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LongText Report for: 6rua-pdb

Name Class
6rua-pdb
HEADER    HYDROLASE                               27-MAY-19   6RUA              
TITLE     STRUCTURE OF RECOMBINANT HUMAN BUTYRYLCHOLINESTERASE IN COMPLEX WITH A
TITLE    2 COUMARIN-BASED FLUORESCENT PROBE LINKED TO SULFONAMIDE TYPE          
TITLE    3 INHIBITOR.                                                           
CAVEAT     6RUA    NAG A 601 HAS WRONG CHIRALITY AT ATOM C1 NAG A 606 HAS WRONG 
CAVEAT   2 6RUA    CHIRALITY AT ATOM C1 FUC A 609 HAS WRONG CHIRALITY AT ATOM   
CAVEAT   3 6RUA    C1 NAG A 612 HAS WRONG CHIRALITY AT ATOM C1 NAG A 615 HAS    
CAVEAT   4 6RUA    WRONG CHIRALITY AT ATOM C1 NAG B 614 HAS WRONG CHIRALITY AT  
CAVEAT   5 6RUA    ATOM C1                                                      
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    HUMAN BUTYRYLCHOLINESTERASE, INSECT CELL, HYDROLASE, FLUORESCENT      
KEYWDS   2 PROBES, SULFONAMIDE, INHIBITOR                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.COQUELLE,D.KNEZ,B.BRUS,S.GOBEC,J.P.COLLETIER                        
REVDAT   1   22-JAN-20 6RUA    0                                                
JRNL        AUTH   S.PAJK,D.KNEZ,U.KOSAK,M.ZOROVIC,X.BRAZZOLOTTO,N.COQUELLE,    
JRNL        AUTH 2 F.NACHON,J.P.COLLETIER,M.ZIVIN,J.STOJAN,S.GOBEC              
JRNL        TITL   DEVELOPMENT OF POTENT REVERSIBLE SELECTIVE INHIBITORS OF     
JRNL        TITL 2 BUTYRYLCHOLINESTERASE AS FLUORESCENT PROBES.                 
JRNL        REF    J ENZYME INHIB MED CHEM       V.  35   498 2020              
JRNL        REFN                   ESSN 1475-6374                               
JRNL        PMID   31914836                                                     
JRNL        DOI    10.1080/14756366.2019.1710502                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (DEV_3139: ???)                               
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.93                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 37465                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.183                           
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1122                            
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 44.9326 -  5.4971    0.98     4714   143  0.1771 0.2058        
REMARK   3     2  5.4971 -  4.3644    0.99     4600   145  0.1484 0.1853        
REMARK   3     3  4.3644 -  3.8131    1.00     4530   138  0.1492 0.2008        
REMARK   3     4  3.8131 -  3.4646    1.00     4546   140  0.1783 0.2750        
REMARK   3     5  3.4646 -  3.2163    0.98     4476   140  0.2106 0.2692        
REMARK   3     6  3.2163 -  3.0267    0.99     4490   145  0.2229 0.3305        
REMARK   3     7  3.0267 -  2.8752    1.00     4495   131  0.2501 0.3005        
REMARK   3     8  2.8752 -  2.7500    1.00     4492   140  0.2534 0.3414        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.060           
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      :  0.006           9093                                  
REMARK   3   ANGLE     :  0.793          12347                                  
REMARK   3   CHIRALITY :  0.048           1369                                  
REMARK   3   PLANARITY :  0.005           1546                                  
REMARK   3   DIHEDRAL  : 13.137           5280                                  
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 6RUA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-MAY-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292102591.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-JUL-14                          
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                       : ID23-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8726                             
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   : 37475                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.930                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : 0.09612                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 12.7100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.69690                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.270                              
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: 1P0I                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE 12% PEG 4000 PH   
REMARK 280  7.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       38.14500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      115.67500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.10000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      115.67500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.14500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.10000            
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: 12590 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 41440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 87.0 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     LEU A   530                                                      
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     LEU B   530                                                      
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     TYR A 282    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A 506    CG   CD   OE1  OE2                                  
REMARK 470     ILE B   4    CG1  CG2  CD1                                       
REMARK 470     LYS B  51    CG   CD   CE   NZ                                   
REMARK 470     SER B  53    OG                                                  
REMARK 470     TYR B 282    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     THR B 483    OG1  CG2                                            
REMARK 470     GLN B 484    CG   CD   OE1  NE2                                  
REMARK 470     ASN B 485    CG   OD1  ND2                                       
REMARK 470     SER B 507    OG                                                  
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   ND2  ASN B   106     O5   NAG B   603              1.71            
REMARK 500   ND2  ASN A   241     O5   NAG A   607              1.84            
REMARK 500   ND2  ASN B   241     O5   NAG B   604              1.99            
REMARK 500   ND2  ASN B   455     O5   NAG B   611              2.02            
REMARK 500   ND2  ASN A    57     O5   NAG A   603              2.05            
REMARK 500   O4   NAG A   612     O5   NAG A   613              2.13            
REMARK 500   O4   NAG A   610     O5   NAG A   611              2.15            
REMARK 500   C6   NAG A   603     C1   FUC A   604              2.16            
REMARK 500   OG   SER A   198     O    HOH A   701              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OH   TYR A   237     O    ARG B   453     1545     2.07            
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    LEU A 236   CB  -  CG  -  CD2 ANGL. DEV. = -12.6 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    ASP A  54     -155.92    -81.30                                   
REMARK 500    ASN A 106       54.99   -166.13                                   
REMARK 500    PHE A 118       11.30     59.87                                   
REMARK 500    ALA A 162       79.68   -164.65                                   
REMARK 500    SER A 198     -122.70     65.57                                   
REMARK 500    LEU A 236      -53.36    -24.80                                   
REMARK 500    ASP A 297      -71.14   -122.92                                   
REMARK 500    TYR A 332       44.31    -98.53                                   
REMARK 500    SER A 362     -178.70    -60.17                                   
REMARK 500    GLU A 383        5.05    -63.75                                   
REMARK 500    PHE A 398      -56.17   -128.04                                   
REMARK 500    ARG A 453        4.76    -66.40                                   
REMARK 500    GLU A 482      -77.35    -93.77                                   
REMARK 500    LYS B   9       -3.45    -58.57                                   
REMARK 500    PHE B  43        2.35     82.16                                   
REMARK 500    ASP B  54     -141.27    -82.60                                   
REMARK 500    SER B  89      145.30   -176.58                                   
REMARK 500    ASN B 106       55.58   -149.47                                   
REMARK 500    ALA B 162       76.28   -157.93                                   
REMARK 500    ASN B 165       17.62     53.39                                   
REMARK 500    SER B 198     -113.53     62.90                                   
REMARK 500    TYR B 282       70.29   -115.77                                   
REMARK 500    ASP B 297      -69.58   -134.67                                   
REMARK 500    GLN B 311       72.83   -102.21                                   
REMARK 500    PHE B 398      -58.47   -128.59                                   
REMARK 500    ASN B 455       45.02    -68.64                                   
REMARK 500    PRO B 480       43.67    -80.78                                   
REMARK 500    GLU B 506      -73.53    -57.27                                   
REMARK 500    PHE B 525      -42.45   -131.54                                   
REMARK 500    PRO B 527        5.28    -69.38                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 792        DISTANCE =  6.05 ANGSTROMS                       
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     KJT B  620                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 620                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 623                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG B 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue KJT B 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 621                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 622                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE B 623                 
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  601 through NAG A 602 bound to ASN A 17                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  603 through FUC A 604 bound to ASN A 57                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
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: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  607 through FUC A 609 bound to ASN A 241                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 615 bound   
REMARK 800  to ASN A 341                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  610 through NAG A 611 bound to ASN A 481                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  612 through FUL A 614 bound to ASN A 486                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
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: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 602 bound   
REMARK 800  to ASN B 57                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
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: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  604 through FUL B 606 bound to ASN B 241                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  607 through FUL B 609 bound to ASN B 256                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 610 bound   
REMARK 800  to ASN B 341                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  611 through FUL B 613 bound to ASN B 455                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 614 bound   
REMARK 800  to ASN B 481                                                        
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5DYT   RELATED DB: PDB                                   
REMARK 900 5DYT CONTAINS THE SAME PROTEIN COMPLEXED WITH THE PARENT COMPOUND    
DBREF  6RUA A    1   574  UNP    P06276   CHLE_HUMAN      29    602             
DBREF  6RUA 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    FUC  A 604      10                                                       
HET    NAG  A 605      14                                                       
HET    NAG  A 606      14                                                       
HET    NAG  A 607      14                                                       
HET    NAG  A 608      14                                                       
HET    FUC  A 609      10                                                       
HET    NAG  A 610      14                                                       
HET    NAG  A 611      14                                                       
HET    NAG  A 612      14                                                       
HET    NAG  A 613      14                                                       
HET    FUL  A 614      10                                                       
HET    NAG  A 615      14                                                       
HET    EDO  A 616       4                                                       
HET    EDO  A 617       4                                                       
HET    EDO  A 618       4                                                       
HET    EDO  A 619       4                                                       
HET     CL  A 620       1                                                       
HET    EDO  A 621       4                                                       
HET     CL  A 622       1                                                       
HET    EDO  A 623       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    FUL  B 606      10                                                       
HET    NAG  B 607      14                                                       
HET    NAG  B 608      14                                                       
HET    FUL  B 609      10                                                       
HET    NAG  B 610      14                                                       
HET    NAG  B 611      14                                                       
HET    NAG  B 612      14                                                       
HET    FUL  B 613      10                                                       
HET    NAG  B 614      14                                                       
HET    PEG  B 615       7                                                       
HET    EDO  B 616       4                                                       
HET    EDO  B 617       4                                                       
HET    EDO  B 618       4                                                       
HET     CL  B 619       1                                                       
HET    KJT  B 620      29                                                       
HET     CL  B 621       1                                                       
HET     CL  B 622       1                                                       
HET    PGE  B 623      10                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     FUL BETA-L-FUCOSE                                                    
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM      CL CHLORIDE ION                                                     
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     KJT DIETHYL-[6-[[2-[2-[2-[NAPHTHALEN-2-YLSULFONYL-                   
HETNAM   2 KJT  [[(3~{R})-1-(PHENYLMETHYL)PIPERIDIN-3-                          
HETNAM   3 KJT  YL]METHYL]AMINO]ETHOXY]ETHOXY]ETHYLAMINO]-OXIDANYL-             
HETNAM   4 KJT  METHYL]-7-OXIDANYLIDENE-1,3,4,4~{A},5,6,8,8~{A}-                
HETNAM   5 KJT  OCTAHYDRONAPHTHALEN-2-YLIDENE]AZANIUM                           
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETSYN     FUL 6-DEOXY-BETA-L-GALACTOSE                                         
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  NAG    23(C8 H15 N O6)                                              
FORMUL   4  FUC    2(C6 H12 O5)                                                 
FORMUL   8  FUL    4(C6 H12 O5)                                                 
FORMUL  10  EDO    9(C2 H6 O2)                                                  
FORMUL  14   CL    5(CL 1-)                                                     
FORMUL  26  PEG    C4 H10 O3                                                    
FORMUL  31  KJT    C44 H63 N4 O6 S 1+                                           
FORMUL  34  PGE    C6 H14 O4                                                    
FORMUL  35  HOH   *175(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 GLY A  149  LEU A  154  1                                   6    
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 SER A  210  SER A  215  1                                   6    
HELIX   10 AB1 SER A  235  GLY A  251  1                                  17    
HELIX   11 AB2 ASN A  256  ARG A  265  1                                  10    
HELIX   12 AB3 ASP A  268  LEU A  274  1                                   7    
HELIX   13 AB4 ASN A  275  VAL A  280  5                                   6    
HELIX   14 AB5 MET A  302  LEU A  309  1                                   8    
HELIX   15 AB6 GLY A  326  LEU A  330  5                                   5    
HELIX   16 AB7 THR A  346  PHE A  358  1                                  13    
HELIX   17 AB8 SER A  362  TYR A  373  1                                  12    
HELIX   18 AB9 GLU A  383  PHE A  398  1                                  16    
HELIX   19 AC1 PHE A  398  GLU A  411  1                                  14    
HELIX   20 AC2 PRO A  431  GLY A  435  5                                   5    
HELIX   21 AC3 GLU A  441  PHE A  446  1                                   6    
HELIX   22 AC4 GLY A  447  ASN A  455  5                                   9    
HELIX   23 AC5 THR A  457  GLY A  478  1                                  22    
HELIX   24 AC6 ARG A  515  PHE A  525  1                                  11    
HELIX   25 AC7 PHE A  526  VAL A  529  5                                   4    
HELIX   26 AC8 LEU B   38  ARG B   42  5                                   5    
HELIX   27 AC9 PHE B   76  MET B   81  1                                   6    
HELIX   28 AD1 LEU B  125  ASP B  129  5                                   5    
HELIX   29 AD2 GLY B  130  ARG B  138  1                                   9    
HELIX   30 AD3 GLY B  149  LEU B  154  1                                   6    
HELIX   31 AD4 ASN B  165  ILE B  182  1                                  18    
HELIX   32 AD5 SER B  198  LEU B  208  1                                  11    
HELIX   33 AD6 SER B  210  PHE B  217  5                                   8    
HELIX   34 AD7 SER B  235  THR B  250  1                                  16    
HELIX   35 AD8 ASN B  256  ARG B  265  1                                  10    
HELIX   36 AD9 ASP B  268  LEU B  274  1                                   7    
HELIX   37 AE1 ASN B  275  VAL B  279  5                                   5    
HELIX   38 AE2 MET B  302  GLY B  310  1                                   9    
HELIX   39 AE3 GLY B  326  VAL B  331  1                                   6    
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  GLY B  447  1                                   7    
HELIX   46 AF1 LEU B  448  GLU B  451  5                                   4    
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  THR A  19  0                                        
SHEET    2 AA211 THR A  24  PRO A  32 -1  O  ALA A  27   N  MET A  16           
SHEET    3 AA211 TYR A  94  ALA A 101 -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  LEU A 110   O  ILE A 140           
SHEET    6 AA211 GLY A 187  GLU A 197  1  O  ASN A 188   N  ALA A 107           
SHEET    7 AA211 ARG A 219  GLN A 223  1  O  GLN A 223   N  GLY A 196           
SHEET    8 AA211 ILE A 317  ASN A 322  1  O  LEU A 318   N  LEU A 222           
SHEET    9 AA211 ALA A 416  PHE A 421  1  O  PHE A 417   N  VAL A 319           
SHEET   10 AA211 LYS A 499  LEU A 503  1  O  LEU A 503   N  TYR A 420           
SHEET   11 AA211 ILE A 510  THR A 512 -1  O  MET A 511   N  TYR A 500           
SHEET    1 AA3 3 ILE B   5  THR B   8  0                                        
SHEET    2 AA3 3 GLY B  11  ARG B  14 -1  O  GLY B  11   N  THR B   8           
SHEET    3 AA3 3 ILE B  55  ASN B  57  1  O  TRP B  56   N  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  VAL B  97   N  PHE B  28           
SHEET    4 AA411 ILE B 140  MET B 144 -1  O  SER B 143   N  ASN B  96           
SHEET    5 AA411 ALA B 107  ILE B 113  1  N  TRP B 112   O  VAL B 142           
SHEET    6 AA411 GLY B 187  GLU B 197  1  O  ASN B 188   N  ALA B 107           
SHEET    7 AA411 ARG B 219  GLN B 223  1  O  ARG B 219   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 421   N  VAL B 321           
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           
SSBOND   1 CYS A   65    CYS A   92                          1555   1555  2.03  
SSBOND   2 CYS A  252    CYS A  263                          1555   1555  2.04  
SSBOND   3 CYS A  400    CYS A  519                          1555   1555  2.05  
SSBOND   4 CYS B   65    CYS B   92                          1555   1555  2.04  
SSBOND   5 CYS B  252    CYS B  263                          1555   1555  2.03  
SSBOND   6 CYS B  400    CYS B  519                          1555   1555  2.04  
LINK         ND2 ASN A  17                 C1  NAG A 601     1555   1555  1.46  
LINK         ND2 ASN A  57                 C1  NAG A 603     1555   1555  1.47  
LINK         ND2 ASN A 106                 C1  NAG A 605     1555   1555  1.44  
LINK         ND2 ASN A 241                 C1  NAG A 607     1555   1555  1.41  
LINK         ND2 ASN A 341                 C1  NAG A 615     1555   1555  1.47  
LINK         ND2 ASN A 481                 C1  NAG A 610     1555   1555  1.47  
LINK         ND2 ASN A 486                 C1  NAG A 612     1555   1555  1.49  
LINK         ND2 ASN B  17                 C1  NAG B 601     1555   1555  1.47  
LINK         ND2 ASN B  57                 C1  NAG B 602     1555   1555  1.48  
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 607     1555   1555  1.45  
LINK         ND2 ASN B 341                 C1  NAG B 610     1555   1555  1.49  
LINK         ND2 ASN B 455                 C1  NAG B 611     1555   1555  1.55  
LINK         ND2 ASN B 481                 C1  NAG B 614     1555   1555  1.49  
LINK         O4  NAG A 601                 C1  NAG A 602     1555   1555  1.46  
LINK         O6  NAG A 603                 C1  FUC A 604     1555   1555  1.43  
LINK         O4  NAG A 605                 C1  NAG A 606     1555   1555  1.48  
LINK         O4  NAG A 607                 C1  NAG A 608     1555   1555  1.45  
LINK         O6  NAG A 607                 C1  FUC A 609     1555   1555  1.47  
LINK         O4  NAG A 610                 C1  NAG A 611     1555   1555  1.51  
LINK         O4  NAG A 612                 C1  NAG A 613     1555   1555  1.50  
LINK         O6  NAG A 612                 C1  FUL A 614     1555   1555  1.47  
LINK         O4  NAG B 604                 C1  NAG B 605     1555   1555  1.45  
LINK         O6  NAG B 604                 C1  FUL B 606     1555   1555  1.52  
LINK         O4  NAG B 607                 C1  NAG B 608     1555   1555  1.46  
LINK         O6  NAG B 607                 C1  FUL B 609     1555   1555  1.45  
LINK         O4  NAG B 611                 C1  NAG B 612     1555   1555  1.45  
LINK         O6  NAG B 611                 C1  FUL B 613     1555   1555  1.46  
CISPEP   1 ALA A  101    PRO A  102          0         3.88                     
CISPEP   2 ALA B  101    PRO B  102          0         3.33                     
SITE     1 AC1  2 HIS A  77  GLU A 443                                          
SITE     1 AC2  3 LYS A 494  THR A 496  HOH A 757                               
SITE     1 AC3  1 GLY A 116                                                     
SITE     1 AC4  5 TYR A  33  SER A  48  LEU A  49  GLN A 176                    
SITE     2 AC4  5 LYS A 180                                                     
SITE     1 AC5  1 ARG A 386                                                     
SITE     1 AC6  4 ASN A 106  THR A 108  ASN A 188  LYS A 476                    
SITE     1 AC7  5 ASN A 228  CYS A 400  PRO A 401  THR A 523                    
SITE     2 AC7  5 HOH A 708                                                     
SITE     1 AC8  7 HIS B  77  SER B 425  LYS B 427  LEU B 428                    
SITE     2 AC8  7 PRO B 429  GLU B 443  TYR B 456                               
SITE     1 AC9  6 PHE A 525  HOH A 744  SER B 368  PHE B 371                    
SITE     2 AC9  6 HIS B 372  PHE B 525                                          
SITE     1 AD1  5 THR B 284  LEU B 286  PHE B 357  ASN B 397                    
SITE     2 AD1  5 HOH B 730                                                     
SITE     1 AD2  7 GLN B  35  PRO B  37  LEU B  41  LYS B  44                    
SITE     2 AD2  7 LYS B  45  PRO B  46  GLN B  47                               
SITE     1 AD3 14 GLY B 116  GLY B 117  GLN B 119  THR B 120                    
SITE     2 AD3 14 SER B 198  TRP B 231  LEU B 286  SER B 287                    
SITE     3 AD3 14 PHE B 329  TRP B 430  MET B 437  HIS B 438                    
SITE     4 AD3 14 TYR B 440  HOH B 720                                          
SITE     1 AD4  2 GLU B 197  HOH B 789                                          
SITE     1 AD5  3 ARG B  42  LYS B 267  PRO B 269                               
SITE     1 AD6 13 LYS B 323  ASP B 324  GLU B 325  GLY B 326                    
SITE     2 AD6 13 THR B 327  ARG B 386  GLU B 387  GLY B 390                    
SITE     3 AD6 13 ASP B 391  GLY B 394  ASP B 395  ILE B 399                    
SITE     4 AD6 13 HOH B 708                                                     
SITE     1 AD7  2 ASN A  17  THR A  24                                          
SITE     1 AD8  2 ILE A  55  ASN A  57                                          
SITE     1 AD9  4 ASN A 106  ASN A 188  LYS A 190  HOH A 710                    
SITE     1 AE1  5 ASN A 241  ASN A 245  PHE A 278  PRO A 281                    
SITE     2 AE1  5 FUL B 613                                                     
SITE     1 AE2  5 SER A 338  ASN A 341  HOH A 711  HOH A 754                    
SITE     2 AE2  5 HOH A 759                                                     
SITE     1 AE3  7 ASN A 479  ASN A 481  GLU A 482  GLN A 484                    
SITE     2 AE3  7 HOH A 725  LEU B  88  GLN B 270                               
SITE     1 AE4  4 ASN A 486  SER A 487  THR A 488  THR A 508                    
SITE     1 AE5  1 ASN B  17                                                     
SITE     1 AE6  2 ARG B  14  ASN B  57                                          
SITE     1 AE7  2 ASN B 106  ASN B 188                                          
SITE     1 AE8  5 TYR B 237  ASN B 241  ASN B 245  LYS B 248                    
SITE     2 AE8  5 PHE B 278                                                     
SITE     1 AE9  2 ASN B 256  GLU B 259                                          
SITE     1 AF1  2 ASN B 341  HOH B 711                                          
SITE     1 AF2  6 ARG A 240  LEU A 244  NAG A 607  LYS B 427                    
SITE     2 AF2  6 ASP B 454  ASN B 455                                          
SITE     1 AF3  2 TYR B 477  ASN B 481                                          
CRYST1   76.290   80.200  231.350  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      0.013108  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012469  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004322        0.00000                         
TER    4211      VAL A 529                                                      
TER    8385      VAL B 529                                                      
MASTER      580    0   46   49   28    0   47    6 8996    2  491   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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