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LongText Report for: 8aev-pdb

Name Class
8aev-pdb
HEADER    HYDROLASE                               13-JUL-22   8AEV              
TITLE     HUMAN ACETYLCHOLINESTERASE IN COMPLEX WITH N,N,N-TRIMETHYL-2-OXO-2-(2-
TITLE    2 (PYRIDIN-2-YLMETHYLENE)HYDRAZINEYL)ETHAN-1-AMINIUM                   
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: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029                                       
KEYWDS    INHIBITOR, COMPLEX, ZINC, ACETYLCHOLINESTERASE, HYDROLASE             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.NACHON,J.DIAS,X.BRAZZOLOTTO                                         
REVDAT   1   14-JUN-23 8AEV    0                                                
JRNL        AUTH   F.NACHON,X.BRAZZOLOTTO,J.DIAS,C.COURAGEUX,W.DROZDZ,X.Y.CAO,  
JRNL        AUTH 2 A.R.STEFANKIEWICZ,J.M.LEHN                                   
JRNL        TITL   GRID-TYPE QUATERNARY METALLOSUPRAMOLECULAR COMPOUNDS INHIBIT 
JRNL        TITL 2 HUMAN CHOLINESTERASES THROUGH DYNAMIC MULTIVALENT            
JRNL        TITL 3 INTERACTIONS.                                                
JRNL        REF    CHEMBIOCHEM                   V.  23 00456 2022              
JRNL        REFN                   ESSN 1439-7633                               
JRNL        PMID   36193860                                                     
JRNL        DOI    10.1002/CBIC.202200456                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.89 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.20.1_4487                                   
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.89                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.64                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 63106                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.185                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.207                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3198                            
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 46.6400 -  8.2100    0.97     2738   155  0.1467 0.1651        
REMARK   3     2  8.2000 -  6.5200    0.98     2728   151  0.1523 0.1700        
REMARK   3     3  6.5200 -  5.7000    0.98     2683   179  0.1579 0.2146        
REMARK   3     4  5.7000 -  5.1800    0.98     2694   150  0.1522 0.1930        
REMARK   3     5  5.1800 -  4.8100    0.98     2737   149  0.1354 0.1569        
REMARK   3     6  4.8100 -  4.5200    0.99     2699   163  0.1284 0.1525        
REMARK   3     7  4.5200 -  4.3000    0.99     2709   163  0.1321 0.1456        
REMARK   3     8  4.3000 -  4.1100    0.98     2693   154  0.1364 0.1583        
REMARK   3     9  4.1100 -  3.9500    0.99     2708   138  0.1591 0.2019        
REMARK   3    10  3.9500 -  3.8100    0.99     2739   129  0.1740 0.1833        
REMARK   3    11  3.8100 -  3.7000    0.99     2713   150  0.1803 0.1886        
REMARK   3    12  3.7000 -  3.5900    0.98     2693   131  0.1916 0.2361        
REMARK   3    13  3.5900 -  3.5000    0.99     2714   146  0.2236 0.2734        
REMARK   3    14  3.5000 -  3.4100    0.99     2706   142  0.2370 0.2702        
REMARK   3    15  3.4100 -  3.3300    0.99     2752   129  0.2746 0.2791        
REMARK   3    16  3.3300 -  3.2600    0.98     2707   120  0.2889 0.3487        
REMARK   3    17  3.2600 -  3.2000    0.98     2712   121  0.2986 0.3320        
REMARK   3    18  3.2000 -  3.1400    0.96     2677   104  0.3085 0.3763        
REMARK   3    19  3.1400 -  3.0800    0.93     2544   135  0.3303 0.3524        
REMARK   3    20  3.0800 -  3.0300    0.91     2510   130  0.3431 0.3334        
REMARK   3    21  3.0300 -  2.9800    0.90     2436   141  0.3550 0.3782        
REMARK   3    22  2.9800 -  2.9300    0.73     2002   121  0.3709 0.4076        
REMARK   3    23  2.9300 -  2.8900    0.60     1614    97  0.3828 0.4063        
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)     : 0.442            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.611           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 76.21                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 88.45                          
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      :  0.010           8821                                  
REMARK   3   ANGLE     :  1.169          12076                                  
REMARK   3   CHIRALITY :  0.063           1301                                  
REMARK   3   PLANARITY :  0.011           1570                                  
REMARK   3   DIHEDRAL  :  9.605           1256                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A): 192.5314  88.9527   7.9246              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4617 T22:   0.5511                                     
REMARK   3      T33:   0.4046 T12:  -0.0692                                     
REMARK   3      T13:   0.1233 T23:  -0.0501                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1648 L22:   2.9076                                     
REMARK   3      L33:   1.5611 L12:  -0.9604                                     
REMARK   3      L13:   0.8281 L23:  -0.8812                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0520 S12:  -0.0917 S13:  -0.1166                       
REMARK   3      S21:   0.1878 S22:   0.0551 S23:   0.3836                       
REMARK   3      S31:  -0.0446 S32:   0.1013 S33:  -0.0118                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A): 156.5312 123.1120 -25.5268              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4320 T22:   0.5642                                     
REMARK   3      T33:   0.7319 T12:  -0.0471                                     
REMARK   3      T13:  -0.0211 T23:  -0.0464                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1247 L22:   2.9337                                     
REMARK   3      L33:   2.7663 L12:  -0.1966                                     
REMARK   3      L13:   1.1327 L23:  -0.3427                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0077 S12:  -0.2285 S13:  -0.3381                       
REMARK   3      S21:  -0.1303 S22:   0.1401 S23:   0.8752                       
REMARK   3      S31:  -0.1147 S32:  -0.4158 S33:  -0.1071                       
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 8AEV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JUL-22.                  
REMARK 100 THE DEPOSITION ID IS D_1292124302.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-JUL-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.873127                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 64879                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.890                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.640                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.5                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : 0.18120                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.4600                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.89                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.99                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 0.580                              
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: 6ZWE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 80.85                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M LISO4, 100 MM HEPES PH7, 60 MM     
REMARK 280  MGSO4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
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   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
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       38.87800            
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       77.75600            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       58.31700            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       97.19500            
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       19.43900            
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 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
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     GLU A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     PRO A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     THR A   262                                                      
REMARK 465     GLY A   263                                                      
REMARK 465     GLY A   264                                                      
REMARK 465     GLU B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     GLY B   261                                                      
REMARK 465     THR B   262                                                      
REMARK 465     GLY B   263                                                      
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   NH1  ARG A   224     O    ALA A   484              2.12            
REMARK 500   O    ARG B    46     NH1  ARG B   274              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A 272   CA  -  CB  -  SG  ANGL. DEV. =   6.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  62       34.08    -93.27                                   
REMARK 500    GLN A  66     -168.97    -76.12                                   
REMARK 500    TIS A 203     -123.80     51.25                                   
REMARK 500    ARG A 219       34.98    -79.12                                   
REMARK 500    PHE A 295       50.25   -151.41                                   
REMARK 500    ASP A 306      -77.40    -67.26                                   
REMARK 500    ASN A 350     -161.59   -119.10                                   
REMARK 500    GLN A 369       64.66     60.29                                   
REMARK 500    PRO A 458      -19.53    -44.92                                   
REMARK 500    ASN A 464       57.31    -97.64                                   
REMARK 500    ARG A 493       57.95   -108.86                                   
REMARK 500    ASP A 494       74.19   -164.99                                   
REMARK 500    LEU A 518      131.98    -36.47                                   
REMARK 500    GLU B   7        4.88    -69.30                                   
REMARK 500    PHE B  47       -6.74     77.81                                   
REMARK 500    ALA B  62       39.07    -93.66                                   
REMARK 500    CYS B  96       13.34   -150.67                                   
REMARK 500    ALA B 127      138.08   -173.32                                   
REMARK 500    ASP B 134      109.97    -54.51                                   
REMARK 500    ARG B 143       58.42     31.18                                   
REMARK 500    ARG B 165       -6.11     69.57                                   
REMARK 500    SER B 196       48.22   -151.83                                   
REMARK 500    TIS B 203     -128.32     45.98                                   
REMARK 500    ASN B 265       45.08    -69.13                                   
REMARK 500    ASP B 266      -38.11   -150.06                                   
REMARK 500    ASP B 306      -76.62    -89.79                                   
REMARK 500    VAL B 367       70.97   -107.41                                   
REMARK 500    TRP B 385        1.02    -60.59                                   
REMARK 500    ARG B 395      -72.09    -56.09                                   
REMARK 500    GLU B 491      107.38    -55.22                                   
REMARK 500    ARG B 493       79.44     56.86                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 625  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 381   ND1                                                    
REMARK 620 2 HIS A 381   ND1  41.4                                              
REMARK 620 3 HIS A 381   NE2  32.4  54.8                                        
REMARK 620 4 HIS B 381   NE2  87.8 103.0  56.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 625  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 381   NE2                                                    
REMARK 620 2 HIS B 381   ND1  79.2                                              
REMARK 620 3 HIS B 381   NE2  56.8  35.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 632  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 452   OE2                                                    
REMARK 620 2 HOH A 754   O   125.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 634  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 488   OD2                                                    
REMARK 620 2 HOH B 728   O    73.6                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 629  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SO4 B 603   O3                                                     
REMARK 620 2 SO4 B 603   O4   48.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 632  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 452   OE2                                                    
REMARK 620 2 HOH B 740   O   135.1                                              
REMARK 620 N                    1                                               
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 8AEN   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN WITH DIFFERENT LIGAND                                   
DBREF  8AEV A    1   543  UNP    P22303   ACES_HUMAN      32    574             
DBREF  8AEV B    1   543  UNP    P22303   ACES_HUMAN      32    574             
SEQRES   1 A  543  GLU GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG          
SEQRES   2 A  543  GLY GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY          
SEQRES   3 A  543  GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU          
SEQRES   4 A  543  PRO PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO          
SEQRES   5 A  543  LYS GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE          
SEQRES   6 A  543  GLN SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO          
SEQRES   7 A  543  GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU          
SEQRES   8 A  543  LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO          
SEQRES   9 A  543  TYR PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP          
SEQRES  10 A  543  ILE TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU          
SEQRES  11 A  543  ASP VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG          
SEQRES  12 A  543  THR VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE          
SEQRES  13 A  543  GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY          
SEQRES  14 A  543  ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP          
SEQRES  15 A  543  VAL GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR          
SEQRES  16 A  543  SER VAL THR LEU PHE GLY GLU TIS ALA GLY ALA ALA SER          
SEQRES  17 A  543  VAL GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU          
SEQRES  18 A  543  PHE HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY          
SEQRES  19 A  543  PRO TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG          
SEQRES  20 A  543  ALA THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY          
SEQRES  21 A  543  GLY THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU          
SEQRES  22 A  543  ARG THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP          
SEQRES  23 A  543  HIS VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE          
SEQRES  24 A  543  VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO          
SEQRES  25 A  543  GLU ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN          
SEQRES  26 A  543  VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE          
SEQRES  27 A  543  LEU VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU          
SEQRES  28 A  543  SER LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG          
SEQRES  29 A  543  VAL GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA          
SEQRES  30 A  543  VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP          
SEQRES  31 A  543  PRO ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY          
SEQRES  32 A  543  ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY          
SEQRES  33 A  543  ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL          
SEQRES  34 A  543  PHE GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP          
SEQRES  35 A  543  MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE          
SEQRES  36 A  543  GLY ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU          
SEQRES  37 A  543  GLU LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA          
SEQRES  38 A  543  ASN PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP          
SEQRES  39 A  543  PRO LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA          
SEQRES  40 A  543  GLN GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL          
SEQRES  41 A  543  ARG ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN          
SEQRES  42 A  543  ARG PHE LEU PRO LYS LEU LEU SER ALA THR                      
SEQRES   1 B  543  GLU GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG          
SEQRES   2 B  543  GLY GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY          
SEQRES   3 B  543  GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU          
SEQRES   4 B  543  PRO PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO          
SEQRES   5 B  543  LYS GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE          
SEQRES   6 B  543  GLN SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO          
SEQRES   7 B  543  GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU          
SEQRES   8 B  543  LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO          
SEQRES   9 B  543  TYR PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP          
SEQRES  10 B  543  ILE TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU          
SEQRES  11 B  543  ASP VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG          
SEQRES  12 B  543  THR VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE          
SEQRES  13 B  543  GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY          
SEQRES  14 B  543  ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP          
SEQRES  15 B  543  VAL GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR          
SEQRES  16 B  543  SER VAL THR LEU PHE GLY GLU TIS ALA GLY ALA ALA SER          
SEQRES  17 B  543  VAL GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU          
SEQRES  18 B  543  PHE HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY          
SEQRES  19 B  543  PRO TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG          
SEQRES  20 B  543  ALA THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY          
SEQRES  21 B  543  GLY THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU          
SEQRES  22 B  543  ARG THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP          
SEQRES  23 B  543  HIS VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE          
SEQRES  24 B  543  VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO          
SEQRES  25 B  543  GLU ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN          
SEQRES  26 B  543  VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE          
SEQRES  27 B  543  LEU VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU          
SEQRES  28 B  543  SER LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG          
SEQRES  29 B  543  VAL GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA          
SEQRES  30 B  543  VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP          
SEQRES  31 B  543  PRO ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY          
SEQRES  32 B  543  ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY          
SEQRES  33 B  543  ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL          
SEQRES  34 B  543  PHE GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP          
SEQRES  35 B  543  MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE          
SEQRES  36 B  543  GLY ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU          
SEQRES  37 B  543  GLU LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA          
SEQRES  38 B  543  ASN PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP          
SEQRES  39 B  543  PRO LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA          
SEQRES  40 B  543  GLN GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL          
SEQRES  41 B  543  ARG ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN          
SEQRES  42 B  543  ARG PHE LEU PRO LYS LEU LEU SER ALA THR                      
MODRES 8AEV TIS A  203  SER  MODIFIED RESIDUE                                   
MODRES 8AEV TIS B  203  SER  MODIFIED RESIDUE                                   
HET    TIS  A 203      10                                                       
HET    TIS  B 203      10                                                       
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    FUC  C   3      10                                                       
HET    NAG  D   1      14                                                       
HET    NAG  D   2      14                                                       
HET    GAL  E   1      12                                                       
HET    SIA  E   2      20                                                       
HET    NAG  F   1      14                                                       
HET    NAG  F   2      14                                                       
HET    FUC  F   3      10                                                       
HET    LWU  A 601      27                                                       
HET    SO4  A 602       5                                                       
HET    SO4  A 603       5                                                       
HET    SO4  A 604       5                                                       
HET    SO4  A 605       5                                                       
HET    SO4  A 606       5                                                       
HET    SO4  A 607       5                                                       
HET    SO4  A 608       5                                                       
HET    SO4  A 609       5                                                       
HET    SO4  A 610       5                                                       
HET     CL  A 611       1                                                       
HET     CL  A 612       1                                                       
HET     CL  A 613       1                                                       
HET     CL  A 614       1                                                       
HET     CL  A 615       1                                                       
HET     CL  A 616       1                                                       
HET     CL  A 617       1                                                       
HET     CL  A 618       1                                                       
HET     CL  A 619       1                                                       
HET     CL  A 620       1                                                       
HET     CL  A 621       1                                                       
HET     CL  A 622       1                                                       
HET     CL  A 623       1                                                       
HET     CL  A 624       1                                                       
HET     ZN  A 625       1                                                       
HET     ZN  A 626       1                                                       
HET     MG  A 627       1                                                       
HET     MG  A 628       1                                                       
HET     MG  A 629       1                                                       
HET     MG  A 630       1                                                       
HET     MG  A 631       1                                                       
HET     MG  A 632       1                                                       
HET     MG  A 633       1                                                       
HET     MG  A 634       1                                                       
HET    SO4  B 601       5                                                       
HET    SO4  B 602       5                                                       
HET    SO4  B 603       5                                                       
HET    SO4  B 604       5                                                       
HET    SO4  B 605       5                                                       
HET    SO4  B 606       5                                                       
HET    SO4  B 607       5                                                       
HET     CL  B 608       1                                                       
HET     CL  B 609       1                                                       
HET     CL  B 610       1                                                       
HET     CL  B 611       1                                                       
HET     CL  B 612       1                                                       
HET     CL  B 613       1                                                       
HET     CL  B 614       1                                                       
HET     CL  B 615       1                                                       
HET     CL  B 616       1                                                       
HET     CL  B 617       1                                                       
HET     CL  B 618       1                                                       
HET     CL  B 619       1                                                       
HET     CL  B 620       1                                                       
HET     CL  B 621       1                                                       
HET     CL  B 622       1                                                       
HET     CL  B 623       1                                                       
HET     CL  B 624       1                                                       
HET     ZN  B 625       1                                                       
HET     ZN  B 626       1                                                       
HET     ZN  B 627       1                                                       
HET     MG  B 628       1                                                       
HET     MG  B 629       1                                                       
HET     MG  B 630       1                                                       
HET     MG  B 631       1                                                       
HET     MG  B 632       1                                                       
HET     MG  B 633       1                                                       
HETNAM     TIS O-(1,1-DIHYDROXYETHYL)-L-SERINE                                  
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     FUC ALPHA-L-FUCOPYRANOSE                                             
HETNAM     GAL BETA-D-GALACTOPYRANOSE                                           
HETNAM     SIA N-ACETYL-ALPHA-NEURAMINIC ACID                                   
HETNAM     LWU 1-(2-(2-((6-(DIHYDROXYMETHYL)-2-PHENYLPYRIMIDIN-4-YL)            
HETNAM   2 LWU  METHYLENE)HYDRAZINEYL)-2-OXOETHYL)PYRIDIN-1-IUM                 
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM      ZN ZINC ION                                                         
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
HETSYN     FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L-              
HETSYN   2 FUC  FUCOSE; FUCOSE                                                  
HETSYN     GAL BETA-D-GALACTOSE; D-GALACTOSE; GALACTOSE                         
HETSYN     SIA N-ACETYLNEURAMINIC ACID; SIALIC ACID; ALPHA-SIALIC               
HETSYN   2 SIA  ACID; O-SIALIC ACID                                             
HETSYN     LWU ~{N}'-[[6-[BIS(OXIDANYL)METHYL]-2-PHENYL-PYRIMIDIN-4-            
HETSYN   2 LWU  YL]METHYL]-2-PYRIDIN-1-YL-ETHANEHYDRAZIDE                       
FORMUL   1  TIS    2(C5 H11 N O5)                                               
FORMUL   3  NAG    6(C8 H15 N O6)                                               
FORMUL   3  FUC    2(C6 H12 O5)                                                 
FORMUL   5  GAL    C6 H12 O6                                                    
FORMUL   5  SIA    C11 H19 N O9                                                 
FORMUL   7  LWU    C19 H20 N5 O3 1+                                             
FORMUL   8  SO4    16(O4 S 2-)                                                  
FORMUL  17   CL    31(CL 1-)                                                    
FORMUL  31   ZN    5(ZN 2+)                                                     
FORMUL  33   MG    14(MG 2+)                                                    
FORMUL  74  HOH   *183(H2 O)                                                    
HELIX    1 AA1 MET A   42  ARG A   46  5                                   5    
HELIX    2 AA2 PHE A   80  MET A   85  1                                   6    
HELIX    3 AA3 LEU A  130  ASP A  134  5                                   5    
HELIX    4 AA4 GLY A  135  ARG A  143  1                                   9    
HELIX    5 AA5 VAL A  153  LEU A  159  1                                   7    
HELIX    6 AA6 ASN A  170  VAL A  187  1                                  18    
HELIX    7 AA7 ALA A  188  PHE A  190  5                                   3    
HELIX    8 AA8 TIS A  203  LEU A  214  1                                  12    
HELIX    9 AA9 GLY A  240  GLY A  256  1                                  17    
HELIX   10 AB1 ASP A  266  THR A  275  1                                  10    
HELIX   11 AB2 PRO A  277  ASN A  283  1                                   7    
HELIX   12 AB3 HIS A  284  LEU A  289  5                                   6    
HELIX   13 AB4 THR A  311  GLY A  319  1                                   9    
HELIX   14 AB5 GLY A  335  VAL A  340  1                                   6    
HELIX   15 AB6 SER A  355  VAL A  367  1                                  13    
HELIX   16 AB7 SER A  371  THR A  383  1                                  13    
HELIX   17 AB8 ASP A  390  VAL A  407  1                                  18    
HELIX   18 AB9 VAL A  407  GLN A  421  1                                  15    
HELIX   19 AC1 PRO A  440  GLY A  444  5                                   5    
HELIX   20 AC2 GLU A  450  PHE A  455  1                                   6    
HELIX   21 AC3 GLY A  456  ASP A  460  5                                   5    
HELIX   22 AC4 THR A  466  GLY A  487  1                                  22    
HELIX   23 AC5 ARG A  525  ARG A  534  1                                  10    
HELIX   24 AC6 ARG A  534  ALA A  542  1                                   9    
HELIX   25 AC7 ASP B    5  GLU B    7  5                                   3    
HELIX   26 AC8 MET B   42  ARG B   46  5                                   5    
HELIX   27 AC9 PHE B   80  MET B   85  1                                   6    
HELIX   28 AD1 LEU B  130  ASP B  134  5                                   5    
HELIX   29 AD2 GLY B  135  ARG B  143  1                                   9    
HELIX   30 AD3 GLY B  154  LEU B  159  1                                   6    
HELIX   31 AD4 ASN B  170  VAL B  187  1                                  18    
HELIX   32 AD5 ALA B  188  PHE B  190  5                                   3    
HELIX   33 AD6 TIS B  203  LEU B  214  1                                  12    
HELIX   34 AD7 SER B  215  GLY B  220  1                                   6    
HELIX   35 AD8 MET B  241  VAL B  255  1                                  15    
HELIX   36 AD9 ASP B  266  ARG B  274  1                                   9    
HELIX   37 AE1 PRO B  277  HIS B  284  1                                   8    
HELIX   38 AE2 THR B  311  ALA B  318  1                                   8    
HELIX   39 AE3 GLY B  335  VAL B  340  1                                   6    
HELIX   40 AE4 SER B  355  VAL B  367  1                                  13    
HELIX   41 AE5 SER B  371  THR B  383  1                                  13    
HELIX   42 AE6 ASP B  390  VAL B  407  1                                  18    
HELIX   43 AE7 VAL B  407  GLN B  421  1                                  15    
HELIX   44 AE8 PRO B  440  GLY B  444  5                                   5    
HELIX   45 AE9 GLU B  450  PHE B  455  1                                   6    
HELIX   46 AF1 GLY B  456  ASP B  460  5                                   5    
HELIX   47 AF2 THR B  466  GLY B  487  1                                  22    
HELIX   48 AF3 ARG B  525  ARG B  534  1                                  10    
HELIX   49 AF4 ARG B  534  THR B  543  1                                  10    
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  ALA A  31   N  ILE A  20           
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 145           
SHEET    6 AA211 GLY A 192  GLU A 202  1  O  SER A 196   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  ALA A 225           
SHEET    9 AA211 ARG A 424  PHE A 430  1  O  PHE A 430   N  VAL A 330           
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 ALA A  38  GLU A  39  0                                        
SHEET    2 AA3 2 GLU A  51  PRO A  52 -1  O  GLU A  51   N  GLU A  39           
SHEET    1 AA4 2 VAL A  68  CYS A  69  0                                        
SHEET    2 AA4 2 LEU A  92  SER A  93  1  O  SER A  93   N  VAL A  68           
SHEET    1 AA5 3 LEU B   9  VAL B  12  0                                        
SHEET    2 AA5 3 GLY B  15  ARG B  18 -1  O  LEU B  17   N  VAL B  10           
SHEET    3 AA5 3 VAL B  59  ASP B  61  1  O  VAL B  60   N  ARG B  16           
SHEET    1 AA611 ILE B  20  LEU B  22  0                                        
SHEET    2 AA611 VAL B  29  PRO B  36 -1  O  VAL B  29   N  LEU B  22           
SHEET    3 AA611 TYR B  98  PRO B 104 -1  O  VAL B 101   N  PHE B  32           
SHEET    4 AA611 VAL B 145  MET B 149 -1  O  SER B 148   N  ASN B 100           
SHEET    5 AA611 THR B 112  ILE B 118  1  N  TRP B 117   O  VAL B 147           
SHEET    6 AA611 GLY B 192  GLU B 202  1  O  THR B 198   N  VAL B 114           
SHEET    7 AA611 ARG B 224  GLN B 228  1  O  VAL B 226   N  LEU B 199           
SHEET    8 AA611 GLN B 325  VAL B 331  1  O  LEU B 327   N  LEU B 227           
SHEET    9 AA611 ARG B 424  PHE B 430  1  O  TYR B 426   N  VAL B 328           
SHEET   10 AA611 GLN B 509  LEU B 513  1  O  VAL B 511   N  VAL B 429           
SHEET   11 AA611 GLU B 519  ARG B 522 -1  O  ARG B 521   N  TYR B 510           
SHEET    1 AA7 2 VAL B  68  CYS B  69  0                                        
SHEET    2 AA7 2 LEU B  92  SER B  93  1  O  SER B  93   N  VAL B  68           
SHEET    1 AA8 2 VAL B 239  GLY B 240  0                                        
SHEET    2 AA8 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  2.08  
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.08  
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.08  
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.07  
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.06  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.04  
LINK         C   GLU A 202                 N   TIS A 203     1555   1555  1.33  
LINK         C   TIS A 203                 N   ALA A 204     1555   1555  1.34  
LINK         ND2 ASN A 265                 C1  NAG D   1     1555   1555  1.43  
LINK         ND2 ASN A 350                 C1  NAG C   1     1555   1555  1.45  
LINK         C   GLU B 202                 N   TIS B 203     1555   1555  1.33  
LINK         C   TIS B 203                 N   ALA B 204     1555   1555  1.33  
LINK         ND2 ASN B 350                 C1  NAG F   1     1555   1555  1.45  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.46  
LINK         O6  NAG C   1                 C1  FUC C   3     1555   1555  1.45  
LINK         O4  NAG D   1                 C1  NAG D   2     1555   1555  1.44  
LINK         O3  GAL E   1                 C2  SIA E   2     1555   1555  1.47  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.49  
LINK         O6  NAG F   1                 C1  FUC F   3     1555   1555  1.46  
LINK         NE2 HIS A 284                ZN    ZN A 626     1555   1555  2.33  
LINK         ND1AHIS A 381                ZN    ZN A 625     1555   1555  2.31  
LINK         ND1BHIS A 381                ZN    ZN A 625     1555   1555  2.34  
LINK         NE2BHIS A 381                ZN    ZN A 625     1555   1555  2.31  
LINK         NE2BHIS A 381                ZN    ZN B 625     1555   1555  2.29  
LINK         OE2 GLU A 452                MG    MG A 632     1555   1555  2.99  
LINK         OD2 ASP A 488                MG    MG A 634     1555   1555  2.37  
LINK         O4  SO4 A 602                MG    MG A 630     1555   1555  3.00  
LINK        ZN    ZN A 625                 NE2AHIS B 381     1555   1555  2.32  
LINK        MG    MG A 629                 O3  SO4 B 603     1555   1555  2.92  
LINK        MG    MG A 629                 O4  SO4 B 603     1555   1555  2.86  
LINK        MG    MG A 631                 O   HOH A 782     1555   1555  2.76  
LINK        MG    MG A 632                 O   HOH A 754     1555   1555  2.66  
LINK        MG    MG A 634                 O   HOH B 728     1555   4765  2.59  
LINK         NE2 HIS B 322                ZN    ZN B 626     1555   1555  2.32  
LINK         ND1BHIS B 381                ZN    ZN B 625     1555   1555  2.33  
LINK         NE2AHIS B 381                ZN    ZN B 625     1555   1555  2.31  
LINK         OE2 GLU B 452                MG    MG B 632     1555   1555  2.59  
LINK        MG    MG B 632                 O   HOH B 740     1555   1555  2.65  
CRYST1  211.833  211.833  116.634  90.00  90.00 120.00 P 61         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      0.004721  0.002725  0.000000        0.00000                         
SCALE2      0.000000  0.005451  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008574        0.00000                         
TER    4162      THR A 543                                                      
TER    8335      THR B 543                                                      
MASTER      403    0   79   49   36    0    0    6 8795    2  305   84          
END                                                                             

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