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LongText Report for: 5k5e-pdb

Name Class
5k5e-pdb
HEADER    HYDROLASE                               23-MAY-16   5K5E              
TITLE     DISCOVERY AND STRUCTURE-ACTIVITY RELATIONSHIPS OF A HIGHLY SELECTIVE  
TITLE    2 BUTYRYLCHOLINESTERASE INHIBITOR BY STRUCTURE-BASED VIRTUAL SCREENING 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLINESTERASE;                                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ACYLCHOLINE ACYLHYDROLASE,BUTYRYLCHOLINE ESTERASE,CHOLINE   
COMPND   5 ESTERASE II,PSEUDOCHOLINESTERASE;                                    
COMPND   6 EC: 3.1.1.8;                                                         
COMPND   7 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: INSECT CELL EXPRESSION VECTOR PTIE1;              
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 266783                                      
KEYWDS    HIGH SELECTIVE INHIBITOR, BUTYRYLCHOLINESTERASE, HYDROLASE            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.DE LA MORA,S.N.DIGHE,G.S.DEORA,B.P.ROSS,F.NACHON,X.BRAZZOLOTTO      
REVDAT   1   27-JUL-16 5K5E    0                                                
SPRSDE     27-JUL-16 5K5E      4AQD                                             
JRNL        AUTH   S.N.DIGHE,G.S.DEORA,E.DE LA MORA,F.NACHON,S.CHAN,M.O.PARAT,  
JRNL        AUTH 2 X.BRAZZOLOTTO,B.P.ROSS                                       
JRNL        TITL   DISCOVERY AND STRUCTURE-ACTIVITY RELATIONSHIPS OF A HIGHLY   
JRNL        TITL 2 SELECTIVE BUTYRYLCHOLINESTERASE INHIBITOR BY STRUCTURE-BASED 
JRNL        TITL 3 VIRTUAL SCREENING.                                           
JRNL        REF    J.MED.CHEM.                                2016              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   27405689                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.6B00356                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.98                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 35270                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.175                           
REMARK   3   R VALUE            (WORKING SET) : 0.173                           
REMARK   3   FREE R VALUE                     : 0.202                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.930                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3257                            
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 19.9847 -  7.8084    0.98     2701   142  0.1519 0.1737        
REMARK   3     2  7.8084 -  6.2604    0.99     2725   141  0.1704 0.1896        
REMARK   3     3  6.2604 -  5.4878    0.99     2729   138  0.1677 0.1847        
REMARK   3     4  5.4878 -  4.9946    1.00     2727   151  0.1598 0.1468        
REMARK   3     5  4.9946 -  4.6414    0.99     2745   134  0.1332 0.1614        
REMARK   3     6  4.6414 -  4.3708    0.99     2768   132  0.1239 0.1690        
REMARK   3     7  4.3708 -  4.1540    0.98     2702   135  0.1375 0.1688        
REMARK   3     8  4.1540 -  3.9746    0.99     2711   151  0.1461 0.1633        
REMARK   3     9  3.9746 -  3.8227    0.99     2701   148  0.1548 0.1840        
REMARK   3    10  3.8227 -  3.6916    1.00     2778   135  0.1637 0.2084        
REMARK   3    11  3.6916 -  3.5769    0.99     2738   137  0.1734 0.2100        
REMARK   3    12  3.5769 -  3.4752    0.99     2729   145  0.1787 0.2255        
REMARK   3    13  3.4752 -  3.3841    0.99     2757   141  0.2062 0.2482        
REMARK   3    14  3.3841 -  3.3019    0.99     2673   140  0.2018 0.2418        
REMARK   3    15  3.3019 -  3.2272    0.99     2724   126  0.2100 0.2640        
REMARK   3    16  3.2272 -  3.1588    0.99     2684   170  0.2257 0.2275        
REMARK   3    17  3.1588 -  3.0958    0.99     2797   138  0.2364 0.2659        
REMARK   3    18  3.0958 -  3.0376    1.00     2712   147  0.2408 0.2339        
REMARK   3    19  3.0376 -  2.9835    1.00     2771   120  0.2459 0.3191        
REMARK   3    20  2.9835 -  2.9331    0.99     2732   147  0.2525 0.3132        
REMARK   3    21  2.9331 -  2.8860    1.00     2780   138  0.2821 0.3205        
REMARK   3    22  2.8860 -  2.8417    0.99     2684   151  0.2888 0.3258        
REMARK   3    23  2.8417 -  2.8000    0.99     2741   150  0.3224 0.3588        
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)     : 0.350            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.880           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 65.70                          
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      :  0.016           9003                                  
REMARK   3   ANGLE     :  1.876          12260                                  
REMARK   3   CHIRALITY :  0.104           1330                                  
REMARK   3   PLANARITY :  0.014           1562                                  
REMARK   3   DIHEDRAL  : 20.621           3289                                  
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):  -5.1721   6.3931  16.6274              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4027 T22:   0.4355                                     
REMARK   3      T33:   0.3209 T12:   0.0592                                     
REMARK   3      T13:  -0.0202 T23:  -0.0205                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7075 L22:   2.3814                                     
REMARK   3      L33:   3.2033 L12:  -0.2432                                     
REMARK   3      L13:   0.6497 L23:  -0.7368                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1721 S12:   0.4288 S13:  -0.1253                       
REMARK   3      S21:  -0.1047 S22:  -0.1587 S23:  -0.1294                       
REMARK   3      S31:   0.1159 S32:   0.2632 S33:  -0.0135                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'B'                                              
REMARK   3    ORIGIN FOR THE GROUP (A): -25.8698 -30.3107  44.4069              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4425 T22:   0.4127                                     
REMARK   3      T33:   0.3572 T12:  -0.0314                                     
REMARK   3      T13:  -0.0200 T23:  -0.0150                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2674 L22:   3.6097                                     
REMARK   3      L33:   3.8495 L12:  -0.4294                                     
REMARK   3      L13:   0.8248 L23:   0.2288                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1000 S12:   0.0719 S13:  -0.2138                       
REMARK   3      S21:   0.1058 S22:   0.0927 S23:   0.0612                       
REMARK   3      S31:   0.4064 S32:  -0.1270 S33:  -0.1782                       
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 5K5E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-MAY-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000221789.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 31-OCT-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35273                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.100                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 4.600                              
REMARK 200  R MERGE                    (I) : 9.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 12.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.87                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.68000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.100                              
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: 4AQD                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.19                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M AMMONIUM ACETATE PH 7.4, 13%        
REMARK 280  POLYETHYLENGLYCOL 3350, VAPOR DIFFUSION, 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       37.90500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      115.31500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.03500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      115.31500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.90500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.03500            
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: 6770 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 40640 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 59.0 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     GLU A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     GLU B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     ASP B     3                                                      
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   OE1  GLU B   161     NH2  ARG B   265              1.59            
REMARK 500   CD   LYS A   348     NE2  GLN A   351              1.61            
REMARK 500   CG   LYS A   348     NE2  GLN A   351              1.68            
REMARK 500   CE   LYS B    12     O    ASP B    54              1.71            
REMARK 500   O    VAL B    20     CZ   ARG B   135              1.77            
REMARK 500   CD   LYS A   348     CD   GLN A   351              1.79            
REMARK 500   OE1  GLN B   223     CZ3  TRP B   471              1.80            
REMARK 500   CG   LYS B    12     CD1  ILE B    55              1.83            
REMARK 500   OE2  GLU B   137     CG   LYS B   469              1.85            
REMARK 500   OD1  ASN B    57     C1   NAG B   602              1.87            
REMARK 500   CG2  THR B   483     N2   NAG B   608              1.88            
REMARK 500   OD1  ASN A    57     C1   NAG A   602              1.88            
REMARK 500   CB   PHE B    21     NH1  ARG B   135              1.92            
REMARK 500   N    GLY B    23     NH2  ARG B   135              1.92            
REMARK 500   CE   LYS B    12     CD1  ILE B    55              1.94            
REMARK 500   OG1  THR A     8     O    GLY A    11              1.95            
REMARK 500   CD   LYS A   348     OE1  GLN A   351              1.96            
REMARK 500   NZ   LYS B    12     O    ASP B    54              1.96            
REMARK 500   OE1  GLU B   422     OG1  THR B   502              1.97            
REMARK 500   O    VAL B    20     NE   ARG B   135              1.98            
REMARK 500   CD   LYS B    12     O    ASP B    54              1.99            
REMARK 500   OD2  ASP A   268     OE1  GLN A   270              2.03            
REMARK 500   NZ   LYS B    44     OE2  GLU B   161              2.03            
REMARK 500   OE1  GLU A   137     NZ   LYS A   469              2.03            
REMARK 500   ND2  ASN A    57     C1   NAG A   602              2.04            
REMARK 500   O    LEU B   463     OG   SER B   466              2.06            
REMARK 500   OG   SER B   198     O    HOH B   701              2.07            
REMARK 500   O    THR B   250     NZ   LYS B   267              2.09            
REMARK 500   CB   THR A   258     NZ   LYS A   262              2.10            
REMARK 500   OG   SER A   198     O    HOH A   701              2.11            
REMARK 500   ND2  ASN A   106     O5   NAG A   603              2.12            
REMARK 500   NH1  ARG B   240     OE2  GLU B   257              2.15            
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     ND2  ASN B   455     1565     1.11            
REMARK 500   OH   TYR A   237     CG   ASN B   455     1565     2.02            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU B 497   CD    GLU B 497   OE1    -0.070                       
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    LYS A 348   C   -  N   -  CA  ANGL. DEV. = -30.0 DEGREES          
REMARK 500    LYS A 348   O   -  C   -  N   ANGL. DEV. = -22.9 DEGREES          
REMARK 500    SER A 466   O   -  C   -  N   ANGL. DEV. = -11.3 DEGREES          
REMARK 500    ASN A 485   C   -  N   -  CA  ANGL. DEV. = -28.8 DEGREES          
REMARK 500    ASN A 485   O   -  C   -  N   ANGL. DEV. = -30.3 DEGREES          
REMARK 500    ASN B  10   C   -  N   -  CA  ANGL. DEV. = -19.8 DEGREES          
REMARK 500    ASN B  10   CA  -  C   -  N   ANGL. DEV. = -23.7 DEGREES          
REMARK 500    SER B  53   C   -  N   -  CA  ANGL. DEV. = -26.6 DEGREES          
REMARK 500    SER B  53   CA  -  C   -  N   ANGL. DEV. = -31.2 DEGREES          
REMARK 500    GLU B 161   C   -  N   -  CA  ANGL. DEV. = -27.9 DEGREES          
REMARK 500    ARG B 240   C   -  N   -  CA  ANGL. DEV. = -17.5 DEGREES          
REMARK 500    GLU B 255   O   -  C   -  N   ANGL. DEV. = -11.8 DEGREES          
REMARK 500    LYS B 348   O   -  C   -  N   ANGL. DEV. = -11.7 DEGREES          
REMARK 500    THR B 483   C   -  N   -  CA  ANGL. DEV. = -26.4 DEGREES          
REMARK 500    THR B 483   O   -  C   -  N   ANGL. DEV. = -24.1 DEGREES          
REMARK 500    ASN B 485   C   -  N   -  CA  ANGL. DEV. = -27.6 DEGREES          
REMARK 500    ASN B 485   O   -  C   -  N   ANGL. DEV. = -20.0 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    THR A  50      -83.89   -104.39                                   
REMARK 500    ASP A  70      109.32    -49.31                                   
REMARK 500    PHE A 118       12.73     56.54                                   
REMARK 500    PHE A 153       15.12   -140.26                                   
REMARK 500    SER A 198     -129.28     57.01                                   
REMARK 500    SER A 226      148.16   -171.05                                   
REMARK 500    TYR A 282     -127.41     56.71                                   
REMARK 500    PRO A 285       -9.77    -59.21                                   
REMARK 500    ASP A 297      -70.36   -124.00                                   
REMARK 500    LYS A 339      -17.21    -48.77                                   
REMARK 500    PHE A 398      -54.85   -130.30                                   
REMARK 500    GLU A 482      -66.07    -91.25                                   
REMARK 500    SER A 507      125.76   -171.19                                   
REMARK 500    LYS B  12      116.61   -163.58                                   
REMARK 500    PHE B  43       -3.60     86.67                                   
REMARK 500    ASP B  54     -160.02   -162.13                                   
REMARK 500    CYS B  92       -1.88   -142.81                                   
REMARK 500    PHE B 118       10.44     51.81                                   
REMARK 500    SER B 198     -123.91     59.43                                   
REMARK 500    ASN B 266       36.21    -98.50                                   
REMARK 500    TYR B 282       76.57   -115.09                                   
REMARK 500    ASP B 297      -77.68   -119.82                                   
REMARK 500    ASP B 301     -169.76   -124.49                                   
REMARK 500    ASP B 324       56.26   -118.70                                   
REMARK 500    ARG B 381      118.46    -34.51                                   
REMARK 500    GLU B 383       26.91    -75.14                                   
REMARK 500    PHE B 398      -57.26   -130.25                                   
REMARK 500    GLU B 411       27.03    -79.98                                   
REMARK 500    ASN B 455        6.25     90.20                                   
REMARK 500    PRO B 480       38.11    -81.02                                   
REMARK 500    PHE B 525      -57.02   -125.58                                   
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 LYS A  348     GLU A  349                  124.57                    
REMARK 500 LYS B    9     ASN B   10                  141.67                    
REMARK 500 ASN B  485     ASN B  486                  139.49                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    TYR A 237         14.92                                           
REMARK 500    LYS A 348        -32.19                                           
REMARK 500    SER A 466        -11.53                                           
REMARK 500    ASN A 485        -34.73                                           
REMARK 500    ASN B  10        -20.53                                           
REMARK 500    SER B  53        -20.51                                           
REMARK 500    ARG B 240        -13.20                                           
REMARK 500    GLU B 255        -14.28                                           
REMARK 500    LYS B 348        -12.12                                           
REMARK 500    THR B 483        -31.36                                           
REMARK 500    ASN B 485        -29.17                                           
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     NAG A  602                                                       
REMARK 610     NAG B  602                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6QS A 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6QS B 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
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: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  603 through NAG A 604 bound to ASN A 106                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 605 bound   
REMARK 800  to ASN A 241                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 606 bound   
REMARK 800  to ASN A 341                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  607 through NAG A 608 bound to ASN A 481                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
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: AD7                                                 
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: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 604 bound   
REMARK 800  to ASN B 241                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 605 bound   
REMARK 800  to ASN B 256                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  606 through NAG B 607 bound to ASN B 341                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 608 bound   
REMARK 800  to ASN B 481                                                        
DBREF  5K5E A    1   529  UNP    P06276   CHLE_HUMAN      29    557             
DBREF  5K5E B    1   529  UNP    P06276   CHLE_HUMAN      29    557             
SEQRES   1 A  529  GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL          
SEQRES   2 A  529  ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL THR          
SEQRES   3 A  529  ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY          
SEQRES   4 A  529  ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP          
SEQRES   5 A  529  SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS          
SEQRES   6 A  529  CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY          
SEQRES   7 A  529  SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP          
SEQRES   8 A  529  CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO          
SEQRES   9 A  529  LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY          
SEQRES  10 A  529  PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY          
SEQRES  11 A  529  LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER          
SEQRES  12 A  529  MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU          
SEQRES  13 A  529  PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE          
SEQRES  14 A  529  ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE          
SEQRES  15 A  529  ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE          
SEQRES  16 A  529  GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU          
SEQRES  17 A  529  LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE          
SEQRES  18 A  529  LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR          
SEQRES  19 A  529  SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA          
SEQRES  20 A  529  LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE          
SEQRES  21 A  529  ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU          
SEQRES  22 A  529  LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU          
SEQRES  23 A  529  SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU          
SEQRES  24 A  529  THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE          
SEQRES  25 A  529  LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU          
SEQRES  26 A  529  GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER          
SEQRES  27 A  529  LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN          
SEQRES  28 A  529  GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE          
SEQRES  29 A  529  GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL          
SEQRES  30 A  529  ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY          
SEQRES  31 A  529  ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU          
SEQRES  32 A  529  GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA          
SEQRES  33 A  529  PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO          
SEQRES  34 A  529  TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE          
SEQRES  35 A  529  GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN          
SEQRES  36 A  529  TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL          
SEQRES  37 A  529  LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN          
SEQRES  38 A  529  GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS          
SEQRES  39 A  529  SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER          
SEQRES  40 A  529  THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG          
SEQRES  41 A  529  PHE TRP THR SER PHE PHE PRO LYS VAL                          
SEQRES   1 B  529  GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL          
SEQRES   2 B  529  ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL THR          
SEQRES   3 B  529  ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY          
SEQRES   4 B  529  ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP          
SEQRES   5 B  529  SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS          
SEQRES   6 B  529  CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY          
SEQRES   7 B  529  SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP          
SEQRES   8 B  529  CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO          
SEQRES   9 B  529  LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY          
SEQRES  10 B  529  PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY          
SEQRES  11 B  529  LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER          
SEQRES  12 B  529  MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU          
SEQRES  13 B  529  PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE          
SEQRES  14 B  529  ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE          
SEQRES  15 B  529  ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE          
SEQRES  16 B  529  GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU          
SEQRES  17 B  529  LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE          
SEQRES  18 B  529  LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR          
SEQRES  19 B  529  SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA          
SEQRES  20 B  529  LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE          
SEQRES  21 B  529  ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU          
SEQRES  22 B  529  LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU          
SEQRES  23 B  529  SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU          
SEQRES  24 B  529  THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE          
SEQRES  25 B  529  LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU          
SEQRES  26 B  529  GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER          
SEQRES  27 B  529  LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN          
SEQRES  28 B  529  GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE          
SEQRES  29 B  529  GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL          
SEQRES  30 B  529  ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY          
SEQRES  31 B  529  ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU          
SEQRES  32 B  529  GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA          
SEQRES  33 B  529  PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO          
SEQRES  34 B  529  TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE          
SEQRES  35 B  529  GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN          
SEQRES  36 B  529  TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL          
SEQRES  37 B  529  LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN          
SEQRES  38 B  529  GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS          
SEQRES  39 B  529  SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER          
SEQRES  40 B  529  THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG          
SEQRES  41 B  529  PHE TRP THR SER PHE PHE PRO LYS VAL                          
HET    NAG  A 601      14                                                       
HET    NAG  A 602      14                                                       
HET    NAG  A 603      14                                                       
HET    NAG  A 604      14                                                       
HET    NAG  A 605      14                                                       
HET    NAG  A 606      14                                                       
HET    NAG  A 607      14                                                       
HET    NAG  A 608      14                                                       
HET    6QS  A 609      36                                                       
HET    EDO  A 610       4                                                       
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    NAG  B 606      14                                                       
HET    NAG  B 607      14                                                       
HET    NAG  B 608      14                                                       
HET    6QS  B 609      36                                                       
HET    EDO  B 610       4                                                       
HET    EDO  B 611       4                                                       
HET    GOL  B 612       6                                                       
HET    GOL  B 613       6                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     6QS [(2~{R})-OXOLAN-2-YL]METHYL 4-(9-ETHYLCARBAZOL-3-YL)-2-          
HETNAM   2 6QS  METHYL-5-OXIDANYLIDENE-4,6,7,8-TETRAHYDRO-1~{H}-                
HETNAM   3 6QS  QUINOLINE-3-CARBOXYLATE                                         
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     GOL GLYCEROL                                                         
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  NAG    16(C8 H15 N O6)                                              
FORMUL   9  6QS    2(C30 H32 N2 O4)                                             
FORMUL  10  EDO    3(C2 H6 O2)                                                  
FORMUL  21  GOL    2(C3 H8 O3)                                                  
FORMUL  23  HOH   *127(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  GLY A  251  1                                  17    
HELIX   11 AB2 ASN A  256  ASN A  266  1                                  11    
HELIX   12 AB3 ASP A  268  ALA A  277  1                                  10    
HELIX   13 AB4 PHE A  278  VAL A  280  5                                   3    
HELIX   14 AB5 MET A  302  GLY A  310  1                                   9    
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  GLU A  451  5                                   5    
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  LEU B  208  1                                  11    
HELIX   34 AD7 SER B  210  PHE B  217  5                                   8    
HELIX   35 AD8 SER B  235  THR B  250  1                                  16    
HELIX   36 AD9 ASN B  256  ASN B  266  1                                  11    
HELIX   37 AE1 ASP B  268  ALA B  277  1                                  10    
HELIX   38 AE2 MET B  302  GLY B  310  1                                   9    
HELIX   39 AE3 GLY B  326  TYR B  332  5                                   7    
HELIX   40 AE4 THR B  346  PHE B  358  1                                  13    
HELIX   41 AE5 SER B  362  TYR B  373  1                                  12    
HELIX   42 AE6 GLU B  383  PHE B  398  1                                  16    
HELIX   43 AE7 PHE B  398  GLU B  411  1                                  14    
HELIX   44 AE8 PRO B  431  GLY B  435  5                                   5    
HELIX   45 AE9 GLU B  441  PHE B  446  1                                   6    
HELIX   46 AF1 GLY B  447  GLU B  451  5                                   5    
HELIX   47 AF2 THR B  457  GLY B  478  1                                  22    
HELIX   48 AF3 ARG B  515  PHE B  525  1                                  11    
HELIX   49 AF4 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  VAL A 141   N  TRP A  98           
SHEET    5 AA211 ALA A 107  ILE A 113  1  N  TRP A 112   O  VAL A 142           
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  ILE A 221   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 421   N  VAL A 321           
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 TRP B  56  ASN B  57  1  O  TRP B  56   N  LYS B  12           
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  LEU B  95   N  ILE B  31           
SHEET    4 AA411 ILE B 140  MET B 144 -1  O  VAL B 141   N  TRP B  98           
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 503   N  TYR B 420           
SHEET   11 AA411 ILE B 510  THR B 512 -1  O  MET B 511   N  TYR B 500           
SHEET    1 AA5 2 SER B  64  CYS B  65  0                                        
SHEET    2 AA5 2 LEU B  88  SER B  89  1  O  SER B  89   N  SER B  64           
SSBOND   1 CYS A   65    CYS A   92                          1555   1555  2.03  
SSBOND   2 CYS A  252    CYS A  263                          1555   1555  2.05  
SSBOND   3 CYS A  400    CYS A  519                          1555   1555  2.06  
SSBOND   4 CYS B   65    CYS B   92                          1555   1555  2.03  
SSBOND   5 CYS B  252    CYS B  263                          1555   1555  2.05  
SSBOND   6 CYS B  400    CYS B  519                          1555   1555  2.06  
LINK         ND2 ASN A  17                 C1  NAG A 601     1555   1555  1.44  
LINK         ND2 ASN A 106                 C1  NAG A 603     1555   1555  1.38  
LINK         ND2 ASN A 241                 C1  NAG A 605     1555   1555  1.45  
LINK         ND2 ASN A 341                 C1  NAG A 606     1555   1555  1.46  
LINK         ND2 ASN A 481                 C1  NAG A 607     1555   1555  1.44  
LINK         ND2 ASN B  17                 C1  NAG B 601     1555   1555  1.44  
LINK         ND2 ASN B 106                 C1  NAG B 603     1555   1555  1.47  
LINK         ND2 ASN B 241                 C1  NAG B 604     1555   1555  1.46  
LINK         ND2 ASN B 256                 C1  NAG B 605     1555   1555  1.45  
LINK         ND2 ASN B 341                 C1  NAG B 606     1555   1555  1.45  
LINK         ND2 ASN B 481                 C1  NAG B 608     1555   1555  1.46  
LINK         O4  NAG A 603                 C1  NAG A 604     1555   1555  1.44  
LINK         O4  NAG A 607                 C1  NAG A 608     1555   1555  1.44  
LINK         O4  NAG B 606                 C1  NAG B 607     1555   1555  1.45  
LINK         CZ  TYR A 237                 ND2 ASN B 455     1555   1565  1.57  
CISPEP   1 ALA A  101    PRO A  102          0        -0.75                     
CISPEP   2 ALA B  101    PRO B  102          0         2.09                     
SITE     1 AC1  2 ARG A  14  ASN A  57                                          
SITE     1 AC2 14 TRP A  82  GLY A 115  GLY A 116  GLY A 117                    
SITE     2 AC2 14 GLU A 197  SER A 198  PRO A 285  SER A 287                    
SITE     3 AC2 14 ALA A 328  PHE A 398  HIS A 438  HOH A 701                    
SITE     4 AC2 14 HOH A 731  HOH A 749                                          
SITE     1 AC3  2 TYR A 396  PRO A 401                                          
SITE     1 AC4  2 ARG B  14  ASN B  57                                          
SITE     1 AC5 12 TRP B  82  GLY B 115  GLY B 116  GLY B 117                    
SITE     2 AC5 12 GLU B 197  SER B 198  PRO B 285  SER B 287                    
SITE     3 AC5 12 ALA B 328  PHE B 329  TYR B 332  HIS B 438                    
SITE     1 AC6  2 HIS B  77  GLU B 443                                          
SITE     1 AC7  2 ASN B 245  PHE B 278                                          
SITE     1 AC8  4 TYR B  61  TRP B  98  ASP B 129  LYS B 131                    
SITE     1 AC9  5 GLU A 411  TRP A 412  LYS B 248  GLY B 251                    
SITE     2 AC9  5 SER B 253                                                     
SITE     1 AD1  3 ILE A   4  ASN A  17  THR A  24                               
SITE     1 AD2  2 ASN A 106  ASN A 188                                          
SITE     1 AD3  3 GLU A 238  ASN A 241  ASN A 245                               
SITE     1 AD4  2 SER A 338  ASN A 341                                          
SITE     1 AD5  7 ASN A 473  TYR A 477  ASN A 481  GLU A 482                    
SITE     2 AD5  7 ASP B  87  LEU B  88  GLN B 270                               
SITE     1 AD6  3 ILE B   4  ASN B  17  THR B  24                               
SITE     1 AD7  2 ASN B 106  ASN B 188                                          
SITE     1 AD8  3 ASN B 241  ASN B 245  PRO B 281                               
SITE     1 AD9  1 ASN B 256                                                     
SITE     1 AE1  3 GLY B 336  SER B 338  ASN B 341                               
SITE     1 AE2  3 ASN B 481  GLU B 482  THR B 483                               
CRYST1   75.810   80.070  230.630  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      0.013191  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012489  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004336        0.00000                         
TER    4216      VAL A 529                                                      
TER    8417      VAL B 529                                                      
MASTER      557    0   23   49   30    0   27    6 8837    2  343   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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