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LongText Report for: 6xt8-pdb

Name Class
6xt8-pdb
HEADER    HYDROLASE                               15-JAN-20   6XT8              
TITLE     CRYSTAL STRUCTURE OF HALOALKANE DEHALOGENASE VARIANT DHAA115 DOMAIN-  
TITLE    2 SWAPPED DIMER TYPE-2                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HALOALKANE DEHALOGENASE VARIANT DHAA115 DOMAIN-SWAPPED     
COMPND   3 DIMER TYPE-2;                                                        
COMPND   4 CHAIN: A, B, C, D;                                                   
COMPND   5 EC: 3.8.1.5;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE   3 ORGANISM_TAXID: 32630;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HALOALKANE DEHALOGENASE, HYDROLASE                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.MARKOVA,J.DAMBORSKY,M.MAREK                                         
REVDAT   1   27-JAN-21 6XT8    0                                                
JRNL        AUTH   K.MARKOVA,J.DAMBORSKY,M.MAREK                                
JRNL        TITL   STRUCTURES OF HALOALKANE DEHALOGENASE VARIANT DHAA115        
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.14_3260                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.53                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 141366                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.960                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7006                            
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 45.5280 -  5.2796    0.96     4436   251  0.1587 0.1574        
REMARK   3     2  5.2796 -  4.1915    0.99     4576   229  0.1345 0.1498        
REMARK   3     3  4.1915 -  3.6620    0.99     4572   232  0.1496 0.1865        
REMARK   3     4  3.6620 -  3.3273    0.93     4294   218  0.1640 0.1746        
REMARK   3     5  3.3273 -  3.0888    0.98     4518   238  0.1725 0.2067        
REMARK   3     6  3.0888 -  2.9068    0.99     4496   275  0.1848 0.2145        
REMARK   3     7  2.9068 -  2.7612    0.99     4521   246  0.1917 0.2262        
REMARK   3     8  2.7612 -  2.6410    0.99     4517   229  0.1885 0.2226        
REMARK   3     9  2.6410 -  2.5394    0.99     4634   229  0.1965 0.2510        
REMARK   3    10  2.5394 -  2.4517    0.99     4550   224  0.1955 0.2418        
REMARK   3    11  2.4517 -  2.3751    0.97     4403   220  0.2013 0.2344        
REMARK   3    12  2.3751 -  2.3072    0.93     4328   221  0.1916 0.2266        
REMARK   3    13  2.3072 -  2.2465    0.98     4426   257  0.1924 0.2448        
REMARK   3    14  2.2465 -  2.1917    0.99     4539   264  0.2071 0.2435        
REMARK   3    15  2.1917 -  2.1418    0.99     4478   230  0.2044 0.2245        
REMARK   3    16  2.1418 -  2.0962    0.99     4599   210  0.2108 0.2387        
REMARK   3    17  2.0962 -  2.0543    0.99     4450   228  0.2131 0.2501        
REMARK   3    18  2.0543 -  2.0156    0.99     4533   242  0.2202 0.2725        
REMARK   3    19  2.0156 -  1.9796    0.99     4486   253  0.2160 0.2573        
REMARK   3    20  1.9796 -  1.9460    0.99     4514   221  0.2149 0.2406        
REMARK   3    21  1.9460 -  1.9146    0.99     4564   245  0.2208 0.2649        
REMARK   3    22  1.9146 -  1.8851    0.98     4494   224  0.2256 0.2759        
REMARK   3    23  1.8851 -  1.8574    0.98     4500   197  0.2338 0.2819        
REMARK   3    24  1.8574 -  1.8313    0.92     4231   229  0.2478 0.2991        
REMARK   3    25  1.8313 -  1.8065    0.97     4378   244  0.2582 0.2920        
REMARK   3    26  1.8065 -  1.7831    0.98     4442   234  0.2611 0.3228        
REMARK   3    27  1.7831 -  1.7608    0.98     4528   219  0.2616 0.3133        
REMARK   3    28  1.7608 -  1.7395    0.98     4451   242  0.2584 0.2948        
REMARK   3    29  1.7395 -  1.7193    0.98     4446   232  0.2733 0.3066        
REMARK   3    30  1.7193 -  1.7000    0.96     4456   223  0.2898 0.3170        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.200            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.880           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.26                          
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
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 6XT8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-JAN-20.                  
REMARK 100 THE DEPOSITION ID IS D_1292106262.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-JUL-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.861                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.6.2                      
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 141424                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 4.600                              
REMARK 200  R MERGE                    (I) : 0.04700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 16.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.73                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.60100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4HZG                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, AMMONIUM NITRATE, BIS-TRIS,    
REMARK 280  PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       82.30650            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 15800 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 21900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -125.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 15430 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 21910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -130.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     HIS A   294                                                      
REMARK 465     HIS A   295                                                      
REMARK 465     HIS A   296                                                      
REMARK 465     HIS A   297                                                      
REMARK 465     HIS A   298                                                      
REMARK 465     HIS A   299                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     HIS B   295                                                      
REMARK 465     HIS B   296                                                      
REMARK 465     HIS B   297                                                      
REMARK 465     HIS B   298                                                      
REMARK 465     HIS B   299                                                      
REMARK 465     MET C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     GLU C     3                                                      
REMARK 465     HIS C   294                                                      
REMARK 465     HIS C   295                                                      
REMARK 465     HIS C   296                                                      
REMARK 465     HIS C   297                                                      
REMARK 465     HIS C   298                                                      
REMARK 465     HIS C   299                                                      
REMARK 465     MET D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     HIS D   295                                                      
REMARK 465     HIS D   296                                                      
REMARK 465     HIS D   297                                                      
REMARK 465     HIS D   298                                                      
REMARK 465     HIS D   299                                                      
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    PRO A  42       51.36   -102.53                                   
REMARK 500    THR A  43     -156.70   -107.23                                   
REMARK 500    GLU A  98      -92.81   -110.98                                   
REMARK 500    ASP A 106     -132.55     55.67                                   
REMARK 500    ASP A 156      -56.60     72.03                                   
REMARK 500    TRP A 198     -118.69     58.84                                   
REMARK 500    VAL A 245      -71.74   -129.51                                   
REMARK 500    LEU A 271      -92.90   -116.32                                   
REMARK 500    PRO B  42       52.34   -106.11                                   
REMARK 500    THR B  43     -154.11   -106.93                                   
REMARK 500    GLU B  98      -90.39   -103.90                                   
REMARK 500    ASP B 106     -131.91     53.17                                   
REMARK 500    ASP B 156      -55.75     72.60                                   
REMARK 500    TRP B 198     -113.67     55.58                                   
REMARK 500    VAL B 245      -72.24   -129.96                                   
REMARK 500    LEU B 271      -93.90   -116.88                                   
REMARK 500    PRO C  42       49.05   -101.85                                   
REMARK 500    THR C  43     -153.56   -103.94                                   
REMARK 500    GLU C  98      -86.18   -108.42                                   
REMARK 500    ASP C 106     -131.61     56.01                                   
REMARK 500    ASP C 156      -50.56     75.08                                   
REMARK 500    TRP C 198      -86.15   -118.20                                   
REMARK 500    ASN C 217      -75.90    -29.87                                   
REMARK 500    VAL C 245      -73.18   -127.18                                   
REMARK 500    LEU C 271      -95.92   -116.12                                   
REMARK 500    PRO D   9       56.13    -91.87                                   
REMARK 500    PRO D  42       53.26   -111.99                                   
REMARK 500    THR D  43     -154.81   -109.04                                   
REMARK 500    SER D  44     -169.54   -162.62                                   
REMARK 500    ASP D 106     -133.74     61.05                                   
REMARK 500    ASP D 156      -44.40     70.97                                   
REMARK 500    TRP D 198      -85.62   -122.72                                   
REMARK 500    VAL D 245      -70.16   -130.79                                   
REMARK 500    LEU D 271      -91.03   -120.44                                   
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 CL A 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PG4 A 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL C 306                  
DBREF  6XT8 A    1   299  PDB    6XT8     6XT8             1    299             
DBREF  6XT8 B    1   299  PDB    6XT8     6XT8             1    299             
DBREF  6XT8 C    1   299  PDB    6XT8     6XT8             1    299             
DBREF  6XT8 D    1   299  PDB    6XT8     6XT8             1    299             
SEQRES   1 A  299  MET SER GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS          
SEQRES   2 A  299  TYR VAL GLU VAL LEU GLY SER ARG MET HIS TYR VAL ASP          
SEQRES   3 A  299  VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS          
SEQRES   4 A  299  GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE          
SEQRES   5 A  299  PRO HIS VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP          
SEQRES   6 A  299  LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP          
SEQRES   7 A  299  TYR ARG PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE          
SEQRES   8 A  299  ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE          
SEQRES   9 A  299  HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS          
SEQRES  10 A  299  ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU          
SEQRES  11 A  299  PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU          
SEQRES  12 A  299  PHE ALA ARG GLU LEU PHE GLN ALA PHE ARG THR PRO ASP          
SEQRES  13 A  299  VAL GLY ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE          
SEQRES  14 A  299  GLU GLY ILE LEU PRO LYS PHE VAL VAL ARG PRO LEU THR          
SEQRES  15 A  299  GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS          
SEQRES  16 A  299  PRO VAL TRP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU          
SEQRES  17 A  299  LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE TRP ALA LEU          
SEQRES  18 A  299  VAL GLU ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL          
SEQRES  19 A  299  PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE          
SEQRES  20 A  299  PRO PRO ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO          
SEQRES  21 A  299  ASN LEU LYS THR VAL PHE ILE GLY PRO GLY LEU HIS TYR          
SEQRES  22 A  299  LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE          
SEQRES  23 A  299  ALA ARG TRP LEU PRO ALA LEU HIS HIS HIS HIS HIS HIS          
SEQRES   1 B  299  MET SER GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS          
SEQRES   2 B  299  TYR VAL GLU VAL LEU GLY SER ARG MET HIS TYR VAL ASP          
SEQRES   3 B  299  VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS          
SEQRES   4 B  299  GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE          
SEQRES   5 B  299  PRO HIS VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP          
SEQRES   6 B  299  LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP          
SEQRES   7 B  299  TYR ARG PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE          
SEQRES   8 B  299  ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE          
SEQRES   9 B  299  HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS          
SEQRES  10 B  299  ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU          
SEQRES  11 B  299  PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU          
SEQRES  12 B  299  PHE ALA ARG GLU LEU PHE GLN ALA PHE ARG THR PRO ASP          
SEQRES  13 B  299  VAL GLY ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE          
SEQRES  14 B  299  GLU GLY ILE LEU PRO LYS PHE VAL VAL ARG PRO LEU THR          
SEQRES  15 B  299  GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS          
SEQRES  16 B  299  PRO VAL TRP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU          
SEQRES  17 B  299  LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE TRP ALA LEU          
SEQRES  18 B  299  VAL GLU ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL          
SEQRES  19 B  299  PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE          
SEQRES  20 B  299  PRO PRO ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO          
SEQRES  21 B  299  ASN LEU LYS THR VAL PHE ILE GLY PRO GLY LEU HIS TYR          
SEQRES  22 B  299  LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE          
SEQRES  23 B  299  ALA ARG TRP LEU PRO ALA LEU HIS HIS HIS HIS HIS HIS          
SEQRES   1 C  299  MET SER GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS          
SEQRES   2 C  299  TYR VAL GLU VAL LEU GLY SER ARG MET HIS TYR VAL ASP          
SEQRES   3 C  299  VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS          
SEQRES   4 C  299  GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE          
SEQRES   5 C  299  PRO HIS VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP          
SEQRES   6 C  299  LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP          
SEQRES   7 C  299  TYR ARG PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE          
SEQRES   8 C  299  ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE          
SEQRES   9 C  299  HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS          
SEQRES  10 C  299  ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU          
SEQRES  11 C  299  PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU          
SEQRES  12 C  299  PHE ALA ARG GLU LEU PHE GLN ALA PHE ARG THR PRO ASP          
SEQRES  13 C  299  VAL GLY ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE          
SEQRES  14 C  299  GLU GLY ILE LEU PRO LYS PHE VAL VAL ARG PRO LEU THR          
SEQRES  15 C  299  GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS          
SEQRES  16 C  299  PRO VAL TRP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU          
SEQRES  17 C  299  LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE TRP ALA LEU          
SEQRES  18 C  299  VAL GLU ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL          
SEQRES  19 C  299  PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE          
SEQRES  20 C  299  PRO PRO ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO          
SEQRES  21 C  299  ASN LEU LYS THR VAL PHE ILE GLY PRO GLY LEU HIS TYR          
SEQRES  22 C  299  LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE          
SEQRES  23 C  299  ALA ARG TRP LEU PRO ALA LEU HIS HIS HIS HIS HIS HIS          
SEQRES   1 D  299  MET SER GLU ILE GLY THR GLY PHE PRO PHE ASP PRO HIS          
SEQRES   2 D  299  TYR VAL GLU VAL LEU GLY SER ARG MET HIS TYR VAL ASP          
SEQRES   3 D  299  VAL GLY PRO ARG ASP GLY THR PRO VAL LEU PHE LEU HIS          
SEQRES   4 D  299  GLY ASN PRO THR SER SER TYR LEU TRP ARG ASN ILE ILE          
SEQRES   5 D  299  PRO HIS VAL ALA PRO SER HIS ARG CYS ILE ALA PRO ASP          
SEQRES   6 D  299  LEU ILE GLY MET GLY LYS SER ASP LYS PRO ASP LEU ASP          
SEQRES   7 D  299  TYR ARG PHE ASP ASP HIS VAL ARG TYR LEU ASP ALA PHE          
SEQRES   8 D  299  ILE GLU ALA LEU GLY LEU GLU GLU VAL VAL LEU VAL ILE          
SEQRES   9 D  299  HIS ASP TRP GLY SER ALA LEU GLY PHE HIS TRP ALA LYS          
SEQRES  10 D  299  ARG ASN PRO GLU ARG VAL LYS GLY ILE ALA PHE MET GLU          
SEQRES  11 D  299  PHE ILE ARG PRO ILE PRO THR TRP ASP GLU TRP PRO GLU          
SEQRES  12 D  299  PHE ALA ARG GLU LEU PHE GLN ALA PHE ARG THR PRO ASP          
SEQRES  13 D  299  VAL GLY ARG GLU LEU ILE ILE ASP GLN ASN ALA PHE ILE          
SEQRES  14 D  299  GLU GLY ILE LEU PRO LYS PHE VAL VAL ARG PRO LEU THR          
SEQRES  15 D  299  GLU VAL GLU MET ASP HIS TYR ARG GLU PRO PHE LEU LYS          
SEQRES  16 D  299  PRO VAL TRP ARG GLU PRO LEU TRP ARG PHE PRO ASN GLU          
SEQRES  17 D  299  LEU PRO ILE ALA GLY GLU PRO ALA ASN ILE TRP ALA LEU          
SEQRES  18 D  299  VAL GLU ALA TYR MET ASN TRP LEU HIS GLN SER PRO VAL          
SEQRES  19 D  299  PRO LYS LEU LEU PHE TRP GLY THR PRO GLY VAL LEU ILE          
SEQRES  20 D  299  PRO PRO ALA GLU ALA ALA ARG LEU ALA GLU SER LEU PRO          
SEQRES  21 D  299  ASN LEU LYS THR VAL PHE ILE GLY PRO GLY LEU HIS TYR          
SEQRES  22 D  299  LEU GLN GLU ASP ASN PRO ASP LEU ILE GLY SER GLU ILE          
SEQRES  23 D  299  ALA ARG TRP LEU PRO ALA LEU HIS HIS HIS HIS HIS HIS          
HET     CL  A 301       1                                                       
HET    GOL  A 302       6                                                       
HET    GOL  A 303       6                                                       
HET    PG4  A 304      13                                                       
HET    EDO  A 305       4                                                       
HET     CL  B 301       1                                                       
HET    GOL  B 302       6                                                       
HET    GOL  B 303       6                                                       
HET     CL  C 301       1                                                       
HET    GOL  C 302       6                                                       
HET    GOL  C 303       6                                                       
HET    GOL  C 304       6                                                       
HET    EDO  C 305       4                                                       
HET     CL  C 306       1                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   5   CL    4(CL 1-)                                                     
FORMUL   6  GOL    7(C3 H8 O3)                                                  
FORMUL   8  PG4    C8 H18 O5                                                    
FORMUL   9  EDO    2(C2 H6 O2)                                                  
FORMUL  19  HOH   *683(H2 O)                                                    
HELIX    1 AA1 SER A   44  ARG A   49  5                                   6    
HELIX    2 AA2 ILE A   51  ALA A   56  1                                   6    
HELIX    3 AA3 ARG A   80  LEU A   95  1                                  16    
HELIX    4 AA4 ASP A  106  ASN A  119  1                                  14    
HELIX    5 AA5 THR A  137  TRP A  141  5                                   5    
HELIX    6 AA6 PRO A  142  ARG A  153  1                                  12    
HELIX    7 AA7 ASP A  156  ILE A  163  1                                   8    
HELIX    8 AA8 ASN A  166  GLY A  171  1                                   6    
HELIX    9 AA9 GLY A  171  PHE A  176  1                                   6    
HELIX   10 AB1 THR A  182  GLU A  191  1                                  10    
HELIX   11 AB2 PRO A  192  LEU A  194  5                                   3    
HELIX   12 AB3 ARG A  199  LEU A  209  1                                  11    
HELIX   13 AB4 PRO A  215  SER A  232  1                                  18    
HELIX   14 AB5 PRO A  248  LEU A  259  1                                  12    
HELIX   15 AB6 TYR A  273  ASN A  278  1                                   6    
HELIX   16 AB7 ASN A  278  LEU A  290  1                                  13    
HELIX   17 AB8 PRO A  291  LEU A  293  5                                   3    
HELIX   18 AB9 SER B   44  ARG B   49  5                                   6    
HELIX   19 AC1 ILE B   51  ALA B   56  1                                   6    
HELIX   20 AC2 ARG B   80  LEU B   95  1                                  16    
HELIX   21 AC3 ASP B  106  ASN B  119  1                                  14    
HELIX   22 AC4 THR B  137  TRP B  141  5                                   5    
HELIX   23 AC5 PRO B  142  ARG B  153  1                                  12    
HELIX   24 AC6 ASP B  156  ILE B  163  1                                   8    
HELIX   25 AC7 ASN B  166  GLY B  171  1                                   6    
HELIX   26 AC8 GLY B  171  PHE B  176  1                                   6    
HELIX   27 AC9 THR B  182  GLU B  191  1                                  10    
HELIX   28 AD1 PRO B  192  LEU B  194  5                                   3    
HELIX   29 AD2 ARG B  199  PHE B  205  1                                   7    
HELIX   30 AD3 PRO B  206  LEU B  209  5                                   4    
HELIX   31 AD4 PRO B  215  SER B  232  1                                  18    
HELIX   32 AD5 PRO B  248  LEU B  259  1                                  12    
HELIX   33 AD6 TYR B  273  ASN B  278  1                                   6    
HELIX   34 AD7 ASN B  278  LEU B  290  1                                  13    
HELIX   35 AD8 PRO B  291  HIS B  294  5                                   4    
HELIX   36 AD9 SER C   44  ARG C   49  5                                   6    
HELIX   37 AE1 ILE C   51  ALA C   56  1                                   6    
HELIX   38 AE2 ARG C   80  LEU C   95  1                                  16    
HELIX   39 AE3 ASP C  106  ASN C  119  1                                  14    
HELIX   40 AE4 THR C  137  TRP C  141  5                                   5    
HELIX   41 AE5 PRO C  142  ARG C  153  1                                  12    
HELIX   42 AE6 ASP C  156  ILE C  163  1                                   8    
HELIX   43 AE7 ASN C  166  GLY C  171  1                                   6    
HELIX   44 AE8 GLY C  171  PHE C  176  1                                   6    
HELIX   45 AE9 THR C  182  GLU C  191  1                                  10    
HELIX   46 AF1 PRO C  192  LEU C  194  5                                   3    
HELIX   47 AF2 ARG C  199  PHE C  205  1                                   7    
HELIX   48 AF3 PRO C  206  LEU C  209  5                                   4    
HELIX   49 AF4 PRO C  215  SER C  232  1                                  18    
HELIX   50 AF5 PRO C  248  LEU C  259  1                                  12    
HELIX   51 AF6 TYR C  273  ASP C  277  5                                   5    
HELIX   52 AF7 ASN C  278  LEU C  290  1                                  13    
HELIX   53 AF8 PRO C  291  LEU C  293  5                                   3    
HELIX   54 AF9 SER D   44  ARG D   49  5                                   6    
HELIX   55 AG1 ILE D   51  ALA D   56  1                                   6    
HELIX   56 AG2 ARG D   80  LEU D   95  1                                  16    
HELIX   57 AG3 ASP D  106  ASN D  119  1                                  14    
HELIX   58 AG4 ALA D  145  ARG D  153  1                                   9    
HELIX   59 AG5 ASP D  156  ILE D  163  1                                   8    
HELIX   60 AG6 ASN D  166  GLY D  171  1                                   6    
HELIX   61 AG7 GLY D  171  PHE D  176  1                                   6    
HELIX   62 AG8 THR D  182  GLU D  191  1                                  10    
HELIX   63 AG9 PRO D  192  LEU D  194  5                                   3    
HELIX   64 AH1 ARG D  199  LEU D  209  1                                  11    
HELIX   65 AH2 PRO D  215  SER D  232  1                                  18    
HELIX   66 AH3 PRO D  248  LEU D  259  1                                  12    
HELIX   67 AH4 TYR D  273  ASP D  277  5                                   5    
HELIX   68 AH5 ASN D  278  LEU D  290  1                                  13    
HELIX   69 AH6 PRO D  291  HIS D  294  5                                   4    
SHEET    1 AA1 8 HIS A  13  VAL A  17  0                                        
SHEET    2 AA1 8 SER A  20  VAL A  27 -1  O  SER A  20   N  VAL A  17           
SHEET    3 AA1 8 CYS A  61  PRO A  64 -1  O  CYS A  61   N  VAL A  27           
SHEET    4 AA1 8 VAL A  35  LEU A  38  1  N  VAL A  35   O  ILE A  62           
SHEET    5 AA1 8 VAL A 100  HIS A 105  1  O  VAL A 101   N  LEU A  36           
SHEET    6 AA1 8 VAL A 123  MET A 129  1  O  ALA A 127   N  LEU A 102           
SHEET    7 AA1 8 LYS B 236  PRO B 243  1  O  LEU B 237   N  PHE A 128           
SHEET    8 AA1 8 LEU B 262  GLY B 270  1  O  VAL B 265   N  LEU B 238           
SHEET    1 AA2 8 LEU A 262  GLY A 270  0                                        
SHEET    2 AA2 8 LYS A 236  PRO A 243  1  N  LEU A 238   O  VAL A 265           
SHEET    3 AA2 8 VAL B 123  MET B 129  1  O  PHE B 128   N  LEU A 237           
SHEET    4 AA2 8 VAL B 100  HIS B 105  1  N  LEU B 102   O  ALA B 127           
SHEET    5 AA2 8 VAL B  35  LEU B  38  1  N  LEU B  36   O  VAL B 101           
SHEET    6 AA2 8 CYS B  61  PRO B  64  1  O  ILE B  62   N  PHE B  37           
SHEET    7 AA2 8 SER B  20  VAL B  27 -1  N  VAL B  27   O  CYS B  61           
SHEET    8 AA2 8 HIS B  13  VAL B  17 -1  N  VAL B  17   O  SER B  20           
SHEET    1 AA3 8 HIS C  13  VAL C  17  0                                        
SHEET    2 AA3 8 SER C  20  VAL C  27 -1  O  SER C  20   N  VAL C  17           
SHEET    3 AA3 8 CYS C  61  PRO C  64 -1  O  CYS C  61   N  VAL C  27           
SHEET    4 AA3 8 VAL C  35  LEU C  38  1  N  VAL C  35   O  ILE C  62           
SHEET    5 AA3 8 VAL C 100  HIS C 105  1  O  VAL C 101   N  LEU C  36           
SHEET    6 AA3 8 VAL C 123  MET C 129  1  O  ALA C 127   N  LEU C 102           
SHEET    7 AA3 8 LYS D 236  PRO D 243  1  O  LEU D 237   N  PHE C 128           
SHEET    8 AA3 8 LEU D 262  GLY D 270  1  O  LYS D 263   N  LEU D 238           
SHEET    1 AA4 8 LEU C 262  GLY C 270  0                                        
SHEET    2 AA4 8 LYS C 236  PRO C 243  1  N  LEU C 238   O  VAL C 265           
SHEET    3 AA4 8 VAL D 123  MET D 129  1  O  PHE D 128   N  LEU C 237           
SHEET    4 AA4 8 VAL D 100  HIS D 105  1  N  LEU D 102   O  ALA D 127           
SHEET    5 AA4 8 VAL D  35  LEU D  38  1  N  LEU D  36   O  VAL D 101           
SHEET    6 AA4 8 CYS D  61  PRO D  64  1  O  ILE D  62   N  PHE D  37           
SHEET    7 AA4 8 SER D  20  VAL D  27 -1  N  VAL D  27   O  CYS D  61           
SHEET    8 AA4 8 HIS D  13  VAL D  17 -1  N  VAL D  17   O  SER D  20           
CISPEP   1 ASN A   41    PRO A   42          0        -6.50                     
CISPEP   2 GLU A  214    PRO A  215          0        -5.65                     
CISPEP   3 THR A  242    PRO A  243          0         2.29                     
CISPEP   4 ASN B   41    PRO B   42          0        -5.04                     
CISPEP   5 GLU B  214    PRO B  215          0        -2.42                     
CISPEP   6 THR B  242    PRO B  243          0         6.48                     
CISPEP   7 ASN C   41    PRO C   42          0        -7.36                     
CISPEP   8 GLU C  214    PRO C  215          0        -3.59                     
CISPEP   9 THR C  242    PRO C  243          0         5.24                     
CISPEP  10 ASN D   41    PRO D   42          0        -1.78                     
CISPEP  11 GLU D  214    PRO D  215          0         0.77                     
CISPEP  12 THR D  242    PRO D  243          0         5.22                     
SITE     1 AC1  5 ASN A  41  TRP A 107  HOH A 407  PHE B 205                    
SITE     2 AC1  5 PRO B 206                                                     
SITE     1 AC2  8 ASP A  89  GLU A  93  ARG A 118  ASN A 119                    
SITE     2 AC2  8 ARG A 122  HOH A 405  HOH A 453  HOH A 473                    
SITE     1 AC3  8 TRP A 138  ARG A 153  HOH A 401  HOH A 518                    
SITE     2 AC3  8 HOH A 532  HOH A 590  ILE B 211  GLU B 214                    
SITE     1 AC4  4 THR A 242  PHE A 266  GLY A 268  PRO A 269                    
SITE     1 AC5  7 GLY A 213  TRP A 219  HOH A 411  HOH A 440                    
SITE     2 AC5  7 GLY B   5  THR B   6  GLY B   7                               
SITE     1 AC6  4 PHE A 205  PRO A 206  ASN B  41  TRP B 107                    
SITE     1 AC7  5 ASP B  89  ARG B 118  ASN B 119  HOH B 428                    
SITE     2 AC7  5 HOH B 543                                                     
SITE     1 AC8  9 PHE B   8  SER B  44  GLY B  70  LYS B  71                    
SITE     2 AC8  9 HIS B 188  GLU B 191  HOH B 404  HOH B 406                    
SITE     3 AC8  9 HOH B 419                                                     
SITE     1 AC9  6 ASN C  41  TRP C 107  PHE C 168  HOH C 409                    
SITE     2 AC9  6 PHE D 205  PRO D 206                                          
SITE     1 AD1  6 GLY C   5  THR C   6  GLY C   7  HOH C 422                    
SITE     2 AD1  6 ASN D 227  GLN D 231                                          
SITE     1 AD2  7 PHE C   8  GLY C  70  LYS C  71  HIS C 188                    
SITE     2 AD2  7 GLU C 191  HOH C 404  HOH C 407                               
SITE     1 AD3  7 ASP C  89  GLU C  93  TRP C 115  ARG C 118                    
SITE     2 AD3  7 ASN C 119  ARG C 122  HOH C 457                               
SITE     1 AD4  2 PHE C 144  HOH C 410                                          
SITE     1 AD5  5 PHE C 205  PRO C 206  ASN D  41  TRP D 107                    
SITE     2 AD5  5 HOH D 387                                                     
CRYST1   44.900  164.613   92.736  90.00 100.92  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.022272  0.000000  0.004298        0.00000                         
SCALE2      0.000000  0.006075  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010982        0.00000                         
TER    2369      LEU A 293                                                      
TER    4749      HIS B 294                                                      
TER    7126      LEU C 293                                                      
TER    9533      HIS D 294                                                      
MASTER      372    0   14   69   32    0   26    610228    4   63   92          
END                                                                             

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
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