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LongText Report for: 5lkr-pdb

Name Class
5lkr-pdb
HEADER    HYDROLASE                               23-JUL-16   5LKR              
TITLE     HUMAN BUTYRYLCHOLINESTERASE COMPLEXED WITH N-PROPARGYLIPERIDINES      
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: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029                                       
KEYWDS    ALZHEIMER DISEASE AD BUTYRYLCHOLINESTERASE N-PROPARGYLIPERIDINES,     
KEYWDS   2 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.COQUELLE,D.KNEZ,J.P.COLLETIER,S.GOBEC                               
REVDAT   1   14-DEC-16 5LKR    0                                                
JRNL        AUTH   U.KOSAK,D.KNEZ,N.COQUELLE,B.BRUS,A.PISLAR,F.NACHON,          
JRNL        AUTH 2 X.BRAZZOLOTTO,J.KOS,J.P.COLLETIER,S.GOBEC                    
JRNL        TITL   N-PROPARGYLPIPERIDINES WITH NAPHTHALENE-2-CARBOXAMIDE OR     
JRNL        TITL 2 NAPHTHALENE-2-SULFONAMIDE MOIETIES: POTENTIAL                
JRNL        TITL 3 MULTIFUNCTIONAL ANTI-ALZHEIMER'S AGENTS.                     
JRNL        REF    BIOORG. MED. CHEM.                         2016              
JRNL        REFN                   ESSN 1464-3391                               
JRNL        PMID   27908752                                                     
JRNL        DOI    10.1016/J.BMC.2016.11.032                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.52 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) : 2.52                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.86                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 45908                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.186                           
REMARK   3   FREE R VALUE                     : 0.238                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2327                            
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 48.8663 -  6.4749    0.99     2757   157  0.1716 0.2400        
REMARK   3     2  6.4749 -  5.1411    1.00     2663   125  0.1778 0.2205        
REMARK   3     3  5.1411 -  4.4918    1.00     2609   140  0.1390 0.1752        
REMARK   3     4  4.4918 -  4.0813    0.99     2549   156  0.1384 0.1776        
REMARK   3     5  4.0813 -  3.7889    1.00     2580   144  0.1546 0.2280        
REMARK   3     6  3.7889 -  3.5656    1.00     2586   139  0.1794 0.2170        
REMARK   3     7  3.5656 -  3.3871    1.00     2561   141  0.1916 0.2316        
REMARK   3     8  3.3871 -  3.2397    1.00     2585   126  0.2098 0.2601        
REMARK   3     9  3.2397 -  3.1150    1.00     2551   154  0.2259 0.2926        
REMARK   3    10  3.1150 -  3.0075    1.00     2589   113  0.2276 0.3291        
REMARK   3    11  3.0075 -  2.9135    0.99     2528   141  0.2455 0.2778        
REMARK   3    12  2.9135 -  2.8302    0.99     2515   116  0.2499 0.3318        
REMARK   3    13  2.8302 -  2.7557    0.99     2556   140  0.2775 0.3333        
REMARK   3    14  2.7557 -  2.6885    0.99     2527   152  0.3137 0.3757        
REMARK   3    15  2.6885 -  2.6274    0.99     2502   138  0.3354 0.3813        
REMARK   3    16  2.6274 -  2.5714    0.98     2495   119  0.3410 0.4147        
REMARK   3    17  2.5714 -  2.5200    0.95     2428   126  0.3707 0.4356        
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)     : 0.430            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.850           
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      :  0.007           8985                                  
REMARK   3   ANGLE     :  0.917          12253                                  
REMARK   3   CHIRALITY :  0.057           1366                                  
REMARK   3   PLANARITY :  0.005           1546                                  
REMARK   3   DIHEDRAL  : 12.924           5198                                  
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 5LKR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JUL-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200000882.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-NOV-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                       : ID30A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.966                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 2M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45918                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.520                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.860                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.06400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 10.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM ACETATE, 18% PEG 4000,     
REMARK 280  20 MM TRIS PH 7.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE       
REMARK 280  293.0K                                                              
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       36.84050            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      114.43450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.73150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      114.43450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.84050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.73150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 A   531                                                      
REMARK 465     MET A   532                                                      
REMARK 465     THR A   533                                                      
REMARK 465     GLY A   534                                                      
REMARK 465     ASN A   535                                                      
REMARK 465     ILE A   536                                                      
REMARK 465     ASP A   537                                                      
REMARK 465     GLU A   538                                                      
REMARK 465     ALA A   539                                                      
REMARK 465     GLU A   540                                                      
REMARK 465     TRP A   541                                                      
REMARK 465     GLU A   542                                                      
REMARK 465     TRP A   543                                                      
REMARK 465     LYS A   544                                                      
REMARK 465     ALA A   545                                                      
REMARK 465     GLY A   546                                                      
REMARK 465     PHE A   547                                                      
REMARK 465     HIS A   548                                                      
REMARK 465     ARG A   549                                                      
REMARK 465     TRP A   550                                                      
REMARK 465     ASN A   551                                                      
REMARK 465     ASN A   552                                                      
REMARK 465     TYR A   553                                                      
REMARK 465     MET A   554                                                      
REMARK 465     MET A   555                                                      
REMARK 465     ASP A   556                                                      
REMARK 465     TRP A   557                                                      
REMARK 465     LYS A   558                                                      
REMARK 465     ASN A   559                                                      
REMARK 465     GLN A   560                                                      
REMARK 465     PHE A   561                                                      
REMARK 465     ASN A   562                                                      
REMARK 465     ASP A   563                                                      
REMARK 465     TYR A   564                                                      
REMARK 465     THR A   565                                                      
REMARK 465     SER A   566                                                      
REMARK 465     LYS A   567                                                      
REMARK 465     LYS A   568                                                      
REMARK 465     GLU A   569                                                      
REMARK 465     SER A   570                                                      
REMARK 465     CYS A   571                                                      
REMARK 465     VAL A   572                                                      
REMARK 465     GLY A   573                                                      
REMARK 465     LEU A   574                                                      
REMARK 465     GLU B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     ASN B   485                                                      
REMARK 465     ASN B   486                                                      
REMARK 465     GLU B   531                                                      
REMARK 465     MET B   532                                                      
REMARK 465     THR B   533                                                      
REMARK 465     GLY B   534                                                      
REMARK 465     ASN B   535                                                      
REMARK 465     ILE B   536                                                      
REMARK 465     ASP B   537                                                      
REMARK 465     GLU B   538                                                      
REMARK 465     ALA B   539                                                      
REMARK 465     GLU B   540                                                      
REMARK 465     TRP B   541                                                      
REMARK 465     GLU B   542                                                      
REMARK 465     TRP B   543                                                      
REMARK 465     LYS B   544                                                      
REMARK 465     ALA B   545                                                      
REMARK 465     GLY B   546                                                      
REMARK 465     PHE B   547                                                      
REMARK 465     HIS B   548                                                      
REMARK 465     ARG B   549                                                      
REMARK 465     TRP B   550                                                      
REMARK 465     ASN B   551                                                      
REMARK 465     ASN B   552                                                      
REMARK 465     TYR B   553                                                      
REMARK 465     MET B   554                                                      
REMARK 465     MET B   555                                                      
REMARK 465     ASP B   556                                                      
REMARK 465     TRP B   557                                                      
REMARK 465     LYS B   558                                                      
REMARK 465     ASN B   559                                                      
REMARK 465     GLN B   560                                                      
REMARK 465     PHE B   561                                                      
REMARK 465     ASN B   562                                                      
REMARK 465     ASP B   563                                                      
REMARK 465     TYR B   564                                                      
REMARK 465     THR B   565                                                      
REMARK 465     SER B   566                                                      
REMARK 465     LYS B   567                                                      
REMARK 465     LYS B   568                                                      
REMARK 465     GLU B   569                                                      
REMARK 465     SER B   570                                                      
REMARK 465     CYS B   571                                                      
REMARK 465     VAL B   572                                                      
REMARK 465     GLY B   573                                                      
REMARK 465     LEU B   574                                                      
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     ARG A  40    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 105    CG   CD   CE   NZ                                   
REMARK 470     LYS A 248    CD   CE   NZ                                        
REMARK 470     GLU A 255    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 271    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 348    CG   CD   CE   NZ                                   
REMARK 470     LYS A 355    CG   CD   CE   NZ                                   
REMARK 470     LYS A 366    CG   CD   CE   NZ                                   
REMARK 470     ARG A 452    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 453    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 506    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 530    CA   C    O    CB   CG   CD1  CD2                   
REMARK 470     ILE B   4    CG1  CG2  CD1                                       
REMARK 470     LYS B  12    CG   CD   CE   NZ                                   
REMARK 470     LYS B  44    CE   NZ                                             
REMARK 470     LYS B  51    CG   CD   CE   NZ                                   
REMARK 470     SER B  53    OG                                                  
REMARK 470     LYS B 190    CG   CD   CE   NZ                                   
REMARK 470     GLU B 257    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 268    CG   OD1  OD2                                       
REMARK 470     GLU B 276    CG   CD   OE1  OE2                                  
REMARK 470     TYR B 282    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP B 454    CG   OD1  OD2                                       
REMARK 470     GLN B 484    CG   CD   OE1  NE2                                  
REMARK 470     SER B 507    CB   OG                                             
REMARK 470     LEU B 530    CA   C    O    CB   CG   CD1  CD2                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O4   NAG B   607     O    HOH B   701              2.09            
REMARK 500   NH1  ARG B   465     O    HOH B   702              2.09            
REMARK 500   OG   SER A   198     O    HOH A   701              2.14            
REMARK 500   NH1  ARG B   240     O    HOH B   703              2.17            
REMARK 500   O3   GOL A   617     O4   PEG A   618              2.19            
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    PHE B 364   CB    PHE B 364   CG     -0.138                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A  43       -3.19     86.71                                   
REMARK 500    THR A  50      -89.73    -81.28                                   
REMARK 500    SER A  53       68.96   -116.25                                   
REMARK 500    ASP A  54     -147.36   -177.34                                   
REMARK 500    CYS A  92       -2.97   -142.46                                   
REMARK 500    PRO A 160       -7.54    -59.63                                   
REMARK 500    ALA A 162       72.59   -157.61                                   
REMARK 500    SER A 198     -124.52     64.33                                   
REMARK 500    TYR A 282     -105.07    -71.38                                   
REMARK 500    ASP A 297      -73.08    -98.75                                   
REMARK 500    TYR A 332       35.63    -92.51                                   
REMARK 500    ARG A 381       74.45     51.37                                   
REMARK 500    PHE A 398      -52.43   -129.48                                   
REMARK 500    GLU A 482      -79.68    -95.94                                   
REMARK 500    GLU A 506      -75.48    -73.85                                   
REMARK 500    PHE A 525      -35.73   -130.18                                   
REMARK 500    LYS B   9       14.65    -69.93                                   
REMARK 500    PHE B  43      -11.00     82.71                                   
REMARK 500    ASP B  54     -136.51    -87.30                                   
REMARK 500    ALA B  58       66.30   -102.13                                   
REMARK 500    ASN B 106       32.43   -152.85                                   
REMARK 500    ALA B 162       70.94   -165.64                                   
REMARK 500    ASN B 181      -15.72   -142.01                                   
REMARK 500    SER B 198     -118.67     66.19                                   
REMARK 500    THR B 218      -66.14    -96.74                                   
REMARK 500    TYR B 282       75.55   -110.45                                   
REMARK 500    ASP B 297      -66.78   -126.82                                   
REMARK 500    THR B 315     -175.30   -172.37                                   
REMARK 500    PHE B 398      -54.78   -132.55                                   
REMARK 500    PRO B 431      171.06    -59.65                                   
REMARK 500    ASP B 454       30.43   -141.13                                   
REMARK 500    GLU B 482     -138.67   -105.97                                   
REMARK 500    THR B 496      -66.69    -94.86                                   
REMARK 500    GLN B 498       73.88     57.15                                   
REMARK 500    GLU B 506      -99.12    -68.07                                   
REMARK 500    ARG B 515       43.19     36.98                                   
REMARK 500    PRO B 527       10.65    -65.18                                   
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 A  604                                                       
REMARK 610     NAG B  606                                                       
REMARK 610     NAG B  612                                                       
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C  SSEQI                                                     
REMARK 615     6YC A   616                                                      
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FUL A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6YC A 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6YC B 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG B 612                 
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  602 through NAG A 603 bound to ASN A 57                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
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: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  607 through FUC A 608 bound to ASN A 241                            
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  609 through NAG A 610 bound to ASN A 341                            
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  611 through NAG A 612 bound to ASN A 481                            
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  613 through NAG A 614 bound to ASN A 486                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 613 bound   
REMARK 800  to ASN B 17                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 601 bound   
REMARK 800  to ASN B 57                                                         
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  602 through NAG B 603 bound to ASN B 106                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  604 through FUL B 605 bound to ASN B 241                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
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: AE4                                                 
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: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 609 bound   
REMARK 800  to ASN B 481                                                        
DBREF  5LKR A    1   574  UNP    P06276   CHLE_HUMAN      29    602             
DBREF  5LKR B    1   574  UNP    P06276   CHLE_HUMAN      29    602             
SEQRES   1 A  574  GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL          
SEQRES   2 A  574  ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL THR          
SEQRES   3 A  574  ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY          
SEQRES   4 A  574  ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP          
SEQRES   5 A  574  SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS          
SEQRES   6 A  574  CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY          
SEQRES   7 A  574  SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP          
SEQRES   8 A  574  CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO          
SEQRES   9 A  574  LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY          
SEQRES  10 A  574  PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY          
SEQRES  11 A  574  LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER          
SEQRES  12 A  574  MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU          
SEQRES  13 A  574  PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE          
SEQRES  14 A  574  ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE          
SEQRES  15 A  574  ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE          
SEQRES  16 A  574  GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU          
SEQRES  17 A  574  LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE          
SEQRES  18 A  574  LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR          
SEQRES  19 A  574  SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA          
SEQRES  20 A  574  LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE          
SEQRES  21 A  574  ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU          
SEQRES  22 A  574  LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU          
SEQRES  23 A  574  SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU          
SEQRES  24 A  574  THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE          
SEQRES  25 A  574  LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU          
SEQRES  26 A  574  GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER          
SEQRES  27 A  574  LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN          
SEQRES  28 A  574  GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE          
SEQRES  29 A  574  GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL          
SEQRES  30 A  574  ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY          
SEQRES  31 A  574  ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU          
SEQRES  32 A  574  GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA          
SEQRES  33 A  574  PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO          
SEQRES  34 A  574  TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE          
SEQRES  35 A  574  GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN          
SEQRES  36 A  574  TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL          
SEQRES  37 A  574  LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN          
SEQRES  38 A  574  GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS          
SEQRES  39 A  574  SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER          
SEQRES  40 A  574  THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG          
SEQRES  41 A  574  PHE TRP THR SER PHE PHE PRO LYS VAL LEU GLU MET THR          
SEQRES  42 A  574  GLY ASN ILE ASP GLU ALA GLU TRP GLU TRP LYS ALA GLY          
SEQRES  43 A  574  PHE HIS ARG TRP ASN ASN TYR MET MET ASP TRP LYS ASN          
SEQRES  44 A  574  GLN PHE ASN ASP TYR THR SER LYS LYS GLU SER CYS VAL          
SEQRES  45 A  574  GLY LEU                                                      
SEQRES   1 B  574  GLU ASP ASP ILE ILE ILE ALA THR LYS ASN GLY LYS VAL          
SEQRES   2 B  574  ARG GLY MET ASN LEU THR VAL PHE GLY GLY THR VAL THR          
SEQRES   3 B  574  ALA PHE LEU GLY ILE PRO TYR ALA GLN PRO PRO LEU GLY          
SEQRES   4 B  574  ARG LEU ARG PHE LYS LYS PRO GLN SER LEU THR LYS TRP          
SEQRES   5 B  574  SER ASP ILE TRP ASN ALA THR LYS TYR ALA ASN SER CYS          
SEQRES   6 B  574  CYS GLN ASN ILE ASP GLN SER PHE PRO GLY PHE HIS GLY          
SEQRES   7 B  574  SER GLU MET TRP ASN PRO ASN THR ASP LEU SER GLU ASP          
SEQRES   8 B  574  CYS LEU TYR LEU ASN VAL TRP ILE PRO ALA PRO LYS PRO          
SEQRES   9 B  574  LYS ASN ALA THR VAL LEU ILE TRP ILE TYR GLY GLY GLY          
SEQRES  10 B  574  PHE GLN THR GLY THR SER SER LEU HIS VAL TYR ASP GLY          
SEQRES  11 B  574  LYS PHE LEU ALA ARG VAL GLU ARG VAL ILE VAL VAL SER          
SEQRES  12 B  574  MET ASN TYR ARG VAL GLY ALA LEU GLY PHE LEU ALA LEU          
SEQRES  13 B  574  PRO GLY ASN PRO GLU ALA PRO GLY ASN MET GLY LEU PHE          
SEQRES  14 B  574  ASP GLN GLN LEU ALA LEU GLN TRP VAL GLN LYS ASN ILE          
SEQRES  15 B  574  ALA ALA PHE GLY GLY ASN PRO LYS SER VAL THR LEU PHE          
SEQRES  16 B  574  GLY GLU SER ALA GLY ALA ALA SER VAL SER LEU HIS LEU          
SEQRES  17 B  574  LEU SER PRO GLY SER HIS SER LEU PHE THR ARG ALA ILE          
SEQRES  18 B  574  LEU GLN SER GLY SER PHE ASN ALA PRO TRP ALA VAL THR          
SEQRES  19 B  574  SER LEU TYR GLU ALA ARG ASN ARG THR LEU ASN LEU ALA          
SEQRES  20 B  574  LYS LEU THR GLY CYS SER ARG GLU ASN GLU THR GLU ILE          
SEQRES  21 B  574  ILE LYS CYS LEU ARG ASN LYS ASP PRO GLN GLU ILE LEU          
SEQRES  22 B  574  LEU ASN GLU ALA PHE VAL VAL PRO TYR GLY THR PRO LEU          
SEQRES  23 B  574  SER VAL ASN PHE GLY PRO THR VAL ASP GLY ASP PHE LEU          
SEQRES  24 B  574  THR ASP MET PRO ASP ILE LEU LEU GLU LEU GLY GLN PHE          
SEQRES  25 B  574  LYS LYS THR GLN ILE LEU VAL GLY VAL ASN LYS ASP GLU          
SEQRES  26 B  574  GLY THR ALA PHE LEU VAL TYR GLY ALA PRO GLY PHE SER          
SEQRES  27 B  574  LYS ASP ASN ASN SER ILE ILE THR ARG LYS GLU PHE GLN          
SEQRES  28 B  574  GLU GLY LEU LYS ILE PHE PHE PRO GLY VAL SER GLU PHE          
SEQRES  29 B  574  GLY LYS GLU SER ILE LEU PHE HIS TYR THR ASP TRP VAL          
SEQRES  30 B  574  ASP ASP GLN ARG PRO GLU ASN TYR ARG GLU ALA LEU GLY          
SEQRES  31 B  574  ASP VAL VAL GLY ASP TYR ASN PHE ILE CYS PRO ALA LEU          
SEQRES  32 B  574  GLU PHE THR LYS LYS PHE SER GLU TRP GLY ASN ASN ALA          
SEQRES  33 B  574  PHE PHE TYR TYR PHE GLU HIS ARG SER SER LYS LEU PRO          
SEQRES  34 B  574  TRP PRO GLU TRP MET GLY VAL MET HIS GLY TYR GLU ILE          
SEQRES  35 B  574  GLU PHE VAL PHE GLY LEU PRO LEU GLU ARG ARG ASP ASN          
SEQRES  36 B  574  TYR THR LYS ALA GLU GLU ILE LEU SER ARG SER ILE VAL          
SEQRES  37 B  574  LYS ARG TRP ALA ASN PHE ALA LYS TYR GLY ASN PRO ASN          
SEQRES  38 B  574  GLU THR GLN ASN ASN SER THR SER TRP PRO VAL PHE LYS          
SEQRES  39 B  574  SER THR GLU GLN LYS TYR LEU THR LEU ASN THR GLU SER          
SEQRES  40 B  574  THR ARG ILE MET THR LYS LEU ARG ALA GLN GLN CYS ARG          
SEQRES  41 B  574  PHE TRP THR SER PHE PHE PRO LYS VAL LEU GLU MET THR          
SEQRES  42 B  574  GLY ASN ILE ASP GLU ALA GLU TRP GLU TRP LYS ALA GLY          
SEQRES  43 B  574  PHE HIS ARG TRP ASN ASN TYR MET MET ASP TRP LYS ASN          
SEQRES  44 B  574  GLN PHE ASN ASP TYR THR SER LYS LYS GLU SER CYS VAL          
SEQRES  45 B  574  GLY LEU                                                      
HET    NAG  A 601      14                                                       
HET    NAG  A 602      14                                                       
HET    NAG  A 603      14                                                       
HET    FUL  A 604      10                                                       
HET    NAG  A 605      14                                                       
HET    NAG  A 606      14                                                       
HET    NAG  A 607      14                                                       
HET    FUC  A 608      10                                                       
HET    NAG  A 609      14                                                       
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    GOL  A 615       6                                                       
HET    6YC  A 616      27                                                       
HET    GOL  A 617       6                                                       
HET    PEG  A 618       7                                                       
HET    NAG  B 601      14                                                       
HET    NAG  B 602      14                                                       
HET    NAG  B 603      14                                                       
HET    NAG  B 604      14                                                       
HET    FUL  B 605      10                                                       
HET    NAG  B 606      14                                                       
HET    NAG  B 607      14                                                       
HET    NAG  B 608      14                                                       
HET    NAG  B 609      14                                                       
HET    GOL  B 610       6                                                       
HET    6YC  B 611      27                                                       
HET    NAG  B 612      14                                                       
HET    NAG  B 613      14                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUL BETA-L-FUCOSE                                                    
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     GOL GLYCEROL                                                         
HETNAM     6YC ~{N}-(2-METHOXYETHYL)-~{N}-[[(3~{S})-1-PROP-2-                   
HETNAM   2 6YC  YNYLPIPERIDIN-3-YL]METHYL]NAPHTHALENE-2-CARBOXAMIDE             
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     FUL 6-DEOXY-BETA-L-GALACTOSE                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  NAG    22(C8 H15 N O6)                                              
FORMUL   5  FUL    2(C6 H12 O5)                                                 
FORMUL   7  FUC    C6 H12 O5                                                    
FORMUL  11  GOL    3(C3 H8 O3)                                                  
FORMUL  12  6YC    2(C23 H28 N2 O2)                                             
FORMUL  14  PEG    C4 H10 O3                                                    
FORMUL  26  HOH   *36(H2 O)                                                     
HELIX    1 AA1 PHE A   76  MET A   81  1                                   6    
HELIX    2 AA2 LEU A  125  ASP A  129  5                                   5    
HELIX    3 AA3 GLY A  130  ARG A  138  1                                   9    
HELIX    4 AA4 GLY A  149  LEU A  154  1                                   6    
HELIX    5 AA5 ASN A  165  ILE A  182  1                                  18    
HELIX    6 AA6 ALA A  183  PHE A  185  5                                   3    
HELIX    7 AA7 SER A  198  LEU A  208  1                                  11    
HELIX    8 AA8 SER A  235  THR A  250  1                                  16    
HELIX    9 AA9 ASN A  256  ARG A  265  1                                  10    
HELIX   10 AB1 ASP A  268  GLU A  276  1                                   9    
HELIX   11 AB2 ALA A  277  VAL A  279  5                                   3    
HELIX   12 AB3 MET A  302  LEU A  309  1                                   8    
HELIX   13 AB4 GLY A  326  VAL A  331  1                                   6    
HELIX   14 AB5 THR A  346  PHE A  358  1                                  13    
HELIX   15 AB6 SER A  362  TYR A  373  1                                  12    
HELIX   16 AB7 GLU A  383  PHE A  398  1                                  16    
HELIX   17 AB8 PHE A  398  GLU A  411  1                                  14    
HELIX   18 AB9 PRO A  431  GLY A  435  5                                   5    
HELIX   19 AC1 GLU A  441  PHE A  446  1                                   6    
HELIX   20 AC2 GLY A  447  ASN A  455  5                                   9    
HELIX   21 AC3 THR A  457  GLY A  478  1                                  22    
HELIX   22 AC4 ARG A  515  PHE A  525  1                                  11    
HELIX   23 AC5 PHE A  526  VAL A  529  5                                   4    
HELIX   24 AC6 LEU B   38  ARG B   42  5                                   5    
HELIX   25 AC7 PHE B   76  MET B   81  1                                   6    
HELIX   26 AC8 LEU B  125  ASP B  129  5                                   5    
HELIX   27 AC9 GLY B  130  ARG B  138  1                                   9    
HELIX   28 AD1 GLY B  149  LEU B  154  1                                   6    
HELIX   29 AD2 ASN B  165  ILE B  182  1                                  18    
HELIX   30 AD3 ALA B  183  PHE B  185  5                                   3    
HELIX   31 AD4 SER B  198  SER B  210  1                                  13    
HELIX   32 AD5 PRO B  211  PHE B  217  5                                   7    
HELIX   33 AD6 SER B  235  THR B  250  1                                  16    
HELIX   34 AD7 ASN B  256  ARG B  265  1                                  10    
HELIX   35 AD8 ASP B  268  LEU B  274  1                                   7    
HELIX   36 AD9 ASN B  275  VAL B  279  5                                   5    
HELIX   37 AE1 MET B  302  LEU B  309  1                                   8    
HELIX   38 AE2 GLY B  326  GLY B  333  5                                   8    
HELIX   39 AE3 THR B  346  PHE B  358  1                                  13    
HELIX   40 AE4 SER B  362  TYR B  373  1                                  12    
HELIX   41 AE5 GLU B  383  PHE B  398  1                                  16    
HELIX   42 AE6 PHE B  398  GLU B  411  1                                  14    
HELIX   43 AE7 PRO B  431  GLY B  435  5                                   5    
HELIX   44 AE8 GLU B  441  PHE B  446  1                                   6    
HELIX   45 AE9 THR B  457  TYR B  477  1                                  21    
HELIX   46 AF1 ARG B  515  PHE B  525  1                                  11    
HELIX   47 AF2 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  GLY A  23   N  VAL A  20           
SHEET    3 AA211 TYR A  94  PRO A 100 -1  O  VAL A  97   N  PHE A  28           
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  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  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 2 SER A  64  CYS A  65  0                                        
SHEET    2 AA3 2 LEU A  88  SER A  89  1  O  SER A  89   N  SER A  64           
SHEET    1 AA4 3 ILE B   5  THR B   8  0                                        
SHEET    2 AA4 3 GLY B  11  ARG B  14 -1  O  VAL B  13   N  ILE B   6           
SHEET    3 AA4 3 ILE B  55  ASN B  57  1  O  TRP B  56   N  ARG B  14           
SHEET    1 AA511 MET B  16  VAL B  20  0                                        
SHEET    2 AA511 GLY B  23  PRO B  32 -1  O  VAL B  25   N  LEU B  18           
SHEET    3 AA511 TYR B  94  ALA B 101 -1  O  LEU B  95   N  ILE B  31           
SHEET    4 AA511 ILE B 140  MET B 144 -1  O  SER B 143   N  ASN B  96           
SHEET    5 AA511 ALA B 107  ILE B 113  1  N  TRP B 112   O  VAL B 142           
SHEET    6 AA511 GLY B 187  GLU B 197  1  O  THR B 193   N  VAL B 109           
SHEET    7 AA511 ARG B 219  GLN B 223  1  O  ILE B 221   N  LEU B 194           
SHEET    8 AA511 ILE B 317  ASN B 322  1  O  LEU B 318   N  LEU B 222           
SHEET    9 AA511 ALA B 416  PHE B 421  1  O  PHE B 421   N  VAL B 321           
SHEET   10 AA511 LYS B 499  LEU B 503  1  O  LEU B 501   N  PHE B 418           
SHEET   11 AA511 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  2.04  
SSBOND   2 CYS A  252    CYS A  263                          1555   1555  2.04  
SSBOND   3 CYS A  400    CYS A  519                          1555   1555  2.06  
SSBOND   4 CYS B   65    CYS B   92                          1555   1555  2.04  
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  57                 C1  NAG A 603     1555   1555  1.44  
LINK         ND2 ASN A 106                 C1  NAG A 605     1555   1555  1.46  
LINK         ND2 ASN A 241                 C1  NAG A 607     1555   1555  1.45  
LINK         ND2 ASN A 341                 C1  NAG A 609     1555   1555  1.45  
LINK         ND2 ASN A 481                 C1  NAG A 611     1555   1555  1.45  
LINK         ND2 ASN A 486                 C1  NAG A 613     1555   1555  1.44  
LINK         ND2 ASN B  17                 C1  NAG B 613     1555   1555  1.44  
LINK         ND2 ASN B  57                 C1  NAG B 601     1555   1555  1.45  
LINK         ND2 ASN B 106                 C1  NAG B 602     1555   1555  1.45  
LINK         ND2 ASN B 241                 C1  NAG B 604     1555   1555  1.43  
LINK         ND2 ASN B 256                 C1  NAG B 607     1555   1555  1.45  
LINK         ND2 ASN B 341                 C1  NAG B 608     1555   1555  1.45  
LINK         ND2 ASN B 481                 C1  NAG B 609     1555   1555  1.45  
LINK         C1  NAG A 602                 O4  NAG A 603     1555   1555  1.45  
LINK         O4  NAG A 605                 C1  NAG A 606     1555   1555  1.48  
LINK         O6  NAG A 607                 C1  FUC A 608     1555   1555  1.45  
LINK         O4  NAG A 609                 C1  NAG A 610     1555   1555  1.43  
LINK         O4  NAG A 611                 C1  NAG A 612     1555   1555  1.44  
LINK         O4  NAG A 613                 C1  NAG A 614     1555   1555  1.44  
LINK         O4  NAG B 602                 C1  NAG B 603     1555   1555  1.44  
LINK         O6  NAG B 604                 C1  FUL B 605     1555   1555  1.45  
CISPEP   1 ALA A  101    PRO A  102          0         0.51                     
CISPEP   2 GLN A  380    ARG A  381          0        -6.06                     
CISPEP   3 ALA B  101    PRO B  102          0         3.73                     
SITE     1 AC1  1 NAG A 603                                                     
SITE     1 AC2  3 ASN A 228  TRP A 522  THR A 523                               
SITE     1 AC3  4 GLY A 117  THR A 120  SER A 198  HOH A 701                    
SITE     1 AC4  2 ASN A 455  PEG A 618                                          
SITE     1 AC5  1 GOL A 617                                                     
SITE     1 AC6  3 GLN B 380  NAG B 604  HOH B 714                               
SITE     1 AC7  5 LEU B  18  TYR B  61  TRP B  98  ASP B 129                    
SITE     2 AC7  5 LYS B 131                                                     
SITE     1 AC8  6 ASN B  68  ASP B  70  GLY B 117  THR B 120                    
SITE     2 AC8  6 SER B 198  TRP B 231                                          
SITE     1 AC9  3 TYR A 237  NAG A 607  ASN B 455                               
SITE     1 AD1  2 ASN A  17  THR A  24                                          
SITE     1 AD2  3 ILE A  55  ASN A  57  FUL A 604                               
SITE     1 AD3  3 ASN A 106  ASN A 188  LYS A 190                               
SITE     1 AD4  5 SER A  53  ASN A 241  ASN A 245  PHE A 278                    
SITE     2 AD4  5 NAG B 612                                                     
SITE     1 AD5  4 PRO A 335  GLY A 336  SER A 338  ASN A 341                    
SITE     1 AD6  6 TYR A 477  ASN A 481  GLU A 482  GLN A 484                    
SITE     2 AD6  6 LEU B  88  GLN B 270                                          
SITE     1 AD7  3 ASN A 486  HOH A 702  HOH B 708                               
SITE     1 AD8  2 ASN B  17  ALA B 101                                          
SITE     1 AD9  1 ASN B  57                                                     
SITE     1 AE1  2 ASN B 106  ASN B 188                                          
SITE     1 AE2  5 TYR B 237  ASN B 241  ASN B 245  PHE B 278                    
SITE     2 AE2  5 NAG B 606                                                     
SITE     1 AE3  4 ASN B 256  GLU B 259  HOH B 701  HOH B 716                    
SITE     1 AE4  3 SER B 338  ASN B 341  HOH B 706                               
SITE     1 AE5  4 TYR B 477  ASN B 481  GLU B 482  THR B 483                    
CRYST1   73.681   79.463  228.869  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      0.013572  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012584  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004369        0.00000                         
TER    4169      LEU A 530                                                      
TER    8300      LEU B 530                                                      
MASTER      556    0   31   47   30    0   28    6 8733    2  443   90          
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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