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LongText Report for: 6ntn-pdb

Name Class
6ntn-pdb
HEADER    HYDROLASE/HYDROLASE INHIBITOR           29-JAN-19   6NTN              
TITLE     CRYSTAL STRUCTURE OF RECOMBINANT HUMAN ACETYLCHOLINESTERASE INHIBITED 
TITLE    2 BY A-230 IN COMPLEX WITH THE REACTIVATOR, HI-6                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ACHE;                                                       
COMPND   5 EC: 3.1.1.7;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ACHE;                                                          
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    HYDROLASE, INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR COMPLEX           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.M.BESTER,M.A.GUELTA,J.J.HEIGHT,S.D.PEGAN                            
REVDAT   1   01-JUL-20 6NTN    0                                                
JRNL        AUTH   J.J.HEIGHT,S.M.BESTER,M.A.GUELTA,S.Y.BAE,J.CHEUNG,S.D.PEGAN  
JRNL        TITL   INSIGHTS INTO INHIBITION OF HUMAN ACETYLCHOLINESTERASE BY    
JRNL        TITL 2 NOVICHOK, A-SERIES NERVE AGENTS                              
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (DEV_3311: ???)                               
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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.33                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 57079                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.173                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.710                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2687                            
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 46.3342 -  7.1880    0.98     3073   162  0.2022 0.2532        
REMARK   3     2  7.1880 -  5.7087    0.99     2941   139  0.1926 0.2125        
REMARK   3     3  5.7087 -  4.9880    1.00     2906   150  0.1581 0.1862        
REMARK   3     4  4.9880 -  4.5324    1.00     2877   150  0.1280 0.1765        
REMARK   3     5  4.5324 -  4.2078    0.99     2904   131  0.1278 0.1754        
REMARK   3     6  4.2078 -  3.9598    0.99     2854   160  0.1372 0.1814        
REMARK   3     7  3.9598 -  3.7616    0.99     2876   117  0.1407 0.1738        
REMARK   3     8  3.7616 -  3.5979    1.00     2839   145  0.1488 0.1653        
REMARK   3     9  3.5979 -  3.4595    1.00     2917   107  0.1540 0.2181        
REMARK   3    10  3.4595 -  3.3401    1.00     2871   128  0.1730 0.2283        
REMARK   3    11  3.3401 -  3.2357    0.99     2773   186  0.1798 0.2434        
REMARK   3    12  3.2357 -  3.1432    1.00     2829   142  0.1908 0.2426        
REMARK   3    13  3.1432 -  3.0605    0.99     2828   130  0.1902 0.2214        
REMARK   3    14  3.0605 -  2.9859    0.99     2834   134  0.1887 0.2380        
REMARK   3    15  2.9859 -  2.9180    0.99     2804   152  0.2009 0.2337        
REMARK   3    16  2.9180 -  2.8559    0.99     2857   140  0.2149 0.2800        
REMARK   3    17  2.8559 -  2.7988    1.00     2834   132  0.2272 0.3185        
REMARK   3    18  2.7988 -  2.7460    1.00     2768   151  0.2394 0.2764        
REMARK   3    19  2.7460 -  2.6969    0.98     2807   131  0.2528 0.3286        
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)     : 0.300            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.830           
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      :  0.004           8711                                  
REMARK   3   ANGLE     :  0.703          11915                                  
REMARK   3   CHIRALITY :  0.046           1290                                  
REMARK   3   PLANARITY :  0.005           1558                                  
REMARK   3   DIHEDRAL  :  4.599           5048                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 4:333 )                            
REMARK   3    ORIGIN FOR THE GROUP (A): -53.7669  30.6040 -19.8656              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5754 T22:   0.4256                                     
REMARK   3      T33:   0.2625 T12:   0.0385                                     
REMARK   3      T13:   0.0109 T23:  -0.0234                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1796 L22:   2.1341                                     
REMARK   3      L33:   3.1606 L12:  -0.5612                                     
REMARK   3      L13:  -0.3195 L23:   0.6974                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0512 S12:  -0.1599 S13:  -0.0589                       
REMARK   3      S21:   0.2572 S22:   0.0303 S23:  -0.0339                       
REMARK   3      S31:   0.2717 S32:  -0.1076 S33:   0.0172                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 334:542 )                          
REMARK   3    ORIGIN FOR THE GROUP (A): -53.2732  36.1061 -43.0759              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6116 T22:   0.6295                                     
REMARK   3      T33:   0.3253 T12:   0.0666                                     
REMARK   3      T13:  -0.0039 T23:   0.0064                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9010 L22:   1.3766                                     
REMARK   3      L33:   2.8065 L12:  -0.1940                                     
REMARK   3      L13:  -1.5600 L23:   0.6896                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0318 S12:   0.2196 S13:   0.1351                       
REMARK   3      S21:  -0.1987 S22:   0.0179 S23:   0.0025                       
REMARK   3      S31:  -0.1967 S32:  -0.3269 S33:  -0.0457                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: ( CHAIN B AND RESID 4:36 )                             
REMARK   3    ORIGIN FOR THE GROUP (A): -29.1489 -19.0887   2.8711              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4999 T22:   0.6976                                     
REMARK   3      T33:   0.3325 T12:   0.0820                                     
REMARK   3      T13:  -0.0162 T23:  -0.0273                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2402 L22:   8.5901                                     
REMARK   3      L33:   3.5191 L12:   6.2997                                     
REMARK   3      L13:   0.9629 L23:  -1.3563                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6231 S12:  -1.2473 S13:  -0.1121                       
REMARK   3      S21:   1.0227 S22:  -0.5701 S23:  -0.0810                       
REMARK   3      S31:   0.2337 S32:   0.0432 S33:   0.0195                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: ( CHAIN B AND RESID 37:327 )                           
REMARK   3    ORIGIN FOR THE GROUP (A): -29.5412 -11.1006 -19.5212              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3643 T22:   0.4986                                     
REMARK   3      T33:   0.2854 T12:   0.0956                                     
REMARK   3      T13:  -0.0159 T23:  -0.0412                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2464 L22:   3.4233                                     
REMARK   3      L33:   2.7156 L12:   0.2699                                     
REMARK   3      L13:   0.1585 L23:  -0.1648                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0056 S12:  -0.1331 S13:   0.1628                       
REMARK   3      S21:  -0.1739 S22:  -0.0360 S23:  -0.0390                       
REMARK   3      S31:  -0.2854 S32:  -0.0138 S33:   0.0151                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: ( CHAIN B AND RESID 328:542 )                          
REMARK   3    ORIGIN FOR THE GROUP (A): -44.7846 -24.6719 -31.0303              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5008 T22:   0.5226                                     
REMARK   3      T33:   0.3340 T12:  -0.0045                                     
REMARK   3      T13:  -0.0334 T23:  -0.0611                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6384 L22:   1.2451                                     
REMARK   3      L33:   5.2052 L12:  -0.4632                                     
REMARK   3      L13:   1.2134 L23:  -1.0410                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0536 S12:  -0.1083 S13:  -0.0588                       
REMARK   3      S21:  -0.0787 S22:   0.0458 S23:   0.1799                       
REMARK   3      S31:   0.0574 S32:  -0.6751 S33:   0.0071                       
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 6NTN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000239407.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-MAR-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 57260                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.697                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : 0.13000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 13.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.75                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.200                              
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: 4EY4                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.28                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15-21% POLYETHYLENE GLYCOL 3350 (PEG)    
REMARK 280  AND 0.17- 0.21M POTASSIUM NITRATE, PH 7.0, VAPOR DIFFUSION,         
REMARK 280  SITTING DROP, TEMPERATURE 295K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      107.89433            
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      215.78867            
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      215.78867            
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      107.89433            
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: 5750 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 37820 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 29.0 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 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000     -107.89433            
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     GLY A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     ARG A   493                                                      
REMARK 465     ASP A   494                                                      
REMARK 465     PRO A   495                                                      
REMARK 465     LYS A   496                                                      
REMARK 465     THR A   543                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     PRO B   259                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     GLY B   261                                                      
REMARK 465     THR B   262                                                      
REMARK 465     GLY B   263                                                      
REMARK 465     GLY B   264                                                      
REMARK 465     ARG B   493                                                      
REMARK 465     ASP B   494                                                      
REMARK 465     PRO B   495                                                      
REMARK 465     LYS B   496                                                      
REMARK 465     ALA B   497                                                      
REMARK 465     THR B   543                                                      
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    ALA A  62       71.75   -101.24                                   
REMARK 500    CYS A  96        9.04   -150.06                                   
REMARK 500    ALA A 167       64.82   -155.95                                   
REMARK 500    SER A 203     -122.76     61.51                                   
REMARK 500    ASP A 306      -87.20    -96.99                                   
REMARK 500    VAL A 407      -65.13   -126.16                                   
REMARK 500    PHE B  47       -3.06     74.03                                   
REMARK 500    ALA B  62       51.31   -118.41                                   
REMARK 500    ASP B  95       91.88    -69.41                                   
REMARK 500    PHE B 158       10.69   -141.31                                   
REMARK 500    ALA B 167       72.72   -153.93                                   
REMARK 500    SER B 203     -129.02     58.03                                   
REMARK 500    ASP B 306      -83.44   -102.18                                   
REMARK 500    VAL B 407      -62.98   -133.70                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HI6 A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue L2Y A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HI6 B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC A    
REMARK 800  605 through NAG A 607 bound to ASN A 265                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC A    
REMARK 800  602 through NAG A 604 bound to ASN A 350                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues FUC B    
REMARK 800  602 through NAG B 604 bound to ASN B 350                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 605 bound   
REMARK 800  to ASN B 464                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide L2Y B 606 and SER B    
REMARK 800  203                                                                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6NTG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6NTH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6NTK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6NTL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 6NTM   RELATED DB: PDB                                   
DBREF  6NTN A    2   543  UNP    P22303   ACES_HUMAN      33    574             
DBREF  6NTN B    2   543  UNP    P22303   ACES_HUMAN      33    574             
SEQRES   1 A  542  GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY          
SEQRES   2 A  542  GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY          
SEQRES   3 A  542  PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO          
SEQRES   4 A  542  PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS          
SEQRES   5 A  542  GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN          
SEQRES   6 A  542  SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY          
SEQRES   7 A  542  PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU          
SEQRES   8 A  542  SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR          
SEQRES   9 A  542  PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE          
SEQRES  10 A  542  TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP          
SEQRES  11 A  542  VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR          
SEQRES  12 A  542  VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY          
SEQRES  13 A  542  PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN          
SEQRES  14 A  542  VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL          
SEQRES  15 A  542  GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER          
SEQRES  16 A  542  VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL          
SEQRES  17 A  542  GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE          
SEQRES  18 A  542  HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO          
SEQRES  19 A  542  TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA          
SEQRES  20 A  542  THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY          
SEQRES  21 A  542  THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG          
SEQRES  22 A  542  THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS          
SEQRES  23 A  542  VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL          
SEQRES  24 A  542  PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU          
SEQRES  25 A  542  ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL          
SEQRES  26 A  542  LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU          
SEQRES  27 A  542  VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER          
SEQRES  28 A  542  LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL          
SEQRES  29 A  542  GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL          
SEQRES  30 A  542  VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO          
SEQRES  31 A  542  ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP          
SEQRES  32 A  542  HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG          
SEQRES  33 A  542  LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE          
SEQRES  34 A  542  GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP MET          
SEQRES  35 A  542  GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY          
SEQRES  36 A  542  ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU          
SEQRES  37 A  542  LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN          
SEQRES  38 A  542  PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO          
SEQRES  39 A  542  LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN          
SEQRES  40 A  542  GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG          
SEQRES  41 A  542  ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG          
SEQRES  42 A  542  PHE LEU PRO LYS LEU LEU SER ALA THR                          
SEQRES   1 B  542  GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY          
SEQRES   2 B  542  GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY          
SEQRES   3 B  542  PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO          
SEQRES   4 B  542  PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS          
SEQRES   5 B  542  GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN          
SEQRES   6 B  542  SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY          
SEQRES   7 B  542  PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU          
SEQRES   8 B  542  SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR          
SEQRES   9 B  542  PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE          
SEQRES  10 B  542  TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP          
SEQRES  11 B  542  VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR          
SEQRES  12 B  542  VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY          
SEQRES  13 B  542  PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN          
SEQRES  14 B  542  VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL          
SEQRES  15 B  542  GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER          
SEQRES  16 B  542  VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL          
SEQRES  17 B  542  GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE          
SEQRES  18 B  542  HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO          
SEQRES  19 B  542  TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA          
SEQRES  20 B  542  THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY          
SEQRES  21 B  542  THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG          
SEQRES  22 B  542  THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS          
SEQRES  23 B  542  VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL          
SEQRES  24 B  542  PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU          
SEQRES  25 B  542  ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL          
SEQRES  26 B  542  LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU          
SEQRES  27 B  542  VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER          
SEQRES  28 B  542  LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL          
SEQRES  29 B  542  GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL          
SEQRES  30 B  542  VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO          
SEQRES  31 B  542  ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP          
SEQRES  32 B  542  HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG          
SEQRES  33 B  542  LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE          
SEQRES  34 B  542  GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP MET          
SEQRES  35 B  542  GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY          
SEQRES  36 B  542  ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU          
SEQRES  37 B  542  LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN          
SEQRES  38 B  542  PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO          
SEQRES  39 B  542  LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN          
SEQRES  40 B  542  GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG          
SEQRES  41 B  542  ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG          
SEQRES  42 B  542  PHE LEU PRO LYS LEU LEU SER ALA THR                          
HET    HI6  A 601      21                                                       
HET    FUC  A 602      10                                                       
HET    NAG  A 603      14                                                       
HET    NAG  A 604      14                                                       
HET    FUC  A 605      10                                                       
HET    NAG  A 606      14                                                       
HET    NAG  A 607      14                                                       
HET    L2Y  A 608      11                                                       
HET    HI6  B 601      21                                                       
HET    FUC  B 602      10                                                       
HET    NAG  B 603      14                                                       
HET    NAG  B 604      14                                                       
HET    NAG  B 605      14                                                       
HET    L2Y  B 606      11                                                       
HETNAM     HI6 4-(AMINOCARBONYL)-1-[({2-[(E)-(HYDROXYIMINO)                     
HETNAM   2 HI6  METHYL]PYRIDINIUM-1-YL}METHOXY)METHYL]PYRIDINIUM                
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     L2Y (S)-N-[(1E)-1-(DIETHYLAMINO)ETHYLIDENE]-P-                       
HETNAM   2 L2Y  METHYLPHOSPHONAMIDIC FLUORIDE                                   
HETSYN     HI6 1-(2-HYDROXY-IMINOMETHYLPYRIDINIUM)-1-(4-CARBOXYAMINO)-          
HETSYN   2 HI6  PYRIDINIUM DIMETHYLETHER                                        
HETSYN     L2Y A-230 (NERVE AGENT)                                              
FORMUL   3  HI6    2(C14 H16 N4 O3 2+)                                          
FORMUL   4  FUC    3(C6 H12 O5)                                                 
FORMUL   4  NAG    7(C8 H15 N O6)                                               
FORMUL   6  L2Y    2(C7 H16 F N2 O P)                                           
FORMUL  11  HOH   *458(H2 O)                                                    
HELIX    1 AA1 ASP A    5  GLU A    7  5                                   3    
HELIX    2 AA2 MET A   42  ARG A   46  5                                   5    
HELIX    3 AA3 PHE A   80  MET A   85  1                                   6    
HELIX    4 AA4 LEU A  130  ASP A  134  5                                   5    
HELIX    5 AA5 GLY A  135  ARG A  143  1                                   9    
HELIX    6 AA6 GLY A  154  LEU A  159  1                                   6    
HELIX    7 AA7 ASN A  170  VAL A  187  1                                  18    
HELIX    8 AA8 ALA A  188  PHE A  190  5                                   3    
HELIX    9 AA9 SER A  203  SER A  215  1                                  13    
HELIX   10 AB1 SER A  215  GLY A  220  1                                   6    
HELIX   11 AB2 GLY A  240  VAL A  255  1                                  16    
HELIX   12 AB3 ASN A  265  THR A  275  1                                  11    
HELIX   13 AB4 PRO A  277  ASN A  283  1                                   7    
HELIX   14 AB5 HIS A  284  LEU A  289  5                                   6    
HELIX   15 AB6 THR A  311  GLY A  319  1                                   9    
HELIX   16 AB7 GLY A  335  VAL A  340  1                                   6    
HELIX   17 AB8 SER A  355  VAL A  367  1                                  13    
HELIX   18 AB9 SER A  371  THR A  383  1                                  13    
HELIX   19 AC1 ASP A  390  VAL A  407  1                                  18    
HELIX   20 AC2 VAL A  407  GLN A  421  1                                  15    
HELIX   21 AC3 PRO A  440  GLY A  444  5                                   5    
HELIX   22 AC4 GLU A  450  PHE A  455  1                                   6    
HELIX   23 AC5 GLY A  456  ASP A  460  5                                   5    
HELIX   24 AC6 THR A  466  GLY A  487  1                                  22    
HELIX   25 AC7 ARG A  525  ARG A  534  1                                  10    
HELIX   26 AC8 PHE A  535  SER A  541  1                                   7    
HELIX   27 AC9 ASP B    5  GLU B    7  5                                   3    
HELIX   28 AD1 MET B   42  ARG B   46  5                                   5    
HELIX   29 AD2 PHE B   80  MET B   85  1                                   6    
HELIX   30 AD3 LEU B  130  ASP B  134  5                                   5    
HELIX   31 AD4 GLY B  135  ARG B  143  1                                   9    
HELIX   32 AD5 VAL B  153  LEU B  159  1                                   7    
HELIX   33 AD6 ASN B  170  VAL B  187  1                                  18    
HELIX   34 AD7 ALA B  188  PHE B  190  5                                   3    
HELIX   35 AD8 SER B  203  LEU B  214  1                                  12    
HELIX   36 AD9 SER B  215  GLY B  220  1                                   6    
HELIX   37 AE1 MET B  241  VAL B  255  1                                  15    
HELIX   38 AE2 ASP B  266  THR B  275  1                                  10    
HELIX   39 AE3 PRO B  277  TRP B  286  1                                  10    
HELIX   40 AE4 HIS B  287  LEU B  289  5                                   3    
HELIX   41 AE5 THR B  311  ALA B  318  1                                   8    
HELIX   42 AE6 GLY B  335  GLY B  342  5                                   8    
HELIX   43 AE7 SER B  355  VAL B  367  1                                  13    
HELIX   44 AE8 SER B  371  THR B  383  1                                  13    
HELIX   45 AE9 ASP B  390  VAL B  407  1                                  18    
HELIX   46 AF1 VAL B  407  GLN B  421  1                                  15    
HELIX   47 AF2 PRO B  440  GLY B  444  5                                   5    
HELIX   48 AF3 GLU B  450  PHE B  455  1                                   6    
HELIX   49 AF4 GLY B  456  ASP B  460  5                                   5    
HELIX   50 AF5 THR B  466  GLY B  487  1                                  22    
HELIX   51 AF6 ARG B  525  ARG B  534  1                                  10    
HELIX   52 AF7 ARG B  534  SER B  541  1                                   8    
SHEET    1 AA1 3 LEU A   9  VAL A  12  0                                        
SHEET    2 AA1 3 GLY A  15  ARG A  18 -1  O  LEU A  17   N  VAL A  10           
SHEET    3 AA1 3 VAL A  59  ASP A  61  1  O  VAL A  60   N  ARG A  16           
SHEET    1 AA211 ILE A  20  LEU A  22  0                                        
SHEET    2 AA211 VAL A  29  PRO A  36 -1  O  VAL A  29   N  LEU A  22           
SHEET    3 AA211 TYR A  98  PRO A 104 -1  O  LEU A  99   N  ILE A  35           
SHEET    4 AA211 VAL A 145  MET A 149 -1  O  SER A 148   N  ASN A 100           
SHEET    5 AA211 THR A 112  ILE A 118  1  N  LEU A 115   O  VAL A 147           
SHEET    6 AA211 GLY A 192  GLU A 202  1  O  THR A 198   N  VAL A 114           
SHEET    7 AA211 ARG A 224  GLN A 228  1  O  ARG A 224   N  LEU A 199           
SHEET    8 AA211 GLN A 325  VAL A 331  1  O  LEU A 327   N  LEU A 227           
SHEET    9 AA211 ARG A 424  PHE A 430  1  O  TYR A 426   N  VAL A 328           
SHEET   10 AA211 GLN A 509  LEU A 513  1  O  LEU A 513   N  VAL A 429           
SHEET   11 AA211 GLU A 519  ARG A 522 -1  O  ARG A 521   N  TYR A 510           
SHEET    1 AA3 2 VAL A  68  CYS A  69  0                                        
SHEET    2 AA3 2 LEU A  92  SER A  93  1  O  SER A  93   N  VAL A  68           
SHEET    1 AA4 3 LEU B   9  VAL B  12  0                                        
SHEET    2 AA4 3 GLY B  15  ARG B  18 -1  O  LEU B  17   N  VAL B  10           
SHEET    3 AA4 3 VAL B  59  ASP B  61  1  O  VAL B  60   N  ARG B  16           
SHEET    1 AA511 ILE B  20  LEU B  22  0                                        
SHEET    2 AA511 VAL B  29  PRO B  36 -1  O  VAL B  29   N  LEU B  22           
SHEET    3 AA511 TYR B  98  PRO B 104 -1  O  THR B 103   N  SER B  30           
SHEET    4 AA511 VAL B 145  MET B 149 -1  O  SER B 148   N  ASN B 100           
SHEET    5 AA511 THR B 112  ILE B 118  1  N  TRP B 117   O  VAL B 147           
SHEET    6 AA511 GLY B 192  GLU B 202  1  O  ASP B 193   N  THR B 112           
SHEET    7 AA511 ARG B 224  GLN B 228  1  O  ARG B 224   N  LEU B 199           
SHEET    8 AA511 GLN B 325  VAL B 331  1  O  LEU B 327   N  LEU B 227           
SHEET    9 AA511 ARG B 424  PHE B 430  1  O  TYR B 426   N  VAL B 328           
SHEET   10 AA511 GLN B 509  LEU B 513  1  O  LEU B 513   N  VAL B 429           
SHEET   11 AA511 GLU B 519  ARG B 522 -1  O  ARG B 521   N  TYR B 510           
SHEET    1 AA6 2 VAL B  68  CYS B  69  0                                        
SHEET    2 AA6 2 LEU B  92  SER B  93  1  O  SER B  93   N  VAL B  68           
SHEET    1 AA7 2 VAL B 239  GLY B 240  0                                        
SHEET    2 AA7 2 VAL B 302  VAL B 303  1  O  VAL B 303   N  VAL B 239           
SSBOND   1 CYS A   69    CYS A   96                          1555   1555  2.04  
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.04  
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.06  
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.05  
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.03  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.06  
LINK         OG  SER A 203                 P09 L2Y A 608     1555   1555  1.56  
LINK         ND2 ASN A 265                 C1  NAG A 606     1555   1555  1.51  
LINK         ND2 ASN A 350                 C1  NAG A 603     1555   1555  1.47  
LINK         OG  SER B 203                 P09 L2Y B 606     1555   1555  1.56  
LINK         ND2 ASN B 350                 C1  NAG B 603     1555   1555  1.40  
LINK         ND2 ASN B 464                 C1  NAG B 605     1555   1555  1.38  
LINK         C1  FUC A 602                 O6  NAG A 603     1555   1555  1.44  
LINK         O4  NAG A 603                 C1  NAG A 604     1555   1555  1.44  
LINK         C1  FUC A 605                 O6  NAG A 606     1555   1555  1.44  
LINK         O4  NAG A 606                 C1  NAG A 607     1555   1555  1.44  
LINK         C1  FUC B 602                 O6  NAG B 603     1555   1555  1.44  
LINK         O4  NAG B 603                 C1  NAG B 604     1555   1555  1.44  
CISPEP   1 TYR A  105    PRO A  106          0         4.06                     
CISPEP   2 CYS A  257    PRO A  258          0        -2.49                     
CISPEP   3 TYR B  105    PRO B  106          0        -2.64                     
CISPEP   4 CYS B  257    PRO B  258          0         6.28                     
SITE     1 AC1  9 TYR A  72  ASP A  74  TYR A 124  VAL A 282                    
SITE     2 AC1  9 GLU A 285  TRP A 286  TYR A 337  TYR A 341                    
SITE     3 AC1  9 HOH A 706                                                     
SITE     1 AC2 10 TRP A  86  GLY A 121  GLY A 122  GLU A 202                    
SITE     2 AC2 10 SER A 203  ALA A 204  PHE A 295  PHE A 297                    
SITE     3 AC2 10 TYR A 337  HIS A 447                                          
SITE     1 AC3  9 TYR B  72  TYR B 124  GLU B 285  TRP B 286                    
SITE     2 AC3  9 PHE B 297  SER B 298  TYR B 337  TYR B 341                    
SITE     3 AC3  9 L2Y B 606                                                     
SITE     1 AC4  4 ASN A 265  THR A 267  GLU A 268  HOH A 779                    
SITE     1 AC5  4 PRO A 344  GLY A 345  SER A 347  ASN A 350                    
SITE     1 AC6  2 GLY B 345  ASN B 350                                          
SITE     1 AC7  2 SER B 462  ASN B 464                                          
SITE     1 AC8 15 GLY B 121  GLY B 122  TYR B 133  GLU B 202                    
SITE     2 AC8 15 ALA B 204  GLY B 205  ALA B 206  ALA B 207                    
SITE     3 AC8 15 GLN B 228  SER B 229  PHE B 295  PHE B 297                    
SITE     4 AC8 15 TYR B 337  HIS B 447  HI6 B 601                               
CRYST1  104.402  104.402  323.683  90.00  90.00 120.00 P 31 2 1     12          
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      0.009578  0.005530  0.000000        0.00000                         
SCALE2      0.000000  0.011060  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003089        0.00000                         
TER    4139      ALA A 542                                                      
TER    8251      ALA B 542                                                      
MASTER      404    0   14   52   34    0   17    6 8899    2  210   84          
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:
ESTHER Home Page and ACEDB Home Page
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