555  1.48  
LINK         ND2 ASN B  59                 C1  NAG B 601     1555   1555  1.41  
LINK         ND2 ASN B 416                 C1  NAG B 603     1555   1555  1.48  
LINK         ND2 ASN B 457                 C1  NAG B 604     1555   1555  1.49  
LINK         O4  NAG B 601                 C1  NAG B 602     1555   1555  1.42  
CISPEP   1 SER A  103    PRO A  104          0         4.37                     
CISPEP   2 SER B  103    PRO B  104          0         2.04                     
SITE     1 AC1  2 GLN A 500  VAL A 518                                          
SITE     1 AC2  3 THR A 376  HOH A1058  GLN B 519                               
SITE     1 AC3  4 VAL A 238  ILE A 296  HOH A 762  HOH A 932                    
SITE     1 AC4  8 MET A 405  HIS A 406  ASN A 409  CYS A 521                    
SITE     2 AC4  8 ASN A 525  GLN A 526  HOH A 701  HOH A 726                    
SITE     1 AC5  3 GLY A  41  ASN A  42  ARG A 267                               
SITE     1 AC6  2 SER A  55  VAL A  57                                          
SITE     1 AC7 15 TRP A  84  TYR A 121  GLU A 199  TRP A 279                    
SITE     2 AC7 15 LEU A 282  SER A 286  PHE A 288  PHE A 290                    
SITE     3 AC7 15 PHE A 330  PHE A 331  TYR A 334  TRP A 432                    
SITE     4 AC7 15 HIS A 440  HOH A 786  HOH A1057                               
SITE     1 AC8  3 SER A  79  MET A  83  HOH A 745                               
SITE     1 AC9  8 LYS A 325  ASP A 326  ARG A 388  ASP A 389                    
SITE     2 AC9  8 TRP A 435  GLY A 437  HOH A 780  HOH A 924                    
SITE     1 AD1  3 ASN A  42  THR B 459  THR B 507                               
SITE     1 AD2  7 MET B 405  HIS B 406  ASN B 409  CYS B 521                    
SITE     2 AD2  7 ASN B 525  HOH B 711  HOH B 724                               
SITE     1 AD3  3 TRP B  58  ASN B  59  EDO B 608                               
SITE     1 AD4  3 SER B  55  VAL B  57  EDO B 607                               
SITE     1 AD5 16 TRP B  84  TYR B 121  GLU B 199  TRP B 279                    
SITE     2 AD5 16 LEU B 282  SER B 286  PHE B 288  PHE B 330                    
SITE     3 AD5 16 PHE B 331  TYR B 334  TRP B 432  HIS B 440                    
SITE     4 AD5 16 HOH B 702  HOH B 727  HOH B 843  HOH B1087                    
SITE     1 AD6  1 TRP B 435                                                     
SITE     1 AD7  5 MET B  83  ASN B 429  HOH B 701  HOH B 707                    
SITE     2 AD7  5 HOH B 762                                                     
SITE     1 AD8  5 ASN B 481  ASN B 483  LYS B 491  HOH B 732                    
SITE     2 AD8  5 HOH B 743                                                     
SITE     1 AD9  5 THR B 412  THR B 496  THR B 497  HOH B 952                    
SITE     2 AD9  5 HOH B1162                                                     
SITE     1 AE1  2 ASN A  59  SER A  61                                          
SITE     1 AE2  5 ASN A 416  HOH A 729  HOH A 735  HOH A 812                    
SITE     2 AE2  5 HOH A 955                                                     
SITE     1 AE3  2 ASN A 457  HOH A 704                                          
SITE     1 AE4  4 ASN B  59  SER B  61  HOH B 717  HOH B 769                    
SITE     1 AE5  3 ASN B 416  HOH B 740  HOH B1081                               
SITE     1 AE6  2 GLU B 455  ASN B 457                                          
CRYST1   91.591  107.926  150.698  90.00  90.00  90.00 P 21 21 21    8          
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      0.010918  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009266  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006636        0.00000                         
TER    4289      THR A 535                                                      
TER    8556      THR B 535                                                      
MASTER      495    0   25   50   32    0   37    6 9793    2  388   88          
END                                                                             

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