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LongText Report for: 5dyt-pdb

Name Class
5dyt-pdb
HEADER    HYDROLASE                               25-SEP-15   5DYT              
TITLE     CRYSTAL STRUCTURE OF HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH N-   
TITLE    2 ((1-BENZYLPIPERIDIN-3-YL)METHYL)-N-METHYLNAPHTHALENE-2-SULFONAMIDE   
CAVEAT     5DYT    NAG A 606 HAS WRONG CHIRALITY AT ATOM C1 NAG A 607 HAS WRONG 
CAVEAT   2 5DYT    CHIRALITY AT ATOM C1 NAG A 608 HAS WRONG CHIRALITY AT ATOM   
CAVEAT   3 5DYT    C1 FUC A 609 HAS WRONG CHIRALITY AT ATOM C1 NAG A 610 HAS    
CAVEAT   4 5DYT    WRONG CHIRALITY AT ATOM C1 NAG A 614 HAS WRONG CHIRALITY AT  
CAVEAT   5 5DYT    ATOM C1 FUC A 615 HAS WRONG CHIRALITY AT ATOM C1 FUC B 610   
CAVEAT   6 5DYT    HAS WRONG CHIRALITY AT ATOM C1 NAG B 611 HAS WRONG           
CAVEAT   7 5DYT    CHIRALITY AT ATOM C1                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLINESTERASE;                                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RSIDUES 28-557;                                        
COMPND   5 SYNONYM: ACYLCHOLINE ACYLHYDROLASE,BUTYRYLCHOLINE ESTERASE,CHOLINE   
COMPND   6 ESTERASE II,PSEUDOCHOLINESTERASE;                                    
COMPND   7 EC: 3.1.1.8;                                                         
COMPND   8 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: BCHE, CHE1;                                                    
SOURCE   6 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FRUIT FLY;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7227                                        
KEYWDS    HUMAN BUTYRYLCHOLINESTERASE, AD, ALZHEIMER DISEASE, SULFONAMIDE,      
KEYWDS   2 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.COQUELLE,B.BRUS,J.P.COLLETIER                                       
REVDAT   1   05-OCT-16 5DYT    0                                                
JRNL        AUTH   U.KOSAK,B.BRUS,D.KNEZ,M.GOBEC,R.SINK,M.ZIVIN,K.SALAT,        
JRNL        AUTH 2 A.PODKOWA,B.FILIPEK,A.WIECKOWSKA,B.MALAWSKA,J.STOJAN,        
JRNL        AUTH 3 N.COQUELLE,J.P.COLLETIER,S.GOBEC                             
JRNL        TITL   DEVELOPMENT OF A NEW SULFONAMIDE INHIBITOR OF                
JRNL        TITL 2 BUTYRYLCHOLINESTERASE WITH IN VIVO ANTI-ALZHEIMER ACTIVITY   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10_2155: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.12                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 47137                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.232                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1414                            
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 46.1278 -  5.4912    0.99     4793   146  0.1739 0.2230        
REMARK   3     2  5.4912 -  4.3596    1.00     4657   150  0.1460 0.1856        
REMARK   3     3  4.3596 -  3.8088    1.00     4576   138  0.1449 0.1962        
REMARK   3     4  3.8088 -  3.4607    1.00     4571   140  0.1767 0.2328        
REMARK   3     5  3.4607 -  3.2127    0.99     4522   143  0.1959 0.2637        
REMARK   3     6  3.2127 -  3.0234    0.99     4539   145  0.2086 0.2575        
REMARK   3     7  3.0234 -  2.8720    1.00     4520   135  0.2249 0.2892        
REMARK   3     8  2.8720 -  2.7470    1.00     4519   135  0.2331 0.3402        
REMARK   3     9  2.7470 -  2.6412    1.00     4501   136  0.2367 0.3010        
REMARK   3    10  2.6412 -  2.5501    1.00     4525   146  0.2572 0.3065        
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)     : 0.340            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.820           
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      :  0.009           9100                                  
REMARK   3   ANGLE     :  1.000          12318                                  
REMARK   3   CHIRALITY :  0.056           1354                                  
REMARK   3   PLANARITY :  0.006           1540                                  
REMARK   3   DIHEDRAL  : 20.644           3333                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5DYT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-SEP-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000214050.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-JUL-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.93903                            
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 : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47153                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.400                              
REMARK 200  R MERGE                    (I) : 0.08070                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 12.4800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.73190                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
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: 1POM                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.55                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 12%              
REMARK 280  POLYETHYLENE GLYCOL 4000., PH 7.4, VAPOR DIFFUSION, HANGING DROP,   
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       38.23500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      115.64000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.11500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      115.64000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.23500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.11500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10820 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 40890 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 99.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     THR A     0                                                      
REMARK 465     GLU A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     THR B     0                                                      
REMARK 465     GLU B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     GLN B   484                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN A 380    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 453    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 506    CD   OE1  OE2                                       
REMARK 470     SER B  53    CB   OG                                             
REMARK 470     LYS B 248    CG   CD   CE   NZ                                   
REMARK 470     ASN B 485    CB   CG   OD1  ND2                                  
REMARK 470     ASN B 486    CG   OD1  ND2                                       
REMARK 470     GLU B 506    CG   CD   OE1  OE2                                  
REMARK 470     SER B 507    CB   OG                                             
REMARK 470     ARG B 509    NE   CZ   NH1  NH2                                  
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   UNK  UNX A   621     UNK  UNX A   623              1.26            
REMARK 500   UNK  UNX B   618     UNK  UNX B   620              1.36            
REMARK 500   UNK  UNX A   622     UNK  UNX A   623              1.54            
REMARK 500   O6   NAG B   604     C1   FUL B   606              1.55            
REMARK 500   ND2  ASN B    57     O5   NAG B   602              1.85            
REMARK 500   UNK  UNX B   619     UNK  UNX B   620              2.00            
REMARK 500   UNK  UNX A   621     UNK  UNX A   622              2.02            
REMARK 500   ND2  ASN A    57     O5   NAG A   602              2.03            
REMARK 500   ND2  ASN A    17     O5   NAG A   601              2.04            
REMARK 500   O    HOH B   778     O    HOH B   811              2.05            
REMARK 500   O    PHE B   217     NZ   LYS B   313              2.06            
REMARK 500   O4   NAG A   611     O5   NAG A   612              2.06            
REMARK 500   O6   NAG A   602     O5   FUC A   604              2.07            
REMARK 500   ND2  ASN A   241     O5   NAG A   607              2.11            
REMARK 500   ND2  ASN B   241     O5   NAG B   604              2.12            
REMARK 500   O    HOH A   772     O    HOH A   800              2.13            
REMARK 500   O4   NAG A   602     C2   NAG A   603              2.14            
REMARK 500   CG   ASN B   106     O5   NAG B   603              2.15            
REMARK 500   O    HOH B   804     O    HOH B   812              2.15            
REMARK 500   O6   NAG B   608     O    HOH B   701              2.16            
REMARK 500   O4   NAG A   613     O5   NAG A   614              2.16            
REMARK 500   O6   NAG B   604     C2   FUL B   606              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OH   TYR A   237     O    ARG B   453     1545     2.12            
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    THR A  50     -111.76    -89.77                                   
REMARK 500    ASP A  54     -170.81    -64.72                                   
REMARK 500    GLN A  67      142.97   -171.89                                   
REMARK 500    ASN A 106       47.81   -160.96                                   
REMARK 500    PHE A 118       12.45     56.90                                   
REMARK 500    ALA A 162       72.24   -159.19                                   
REMARK 500    SER A 198     -124.11     64.33                                   
REMARK 500    ASP A 297      -71.79   -135.24                                   
REMARK 500    ASP A 375       68.80    -68.58                                   
REMARK 500    GLN A 380      110.46   -170.16                                   
REMARK 500    ARG A 381       70.92     49.46                                   
REMARK 500    PHE A 398      -55.84   -124.30                                   
REMARK 500    ARG A 453        6.15    -67.80                                   
REMARK 500    GLU A 482      -73.78   -102.37                                   
REMARK 500    LYS B   9       -8.09    -59.90                                   
REMARK 500    PHE B  43       -1.95     79.92                                   
REMARK 500    ASP B  54     -162.86    -62.01                                   
REMARK 500    SER B  89      144.13   -177.09                                   
REMARK 500    ASN B 106       54.72   -158.28                                   
REMARK 500    PHE B 118       -1.00     62.34                                   
REMARK 500    PRO B 160       -7.06    -59.71                                   
REMARK 500    ALA B 162       74.03   -155.83                                   
REMARK 500    SER B 198     -120.22     65.18                                   
REMARK 500    THR B 218      -62.21   -108.32                                   
REMARK 500    TYR B 282       72.36   -119.81                                   
REMARK 500    PRO B 285       -8.84    -59.81                                   
REMARK 500    ASP B 297      -73.37   -142.45                                   
REMARK 500    ASP B 379       22.76    -75.72                                   
REMARK 500    PHE B 398      -66.18   -131.30                                   
REMARK 500    ASN B 455       33.66    -71.99                                   
REMARK 500    GLU B 506      -83.48    -61.01                                   
REMARK 500    PHE B 525      -52.38   -126.67                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ALA A  155     LEU A  156                  149.08                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     FUL B  606                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5HB A 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FUL B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 5HB B 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 601 bound   
REMARK 800  to ASN A 17                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  602 through FUC A 604 bound to ASN A 57                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  605 through NAG A 606 bound to ASN A 106                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  607 through FUC A 609 bound to ASN A 241                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 610 bound   
REMARK 800  to ASN A 341                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  611 through NAG A 612 bound to ASN A 481                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  613 through FUC A 615 bound to ASN A 486                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 601 bound   
REMARK 800  to ASN B 17                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 602 bound   
REMARK 800  to ASN B 57                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 603 bound   
REMARK 800  to ASN B 106                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  604 through NAG B 605 bound to ASN B 241                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 607 bound   
REMARK 800  to ASN B 256                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 608 bound   
REMARK 800  to ASN B 341                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  609 through FUC B 610 bound to ASN B 455                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 611 bound   
REMARK 800  to ASN B 481                                                        
DBREF  5DYT A    0   529  UNP    P06276   CHLE_HUMAN      28    557             
DBREF  5DYT B    0   529  UNP    P06276   CHLE_HUMAN      28    557             
SEQRES   1 A  530  THR GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS          
SEQRES   2 A  530  VAL ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL          
SEQRES   3 A  530  THR ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU          
SEQRES   4 A  530  GLY ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS          
SEQRES   5 A  530  TRP SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER          
SEQRES   6 A  530  CYS CSO GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS          
SEQRES   7 A  530  GLY SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU          
SEQRES   8 A  530  ASP CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS          
SEQRES   9 A  530  PRO LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY          
SEQRES  10 A  530  GLY PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP          
SEQRES  11 A  530  GLY LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL          
SEQRES  12 A  530  SER MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA          
SEQRES  13 A  530  LEU PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU          
SEQRES  14 A  530  PHE ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN          
SEQRES  15 A  530  ILE ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU          
SEQRES  16 A  530  PHE GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS          
SEQRES  17 A  530  LEU LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA          
SEQRES  18 A  530  ILE LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL          
SEQRES  19 A  530  THR SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU          
SEQRES  20 A  530  ALA LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU          
SEQRES  21 A  530  ILE ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE          
SEQRES  22 A  530  LEU LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO          
SEQRES  23 A  530  LEU SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE          
SEQRES  24 A  530  LEU THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN          
SEQRES  25 A  530  PHE LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP          
SEQRES  26 A  530  GLU GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE          
SEQRES  27 A  530  SER LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE          
SEQRES  28 A  530  GLN GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU          
SEQRES  29 A  530  PHE GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP          
SEQRES  30 A  530  VAL ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU          
SEQRES  31 A  530  GLY ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA          
SEQRES  32 A  530  LEU GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN          
SEQRES  33 A  530  ALA PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU          
SEQRES  34 A  530  PRO TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU          
SEQRES  35 A  530  ILE GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP          
SEQRES  36 A  530  ASN TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE          
SEQRES  37 A  530  VAL LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO          
SEQRES  38 A  530  ASN GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE          
SEQRES  39 A  530  LYS SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU          
SEQRES  40 A  530  SER THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS          
SEQRES  41 A  530  ARG PHE TRP THR SER PHE PHE PRO LYS VAL                      
SEQRES   1 B  530  THR GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS          
SEQRES   2 B  530  VAL ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL          
SEQRES   3 B  530  THR ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU          
SEQRES   4 B  530  GLY ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS          
SEQRES   5 B  530  TRP SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER          
SEQRES   6 B  530  CYS CSO GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS          
SEQRES   7 B  530  GLY SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU          
SEQRES   8 B  530  ASP CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS          
SEQRES   9 B  530  PRO LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY          
SEQRES  10 B  530  GLY PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP          
SEQRES  11 B  530  GLY LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL          
SEQRES  12 B  530  SER MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA          
SEQRES  13 B  530  LEU PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU          
SEQRES  14 B  530  PHE ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN          
SEQRES  15 B  530  ILE ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU          
SEQRES  16 B  530  PHE GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS          
SEQRES  17 B  530  LEU LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA          
SEQRES  18 B  530  ILE LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL          
SEQRES  19 B  530  THR SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU          
SEQRES  20 B  530  ALA LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU          
SEQRES  21 B  530  ILE ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE          
SEQRES  22 B  530  LEU LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO          
SEQRES  23 B  530  LEU SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE          
SEQRES  24 B  530  LEU THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN          
SEQRES  25 B  530  PHE LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP          
SEQRES  26 B  530  GLU GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE          
SEQRES  27 B  530  SER LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE          
SEQRES  28 B  530  GLN GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU          
SEQRES  29 B  530  PHE GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP          
SEQRES  30 B  530  VAL ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU          
SEQRES  31 B  530  GLY ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA          
SEQRES  32 B  530  LEU GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN          
SEQRES  33 B  530  ALA PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU          
SEQRES  34 B  530  PRO TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU          
SEQRES  35 B  530  ILE GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP          
SEQRES  36 B  530  ASN TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE          
SEQRES  37 B  530  VAL LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO          
SEQRES  38 B  530  ASN GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE          
SEQRES  39 B  530  LYS SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU          
SEQRES  40 B  530  SER THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS          
SEQRES  41 B  530  ARG PHE TRP THR SER PHE PHE PRO LYS VAL                      
MODRES 5DYT CSO A   66  CYS  MODIFIED RESIDUE                                   
MODRES 5DYT CSO B   66  CYS  MODIFIED RESIDUE                                   
HET    CSO  A  66       7                                                       
HET    CSO  B  66       7                                                       
HET    NAG  A 601      14                                                       
HET    NAG  A 602      14                                                       
HET    NAG  A 603      14                                                       
HET    FUC  A 604      10                                                       
HET    NAG  A 605      14                                                       
HET    NAG  A 606      14                                                       
HET    NAG  A 607      14                                                       
HET    NAG  A 608      14                                                       
HET    FUC  A 609      10                                                       
HET    NAG  A 610      14                                                       
HET    NAG  A 611      14                                                       
HET    NAG  A 612      14                                                       
HET    NAG  A 613      14                                                       
HET    NAG  A 614      14                                                       
HET    FUC  A 615      10                                                       
HET    5HB  A 616      29                                                       
HET    GOL  A 617       6                                                       
HET    GOL  A 618       6                                                       
HET    GOL  A 619       6                                                       
HET    EDO  A 620       4                                                       
HET    UNX  A 621       1                                                       
HET    UNX  A 622       1                                                       
HET    UNX  A 623       1                                                       
HET    NAG  B 601      14                                                       
HET    NAG  B 602      14                                                       
HET    NAG  B 603      14                                                       
HET    NAG  B 604      14                                                       
HET    NAG  B 605      14                                                       
HET    FUL  B 606      10                                                       
HET    NAG  B 607      14                                                       
HET    NAG  B 608      14                                                       
HET    NAG  B 609      14                                                       
HET    FUC  B 610      10                                                       
HET    NAG  B 611      14                                                       
HET    5HB  B 612      29                                                       
HET    GOL  B 613       6                                                       
HET    GOL  B 614       6                                                       
HET    EDO  B 615       4                                                       
HET    EDO  B 616       4                                                       
HET    EDO  B 617       4                                                       
HET    UNX  B 618       1                                                       
HET    UNX  B 619       1                                                       
HET    UNX  B 620       1                                                       
HET    PEG  B 621       7                                                       
HETNAM     CSO S-HYDROXYCYSTEINE                                                
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     5HB N-{[(3R)-1-BENZYLPIPERIDIN-3-YL]METHYL}-N-                       
HETNAM   2 5HB  METHYLNAPHTHALENE-2-SULFONAMIDE                                 
HETNAM     GOL GLYCEROL                                                         
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     UNX UNKNOWN ATOM OR ION                                              
HETNAM     FUL BETA-L-FUCOSE                                                    
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     FUL 6-DEOXY-BETA-L-GALACTOSE                                         
FORMUL   1  CSO    2(C3 H7 N O3 S)                                              
FORMUL   3  NAG    21(C8 H15 N O6)                                              
FORMUL   4  FUC    4(C6 H12 O5)                                                 
FORMUL  10  5HB    2(C24 H28 N2 O2 S)                                           
FORMUL  11  GOL    5(C3 H8 O3)                                                  
FORMUL  14  EDO    4(C2 H6 O2)                                                  
FORMUL  15  UNX    6(X)                                                         
FORMUL  22  FUL    C6 H12 O5                                                    
FORMUL  36  PEG    C4 H10 O3                                                    
FORMUL  37  HOH   *232(H2 O)                                                    
HELIX    1 AA1 LEU A   38  ARG A   42  5                                   5    
HELIX    2 AA2 PHE A   76  MET A   81  1                                   6    
HELIX    3 AA3 LEU A  125  ASP A  129  5                                   5    
HELIX    4 AA4 GLY A  130  ARG A  138  1                                   9    
HELIX    5 AA5 VAL A  148  LEU A  154  1                                   7    
HELIX    6 AA6 ASN A  165  ILE A  182  1                                  18    
HELIX    7 AA7 ALA A  183  PHE A  185  5                                   3    
HELIX    8 AA8 SER A  198  SER A  210  1                                  13    
HELIX    9 AA9 PRO A  211  PHE A  217  5                                   7    
HELIX   10 AB1 SER A  235  THR A  250  1                                  16    
HELIX   11 AB2 ASN A  256  LYS A  267  1                                  12    
HELIX   12 AB3 ASP A  268  LEU A  274  1                                   7    
HELIX   13 AB4 ASN A  275  VAL A  280  5                                   6    
HELIX   14 AB5 MET A  302  LEU A  309  1                                   8    
HELIX   15 AB6 GLY A  326  VAL A  331  1                                   6    
HELIX   16 AB7 THR A  346  PHE A  358  1                                  13    
HELIX   17 AB8 SER A  362  TYR A  373  1                                  12    
HELIX   18 AB9 GLU A  383  PHE A  398  1                                  16    
HELIX   19 AC1 PHE A  398  GLU A  411  1                                  14    
HELIX   20 AC2 PRO A  431  GLY A  435  5                                   5    
HELIX   21 AC3 GLU A  441  PHE A  446  1                                   6    
HELIX   22 AC4 GLY A  447  ASN A  455  5                                   9    
HELIX   23 AC5 THR A  457  GLY A  478  1                                  22    
HELIX   24 AC6 ARG A  515  PHE A  525  1                                  11    
HELIX   25 AC7 PHE A  526  VAL A  529  5                                   4    
HELIX   26 AC8 LEU B   38  ARG B   42  5                                   5    
HELIX   27 AC9 PHE B   76  MET B   81  1                                   6    
HELIX   28 AD1 LEU B  125  ASP B  129  5                                   5    
HELIX   29 AD2 GLY B  130  ARG B  138  1                                   9    
HELIX   30 AD3 GLY B  149  LEU B  154  1                                   6    
HELIX   31 AD4 ASN B  165  ILE B  182  1                                  18    
HELIX   32 AD5 ALA B  183  PHE B  185  5                                   3    
HELIX   33 AD6 SER B  198  SER B  210  1                                  13    
HELIX   34 AD7 PRO B  211  PHE B  217  5                                   7    
HELIX   35 AD8 SER B  235  THR B  250  1                                  16    
HELIX   36 AD9 ASN B  256  ARG B  265  1                                  10    
HELIX   37 AE1 ASP B  268  LEU B  274  1                                   7    
HELIX   38 AE2 ASN B  275  VAL B  279  5                                   5    
HELIX   39 AE3 MET B  302  LEU B  309  1                                   8    
HELIX   40 AE4 GLY B  326  VAL B  331  1                                   6    
HELIX   41 AE5 THR B  346  PHE B  358  1                                  13    
HELIX   42 AE6 SER B  362  TYR B  373  1                                  12    
HELIX   43 AE7 GLU B  383  PHE B  398  1                                  16    
HELIX   44 AE8 PHE B  398  GLU B  411  1                                  14    
HELIX   45 AE9 PRO B  431  GLY B  435  5                                   5    
HELIX   46 AF1 GLU B  441  PHE B  446  1                                   6    
HELIX   47 AF2 GLY B  447  GLU B  451  5                                   5    
HELIX   48 AF3 THR B  457  GLY B  478  1                                  22    
HELIX   49 AF4 ARG B  515  PHE B  525  1                                  11    
HELIX   50 AF5 PHE B  526  VAL B  529  5                                   4    
SHEET    1 AA1 3 ILE A   5  THR A   8  0                                        
SHEET    2 AA1 3 GLY A  11  ARG A  14 -1  O  VAL A  13   N  ILE A   6           
SHEET    3 AA1 3 ILE A  55  ASN A  57  1  O  TRP A  56   N  ARG A  14           
SHEET    1 AA211 MET A  16  VAL A  20  0                                        
SHEET    2 AA211 GLY A  23  PRO A  32 -1  O  ALA A  27   N  MET A  16           
SHEET    3 AA211 TYR A  94  PRO A 100 -1  O  LEU A  95   N  ILE A  31           
SHEET    4 AA211 ILE A 140  MET A 144 -1  O  SER A 143   N  ASN A  96           
SHEET    5 AA211 ALA A 107  ILE A 113  1  N  LEU A 110   O  ILE A 140           
SHEET    6 AA211 GLY A 187  GLU A 197  1  O  ASN A 188   N  ALA A 107           
SHEET    7 AA211 ARG A 219  GLN A 223  1  O  ARG A 219   N  LEU A 194           
SHEET    8 AA211 ILE A 317  ASN A 322  1  O  LEU A 318   N  LEU A 222           
SHEET    9 AA211 ALA A 416  PHE A 421  1  O  PHE A 417   N  VAL A 319           
SHEET   10 AA211 LYS A 499  LEU A 503  1  O  LEU A 503   N  TYR A 420           
SHEET   11 AA211 ILE A 510  THR A 512 -1  O  MET A 511   N  TYR A 500           
SHEET    1 AA3 3 ILE B   5  THR B   8  0                                        
SHEET    2 AA3 3 GLY B  11  ARG B  14 -1  O  GLY B  11   N  THR B   8           
SHEET    3 AA3 3 ILE B  55  ASN B  57  1  O  TRP B  56   N  ARG B  14           
SHEET    1 AA411 MET B  16  VAL B  20  0                                        
SHEET    2 AA411 GLY B  23  PRO B  32 -1  O  VAL B  25   N  LEU B  18           
SHEET    3 AA411 TYR B  94  PRO B 100 -1  O  VAL B  97   N  PHE B  28           
SHEET    4 AA411 ILE B 140  MET B 144 -1  O  SER B 143   N  ASN B  96           
SHEET    5 AA411 ALA B 107  ILE B 113  1  N  TRP B 112   O  VAL B 142           
SHEET    6 AA411 GLY B 187  GLU B 197  1  O  PHE B 195   N  ILE B 111           
SHEET    7 AA411 ARG B 219  GLN B 223  1  O  ILE B 221   N  LEU B 194           
SHEET    8 AA411 ILE B 317  ASN B 322  1  O  LEU B 318   N  LEU B 222           
SHEET    9 AA411 ALA B 416  PHE B 421  1  O  PHE B 417   N  VAL B 319           
SHEET   10 AA411 LYS B 499  LEU B 503  1  O  LEU B 501   N  PHE B 418           
SHEET   11 AA411 ILE B 510  THR B 512 -1  O  MET B 511   N  TYR B 500           
SSBOND   1 CYS A   65    CYS A   92                          1555   1555  2.05  
SSBOND   2 CYS A  252    CYS A  263                          1555   1555  2.05  
SSBOND   3 CYS A  400    CYS A  519                          1555   1555  2.05  
SSBOND   4 CYS B   65    CYS B   92                          1555   1555  2.05  
SSBOND   5 CYS B  252    CYS B  263                          1555   1555  2.05  
SSBOND   6 CYS B  400    CYS B  519                          1555   1555  2.05  
LINK         ND2 ASN A  17                 C1  NAG A 601     1555   1555  1.52  
LINK         ND2 ASN A  57                 C1  NAG A 602     1555   1555  1.45  
LINK         C   CYS A  65                 N   CSO A  66     1555   1555  1.33  
LINK         C   CSO A  66                 N   GLN A  67     1555   1555  1.32  
LINK         ND2 ASN A 106                 C1  NAG A 605     1555   1555  1.40  
LINK         ND2 ASN A 241                 C1  NAG A 607     1555   1555  1.48  
LINK         ND2 ASN A 341                 C1  NAG A 610     1555   1555  1.50  
LINK         ND2 ASN A 481                 C1  NAG A 611     1555   1555  1.45  
LINK         ND2 ASN A 486                 C1  NAG A 613     1555   1555  1.45  
LINK         ND2 ASN B  17                 C1  NAG B 601     1555   1555  1.47  
LINK         ND2 ASN B  57                 C1  NAG B 602     1555   1555  1.47  
LINK         C   CYS B  65                 N   CSO B  66     1555   1555  1.33  
LINK         C   CSO B  66                 N   GLN B  67     1555   1555  1.33  
LINK         ND2 ASN B 106                 C1  NAG B 603     1555   1555  1.52  
LINK         ND2 ASN B 106                 O5  NAG B 603     1555   1555  1.31  
LINK         ND2 ASN B 241                 C1  NAG B 604     1555   1555  1.49  
LINK         ND2 ASN B 256                 C1  NAG B 607     1555   1555  1.45  
LINK         ND2 ASN B 341                 C1  NAG B 608     1555   1555  1.51  
LINK         ND2 ASN B 455                 C1  NAG B 609     1555   1555  1.46  
LINK         ND2 ASN B 481                 C1  NAG B 611     1555   1555  1.48  
LINK         O4  NAG A 602                 C1  NAG A 603     1555   1555  1.46  
LINK         O6  NAG A 602                 C1  FUC A 604     1555   1555  1.39  
LINK         O4  NAG A 605                 C1  NAG A 606     1555   1555  1.54  
LINK         O4  NAG A 607                 C1  NAG A 608     1555   1555  1.46  
LINK         O6  NAG A 607                 C1  FUC A 609     1555   1555  1.50  
LINK         O4  NAG A 611                 C1  NAG A 612     1555   1555  1.50  
LINK         O4  NAG A 613                 C1  NAG A 614     1555   1555  1.41  
LINK         O6  NAG A 613                 C1  FUC A 615     1555   1555  1.46  
LINK         O4  NAG B 604                 C1  NAG B 605     1555   1555  1.49  
LINK         O6  NAG B 609                 C1  FUC B 610     1555   1555  1.48  
CISPEP   1 ALA A  101    PRO A  102          0         1.90                     
CISPEP   2 GLN A  380    ARG A  381          0        -0.04                     
CISPEP   3 ALA B  101    PRO B  102          0         2.03                     
SITE     1 AC1  9 GLY A 116  GLY A 117  GLN A 119  THR A 120                    
SITE     2 AC1  9 SER A 198  SER A 287  TRP A 430  HIS A 438                    
SITE     3 AC1  9 HOH A 703                                                     
SITE     1 AC2  4 LEU A  18  TRP A  98  ASP A 129  LYS A 131                    
SITE     1 AC3  6 ASN A 228  TYR A 396  PRO A 401  TRP A 522                    
SITE     2 AC3  6 THR A 523  HOH A 760                                          
SITE     1 AC4  5 TYR A  33  SER A  48  LEU A  49  LEU A 173                    
SITE     2 AC4  5 TRP A 177                                                     
SITE     1 AC5  2 HIS A  77  GLU A 443                                          
SITE     1 AC6  3 PHE B 278  NAG B 604  NAG B 605                               
SITE     1 AC7 15 GLY B 116  GLY B 117  GLN B 119  THR B 120                    
SITE     2 AC7 15 SER B 198  TRP B 231  LEU B 286  SER B 287                    
SITE     3 AC7 15 PHE B 329  TRP B 430  MET B 437  HIS B 438                    
SITE     4 AC7 15 TYR B 440  HOH B 711  HOH B 812                               
SITE     1 AC8  5 LEU B  18  TYR B  61  TRP B  98  ASP B 129                    
SITE     2 AC8  5 LYS B 131                                                     
SITE     1 AC9  6 TRP B 231  LEU B 286  SER B 287  VAL B 288                    
SITE     2 AC9  6 ASN B 397  EDO B 616                                          
SITE     1 AD1  3 ARG B  42  LYS B 267  PRO B 269                               
SITE     1 AD2  7 PRO B 230  TRP B 231  VAL B 233  THR B 234                    
SITE     2 AD2  7 GLU B 238  VAL B 288  GOL B 614                               
SITE     1 AD3  1 ASN B 455                                                     
SITE     1 AD4  7 HIS B  77  MET B  81  SER B 425  LYS B 427                    
SITE     2 AD4  7 LEU B 428  PRO B 429  GLU B 443                               
SITE     1 AD5  1 ASN A  17                                                     
SITE     1 AD6  2 ILE A  55  ASN A  57                                          
SITE     1 AD7  3 ASN A 106  ASN A 188  LYS A 190                               
SITE     1 AD8  7 ASN A 241  ASN A 245  LYS A 248  PHE A 278                    
SITE     2 AD8  7 PRO A 281  NAG B 609  FUC B 610                               
SITE     1 AD9  5 SER A 338  ASN A 341  HOH A 713  HOH A 793                    
SITE     2 AD9  5 HOH A 798                                                     
SITE     1 AE1 10 TYR A 477  ASN A 479  ASN A 481  GLU A 482                    
SITE     2 AE1 10 THR A 483  GLN A 484  CSO B  66  ASP B  87                    
SITE     3 AE1 10 LEU B  88  GLN B 270                                          
SITE     1 AE2  4 ASN A 486  SER A 487  THR A 488  THR A 508                    
SITE     1 AE3  2 ILE B   4  ASN B  17                                          
SITE     1 AE4  1 ASN B  57                                                     
SITE     1 AE5  3 ASN B 106  ASN B 188  HOH B 703                               
SITE     1 AE6  6 TYR B 237  ASN B 241  ASN B 245  TYR B 282                    
SITE     2 AE6  6 FUL B 606  HOH B 785                                          
SITE     1 AE7  2 ASN B 256  GLU B 411                                          
SITE     1 AE8  5 SER B 338  ASN B 341  HOH B 701  HOH B 716                    
SITE     2 AE8  5 HOH B 744                                                     
SITE     1 AE9  6 TYR A 237  ARG A 240  NAG A 607  LYS B 427                    
SITE     2 AE9  6 ASP B 454  ASN B 455                                          
SITE     1 AF1  4 TYR B 477  ASN B 481  GLU B 482  HOH B 756                    
CRYST1   76.470   80.230  231.280  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013077  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012464  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004324        0.00000                         
TER    4211      VAL A 529                                                      
TER    8372      VAL B 529                                                      
MASTER      479    0   46   50   28    0   46    6 9040    2  500   82          
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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