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LongText Report for: 5hf9-pdb

Name Class
5hf9-pdb
HEADER    HYDROLASE                               06-JAN-16   5HF9              
TITLE     CRYSTAL STRUCTURE OF HUMAN ACETYLCHOLINESTERASE IN COMPLEX WITH       
TITLE    2 PARAOXON AND HI6                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 33 TO 574;                  
COMPND   5 SYNONYM: ACHE;                                                       
COMPND   6 EC: 3.1.1.7;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ACHE;                                                          
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    ACETYLCHOLINESTERASE, HYDROLASE                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.F.FRANKLIN,M.J.RUDOLPH,C.GINTER,M.S.CASSIDY,J.CHEUNG                
REVDAT   1   22-JUN-16 5HF9    0                                                
JRNL        AUTH   M.C.FRANKLIN,M.J.RUDOLPH,C.GINTER,M.S.CASSIDY,J.CHEUNG       
JRNL        TITL   STRUCTURES OF PARAOXON-INHIBITED HUMAN ACETYLCHOLINESTERASE  
JRNL        TITL 2 REVEAL PERTURBATIONS OF THE ACYL LOOP AND THE DIMER          
JRNL        TITL 3 INTERFACE.                                                   
JRNL        REF    PROTEINS                                   2016              
JRNL        REFN                   ESSN 1097-0134                               
JRNL        PMID   27191504                                                     
JRNL        DOI    10.1002/PROT.25073                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.42                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 106625                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5346                            
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 45.4274 -  6.8182    1.00     3746   180  0.1782 0.2017        
REMARK   3     2  6.8182 -  5.4147    1.00     3541   209  0.1636 0.1982        
REMARK   3     3  5.4147 -  4.7310    1.00     3543   170  0.1388 0.1621        
REMARK   3     4  4.7310 -  4.2988    1.00     3489   190  0.1306 0.1521        
REMARK   3     5  4.2988 -  3.9909    1.00     3482   171  0.1562 0.2110        
REMARK   3     6  3.9909 -  3.7557    0.98     3382   180  0.1914 0.2367        
REMARK   3     7  3.7557 -  3.5677    0.99     3454   168  0.2132 0.2464        
REMARK   3     8  3.5677 -  3.4125    0.99     3363   191  0.2300 0.2538        
REMARK   3     9  3.4125 -  3.2811    1.00     3466   186  0.1990 0.2263        
REMARK   3    10  3.2811 -  3.1679    1.00     3455   170  0.1965 0.2494        
REMARK   3    11  3.1679 -  3.0689    1.00     3420   178  0.1881 0.2504        
REMARK   3    12  3.0689 -  2.9812    1.00     3418   184  0.1877 0.2453        
REMARK   3    13  2.9812 -  2.9027    1.00     3459   164  0.1972 0.2576        
REMARK   3    14  2.9027 -  2.8319    1.00     3420   174  0.1923 0.2412        
REMARK   3    15  2.8319 -  2.7676    1.00     3374   192  0.1927 0.2475        
REMARK   3    16  2.7676 -  2.7087    1.00     3422   168  0.2101 0.2519        
REMARK   3    17  2.7087 -  2.6545    0.98     3342   183  0.3413 0.3984        
REMARK   3    18  2.6545 -  2.6044    1.00     3424   206  0.2550 0.2996        
REMARK   3    19  2.6044 -  2.5579    1.00     3432   163  0.2389 0.3296        
REMARK   3    20  2.5579 -  2.5145    1.00     3364   176  0.2398 0.2881        
REMARK   3    21  2.5145 -  2.4740    1.00     3382   206  0.2442 0.2725        
REMARK   3    22  2.4740 -  2.4359    1.00     3388   174  0.2622 0.3139        
REMARK   3    23  2.4359 -  2.4001    1.00     3414   179  0.2645 0.2707        
REMARK   3    24  2.4001 -  2.3663    1.00     3393   188  0.2818 0.3206        
REMARK   3    25  2.3663 -  2.3343    1.00     3366   181  0.2986 0.3670        
REMARK   3    26  2.3343 -  2.3040    1.00     3357   166  0.3201 0.3790        
REMARK   3    27  2.3040 -  2.2752    1.00     3399   189  0.3318 0.3460        
REMARK   3    28  2.2752 -  2.2478    0.70     2354   129  0.4917 0.5213        
REMARK   3    29  2.2478 -  2.2217    0.86     2956   150  0.4472 0.4702        
REMARK   3    30  2.2217 -  2.1967    0.97     3274   181  0.3800 0.4256        
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)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.120           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 34.06                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 48.15                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.010           8816                                  
REMARK   3   ANGLE     :  1.214          12040                                  
REMARK   3   CHIRALITY :  0.050           1286                                  
REMARK   3   PLANARITY :  0.007           1580                                  
REMARK   3   DIHEDRAL  : 14.793           3178                                  
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 5HF9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JAN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000216490.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-MAY-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.075                              
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 108212                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 7.800                              
REMARK 200  R MERGE                    (I) : 0.13000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 5.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.24                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.67500                            
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: NULL                                                  
REMARK 200 STARTING MODEL: 4EY4                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 72.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15 - 18% PEG3350, 0.2M POTASSIUM         
REMARK 280  NITRATE, PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      108.13833            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      216.27667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      216.27667            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      108.13833            
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: 7660 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 37990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 58.0 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     GLY A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     PRO A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     THR A   262                                                      
REMARK 465     GLY A   263                                                      
REMARK 465     GLY A   264                                                      
REMARK 465     PRO A   495                                                      
REMARK 465     LYS A   496                                                      
REMARK 465     ALA A   497                                                      
REMARK 465     THR A   543                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     GLY B   261                                                      
REMARK 465     ARG B   493                                                      
REMARK 465     ASP B   494                                                      
REMARK 465     PRO B   495                                                      
REMARK 465     LYS B   496                                                      
REMARK 465     THR B   543                                                      
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   O    HOH B   930     O    HOH B   934              2.10            
REMARK 500   OD1  ASP B   304     O    HOH B   701              2.12            
REMARK 500   NE2  GLN A   527     O    HOH A   702              2.17            
REMARK 500   NE2  GLN B   527     O    HOH B   702              2.18            
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  47       -5.40     76.12                                   
REMARK 500    ALA A  62       55.70   -112.68                                   
REMARK 500    SER A 203     -121.08     58.39                                   
REMARK 500    ASP A 306      -90.83    -87.70                                   
REMARK 500    VAL A 407      -62.48   -126.28                                   
REMARK 500    SER A 462       -8.36    -58.30                                   
REMARK 500    ASP A 514     -168.20   -162.48                                   
REMARK 500    SER A 541      -75.06    -55.19                                   
REMARK 500    PHE B  47       -0.90     73.72                                   
REMARK 500    ALA B  62       70.72   -103.49                                   
REMARK 500    ALA B 167       75.09   -153.93                                   
REMARK 500    SER B 203     -124.47     59.02                                   
REMARK 500    ASP B 306      -92.00   -101.55                                   
REMARK 500    TYR B 341       35.36    -98.60                                   
REMARK 500    HIS B 387       57.21   -146.46                                   
REMARK 500    VAL B 407      -61.89   -127.87                                   
REMARK 500    ASN B 464       51.55   -112.03                                   
REMARK 500    GLU B 491      109.84    -56.35                                   
REMARK 500    ARG B 525       58.61     37.32                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DEP A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HI6 A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PE8 B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NO3 B 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HI6 B 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  601 through NAG A 603 bound to ASN A 350                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 604 bound   
REMARK 800  to ASN B 265                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  601 through NAG B 603 bound to ASN B 350                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide DEP B 605 and SER B    
REMARK 800  203                                                                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5HF5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5HF6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5HF8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5HFA   RELATED DB: PDB                                   
DBREF  5HF9 A    2   543  UNP    P22303   ACES_HUMAN      33    574             
DBREF  5HF9 B    2   543  UNP    P22303   ACES_HUMAN      33    574             
SEQRES   1 A  542  GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY          
SEQRES   2 A  542  GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY          
SEQRES   3 A  542  PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO          
SEQRES   4 A  542  PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS          
SEQRES   5 A  542  GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN          
SEQRES   6 A  542  SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY          
SEQRES   7 A  542  PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU          
SEQRES   8 A  542  SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR          
SEQRES   9 A  542  PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE          
SEQRES  10 A  542  TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP          
SEQRES  11 A  542  VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR          
SEQRES  12 A  542  VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY          
SEQRES  13 A  542  PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN          
SEQRES  14 A  542  VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL          
SEQRES  15 A  542  GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER          
SEQRES  16 A  542  VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL          
SEQRES  17 A  542  GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE          
SEQRES  18 A  542  HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO          
SEQRES  19 A  542  TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA          
SEQRES  20 A  542  THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY          
SEQRES  21 A  542  THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG          
SEQRES  22 A  542  THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS          
SEQRES  23 A  542  VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL          
SEQRES  24 A  542  PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU          
SEQRES  25 A  542  ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL          
SEQRES  26 A  542  LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU          
SEQRES  27 A  542  VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER          
SEQRES  28 A  542  LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL          
SEQRES  29 A  542  GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL          
SEQRES  30 A  542  VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO          
SEQRES  31 A  542  ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP          
SEQRES  32 A  542  HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG          
SEQRES  33 A  542  LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE          
SEQRES  34 A  542  GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP MET          
SEQRES  35 A  542  GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY          
SEQRES  36 A  542  ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU          
SEQRES  37 A  542  LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN          
SEQRES  38 A  542  PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO          
SEQRES  39 A  542  LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN          
SEQRES  40 A  542  GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG          
SEQRES  41 A  542  ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG          
SEQRES  42 A  542  PHE LEU PRO LYS LEU LEU SER ALA THR                          
SEQRES   1 B  542  GLY ARG GLU ASP ALA GLU LEU LEU VAL THR VAL ARG GLY          
SEQRES   2 B  542  GLY ARG LEU ARG GLY ILE ARG LEU LYS THR PRO GLY GLY          
SEQRES   3 B  542  PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO          
SEQRES   4 B  542  PRO MET GLY PRO ARG ARG PHE LEU PRO PRO GLU PRO LYS          
SEQRES   5 B  542  GLN PRO TRP SER GLY VAL VAL ASP ALA THR THR PHE GLN          
SEQRES   6 B  542  SER VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO GLY          
SEQRES   7 B  542  PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU LEU          
SEQRES   8 B  542  SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO TYR          
SEQRES   9 B  542  PRO ARG PRO THR SER PRO THR PRO VAL LEU VAL TRP ILE          
SEQRES  10 B  542  TYR GLY GLY GLY PHE TYR SER GLY ALA SER SER LEU ASP          
SEQRES  11 B  542  VAL TYR ASP GLY ARG PHE LEU VAL GLN ALA GLU ARG THR          
SEQRES  12 B  542  VAL LEU VAL SER MET ASN TYR ARG VAL GLY ALA PHE GLY          
SEQRES  13 B  542  PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY ASN          
SEQRES  14 B  542  VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP VAL          
SEQRES  15 B  542  GLN GLU ASN VAL ALA ALA PHE GLY GLY ASP PRO THR SER          
SEQRES  16 B  542  VAL THR LEU PHE GLY GLU SER ALA GLY ALA ALA SER VAL          
SEQRES  17 B  542  GLY MET HIS LEU LEU SER PRO PRO SER ARG GLY LEU PHE          
SEQRES  18 B  542  HIS ARG ALA VAL LEU GLN SER GLY ALA PRO ASN GLY PRO          
SEQRES  19 B  542  TRP ALA THR VAL GLY MET GLY GLU ALA ARG ARG ARG ALA          
SEQRES  20 B  542  THR GLN LEU ALA HIS LEU VAL GLY CYS PRO PRO GLY GLY          
SEQRES  21 B  542  THR GLY GLY ASN ASP THR GLU LEU VAL ALA CYS LEU ARG          
SEQRES  22 B  542  THR ARG PRO ALA GLN VAL LEU VAL ASN HIS GLU TRP HIS          
SEQRES  23 B  542  VAL LEU PRO GLN GLU SER VAL PHE ARG PHE SER PHE VAL          
SEQRES  24 B  542  PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO GLU          
SEQRES  25 B  542  ALA LEU ILE ASN ALA GLY ASP PHE HIS GLY LEU GLN VAL          
SEQRES  26 B  542  LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE LEU          
SEQRES  27 B  542  VAL TYR GLY ALA PRO GLY PHE SER LYS ASP ASN GLU SER          
SEQRES  28 B  542  LEU ILE SER ARG ALA GLU PHE LEU ALA GLY VAL ARG VAL          
SEQRES  29 B  542  GLY VAL PRO GLN VAL SER ASP LEU ALA ALA GLU ALA VAL          
SEQRES  30 B  542  VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP PRO          
SEQRES  31 B  542  ALA ARG LEU ARG GLU ALA LEU SER ASP VAL VAL GLY ASP          
SEQRES  32 B  542  HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY ARG          
SEQRES  33 B  542  LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR VAL PHE          
SEQRES  34 B  542  GLU HIS ARG ALA SER THR LEU SER TRP PRO LEU TRP MET          
SEQRES  35 B  542  GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE GLY          
SEQRES  36 B  542  ILE PRO LEU ASP PRO SER ARG ASN TYR THR ALA GLU GLU          
SEQRES  37 B  542  LYS ILE PHE ALA GLN ARG LEU MET ARG TYR TRP ALA ASN          
SEQRES  38 B  542  PHE ALA ARG THR GLY ASP PRO ASN GLU PRO ARG ASP PRO          
SEQRES  39 B  542  LYS ALA PRO GLN TRP PRO PRO TYR THR ALA GLY ALA GLN          
SEQRES  40 B  542  GLN TYR VAL SER LEU ASP LEU ARG PRO LEU GLU VAL ARG          
SEQRES  41 B  542  ARG GLY LEU ARG ALA GLN ALA CYS ALA PHE TRP ASN ARG          
SEQRES  42 B  542  PHE LEU PRO LYS LEU LEU SER ALA THR                          
HET    NAG  A 601      14                                                       
HET    FUC  A 602      10                                                       
HET    NAG  A 603      14                                                       
HET    DEP  A 604       8                                                       
HET    EDO  A 605       4                                                       
HET    EDO  A 606       4                                                       
HET    HI6  A 607      21                                                       
HET    NAG  B 601      14                                                       
HET    FUC  B 602      10                                                       
HET    NAG  B 603      14                                                       
HET    NAG  B 604      14                                                       
HET    DEP  B 605       8                                                       
HET    PE8  B 606      25                                                       
HET    EDO  B 607       4                                                       
HET    EDO  B 608       4                                                       
HET    NO3  B 609       4                                                       
HET    HI6  B 610      21                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     DEP DIETHYL PHOSPHONATE                                              
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     HI6 4-(AMINOCARBONYL)-1-[({2-[(E)-(HYDROXYIMINO)                     
HETNAM   2 HI6  METHYL]PYRIDINIUM-1-YL}METHOXY)METHYL]PYRIDINIUM                
HETNAM     PE8 3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL                    
HETNAM     NO3 NITRATE ION                                                      
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     HI6 1-(2-HYDROXY-IMINOMETHYLPYRIDINIUM)-1-(4-CARBOXYAMINO)-          
HETSYN   2 HI6  PYRIDINIUM DIMETHYLETHER                                        
FORMUL   3  NAG    5(C8 H15 N O6)                                               
FORMUL   3  FUC    2(C6 H12 O5)                                                 
FORMUL   4  DEP    2(C4 H11 O3 P)                                               
FORMUL   5  EDO    4(C2 H6 O2)                                                  
FORMUL   7  HI6    2(C14 H16 N4 O3 2+)                                          
FORMUL  11  PE8    C16 H34 O9                                                   
FORMUL  14  NO3    N O3 1-                                                      
FORMUL  16  HOH   *590(H2 O)                                                    
HELIX    1 AA1 ASP A    5  GLU A    7  5                                   3    
HELIX    2 AA2 MET A   42  ARG A   46  5                                   5    
HELIX    3 AA3 PHE A   80  MET A   85  1                                   6    
HELIX    4 AA4 LEU A  130  ASP A  134  5                                   5    
HELIX    5 AA5 GLY A  135  ARG A  143  1                                   9    
HELIX    6 AA6 VAL A  153  LEU A  159  1                                   7    
HELIX    7 AA7 ASN A  170  VAL A  187  1                                  18    
HELIX    8 AA8 ALA A  188  PHE A  190  5                                   3    
HELIX    9 AA9 SER A  203  LEU A  214  1                                  12    
HELIX   10 AB1 SER A  215  GLY A  220  1                                   6    
HELIX   11 AB2 MET A  241  VAL A  255  1                                  15    
HELIX   12 AB3 ASP A  266  THR A  275  1                                  10    
HELIX   13 AB4 PRO A  277  GLU A  285  1                                   9    
HELIX   14 AB5 TRP A  286  LEU A  289  5                                   4    
HELIX   15 AB6 THR A  311  GLY A  319  1                                   9    
HELIX   16 AB7 GLY A  335  VAL A  340  1                                   6    
HELIX   17 AB8 SER A  355  VAL A  367  1                                  13    
HELIX   18 AB9 SER A  371  THR A  383  1                                  13    
HELIX   19 AC1 ASP A  390  VAL A  407  1                                  18    
HELIX   20 AC2 VAL A  407  GLN A  421  1                                  15    
HELIX   21 AC3 PRO A  440  GLY A  444  5                                   5    
HELIX   22 AC4 GLU A  450  PHE A  455  1                                   6    
HELIX   23 AC5 GLY A  456  ASP A  460  5                                   5    
HELIX   24 AC6 THR A  466  GLY A  487  1                                  22    
HELIX   25 AC7 ARG A  525  ARG A  534  1                                  10    
HELIX   26 AC8 ARG A  534  ALA A  542  1                                   9    
HELIX   27 AC9 ASP B    5  GLU B    7  5                                   3    
HELIX   28 AD1 MET B   42  ARG B   46  5                                   5    
HELIX   29 AD2 PHE B   80  MET B   85  1                                   6    
HELIX   30 AD3 LEU B  130  ASP B  134  5                                   5    
HELIX   31 AD4 GLY B  135  ARG B  143  1                                   9    
HELIX   32 AD5 VAL B  153  LEU B  159  1                                   7    
HELIX   33 AD6 ASN B  170  VAL B  187  1                                  18    
HELIX   34 AD7 ALA B  188  PHE B  190  5                                   3    
HELIX   35 AD8 SER B  203  LEU B  214  1                                  12    
HELIX   36 AD9 SER B  215  GLY B  220  1                                   6    
HELIX   37 AE1 MET B  241  VAL B  255  1                                  15    
HELIX   38 AE2 ASN B  265  THR B  275  1                                  11    
HELIX   39 AE3 PRO B  277  GLU B  285  1                                   9    
HELIX   40 AE4 TRP B  286  LEU B  289  5                                   4    
HELIX   41 AE5 THR B  311  GLY B  319  1                                   9    
HELIX   42 AE6 GLY B  335  VAL B  340  1                                   6    
HELIX   43 AE7 SER B  355  VAL B  367  1                                  13    
HELIX   44 AE8 SER B  371  THR B  383  1                                  13    
HELIX   45 AE9 ASP B  390  VAL B  407  1                                  18    
HELIX   46 AF1 VAL B  407  GLN B  421  1                                  15    
HELIX   47 AF2 PRO B  440  GLY B  444  5                                   5    
HELIX   48 AF3 GLU B  450  PHE B  455  1                                   6    
HELIX   49 AF4 GLY B  456  ASP B  460  5                                   5    
HELIX   50 AF5 THR B  466  GLY B  487  1                                  22    
HELIX   51 AF6 ARG B  525  ARG B  534  1                                  10    
HELIX   52 AF7 PHE B  535  ALA B  542  1                                   8    
SHEET    1 AA1 3 LEU A   9  VAL A  12  0                                        
SHEET    2 AA1 3 GLY A  15  ARG A  18 -1  O  GLY A  15   N  VAL A  12           
SHEET    3 AA1 3 VAL A  59  ASP A  61  1  O  VAL A  60   N  ARG A  16           
SHEET    1 AA211 ILE A  20  LEU A  22  0                                        
SHEET    2 AA211 VAL A  29  PRO A  36 -1  O  VAL A  29   N  LEU A  22           
SHEET    3 AA211 TYR A  98  PRO A 104 -1  O  VAL A 101   N  PHE A  32           
SHEET    4 AA211 VAL A 145  MET A 149 -1  O  SER A 148   N  ASN A 100           
SHEET    5 AA211 THR A 112  ILE A 118  1  N  TRP A 117   O  VAL A 147           
SHEET    6 AA211 GLY A 192  GLU A 202  1  O  SER A 196   N  VAL A 114           
SHEET    7 AA211 ARG A 224  GLN A 228  1  O  VAL A 226   N  LEU A 199           
SHEET    8 AA211 GLN A 325  VAL A 331  1  O  LEU A 327   N  LEU A 227           
SHEET    9 AA211 ARG A 424  PHE A 430  1  O  PHE A 430   N  VAL A 330           
SHEET   10 AA211 GLN A 509  LEU A 513  1  O  LEU A 513   N  VAL A 429           
SHEET   11 AA211 GLU A 519  ARG A 522 -1  O  ARG A 521   N  TYR A 510           
SHEET    1 AA3 2 VAL A 239  GLY A 240  0                                        
SHEET    2 AA3 2 VAL A 302  VAL A 303  1  O  VAL A 303   N  VAL A 239           
SHEET    1 AA4 3 LEU B   9  VAL B  12  0                                        
SHEET    2 AA4 3 GLY B  15  ARG B  18 -1  O  LEU B  17   N  VAL B  10           
SHEET    3 AA4 3 VAL B  59  ASP B  61  1  O  VAL B  60   N  ARG B  16           
SHEET    1 AA511 ILE B  20  LEU B  22  0                                        
SHEET    2 AA511 VAL B  29  PRO B  36 -1  O  VAL B  29   N  LEU B  22           
SHEET    3 AA511 TYR B  98  PRO B 104 -1  O  VAL B 101   N  PHE B  32           
SHEET    4 AA511 VAL B 145  MET B 149 -1  O  SER B 148   N  ASN B 100           
SHEET    5 AA511 THR B 112  ILE B 118  1  N  TRP B 117   O  VAL B 147           
SHEET    6 AA511 GLY B 192  GLU B 202  1  O  ASP B 193   N  THR B 112           
SHEET    7 AA511 ARG B 224  GLN B 228  1  O  VAL B 226   N  LEU B 199           
SHEET    8 AA511 GLN B 325  VAL B 331  1  O  LEU B 327   N  LEU B 227           
SHEET    9 AA511 ARG B 424  PHE B 430  1  O  PHE B 430   N  VAL B 330           
SHEET   10 AA511 GLN B 509  LEU B 513  1  O  LEU B 513   N  VAL B 429           
SHEET   11 AA511 GLU B 519  ARG B 522 -1  O  ARG B 521   N  TYR B 510           
SHEET    1 AA6 2 VAL B  68  CYS B  69  0                                        
SHEET    2 AA6 2 LEU B  92  SER B  93  1  O  SER B  93   N  VAL B  68           
SHEET    1 AA7 2 VAL B 239  GLY B 240  0                                        
SHEET    2 AA7 2 VAL B 302  VAL B 303  1  O  VAL B 303   N  VAL B 239           
SSBOND   1 CYS A   69    CYS A   96                          1555   1555  2.06  
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.07  
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.05  
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.08  
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.08  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.02  
LINK         OG  SER A 203                 P  ADEP A 604     1555   1555  1.59  
LINK         ND2 ASN A 350                 C1  NAG A 601     1555   1555  1.45  
LINK         OG  SER B 203                 P  ADEP B 605     1555   1555  1.60  
LINK         ND2 ASN B 265                 C1  NAG B 604     1555   1555  1.45  
LINK         ND2 ASN B 350                 C1  NAG B 601     1555   1555  1.46  
LINK         O4  NAG A 601                 C1  NAG A 603     1555   1555  1.45  
LINK         O6  NAG A 601                 C1  FUC A 602     1555   1555  1.45  
LINK         O4  NAG B 601                 C1  NAG B 603     1555   1555  1.46  
LINK         O6  NAG B 601                 C1  FUC B 602     1555   1555  1.45  
CISPEP   1 TYR A  105    PRO A  106          0        -3.09                     
CISPEP   2 TYR B  105    PRO B  106          0         5.60                     
CISPEP   3 CYS B  257    PRO B  258          0        -1.23                     
SITE     1 AC1  9 GLY A 121  GLY A 122  SER A 203  ALA A 204                    
SITE     2 AC1  9 TRP A 236  PHE A 295  PHE A 297  HIS A 447                    
SITE     3 AC1  9 HI6 A 607                                                     
SITE     1 AC2  8 TYR A 382  THR A 383  ASP A 384  HIS A 387                    
SITE     2 AC2  8 PRO A 388  ARG A 393  ALA A 397  HOH A 721                    
SITE     1 AC3  7 GLN A 508  ALA A 526  ALA A 530  ARG A 534                    
SITE     2 AC3  7 HOH A 842  HOH A 852  HOH A 899                               
SITE     1 AC4 10 TYR A  72  TYR A 124  VAL A 282  GLU A 285                    
SITE     2 AC4 10 TRP A 286  VAL A 294  PHE A 295  TYR A 337                    
SITE     3 AC4 10 TYR A 341  DEP A 604                                          
SITE     1 AC5  8 ASN A 283  GLY B 163  MET B 241  ASP B 304                    
SITE     2 AC5  8 GLY B 305  ASP B 306  SER B 309  HOH B 710                    
SITE     1 AC6  8 TYR B 382  THR B 383  ASP B 384  HIS B 387                    
SITE     2 AC6  8 PRO B 388  ARG B 393  ALA B 397  HOH B 755                    
SITE     1 AC7  5 HOH A 728  GLN B 508  ALA B 526  ARG B 534                    
SITE     2 AC7  5 HOH B 863                                                     
SITE     1 AC8  6 VAL A 280  HIS A 284  PRO B 162  MET B 241                    
SITE     2 AC8  6 GLY B 242  ARG B 245                                          
SITE     1 AC9  9 TYR B  72  ASP B  74  TYR B 124  VAL B 282                    
SITE     2 AC9  9 GLU B 285  TRP B 286  TYR B 337  TYR B 341                    
SITE     3 AC9  9 HOH B 725                                                     
SITE     1 AD1  5 PRO A 344  GLY A 345  SER A 347  ASN A 350                    
SITE     2 AD1  5 HOH A 917                                                     
SITE     1 AD2  1 ASN B 265                                                     
SITE     1 AD3  5 PRO B 344  GLY B 345  SER B 347  ASN B 350                    
SITE     2 AD3  5 HOH B 891                                                     
SITE     1 AD4 14 GLY B 120  GLY B 121  GLY B 122  GLU B 202                    
SITE     2 AD4 14 ALA B 204  GLY B 205  ALA B 206  ALA B 207                    
SITE     3 AD4 14 GLN B 228  SER B 229  GLY B 230  TRP B 236                    
SITE     4 AD4 14 PHE B 295  HIS B 447                                          
CRYST1  105.931  105.931  324.415  90.00  90.00 120.00 P 31 2 1     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009440  0.005450  0.000000        0.00000                         
SCALE2      0.000000  0.010900  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003082        0.00000                         
TER    4175      ALA A 542                                                      
TER    8352      ALA B 542                                                      
MASTER      369    0   17   52   34    0   30    6 9051    2  210   84          
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
AcePerl Lincoln Stein Home Page
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