Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 5e4t-pdb

Name Class
5e4t-pdb
HEADER    HYDROLASE                               07-OCT-15   5E4T              
TITLE     ACETYCHOLINESTERASE METHYLENE BLUE WITH PEG                           
CAVEAT     5E4T    FUC A 602 HAS WRONG CHIRALITY AT ATOM C1 NAG A 608 HAS WRONG 
CAVEAT   2 5E4T    CHIRALITY AT ATOM C1                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ACHE;                                                       
COMPND   5 EC: 3.1.1.7                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: TORPEDO CALIFORNICA;                            
SOURCE   3 ORGANISM_COMMON: PACIFIC ELECTRIC RAY;                               
SOURCE   4 ORGANISM_TAXID: 7787                                                 
KEYWDS    INHIBITOR, HYDROLASE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    O.DYM                                                                 
REVDAT   1   30-MAR-16 5E4T    0                                                
SPRSDE     30-MAR-16 5E4T      2W9I                                             
JRNL        AUTH   O.DYM,W.SONG,C.FELDER,E.ROTH,V.SHNYROV,Y.ASHANI,Y.XU,        
JRNL        AUTH 2 R.P.JOOSTEN,L.WEINER,J.L.SUSSMAN,I.SILMAN                    
JRNL        TITL   THE IMPACT OF CRYSTALLIZATION CONDITIONS ON STRUCTURE-BASED  
JRNL        TITL 2 DRUG DESIGN: A CASE STUDY ON THE METHYLENE                   
JRNL        TITL 3 BLUE/ACETYLCHOLINESTERASE COMPLEX.                           
JRNL        REF    PROTEIN SCI.                               2016              
JRNL        REFN                   ESSN 1469-896X                               
JRNL        PMID   26990888                                                     
JRNL        DOI    10.1002/PRO.2923                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.43 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.43                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 96.23                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 35110                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.175                           
REMARK   3   R VALUE            (WORKING SET) : 0.173                           
REMARK   3   FREE R VALUE                     : 0.206                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1909                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.43                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.49                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2576                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.68                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2260                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 109                          
REMARK   3   BIN FREE R VALUE                    : 0.3030                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4206                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 325                                     
REMARK   3   SOLVENT ATOMS            : 165                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.17000                                              
REMARK   3    B22 (A**2) : 0.17000                                              
REMARK   3    B33 (A**2) : -0.56000                                             
REMARK   3    B12 (A**2) : 0.09000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.231         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.188         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.121         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.878        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.944                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4656 ; 0.005 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4326 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6270 ; 1.089 ; 2.002       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9936 ; 0.895 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   535 ; 5.736 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   204 ;31.981 ;23.971       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   692 ;12.250 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;13.398 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   674 ; 0.116 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5032 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1069 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2131 ; 0.907 ; 3.215       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2130 ; 0.906 ; 3.214       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2663 ; 1.549 ; 4.820       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2664 ; 1.549 ; 4.822       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2525 ; 1.136 ; 3.742       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2525 ; 1.136 ; 3.742       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3606 ; 1.853 ; 5.434       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  5324 ; 3.859 ;27.789       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  5325 ; 3.859 ;27.799       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     4        A   535                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.8687  64.7521  56.2321              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0215 T22:   0.0063                                     
REMARK   3      T33:   0.0613 T12:   0.0001                                     
REMARK   3      T13:  -0.0121 T23:  -0.0122                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2870 L22:   1.0798                                     
REMARK   3      L33:   1.8716 L12:  -0.0938                                     
REMARK   3      L13:   0.4055 L23:  -0.2831                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0344 S12:  -0.0315 S13:   0.0651                       
REMARK   3      S21:   0.0061 S22:  -0.0528 S23:  -0.0314                       
REMARK   3      S31:  -0.1024 S32:   0.0084 S33:   0.0184                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5E4T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-OCT-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000214364.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH3R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35368                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.430                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 96.230                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : 0.05000                            
REMARK 200   FOR THE DATA SET  : 34.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.43                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.52                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 5.500                              
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: 2W9I                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 46% PEG200 (V/V) IN 100 MM NACL/1 MM     
REMARK 280  MES, PH 6.5., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K       
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       45.69667            
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       91.39333            
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       91.39333            
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       45.69667            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8610 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22050 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 106.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ASP A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     ALA A   536                                                      
REMARK 465     CYS A   537                                                      
REMARK 465     ASP A   538                                                      
REMARK 465     GLY A   539                                                      
REMARK 465     GLU A   540                                                      
REMARK 465     LEU A   541                                                      
REMARK 465     SER A   542                                                      
REMARK 465     SER A   543                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A  19    NE   CZ   NH1  NH2                                  
REMARK 470     ASN A  42    OD1  ND2                                            
REMARK 470     LYS A  52    CE   NZ                                             
REMARK 470     GLU A  89    CD   OE1  OE2                                       
REMARK 470     GLU A 260    CD   OE1  OE2                                       
REMARK 470     GLU A 268    CD   OE1  OE2                                       
REMARK 470     GLU A 299    CD   OE1  OE2                                       
REMARK 470     LYS A 454    CG   CD   CE   NZ                                   
REMARK 470     HIS A 486    CG   ND1  CD2  CE1  NE2                             
REMARK 470     SER A 487    OG                                                  
REMARK 470     GLN A 488    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 491    CE   NZ                                             
REMARK 470     LYS A 498    CE   NZ                                             
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    VAL A  22      112.59   -163.12                                   
REMARK 500    PHE A  45      -11.50     75.01                                   
REMARK 500    SER A 108       84.88   -160.32                                   
REMARK 500    LEU A 158       79.60   -116.18                                   
REMARK 500    SER A 200     -118.34     61.88                                   
REMARK 500    GLU A 299      -74.99   -125.39                                   
REMARK 500    THR A 317     -159.05   -152.89                                   
REMARK 500    ASP A 380       59.20   -162.94                                   
REMARK 500    VAL A 400      -62.67   -130.80                                   
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 MBT A 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 623                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 625                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 626                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 627                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 628                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 629                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 630                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 631                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 632                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 633                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 634                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 636                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 637                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 638                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  601 through FUC A 602 bound to ASN A 59                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  603 through MAN A 606 bound to ASN A 416                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  607 through MAN A 611 bound to ASN A 457                            
DBREF  5E4T A    1   543  UNP    P04058   ACES_TORCA      22    564             
SEQRES   1 A  543  ASP ASP HIS SER GLU LEU LEU VAL ASN THR LYS SER GLY          
SEQRES   2 A  543  LYS VAL MET GLY THR ARG VAL PRO VAL LEU SER SER HIS          
SEQRES   3 A  543  ILE SER ALA PHE LEU GLY ILE PRO PHE ALA GLU PRO PRO          
SEQRES   4 A  543  VAL GLY ASN MET ARG PHE ARG ARG PRO GLU PRO LYS LYS          
SEQRES   5 A  543  PRO TRP SER GLY VAL TRP ASN ALA SER THR TYR PRO ASN          
SEQRES   6 A  543  ASN CYS GLN GLN TYR VAL ASP GLU GLN PHE PRO GLY PHE          
SEQRES   7 A  543  SER GLY SER GLU MET TRP ASN PRO ASN ARG GLU MET SER          
SEQRES   8 A  543  GLU ASP CYS LEU TYR LEU ASN ILE TRP VAL PRO SER PRO          
SEQRES   9 A  543  ARG PRO LYS SER THR THR VAL MET VAL TRP ILE TYR GLY          
SEQRES  10 A  543  GLY GLY PHE TYR SER GLY SER SER THR LEU ASP VAL TYR          
SEQRES  11 A  543  ASN GLY LYS TYR LEU ALA TYR THR GLU GLU VAL VAL LEU          
SEQRES  12 A  543  VAL SER LEU SER TYR ARG VAL GLY ALA PHE GLY PHE LEU          
SEQRES  13 A  543  ALA LEU HIS GLY SER GLN GLU ALA PRO GLY ASN VAL GLY          
SEQRES  14 A  543  LEU LEU ASP GLN ARG MET ALA LEU GLN TRP VAL HIS ASP          
SEQRES  15 A  543  ASN ILE GLN PHE PHE GLY GLY ASP PRO LYS THR VAL THR          
SEQRES  16 A  543  ILE PHE GLY GLU SER ALA GLY GLY ALA SER VAL GLY MET          
SEQRES  17 A  543  HIS ILE LEU SER PRO GLY SER ARG ASP LEU PHE ARG ARG          
SEQRES  18 A  543  ALA ILE LEU GLN SER GLY SER PRO ASN CYS PRO TRP ALA          
SEQRES  19 A  543  SER VAL SER VAL ALA GLU GLY ARG ARG ARG ALA VAL GLU          
SEQRES  20 A  543  LEU GLY ARG ASN LEU ASN CYS ASN LEU ASN SER ASP GLU          
SEQRES  21 A  543  GLU LEU ILE HIS CYS LEU ARG GLU LYS LYS PRO GLN GLU          
SEQRES  22 A  543  LEU ILE ASP VAL GLU TRP ASN VAL LEU PRO PHE ASP SER          
SEQRES  23 A  543  ILE PHE ARG PHE SER PHE VAL PRO VAL ILE ASP GLY GLU          
SEQRES  24 A  543  PHE PHE PRO THR SER LEU GLU SER MET LEU ASN SER GLY          
SEQRES  25 A  543  ASN PHE LYS LYS THR GLN ILE LEU LEU GLY VAL ASN LYS          
SEQRES  26 A  543  ASP GLU GLY SER PHE PHE LEU LEU TYR GLY ALA PRO GLY          
SEQRES  27 A  543  PHE SER LYS ASP SER GLU SER LYS ILE SER ARG GLU ASP          
SEQRES  28 A  543  PHE MET SER GLY VAL LYS LEU SER VAL PRO HIS ALA ASN          
SEQRES  29 A  543  ASP LEU GLY LEU ASP ALA VAL THR LEU GLN TYR THR ASP          
SEQRES  30 A  543  TRP MET ASP ASP ASN ASN GLY ILE LYS ASN ARG ASP GLY          
SEQRES  31 A  543  LEU ASP ASP ILE VAL GLY ASP HIS ASN VAL ILE CYS PRO          
SEQRES  32 A  543  LEU MET HIS PHE VAL ASN LYS TYR THR LYS PHE GLY ASN          
SEQRES  33 A  543  GLY THR TYR LEU TYR PHE PHE ASN HIS ARG ALA SER ASN          
SEQRES  34 A  543  LEU VAL TRP PRO GLU TRP MET GLY VAL ILE HIS GLY TYR          
SEQRES  35 A  543  GLU ILE GLU PHE VAL PHE GLY LEU PRO LEU VAL LYS GLU          
SEQRES  36 A  543  LEU ASN TYR THR ALA GLU GLU GLU ALA LEU SER ARG ARG          
SEQRES  37 A  543  ILE MET HIS TYR TRP ALA THR PHE ALA LYS THR GLY ASN          
SEQRES  38 A  543  PRO ASN GLU PRO HIS SER GLN GLU SER LYS TRP PRO LEU          
SEQRES  39 A  543  PHE THR THR LYS GLU GLN LYS PHE ILE ASP LEU ASN THR          
SEQRES  40 A  543  GLU PRO MET LYS VAL HIS GLN ARG LEU ARG VAL GLN MET          
SEQRES  41 A  543  CYS VAL PHE TRP ASN GLN PHE LEU PRO LYS LEU LEU ASN          
SEQRES  42 A  543  ALA THR ALA CYS ASP GLY GLU LEU SER SER                      
HET    NAG  A 601      14                                                       
HET    FUC  A 602      10                                                       
HET    NAG  A 603      14                                                       
HET    NAG  A 604      14                                                       
HET    BMA  A 605      11                                                       
HET    MAN  A 606      11                                                       
HET    NAG  A 607      14                                                       
HET    NAG  A 608      14                                                       
HET    BMA  A 609      11                                                       
HET    MAN  A 610      11                                                       
HET    MAN  A 611      11                                                       
HET    MBT  A 612      20                                                       
HET    PEG  A 613       7                                                       
HET    PEG  A 614       7                                                       
HET    PEG  A 615       7                                                       
HET    PEG  A 616       7                                                       
HET    PEG  A 617       7                                                       
HET    PEG  A 618       7                                                       
HET    PEG  A 619       7                                                       
HET    PEG  A 620       7                                                       
HET    PEG  A 621       7                                                       
HET    PEG  A 622       7                                                       
HET    PEG  A 623       7                                                       
HET    PEG  A 624       7                                                       
HET    PGE  A 625      10                                                       
HET    PGE  A 626      10                                                       
HET    PGE  A 627      10                                                       
HET    PGE  A 628      10                                                       
HET    PGE  A 629      10                                                       
HET    EDO  A 630       4                                                       
HET    EDO  A 631       4                                                       
HET    EDO  A 632       4                                                       
HET    EDO  A 633       4                                                       
HET    EDO  A 634       4                                                       
HET    EDO  A 635       4                                                       
HET    EDO  A 636       4                                                       
HET    EDO  A 637       4                                                       
HET    EDO  A 638       4                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     FUC ALPHA-L-FUCOSE                                                   
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM     MBT 3,7-BIS(DIMETHYLAMINO)PHENOTHIAZIN-5-IUM                         
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     MBT METHYLENE BLUE                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  NAG    5(C8 H15 N O6)                                               
FORMUL   2  FUC    C6 H12 O5                                                    
FORMUL   3  BMA    2(C6 H12 O6)                                                 
FORMUL   3  MAN    3(C6 H12 O6)                                                 
FORMUL   5  MBT    C16 H18 N3 S 1+                                              
FORMUL   6  PEG    12(C4 H10 O3)                                                
FORMUL  18  PGE    5(C6 H14 O4)                                                 
FORMUL  23  EDO    9(C2 H6 O2)                                                  
FORMUL  32  HOH   *165(H2 O)                                                    
HELIX    1 AA1 VAL A   40  ARG A   44  5                                   5    
HELIX    2 AA2 PHE A   78  MET A   83  1                                   6    
HELIX    3 AA3 LEU A  127  ASN A  131  5                                   5    
HELIX    4 AA4 GLY A  132  GLU A  140  1                                   9    
HELIX    5 AA5 VAL A  150  LEU A  156  1                                   7    
HELIX    6 AA6 ASN A  167  ILE A  184  1                                  18    
HELIX    7 AA7 GLN A  185  PHE A  187  5                                   3    
HELIX    8 AA8 SER A  200  SER A  212  1                                  13    
HELIX    9 AA9 SER A  215  PHE A  219  5                                   5    
HELIX   10 AB1 SER A  237  LEU A  252  1                                  16    
HELIX   11 AB2 SER A  258  LYS A  269  1                                  12    
HELIX   12 AB3 LYS A  270  GLU A  278  1                                   9    
HELIX   13 AB4 TRP A  279  LEU A  282  5                                   4    
HELIX   14 AB5 SER A  304  GLY A  312  1                                   9    
HELIX   15 AB6 GLY A  328  TYR A  334  1                                   7    
HELIX   16 AB7 SER A  348  VAL A  360  1                                  13    
HELIX   17 AB8 ASN A  364  TYR A  375  1                                  12    
HELIX   18 AB9 ASN A  383  VAL A  400  1                                  18    
HELIX   19 AC1 VAL A  400  GLY A  415  1                                  16    
HELIX   20 AC2 PRO A  433  GLY A  437  5                                   5    
HELIX   21 AC3 GLU A  443  PHE A  448  1                                   6    
HELIX   22 AC4 GLY A  449  ASN A  457  5                                   9    
HELIX   23 AC5 THR A  459  GLY A  480  1                                  22    
HELIX   24 AC6 ARG A  517  GLN A  526  1                                  10    
HELIX   25 AC7 GLN A  526  THR A  535  1                                  10    
SHEET    1 AA1 3 LEU A   7  THR A  10  0                                        
SHEET    2 AA1 3 GLY A  13  MET A  16 -1  O  VAL A  15   N  VAL A   8           
SHEET    3 AA1 3 VAL A  57  ASN A  59  1  O  TRP A  58   N  LYS A  14           
SHEET    1 AA211 THR A  18  VAL A  22  0                                        
SHEET    2 AA211 SER A  25  PRO A  34 -1  O  ILE A  27   N  VAL A  20           
SHEET    3 AA211 TYR A  96  VAL A 101 -1  O  ILE A  99   N  PHE A  30           
SHEET    4 AA211 VAL A 142  SER A 145 -1  O  SER A 145   N  ASN A  98           
SHEET    5 AA211 THR A 109  ILE A 115  1  N  TRP A 114   O  VAL A 144           
SHEET    6 AA211 GLY A 189  GLU A 199  1  O  ASP A 190   N  THR A 109           
SHEET    7 AA211 ARG A 221  GLN A 225  1  O  GLN A 225   N  GLY A 198           
SHEET    8 AA211 GLN A 318  ASN A 324  1  O  LEU A 320   N  ALA A 222           
SHEET    9 AA211 GLY A 417  PHE A 423  1  O  PHE A 423   N  VAL A 323           
SHEET   10 AA211 LYS A 501  LEU A 505  1  O  ILE A 503   N  PHE A 422           
SHEET   11 AA211 VAL A 512  GLN A 514 -1  O  HIS A 513   N  PHE A 502           
SSBOND   1 CYS A   67    CYS A   94                          1555   1555  2.06  
SSBOND   2 CYS A  254    CYS A  265                          1555   1555  2.04  
SSBOND   3 CYS A  402    CYS A  521                          1555   1555  2.05  
LINK         ND2 ASN A  59                 C1  NAG A 601     1555   1555  1.46  
LINK         ND2 ASN A 416                 C1  NAG A 603     1555   1555  1.45  
LINK         ND2 ASN A 457                 C1  NAG A 607     1555   1555  1.46  
LINK         O6  NAG A 601                 C1  FUC A 602     1555   1555  1.45  
LINK         O4  NAG A 603                 C1  NAG A 604     1555   1555  1.44  
LINK         O4  NAG A 604                 C1  BMA A 605     1555   1555  1.44  
LINK         O3  BMA A 605                 C1  MAN A 606     1555   1555  1.45  
LINK         O4  NAG A 607                 C1  NAG A 608     1555   1555  1.45  
LINK         O4  NAG A 608                 C1  BMA A 609     1555   1555  1.45  
LINK         O3  BMA A 609                 C1  MAN A 610     1555   1555  1.45  
LINK         O2  MAN A 610                 C1  MAN A 611     1555   1555  1.44  
CISPEP   1 SER A  103    PRO A  104          0         0.31                     
SITE     1 AC1  8 TYR A  70  TYR A 121  GLN A 185  TRP A 279                    
SITE     2 AC1  8 TYR A 334  PEG A 614  PGE A 625  PGE A 629                    
SITE     1 AC2  3 ASN A 230  SER A 235  HOH A 769                               
SITE     1 AC3  6 GLN A  74  HIS A 181  LYS A 192  TYR A 334                    
SITE     2 AC3  6 GLY A 335  MBT A 612                                          
SITE     1 AC4  1 ASP A 297                                                     
SITE     1 AC5  6 ARG A 105  PRO A 106  GLN A 185  PHE A 186                    
SITE     2 AC5  6 ASN A 251  PEG A 621                                          
SITE     1 AC6  2 HIS A 513  HOH A 749                                          
SITE     1 AC7  7 LYS A 325  ASP A 326  ASP A 389  ASP A 393                    
SITE     2 AC7  7 GLU A 434  EDO A 630  HOH A 762                               
SITE     1 AC8  3 TYR A  63  TRP A 100  ASN A 131                               
SITE     1 AC9  1 LYS A  14                                                     
SITE     1 AD1  3 GLU A 247  ARG A 250  PEG A 616                               
SITE     1 AD2  1 LYS A 346                                                     
SITE     1 AD3  1 LEU A 494                                                     
SITE     1 AD4  7 GLY A 117  GLY A 118  TYR A 121  GLU A 199                    
SITE     2 AD4  7 MBT A 612  HOH A 701  HOH A 736                               
SITE     1 AD5  4 VAL A  57  TRP A  58  ASN A  59  NAG A 601                    
SITE     1 AD6  2 GLU A 499  LYS A 501                                          
SITE     1 AD7  5 ASN A   9  ARG A 243  GLU A 247  VAL A 281                    
SITE     2 AD7  5 LEU A 282                                                     
SITE     1 AD8 10 LYS A  11  ASP A 182  GLN A 185  TRP A 279                    
SITE     2 AD8 10 ASP A 285  SER A 286  TYR A 334  GLY A 335                    
SITE     3 AD8 10 MBT A 612  HOH A 810                                          
SITE     1 AD9  5 GLU A 344  ILE A 385  ARG A 388  PEG A 618                    
SITE     2 AD9  5 HOH A 790                                                     
SITE     1 AE1  4 PRO A 232  ARG A 289  PRO A 361  HIS A 362                    
SITE     1 AE2  2 LYS A  11  TRP A  54                                          
SITE     1 AE3  1 TRP A 432                                                     
SITE     1 AE4  4 THR A 109  GLU A 139  GLU A 140  LYS A 478                    
SITE     1 AE5  3 ARG A  44  GLU A 268  LYS A 269                               
SITE     1 AE6  2 SER A  55  VAL A  57                                          
SITE     1 AE7  3 HIS A 406  ASN A 525  HOH A 763                               
SITE     1 AE8  3 ASN A  59  SER A  61  PGE A 626                               
SITE     1 AE9  4 ASN A 255  GLU A 261  ASN A 416  MAN A 611                    
SITE     1 AF1  7 LYS A 413  PHE A 414  GLY A 415  LEU A 456                    
SITE     2 AF1  7 ASN A 457  NAG A 603  NAG A 604                               
CRYST1  111.114  111.114  137.090  90.00  90.00 120.00 P 31 2 1      6          
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      0.009000  0.005196  0.000000        0.00000                         
SCALE2      0.000000  0.010392  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007294        0.00000                         
TER    4218      THR A 535                                                      
MASTER      443    0   38   25   14    0   38    6 4696    1  334   42          
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
webmaster

Acknowledgements and disclaimer