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LongText Report for: 5y5r-pdb

Name Class
5y5r-pdb
HEADER    HYDROLASE                               09-AUG-17   5Y5R              
TITLE     CRYSTAL STRUCTURE OF A NOVEL PYRETHROID HYDROLASE PYTH WITH BIF       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PYRETHROID HYDROLASE;                                      
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 FRAGMENT: UNP RESIDUES 2-280;                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SPHINGOBIUM FANIAE;                             
SOURCE   3 ORGANISM_TAXID: 570446;                                              
SOURCE   4 GENE: PYTH;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PYTH, HYDROLASE                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.Q.XU,T.T.RAN,W.W.WANG                                               
REVDAT   1   15-AUG-18 5Y5R    0                                                
JRNL        AUTH   D.Q.XU,T.T.RAN,J.HE,W.W.WANG                                 
JRNL        TITL   STRUCTURE AND CATALYTIC MECHANISM OF A NOVEL PYRETHROID      
JRNL        TITL 2 HYDROLASE FROM SPHINGOBIUM FANIAE JZ-2                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (DEV_2247: ???)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.91                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 139583                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.276                           
REMARK   3   R VALUE            (WORKING SET) : 0.273                           
REMARK   3   FREE R VALUE                     : 0.322                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7012                            
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 19.9144 -  5.8513    1.00     4766   250  0.1992 0.2296        
REMARK   3     2  5.8513 -  4.6640    1.00     4600   221  0.2109 0.2362        
REMARK   3     3  4.6640 -  4.0802    1.00     4535   249  0.2049 0.2705        
REMARK   3     4  4.0802 -  3.7098    1.00     4508   231  0.2319 0.2777        
REMARK   3     5  3.7098 -  3.4453    1.00     4453   247  0.2349 0.2997        
REMARK   3     6  3.4453 -  3.2431    1.00     4461   264  0.2609 0.2998        
REMARK   3     7  3.2431 -  3.0813    1.00     4457   239  0.2737 0.3367        
REMARK   3     8  3.0813 -  2.9476    1.00     4439   251  0.2907 0.3545        
REMARK   3     9  2.9476 -  2.8345    1.00     4467   213  0.2981 0.3422        
REMARK   3    10  2.8345 -  2.7369    1.00     4459   239  0.2897 0.3298        
REMARK   3    11  2.7369 -  2.6516    1.00     4405   237  0.2747 0.3213        
REMARK   3    12  2.6516 -  2.5759    1.00     4455   243  0.2933 0.3407        
REMARK   3    13  2.5759 -  2.5082    1.00     4424   235  0.3044 0.3788        
REMARK   3    14  2.5082 -  2.4472    1.00     4354   270  0.3130 0.3631        
REMARK   3    15  2.4472 -  2.3916    1.00     4430   229  0.3177 0.3642        
REMARK   3    16  2.3916 -  2.3408    1.00     4404   233  0.3148 0.3870        
REMARK   3    17  2.3408 -  2.2941    1.00     4434   212  0.3244 0.3930        
REMARK   3    18  2.2941 -  2.2508    1.00     4400   241  0.3436 0.3697        
REMARK   3    19  2.2508 -  2.2107    1.00     4441   211  0.3390 0.4096        
REMARK   3    20  2.2107 -  2.1732    1.00     4416   225  0.3313 0.3613        
REMARK   3    21  2.1732 -  2.1382    1.00     4394   225  0.3312 0.3904        
REMARK   3    22  2.1382 -  2.1054    1.00     4414   245  0.3533 0.4244        
REMARK   3    23  2.1054 -  2.0744    1.00     4401   225  0.3601 0.4136        
REMARK   3    24  2.0744 -  2.0453    1.00     4406   237  0.3679 0.4270        
REMARK   3    25  2.0453 -  2.0176    1.00     4390   236  0.3580 0.3925        
REMARK   3    26  2.0176 -  1.9915    1.00     4382   217  0.3475 0.3756        
REMARK   3    27  1.9915 -  1.9666    1.00     4410   219  0.3583 0.3773        
REMARK   3    28  1.9666 -  1.9429    1.00     4377   247  0.3567 0.4010        
REMARK   3    29  1.9429 -  1.9203    1.00     4410   216  0.3987 0.4588        
REMARK   3    30  1.9203 -  1.8988    0.84     3679   205  0.3729 0.3697        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 36.020           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.011          11917                                  
REMARK   3   ANGLE     :  1.461          16353                                  
REMARK   3   CHIRALITY :  0.075           1819                                  
REMARK   3   PLANARITY :  0.010           2178                                  
REMARK   3   DIHEDRAL  : 16.896           7053                                  
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 5Y5R COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-AUG-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300004682.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 139606                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.899                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 14.90                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 7.9100                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.01                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 14.10                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.180                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, PH 7.7, VAPOR          
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       84.42850            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       84.42850            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       61.93200            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       84.42850            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       84.42850            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       61.93200            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       84.42850            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       84.42850            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       61.93200            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       84.42850            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       84.42850            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       61.93200            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
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: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F                                     
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     MSE A     1                                                      
REMARK 465     GLU A   162                                                      
REMARK 465     ARG A   255                                                      
REMARK 465     GLN A   256                                                      
REMARK 465     THR A   257                                                      
REMARK 465     ALA A   258                                                      
REMARK 465     THR A   259                                                      
REMARK 465     LYS A   260                                                      
REMARK 465     ALA A   261                                                      
REMARK 465     GLY A   262                                                      
REMARK 465     PRO A   263                                                      
REMARK 465     ASP A   264                                                      
REMARK 465     ARG A   265                                                      
REMARK 465     PRO A   266                                                      
REMARK 465     ALA A   267                                                      
REMARK 465     GLY A   268                                                      
REMARK 465     ALA A   269                                                      
REMARK 465     ASP A   270                                                      
REMARK 465     GLY A   271                                                      
REMARK 465     GLY A   272                                                      
REMARK 465     ARG A   273                                                      
REMARK 465     ALA A   274                                                      
REMARK 465     ASP A   275                                                      
REMARK 465     ARG A   276                                                      
REMARK 465     ALA A   277                                                      
REMARK 465     ASP A   278                                                      
REMARK 465     LEU A   279                                                      
REMARK 465     PRO A   280                                                      
REMARK 465     LEU A   281                                                      
REMARK 465     GLU A   282                                                      
REMARK 465     HIS A   283                                                      
REMARK 465     HIS A   284                                                      
REMARK 465     HIS A   285                                                      
REMARK 465     HIS A   286                                                      
REMARK 465     HIS A   287                                                      
REMARK 465     HIS A   288                                                      
REMARK 465     MSE B     1                                                      
REMARK 465     GLU B   162                                                      
REMARK 465     ARG B   255                                                      
REMARK 465     GLN B   256                                                      
REMARK 465     THR B   257                                                      
REMARK 465     ALA B   258                                                      
REMARK 465     THR B   259                                                      
REMARK 465     LYS B   260                                                      
REMARK 465     ALA B   261                                                      
REMARK 465     GLY B   262                                                      
REMARK 465     PRO B   263                                                      
REMARK 465     ASP B   264                                                      
REMARK 465     ARG B   265                                                      
REMARK 465     PRO B   266                                                      
REMARK 465     ALA B   267                                                      
REMARK 465     GLY B   268                                                      
REMARK 465     ALA B   269                                                      
REMARK 465     ASP B   270                                                      
REMARK 465     GLY B   271                                                      
REMARK 465     GLY B   272                                                      
REMARK 465     ARG B   273                                                      
REMARK 465     ALA B   274                                                      
REMARK 465     ASP B   275                                                      
REMARK 465     ARG B   276                                                      
REMARK 465     ALA B   277                                                      
REMARK 465     ASP B   278                                                      
REMARK 465     LEU B   279                                                      
REMARK 465     PRO B   280                                                      
REMARK 465     LEU B   281                                                      
REMARK 465     GLU B   282                                                      
REMARK 465     HIS B   283                                                      
REMARK 465     HIS B   284                                                      
REMARK 465     HIS B   285                                                      
REMARK 465     HIS B   286                                                      
REMARK 465     HIS B   287                                                      
REMARK 465     HIS B   288                                                      
REMARK 465     MSE C     1                                                      
REMARK 465     GLU C   162                                                      
REMARK 465     ARG C   255                                                      
REMARK 465     GLN C   256                                                      
REMARK 465     THR C   257                                                      
REMARK 465     ALA C   258                                                      
REMARK 465     THR C   259                                                      
REMARK 465     LYS C   260                                                      
REMARK 465     ALA C   261                                                      
REMARK 465     GLY C   262                                                      
REMARK 465     PRO C   263                                                      
REMARK 465     ASP C   264                                                      
REMARK 465     ARG C   265                                                      
REMARK 465     PRO C   266                                                      
REMARK 465     ALA C   267                                                      
REMARK 465     GLY C   268                                                      
REMARK 465     ALA C   269                                                      
REMARK 465     ASP C   270                                                      
REMARK 465     GLY C   271                                                      
REMARK 465     GLY C   272                                                      
REMARK 465     ARG C   273                                                      
REMARK 465     ALA C   274                                                      
REMARK 465     ASP C   275                                                      
REMARK 465     ARG C   276                                                      
REMARK 465     ALA C   277                                                      
REMARK 465     ASP C   278                                                      
REMARK 465     LEU C   279                                                      
REMARK 465     PRO C   280                                                      
REMARK 465     LEU C   281                                                      
REMARK 465     GLU C   282                                                      
REMARK 465     HIS C   283                                                      
REMARK 465     HIS C   284                                                      
REMARK 465     HIS C   285                                                      
REMARK 465     HIS C   286                                                      
REMARK 465     HIS C   287                                                      
REMARK 465     HIS C   288                                                      
REMARK 465     MSE D     1                                                      
REMARK 465     ARG D   255                                                      
REMARK 465     GLN D   256                                                      
REMARK 465     THR D   257                                                      
REMARK 465     ALA D   258                                                      
REMARK 465     THR D   259                                                      
REMARK 465     LYS D   260                                                      
REMARK 465     ALA D   261                                                      
REMARK 465     GLY D   262                                                      
REMARK 465     PRO D   263                                                      
REMARK 465     ASP D   264                                                      
REMARK 465     ARG D   265                                                      
REMARK 465     PRO D   266                                                      
REMARK 465     ALA D   267                                                      
REMARK 465     GLY D   268                                                      
REMARK 465     ALA D   269                                                      
REMARK 465     ASP D   270                                                      
REMARK 465     GLY D   271                                                      
REMARK 465     GLY D   272                                                      
REMARK 465     ARG D   273                                                      
REMARK 465     ALA D   274                                                      
REMARK 465     ASP D   275                                                      
REMARK 465     ARG D   276                                                      
REMARK 465     ALA D   277                                                      
REMARK 465     ASP D   278                                                      
REMARK 465     LEU D   279                                                      
REMARK 465     PRO D   280                                                      
REMARK 465     LEU D   281                                                      
REMARK 465     GLU D   282                                                      
REMARK 465     HIS D   283                                                      
REMARK 465     HIS D   284                                                      
REMARK 465     HIS D   285                                                      
REMARK 465     HIS D   286                                                      
REMARK 465     HIS D   287                                                      
REMARK 465     HIS D   288                                                      
REMARK 465     MSE E     1                                                      
REMARK 465     GLU E   162                                                      
REMARK 465     GLY E   163                                                      
REMARK 465     ARG E   255                                                      
REMARK 465     GLN E   256                                                      
REMARK 465     THR E   257                                                      
REMARK 465     ALA E   258                                                      
REMARK 465     THR E   259                                                      
REMARK 465     LYS E   260                                                      
REMARK 465     ALA E   261                                                      
REMARK 465     GLY E   262                                                      
REMARK 465     PRO E   263                                                      
REMARK 465     ASP E   264                                                      
REMARK 465     ARG E   265                                                      
REMARK 465     PRO E   266                                                      
REMARK 465     ALA E   267                                                      
REMARK 465     GLY E   268                                                      
REMARK 465     ALA E   269                                                      
REMARK 465     ASP E   270                                                      
REMARK 465     GLY E   271                                                      
REMARK 465     GLY E   272                                                      
REMARK 465     ARG E   273                                                      
REMARK 465     ALA E   274                                                      
REMARK 465     ASP E   275                                                      
REMARK 465     ARG E   276                                                      
REMARK 465     ALA E   277                                                      
REMARK 465     ASP E   278                                                      
REMARK 465     LEU E   279                                                      
REMARK 465     PRO E   280                                                      
REMARK 465     LEU E   281                                                      
REMARK 465     GLU E   282                                                      
REMARK 465     HIS E   283                                                      
REMARK 465     HIS E   284                                                      
REMARK 465     HIS E   285                                                      
REMARK 465     HIS E   286                                                      
REMARK 465     HIS E   287                                                      
REMARK 465     HIS E   288                                                      
REMARK 465     MSE F     1                                                      
REMARK 465     GLY F   161                                                      
REMARK 465     TYR F   254                                                      
REMARK 465     ARG F   255                                                      
REMARK 465     GLN F   256                                                      
REMARK 465     THR F   257                                                      
REMARK 465     ALA F   258                                                      
REMARK 465     THR F   259                                                      
REMARK 465     LYS F   260                                                      
REMARK 465     ALA F   261                                                      
REMARK 465     GLY F   262                                                      
REMARK 465     PRO F   263                                                      
REMARK 465     ASP F   264                                                      
REMARK 465     ARG F   265                                                      
REMARK 465     PRO F   266                                                      
REMARK 465     ALA F   267                                                      
REMARK 465     GLY F   268                                                      
REMARK 465     ALA F   269                                                      
REMARK 465     ASP F   270                                                      
REMARK 465     GLY F   271                                                      
REMARK 465     GLY F   272                                                      
REMARK 465     ARG F   273                                                      
REMARK 465     ALA F   274                                                      
REMARK 465     ASP F   275                                                      
REMARK 465     ARG F   276                                                      
REMARK 465     ALA F   277                                                      
REMARK 465     ASP F   278                                                      
REMARK 465     LEU F   279                                                      
REMARK 465     PRO F   280                                                      
REMARK 465     LEU F   281                                                      
REMARK 465     GLU F   282                                                      
REMARK 465     HIS F   283                                                      
REMARK 465     HIS F   284                                                      
REMARK 465     HIS F   285                                                      
REMARK 465     HIS F   286                                                      
REMARK 465     HIS F   287                                                      
REMARK 465     HIS F   288                                                      
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 C  32    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 188    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU E  74    CG   CD1  CD2                                       
REMARK 470     ASP E  93    CG   OD1  OD2                                       
REMARK 470     LYS E  94    CG   CD   CE   NZ                                   
REMARK 470     ILE E 132    CG1  CG2  CD1                                       
REMARK 470     GLU E 137    CG   CD   OE1  OE2                                  
REMARK 470     ARG E 139    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR F   4    OG1  CG2                                            
REMARK 470     ILE F   9    CG1  CG2  CD1                                       
REMARK 470     ARG F  32    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL F  52    CG1  CG2                                            
REMARK 470     ASP F  53    CG   OD1  OD2                                       
REMARK 470     GLU F  55    CG   CD   OE1  OE2                                  
REMARK 470     VAL F  61    CG1  CG2                                            
REMARK 470     ARG F  67    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU F  69    CG   CD   OE1  OE2                                  
REMARK 470     LEU F  74    CG   CD1  CD2                                       
REMARK 470     LEU F  75    CG   CD1  CD2                                       
REMARK 470     LEU F  79    CG   CD1  CD2                                       
REMARK 470     LEU F  87    CG   CD1  CD2                                       
REMARK 470     ASP F  93    CG   OD1  OD2                                       
REMARK 470     LYS F  94    CG   CD   CE   NZ                                   
REMARK 470     LEU F  98    CG   CD1  CD2                                       
REMARK 470     THR F 181    OG1  CG2                                            
REMARK 470     GLU F 186    CG   CD   OE1  OE2                                  
REMARK 470     ARG F 188    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU F 190    CG   CD1  CD2                                       
REMARK 470     GLU F 191    CG   CD   OE1  OE2                                  
REMARK 470     ILE F 192    CG1  CG2  CD1                                       
REMARK 470     GLU F 253    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    MSE F    54     OG1  THR F    58              1.85            
REMARK 500   OG   SER F    78     C17  8NL F   301              2.00            
REMARK 500   OG   SER F    78     C19  8NL F   301              2.01            
REMARK 500   O    HOH B   504     O    HOH B   506              2.04            
REMARK 500   O    HOH D   454     O    HOH D   475              2.04            
REMARK 500   O    HOH E   432     O    HOH E   441              2.08            
REMARK 500   O    GLY A    30     O    HOH A   401              2.09            
REMARK 500   O    HOH C   462     O    HOH C   470              2.10            
REMARK 500   O    MSE F   185     O    HOH F   401              2.11            
REMARK 500   O    TYR E   254     O    HOH E   401              2.11            
REMARK 500   O    HOH A   488     O    HOH A   498              2.11            
REMARK 500   O    HOH B   436     O    HOH B   483              2.11            
REMARK 500   OG1  THR E   106     O    HOH E   402              2.12            
REMARK 500   O    HOH B   502     O    HOH B   505              2.14            
REMARK 500   O    HOH D   420     O    HOH D   464              2.15            
REMARK 500   OE2  GLU E   198     OG   SER E   225              2.15            
REMARK 500   OD1  ASP F    45     O    HOH F   402              2.15            
REMARK 500   O    GLU D    55     O    HOH D   401              2.16            
REMARK 500   O    GLU F   137     O    HOH F   403              2.17            
REMARK 500   O    ARG C   123     O    HOH C   401              2.18            
REMARK 500   NE2  GLN A   172     O    HOH A   402              2.18            
REMARK 500   O    HOH A   486     O    HOH D   473              2.18            
REMARK 500   OE1  GLU B    55     NH2  ARG B    59              2.18            
REMARK 500   O    HOH F   439     O    HOH F   440              2.19            
REMARK 500   O    HOH C   410     O    HOH C   454              2.19            
REMARK 500   OD1  ASP A   136     O    HOH A   403              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   N    MSE E   164     OE1  GLU F   149     8554     1.95            
REMARK 500   O    HOH B   415     O    HOH F   404     3555     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  78     -116.31     49.48                                   
REMARK 500    THR A 102       57.69     31.41                                   
REMARK 500    SER A 229     -147.06    -90.20                                   
REMARK 500    ALA A 250       79.78   -164.05                                   
REMARK 500    SER B  78     -115.48     51.78                                   
REMARK 500    THR B 102       56.02     31.25                                   
REMARK 500    THR B 125       68.13   -119.57                                   
REMARK 500    MSE B 164     -176.54    -65.41                                   
REMARK 500    SER B 229     -147.91    -93.29                                   
REMARK 500    ALA B 250       81.70   -162.67                                   
REMARK 500    GLU C  69      -71.11    -62.00                                   
REMARK 500    SER C  78     -121.99     53.65                                   
REMARK 500    THR C 102       55.28     31.00                                   
REMARK 500    THR C 125       68.67   -120.00                                   
REMARK 500    SER C 229     -146.23    -90.66                                   
REMARK 500    MSE C 236       69.41   -153.11                                   
REMARK 500    ALA C 250       82.43   -161.64                                   
REMARK 500    LEU D  13       10.52     59.93                                   
REMARK 500    SER D  78     -118.91     49.31                                   
REMARK 500    THR D 102       54.05     29.70                                   
REMARK 500    SER D 229     -150.25    -89.55                                   
REMARK 500    MSE D 236       59.26   -147.64                                   
REMARK 500    ALA D 250       81.20   -164.10                                   
REMARK 500    ASP E  53     -168.12   -163.81                                   
REMARK 500    SER E  78     -109.56     53.61                                   
REMARK 500    THR E 102       59.02     34.65                                   
REMARK 500    PRO E 160       99.40    -59.34                                   
REMARK 500    SER E 229     -155.57    -88.93                                   
REMARK 500    MSE E 236       66.13   -152.03                                   
REMARK 500    ALA E 250       82.34   -165.05                                   
REMARK 500    GLU E 253       41.33   -147.27                                   
REMARK 500    SER F  78     -115.39     58.87                                   
REMARK 500    THR F 102       57.35     32.40                                   
REMARK 500    GLU F 137       60.82     61.44                                   
REMARK 500    PRO F 184      -17.14    -49.97                                   
REMARK 500    SER F 229     -149.49    -90.12                                   
REMARK 500    ALA F 250       77.88   -163.84                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 507        DISTANCE =  6.78 ANGSTROMS                       
REMARK 525    HOH B 508        DISTANCE =  7.83 ANGSTROMS                       
REMARK 525    HOH D 481        DISTANCE =  6.09 ANGSTROMS                       
REMARK 525    HOH D 482        DISTANCE =  6.39 ANGSTROMS                       
REMARK 525    HOH F 442        DISTANCE =  6.13 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8NL A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8NL B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8NL C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8NL D 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8NL E 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 E 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8NL F 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 F 302                 
DBREF  5Y5R A    2   280  UNP    D0VUS3   D0VUS3_9SPHN     2    280             
DBREF  5Y5R B    2   280  UNP    D0VUS3   D0VUS3_9SPHN     2    280             
DBREF  5Y5R C    2   280  UNP    D0VUS3   D0VUS3_9SPHN     2    280             
DBREF  5Y5R D    2   280  UNP    D0VUS3   D0VUS3_9SPHN     2    280             
DBREF  5Y5R E    2   280  UNP    D0VUS3   D0VUS3_9SPHN     2    280             
DBREF  5Y5R F    2   280  UNP    D0VUS3   D0VUS3_9SPHN     2    280             
SEQADV 5Y5R MSE A    1  UNP  D0VUS3              INITIATING METHIONINE          
SEQADV 5Y5R LEU A  281  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R GLU A  282  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS A  283  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS A  284  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS A  285  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS A  286  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS A  287  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS A  288  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R MSE B    1  UNP  D0VUS3              INITIATING METHIONINE          
SEQADV 5Y5R LEU B  281  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R GLU B  282  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS B  283  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS B  284  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS B  285  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS B  286  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS B  287  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS B  288  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R MSE C    1  UNP  D0VUS3              INITIATING METHIONINE          
SEQADV 5Y5R LEU C  281  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R GLU C  282  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS C  283  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS C  284  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS C  285  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS C  286  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS C  287  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS C  288  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R MSE D    1  UNP  D0VUS3              INITIATING METHIONINE          
SEQADV 5Y5R LEU D  281  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R GLU D  282  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS D  283  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS D  284  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS D  285  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS D  286  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS D  287  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS D  288  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R MSE E    1  UNP  D0VUS3              INITIATING METHIONINE          
SEQADV 5Y5R LEU E  281  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R GLU E  282  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS E  283  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS E  284  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS E  285  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS E  286  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS E  287  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS E  288  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R MSE F    1  UNP  D0VUS3              INITIATING METHIONINE          
SEQADV 5Y5R LEU F  281  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R GLU F  282  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS F  283  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS F  284  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS F  285  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS F  286  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS F  287  UNP  D0VUS3              EXPRESSION TAG                 
SEQADV 5Y5R HIS F  288  UNP  D0VUS3              EXPRESSION TAG                 
SEQRES   1 A  288  MSE THR VAL THR ASP ILE ILE LEU ILE HIS GLY ALA LEU          
SEQRES   2 A  288  ASN ARG GLY ALA CYS TYR ASP ALA VAL VAL PRO LEU LEU          
SEQRES   3 A  288  GLU ALA ARG GLY TYR ARG VAL HIS ALA PRO ASP LEU THR          
SEQRES   4 A  288  GLY HIS THR PRO GLY ASP GLY GLY HIS LEU SER VAL VAL          
SEQRES   5 A  288  ASP MSE GLU HIS TYR THR ARG PRO VAL ALA ASP ILE LEU          
SEQRES   6 A  288  ALA ARG ALA GLU GLY GLN SER ILE LEU LEU GLY HIS SER          
SEQRES   7 A  288  LEU GLY GLY ALA SER ILE SER TRP LEU ALA GLN HIS HIS          
SEQRES   8 A  288  PRO ASP LYS VAL ALA GLY LEU ILE TYR LEU THR ALA VAL          
SEQRES   9 A  288  LEU THR ALA PRO GLY VAL THR PRO GLU THR PHE VAL LEU          
SEQRES  10 A  288  PRO GLY GLU PRO ASN ARG GLY THR PRO HIS ALA LEU ASP          
SEQRES  11 A  288  LEU ILE GLN PRO VAL ASP GLU GLY ARG GLY LEU GLN ALA          
SEQRES  12 A  288  ASP PHE SER ARG LEU GLU ARG LEU ARG GLU VAL PHE MSE          
SEQRES  13 A  288  GLY ASP TYR PRO GLY GLU GLY MSE PRO PRO ALA GLU HIS          
SEQRES  14 A  288  PHE ILE GLN THR GLN SER THR VAL PRO PHE GLY THR PRO          
SEQRES  15 A  288  ASN PRO MSE GLU GLY ARG ALA LEU GLU ILE PRO ARG LEU          
SEQRES  16 A  288  TYR ILE GLU ALA LEU ASP ASP VAL VAL LEU PRO ILE ALA          
SEQRES  17 A  288  VAL GLN ARG GLN MSE GLN LYS GLU PHE PRO GLY PRO VAL          
SEQRES  18 A  288  ALA VAL VAL SER LEU PRO ALA SER HIS ALA PRO TYR TYR          
SEQRES  19 A  288  SER MSE PRO GLU ARG LEU ALA GLU ALA ILE ALA ASP PHE          
SEQRES  20 A  288  ALA ASP ALA PRO ALA GLU TYR ARG GLN THR ALA THR LYS          
SEQRES  21 A  288  ALA GLY PRO ASP ARG PRO ALA GLY ALA ASP GLY GLY ARG          
SEQRES  22 A  288  ALA ASP ARG ALA ASP LEU PRO LEU GLU HIS HIS HIS HIS          
SEQRES  23 A  288  HIS HIS                                                      
SEQRES   1 B  288  MSE THR VAL THR ASP ILE ILE LEU ILE HIS GLY ALA LEU          
SEQRES   2 B  288  ASN ARG GLY ALA CYS TYR ASP ALA VAL VAL PRO LEU LEU          
SEQRES   3 B  288  GLU ALA ARG GLY TYR ARG VAL HIS ALA PRO ASP LEU THR          
SEQRES   4 B  288  GLY HIS THR PRO GLY ASP GLY GLY HIS LEU SER VAL VAL          
SEQRES   5 B  288  ASP MSE GLU HIS TYR THR ARG PRO VAL ALA ASP ILE LEU          
SEQRES   6 B  288  ALA ARG ALA GLU GLY GLN SER ILE LEU LEU GLY HIS SER          
SEQRES   7 B  288  LEU GLY GLY ALA SER ILE SER TRP LEU ALA GLN HIS HIS          
SEQRES   8 B  288  PRO ASP LYS VAL ALA GLY LEU ILE TYR LEU THR ALA VAL          
SEQRES   9 B  288  LEU THR ALA PRO GLY VAL THR PRO GLU THR PHE VAL LEU          
SEQRES  10 B  288  PRO GLY GLU PRO ASN ARG GLY THR PRO HIS ALA LEU ASP          
SEQRES  11 B  288  LEU ILE GLN PRO VAL ASP GLU GLY ARG GLY LEU GLN ALA          
SEQRES  12 B  288  ASP PHE SER ARG LEU GLU ARG LEU ARG GLU VAL PHE MSE          
SEQRES  13 B  288  GLY ASP TYR PRO GLY GLU GLY MSE PRO PRO ALA GLU HIS          
SEQRES  14 B  288  PHE ILE GLN THR GLN SER THR VAL PRO PHE GLY THR PRO          
SEQRES  15 B  288  ASN PRO MSE GLU GLY ARG ALA LEU GLU ILE PRO ARG LEU          
SEQRES  16 B  288  TYR ILE GLU ALA LEU ASP ASP VAL VAL LEU PRO ILE ALA          
SEQRES  17 B  288  VAL GLN ARG GLN MSE GLN LYS GLU PHE PRO GLY PRO VAL          
SEQRES  18 B  288  ALA VAL VAL SER LEU PRO ALA SER HIS ALA PRO TYR TYR          
SEQRES  19 B  288  SER MSE PRO GLU ARG LEU ALA GLU ALA ILE ALA ASP PHE          
SEQRES  20 B  288  ALA ASP ALA PRO ALA GLU TYR ARG GLN THR ALA THR LYS          
SEQRES  21 B  288  ALA GLY PRO ASP ARG PRO ALA GLY ALA ASP GLY GLY ARG          
SEQRES  22 B  288  ALA ASP ARG ALA ASP LEU PRO LEU GLU HIS HIS HIS HIS          
SEQRES  23 B  288  HIS HIS                                                      
SEQRES   1 C  288  MSE THR VAL THR ASP ILE ILE LEU ILE HIS GLY ALA LEU          
SEQRES   2 C  288  ASN ARG GLY ALA CYS TYR ASP ALA VAL VAL PRO LEU LEU          
SEQRES   3 C  288  GLU ALA ARG GLY TYR ARG VAL HIS ALA PRO ASP LEU THR          
SEQRES   4 C  288  GLY HIS THR PRO GLY ASP GLY GLY HIS LEU SER VAL VAL          
SEQRES   5 C  288  ASP MSE GLU HIS TYR THR ARG PRO VAL ALA ASP ILE LEU          
SEQRES   6 C  288  ALA ARG ALA GLU GLY GLN SER ILE LEU LEU GLY HIS SER          
SEQRES   7 C  288  LEU GLY GLY ALA SER ILE SER TRP LEU ALA GLN HIS HIS          
SEQRES   8 C  288  PRO ASP LYS VAL ALA GLY LEU ILE TYR LEU THR ALA VAL          
SEQRES   9 C  288  LEU THR ALA PRO GLY VAL THR PRO GLU THR PHE VAL LEU          
SEQRES  10 C  288  PRO GLY GLU PRO ASN ARG GLY THR PRO HIS ALA LEU ASP          
SEQRES  11 C  288  LEU ILE GLN PRO VAL ASP GLU GLY ARG GLY LEU GLN ALA          
SEQRES  12 C  288  ASP PHE SER ARG LEU GLU ARG LEU ARG GLU VAL PHE MSE          
SEQRES  13 C  288  GLY ASP TYR PRO GLY GLU GLY MSE PRO PRO ALA GLU HIS          
SEQRES  14 C  288  PHE ILE GLN THR GLN SER THR VAL PRO PHE GLY THR PRO          
SEQRES  15 C  288  ASN PRO MSE GLU GLY ARG ALA LEU GLU ILE PRO ARG LEU          
SEQRES  16 C  288  TYR ILE GLU ALA LEU ASP ASP VAL VAL LEU PRO ILE ALA          
SEQRES  17 C  288  VAL GLN ARG GLN MSE GLN LYS GLU PHE PRO GLY PRO VAL          
SEQRES  18 C  288  ALA VAL VAL SER LEU PRO ALA SER HIS ALA PRO TYR TYR          
SEQRES  19 C  288  SER MSE PRO GLU ARG LEU ALA GLU ALA ILE ALA ASP PHE          
SEQRES  20 C  288  ALA ASP ALA PRO ALA GLU TYR ARG GLN THR ALA THR LYS          
SEQRES  21 C  288  ALA GLY PRO ASP ARG PRO ALA GLY ALA ASP GLY GLY ARG          
SEQRES  22 C  288  ALA ASP ARG ALA ASP LEU PRO LEU GLU HIS HIS HIS HIS          
SEQRES  23 C  288  HIS HIS                                                      
SEQRES   1 D  288  MSE THR VAL THR ASP ILE ILE LEU ILE HIS GLY ALA LEU          
SEQRES   2 D  288  ASN ARG GLY ALA CYS TYR ASP ALA VAL VAL PRO LEU LEU          
SEQRES   3 D  288  GLU ALA ARG GLY TYR ARG VAL HIS ALA PRO ASP LEU THR          
SEQRES   4 D  288  GLY HIS THR PRO GLY ASP GLY GLY HIS LEU SER VAL VAL          
SEQRES   5 D  288  ASP MSE GLU HIS TYR THR ARG PRO VAL ALA ASP ILE LEU          
SEQRES   6 D  288  ALA ARG ALA GLU GLY GLN SER ILE LEU LEU GLY HIS SER          
SEQRES   7 D  288  LEU GLY GLY ALA SER ILE SER TRP LEU ALA GLN HIS HIS          
SEQRES   8 D  288  PRO ASP LYS VAL ALA GLY LEU ILE TYR LEU THR ALA VAL          
SEQRES   9 D  288  LEU THR ALA PRO GLY VAL THR PRO GLU THR PHE VAL LEU          
SEQRES  10 D  288  PRO GLY GLU PRO ASN ARG GLY THR PRO HIS ALA LEU ASP          
SEQRES  11 D  288  LEU ILE GLN PRO VAL ASP GLU GLY ARG GLY LEU GLN ALA          
SEQRES  12 D  288  ASP PHE SER ARG LEU GLU ARG LEU ARG GLU VAL PHE MSE          
SEQRES  13 D  288  GLY ASP TYR PRO GLY GLU GLY MSE PRO PRO ALA GLU HIS          
SEQRES  14 D  288  PHE ILE GLN THR GLN SER THR VAL PRO PHE GLY THR PRO          
SEQRES  15 D  288  ASN PRO MSE GLU GLY ARG ALA LEU GLU ILE PRO ARG LEU          
SEQRES  16 D  288  TYR ILE GLU ALA LEU ASP ASP VAL VAL LEU PRO ILE ALA          
SEQRES  17 D  288  VAL GLN ARG GLN MSE GLN LYS GLU PHE PRO GLY PRO VAL          
SEQRES  18 D  288  ALA VAL VAL SER LEU PRO ALA SER HIS ALA PRO TYR TYR          
SEQRES  19 D  288  SER MSE PRO GLU ARG LEU ALA GLU ALA ILE ALA ASP PHE          
SEQRES  20 D  288  ALA ASP ALA PRO ALA GLU TYR ARG GLN THR ALA THR LYS          
SEQRES  21 D  288  ALA GLY PRO ASP ARG PRO ALA GLY ALA ASP GLY GLY ARG          
SEQRES  22 D  288  ALA ASP ARG ALA ASP LEU PRO LEU GLU HIS HIS HIS HIS          
SEQRES  23 D  288  HIS HIS                                                      
SEQRES   1 E  288  MSE THR VAL THR ASP ILE ILE LEU ILE HIS GLY ALA LEU          
SEQRES   2 E  288  ASN ARG GLY ALA CYS TYR ASP ALA VAL VAL PRO LEU LEU          
SEQRES   3 E  288  GLU ALA ARG GLY TYR ARG VAL HIS ALA PRO ASP LEU THR          
SEQRES   4 E  288  GLY HIS THR PRO GLY ASP GLY GLY HIS LEU SER VAL VAL          
SEQRES   5 E  288  ASP MSE GLU HIS TYR THR ARG PRO VAL ALA ASP ILE LEU          
SEQRES   6 E  288  ALA ARG ALA GLU GLY GLN SER ILE LEU LEU GLY HIS SER          
SEQRES   7 E  288  LEU GLY GLY ALA SER ILE SER TRP LEU ALA GLN HIS HIS          
SEQRES   8 E  288  PRO ASP LYS VAL ALA GLY LEU ILE TYR LEU THR ALA VAL          
SEQRES   9 E  288  LEU THR ALA PRO GLY VAL THR PRO GLU THR PHE VAL LEU          
SEQRES  10 E  288  PRO GLY GLU PRO ASN ARG GLY THR PRO HIS ALA LEU ASP          
SEQRES  11 E  288  LEU ILE GLN PRO VAL ASP GLU GLY ARG GLY LEU GLN ALA          
SEQRES  12 E  288  ASP PHE SER ARG LEU GLU ARG LEU ARG GLU VAL PHE MSE          
SEQRES  13 E  288  GLY ASP TYR PRO GLY GLU GLY MSE PRO PRO ALA GLU HIS          
SEQRES  14 E  288  PHE ILE GLN THR GLN SER THR VAL PRO PHE GLY THR PRO          
SEQRES  15 E  288  ASN PRO MSE GLU GLY ARG ALA LEU GLU ILE PRO ARG LEU          
SEQRES  16 E  288  TYR ILE GLU ALA LEU ASP ASP VAL VAL LEU PRO ILE ALA          
SEQRES  17 E  288  VAL GLN ARG GLN MSE GLN LYS GLU PHE PRO GLY PRO VAL          
SEQRES  18 E  288  ALA VAL VAL SER LEU PRO ALA SER HIS ALA PRO TYR TYR          
SEQRES  19 E  288  SER MSE PRO GLU ARG LEU ALA GLU ALA ILE ALA ASP PHE          
SEQRES  20 E  288  ALA ASP ALA PRO ALA GLU TYR ARG GLN THR ALA THR LYS          
SEQRES  21 E  288  ALA GLY PRO ASP ARG PRO ALA GLY ALA ASP GLY GLY ARG          
SEQRES  22 E  288  ALA ASP ARG ALA ASP LEU PRO LEU GLU HIS HIS HIS HIS          
SEQRES  23 E  288  HIS HIS                                                      
SEQRES   1 F  288  MSE THR VAL THR ASP ILE ILE LEU ILE HIS GLY ALA LEU          
SEQRES   2 F  288  ASN ARG GLY ALA CYS TYR ASP ALA VAL VAL PRO LEU LEU          
SEQRES   3 F  288  GLU ALA ARG GLY TYR ARG VAL HIS ALA PRO ASP LEU THR          
SEQRES   4 F  288  GLY HIS THR PRO GLY ASP GLY GLY HIS LEU SER VAL VAL          
SEQRES   5 F  288  ASP MSE GLU HIS TYR THR ARG PRO VAL ALA ASP ILE LEU          
SEQRES   6 F  288  ALA ARG ALA GLU GLY GLN SER ILE LEU LEU GLY HIS SER          
SEQRES   7 F  288  LEU GLY GLY ALA SER ILE SER TRP LEU ALA GLN HIS HIS          
SEQRES   8 F  288  PRO ASP LYS VAL ALA GLY LEU ILE TYR LEU THR ALA VAL          
SEQRES   9 F  288  LEU THR ALA PRO GLY VAL THR PRO GLU THR PHE VAL LEU          
SEQRES  10 F  288  PRO GLY GLU PRO ASN ARG GLY THR PRO HIS ALA LEU ASP          
SEQRES  11 F  288  LEU ILE GLN PRO VAL ASP GLU GLY ARG GLY LEU GLN ALA          
SEQRES  12 F  288  ASP PHE SER ARG LEU GLU ARG LEU ARG GLU VAL PHE MSE          
SEQRES  13 F  288  GLY ASP TYR PRO GLY GLU GLY MSE PRO PRO ALA GLU HIS          
SEQRES  14 F  288  PHE ILE GLN THR GLN SER THR VAL PRO PHE GLY THR PRO          
SEQRES  15 F  288  ASN PRO MSE GLU GLY ARG ALA LEU GLU ILE PRO ARG LEU          
SEQRES  16 F  288  TYR ILE GLU ALA LEU ASP ASP VAL VAL LEU PRO ILE ALA          
SEQRES  17 F  288  VAL GLN ARG GLN MSE GLN LYS GLU PHE PRO GLY PRO VAL          
SEQRES  18 F  288  ALA VAL VAL SER LEU PRO ALA SER HIS ALA PRO TYR TYR          
SEQRES  19 F  288  SER MSE PRO GLU ARG LEU ALA GLU ALA ILE ALA ASP PHE          
SEQRES  20 F  288  ALA ASP ALA PRO ALA GLU TYR ARG GLN THR ALA THR LYS          
SEQRES  21 F  288  ALA GLY PRO ASP ARG PRO ALA GLY ALA ASP GLY GLY ARG          
SEQRES  22 F  288  ALA ASP ARG ALA ASP LEU PRO LEU GLU HIS HIS HIS HIS          
SEQRES  23 F  288  HIS HIS                                                      
MODRES 5Y5R MSE A   54  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE A  156  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE A  164  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE A  185  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE A  213  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE A  236  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE B   54  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE B  156  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE B  164  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE B  185  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE B  213  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE B  236  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE C   54  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE C  156  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE C  164  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE C  185  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE C  213  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE C  236  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE D   54  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE D  156  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE D  164  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE D  185  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE D  213  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE D  236  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE E   54  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE E  156  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE E  164  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE E  185  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE E  213  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE E  236  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE F   54  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE F  156  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE F  164  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE F  185  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE F  213  MET  MODIFIED RESIDUE                                   
MODRES 5Y5R MSE F  236  MET  MODIFIED RESIDUE                                   
HET    MSE  A  54       8                                                       
HET    MSE  A 156       8                                                       
HET    MSE  A 164       8                                                       
HET    MSE  A 185       8                                                       
HET    MSE  A 213       8                                                       
HET    MSE  A 236       8                                                       
HET    MSE  B  54       8                                                       
HET    MSE  B 156       8                                                       
HET    MSE  B 164       8                                                       
HET    MSE  B 185       8                                                       
HET    MSE  B 213       8                                                       
HET    MSE  B 236       8                                                       
HET    MSE  C  54       8                                                       
HET    MSE  C 156       8                                                       
HET    MSE  C 164       8                                                       
HET    MSE  C 185       8                                                       
HET    MSE  C 213       8                                                       
HET    MSE  C 236       8                                                       
HET    MSE  D  54       8                                                       
HET    MSE  D 156       8                                                       
HET    MSE  D 164       8                                                       
HET    MSE  D 185       8                                                       
HET    MSE  D 213       8                                                       
HET    MSE  D 236       8                                                       
HET    MSE  E  54       8                                                       
HET    MSE  E 156       8                                                       
HET    MSE  E 164       8                                                       
HET    MSE  E 185       8                                                       
HET    MSE  E 213       8                                                       
HET    MSE  E 236       8                                                       
HET    MSE  F  54       8                                                       
HET    MSE  F 156       8                                                       
HET    MSE  F 164       8                                                       
HET    MSE  F 185       8                                                       
HET    MSE  F 213       8                                                       
HET    MSE  F 236       8                                                       
HET    8NL  A 301      29                                                       
HET    SO4  A 302       5                                                       
HET    8NL  B 301      29                                                       
HET    SO4  B 302       5                                                       
HET    8NL  C 301      29                                                       
HET    SO4  C 302       5                                                       
HET    8NL  D 301      29                                                       
HET    SO4  D 302       5                                                       
HET    8NL  E 301      29                                                       
HET    SO4  E 302       5                                                       
HET    8NL  F 301      29                                                       
HET    SO4  F 302       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     8NL (2-METHYL-3-PHENYL-PHENYL)METHYL (1~{S})-3-[(~{E})-2-            
HETNAM   2 8NL  CHLORANYL-3,3,3-TRIS(FLUORANYL)PROP-1-ENYL]-2,2-                
HETNAM   3 8NL  DIMETHYL-CYCLOPROPANE-1-CARBOXYLATE                             
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  MSE    36(C5 H11 N O2 SE)                                           
FORMUL   7  8NL    6(C23 H22 CL F3 O2)                                          
FORMUL   8  SO4    6(O4 S 2-)                                                   
FORMUL  19  HOH   *471(H2 O)                                                    
HELIX    1 AA1 ARG A   15  ASP A   20  5                                   6    
HELIX    2 AA2 VAL A   22  ARG A   29  1                                   8    
HELIX    3 AA3 GLY A   47  VAL A   51  5                                   5    
HELIX    4 AA4 ASP A   53  THR A   58  1                                   6    
HELIX    5 AA5 THR A   58  ALA A   68  1                                  11    
HELIX    6 AA6 LEU A   79  HIS A   91  1                                  13    
HELIX    7 AA7 PRO A  112  LEU A  117  1                                   6    
HELIX    8 AA8 THR A  125  LEU A  131  1                                   7    
HELIX    9 AA9 ARG A  147  MSE A  156  1                                  10    
HELIX   10 AB1 PRO A  166  PHE A  170  5                                   5    
HELIX   11 AB2 VAL A  177  THR A  181  5                                   5    
HELIX   12 AB3 GLU A  186  ILE A  192  5                                   7    
HELIX   13 AB4 PRO A  206  PHE A  217  1                                  12    
HELIX   14 AB5 ALA A  231  MSE A  236  1                                   6    
HELIX   15 AB6 MSE A  236  ALA A  250  1                                  15    
HELIX   16 AB7 ARG B   15  ASP B   20  5                                   6    
HELIX   17 AB8 VAL B   22  ALA B   28  1                                   7    
HELIX   18 AB9 GLY B   47  VAL B   51  5                                   5    
HELIX   19 AC1 ASP B   53  THR B   58  1                                   6    
HELIX   20 AC2 THR B   58  ARG B   67  1                                  10    
HELIX   21 AC3 LEU B   79  HIS B   91  1                                  13    
HELIX   22 AC4 PRO B  112  LEU B  117  1                                   6    
HELIX   23 AC5 THR B  125  LEU B  131  1                                   7    
HELIX   24 AC6 ARG B  147  MSE B  156  1                                  10    
HELIX   25 AC7 PRO B  166  PHE B  170  5                                   5    
HELIX   26 AC8 THR B  176  THR B  181  1                                   6    
HELIX   27 AC9 GLU B  186  ILE B  192  5                                   7    
HELIX   28 AD1 PRO B  206  GLU B  216  1                                  11    
HELIX   29 AD2 ALA B  231  MSE B  236  1                                   6    
HELIX   30 AD3 MSE B  236  ALA B  250  1                                  15    
HELIX   31 AD4 ARG C   15  ASP C   20  5                                   6    
HELIX   32 AD5 VAL C   22  ARG C   29  1                                   8    
HELIX   33 AD6 GLY C   47  VAL C   51  5                                   5    
HELIX   34 AD7 ASP C   53  THR C   58  1                                   6    
HELIX   35 AD8 THR C   58  ALA C   68  1                                  11    
HELIX   36 AD9 LEU C   79  HIS C   91  1                                  13    
HELIX   37 AE1 PRO C  112  LEU C  117  1                                   6    
HELIX   38 AE2 THR C  125  LEU C  131  1                                   7    
HELIX   39 AE3 ARG C  147  MSE C  156  1                                  10    
HELIX   40 AE4 PRO C  166  PHE C  170  5                                   5    
HELIX   41 AE5 THR C  176  THR C  181  1                                   6    
HELIX   42 AE6 GLU C  186  ILE C  192  5                                   7    
HELIX   43 AE7 PRO C  206  PHE C  217  1                                  12    
HELIX   44 AE8 ALA C  231  MSE C  236  1                                   6    
HELIX   45 AE9 MSE C  236  ALA C  250  1                                  15    
HELIX   46 AF1 PRO C  251  TYR C  254  5                                   4    
HELIX   47 AF2 ARG D   15  ASP D   20  5                                   6    
HELIX   48 AF3 VAL D   22  ARG D   29  1                                   8    
HELIX   49 AF4 GLY D   47  VAL D   51  5                                   5    
HELIX   50 AF5 ASP D   53  THR D   58  1                                   6    
HELIX   51 AF6 THR D   58  ARG D   67  1                                  10    
HELIX   52 AF7 LEU D   79  HIS D   91  1                                  13    
HELIX   53 AF8 PRO D  112  LEU D  117  1                                   6    
HELIX   54 AF9 THR D  125  LEU D  131  1                                   7    
HELIX   55 AG1 ARG D  147  MSE D  156  1                                  10    
HELIX   56 AG2 PRO D  166  PHE D  170  5                                   5    
HELIX   57 AG3 THR D  176  THR D  181  1                                   6    
HELIX   58 AG4 GLU D  186  ILE D  192  5                                   7    
HELIX   59 AG5 PRO D  206  PHE D  217  1                                  12    
HELIX   60 AG6 ALA D  231  MSE D  236  1                                   6    
HELIX   61 AG7 MSE D  236  ALA D  250  1                                  15    
HELIX   62 AG8 ARG E   15  ASP E   20  5                                   6    
HELIX   63 AG9 VAL E   22  ARG E   29  1                                   8    
HELIX   64 AH1 GLY E   47  VAL E   51  5                                   5    
HELIX   65 AH2 ASP E   53  THR E   58  1                                   6    
HELIX   66 AH3 THR E   58  ALA E   68  1                                  11    
HELIX   67 AH4 LEU E   79  HIS E   91  1                                  13    
HELIX   68 AH5 PRO E  112  LEU E  117  1                                   6    
HELIX   69 AH6 THR E  125  LEU E  131  1                                   7    
HELIX   70 AH7 ARG E  147  MSE E  156  1                                  10    
HELIX   71 AH8 PRO E  166  PHE E  170  5                                   5    
HELIX   72 AH9 THR E  176  THR E  181  1                                   6    
HELIX   73 AI1 GLU E  186  ILE E  192  5                                   7    
HELIX   74 AI2 PRO E  206  PHE E  217  1                                  12    
HELIX   75 AI3 ALA E  231  MSE E  236  1                                   6    
HELIX   76 AI4 MSE E  236  ALA E  250  1                                  15    
HELIX   77 AI5 PRO E  251  TYR E  254  5                                   4    
HELIX   78 AI6 ARG F   15  ASP F   20  5                                   6    
HELIX   79 AI7 VAL F   22  ALA F   28  1                                   7    
HELIX   80 AI8 GLY F   47  VAL F   51  5                                   5    
HELIX   81 AI9 ASP F   53  THR F   58  1                                   6    
HELIX   82 AJ1 THR F   58  ARG F   67  1                                  10    
HELIX   83 AJ2 LEU F   79  HIS F   91  1                                  13    
HELIX   84 AJ3 PRO F  112  LEU F  117  1                                   6    
HELIX   85 AJ4 THR F  125  LEU F  131  1                                   7    
HELIX   86 AJ5 ARG F  147  MSE F  156  1                                  10    
HELIX   87 AJ6 PRO F  166  PHE F  170  5                                   5    
HELIX   88 AJ7 THR F  176  THR F  181  1                                   6    
HELIX   89 AJ8 GLU F  186  ILE F  192  5                                   7    
HELIX   90 AJ9 PRO F  206  GLU F  216  1                                  11    
HELIX   91 AK1 ALA F  231  MSE F  236  1                                   6    
HELIX   92 AK2 MSE F  236  ALA F  250  1                                  15    
SHEET    1 AA1 6 ARG A  32  HIS A  34  0                                        
SHEET    2 AA1 6 VAL A   3  ILE A   9  1  N  LEU A   8   O  HIS A  34           
SHEET    3 AA1 6 GLN A  71  HIS A  77  1  O  ILE A  73   N  ILE A   7           
SHEET    4 AA1 6 VAL A  95  LEU A 101  1  O  ILE A  99   N  LEU A  74           
SHEET    5 AA1 6 ARG A 194  ALA A 199  1  O  LEU A 195   N  TYR A 100           
SHEET    6 AA1 6 ALA A 222  LEU A 226  1  O  ALA A 222   N  TYR A 196           
SHEET    1 AA2 3 ILE A 132  VAL A 135  0                                        
SHEET    2 AA2 3 GLY A 140  ALA A 143 -1  O  GLN A 142   N  GLN A 133           
SHEET    3 AA2 3 GLN A 174  SER A 175 -1  O  GLN A 174   N  LEU A 141           
SHEET    1 AA3 6 ARG B  32  HIS B  34  0                                        
SHEET    2 AA3 6 VAL B   3  ILE B   9  1  N  LEU B   8   O  HIS B  34           
SHEET    3 AA3 6 GLN B  71  HIS B  77  1  O  LEU B  75   N  ILE B   7           
SHEET    4 AA3 6 VAL B  95  LEU B 101  1  O  LEU B 101   N  GLY B  76           
SHEET    5 AA3 6 ARG B 194  ALA B 199  1  O  LEU B 195   N  TYR B 100           
SHEET    6 AA3 6 ALA B 222  LEU B 226  1  O  VAL B 224   N  GLU B 198           
SHEET    1 AA4 3 ILE B 132  VAL B 135  0                                        
SHEET    2 AA4 3 GLY B 140  ALA B 143 -1  O  GLN B 142   N  GLN B 133           
SHEET    3 AA4 3 GLN B 174  SER B 175 -1  O  GLN B 174   N  LEU B 141           
SHEET    1 AA5 6 ARG C  32  HIS C  34  0                                        
SHEET    2 AA5 6 VAL C   3  ILE C   9  1  N  LEU C   8   O  HIS C  34           
SHEET    3 AA5 6 GLN C  71  HIS C  77  1  O  LEU C  75   N  ILE C   9           
SHEET    4 AA5 6 VAL C  95  LEU C 101  1  O  ILE C  99   N  LEU C  74           
SHEET    5 AA5 6 ARG C 194  ALA C 199  1  O  LEU C 195   N  TYR C 100           
SHEET    6 AA5 6 ALA C 222  LEU C 226  1  O  ALA C 222   N  ARG C 194           
SHEET    1 AA6 3 ILE C 132  VAL C 135  0                                        
SHEET    2 AA6 3 GLY C 140  ALA C 143 -1  O  GLY C 140   N  VAL C 135           
SHEET    3 AA6 3 GLN C 174  SER C 175 -1  O  GLN C 174   N  LEU C 141           
SHEET    1 AA7 6 ARG D  32  HIS D  34  0                                        
SHEET    2 AA7 6 VAL D   3  ILE D   9  1  N  ILE D   6   O  ARG D  32           
SHEET    3 AA7 6 GLN D  71  HIS D  77  1  O  ILE D  73   N  ILE D   7           
SHEET    4 AA7 6 VAL D  95  LEU D 101  1  O  ALA D  96   N  SER D  72           
SHEET    5 AA7 6 ARG D 194  ALA D 199  1  O  LEU D 195   N  TYR D 100           
SHEET    6 AA7 6 ALA D 222  LEU D 226  1  O  ALA D 222   N  TYR D 196           
SHEET    1 AA8 3 ILE D 132  VAL D 135  0                                        
SHEET    2 AA8 3 GLY D 140  ALA D 143 -1  O  GLY D 140   N  VAL D 135           
SHEET    3 AA8 3 GLN D 174  SER D 175 -1  O  GLN D 174   N  LEU D 141           
SHEET    1 AA9 6 ARG E  32  HIS E  34  0                                        
SHEET    2 AA9 6 VAL E   3  ILE E   9  1  N  LEU E   8   O  HIS E  34           
SHEET    3 AA9 6 GLN E  71  HIS E  77  1  O  LEU E  75   N  ILE E   9           
SHEET    4 AA9 6 VAL E  95  LEU E 101  1  O  LEU E 101   N  GLY E  76           
SHEET    5 AA9 6 ARG E 194  ALA E 199  1  O  ILE E 197   N  TYR E 100           
SHEET    6 AA9 6 ALA E 222  LEU E 226  1  O  LEU E 226   N  GLU E 198           
SHEET    1 AB1 3 ILE E 132  VAL E 135  0                                        
SHEET    2 AB1 3 GLY E 140  ALA E 143 -1  O  GLN E 142   N  GLN E 133           
SHEET    3 AB1 3 THR E 173  SER E 175 -1  O  GLN E 174   N  LEU E 141           
SHEET    1 AB2 6 ARG F  32  HIS F  34  0                                        
SHEET    2 AB2 6 VAL F   3  ILE F   9  1  N  ILE F   6   O  ARG F  32           
SHEET    3 AB2 6 GLN F  71  HIS F  77  1  O  ILE F  73   N  ILE F   7           
SHEET    4 AB2 6 VAL F  95  LEU F 101  1  O  ILE F  99   N  GLY F  76           
SHEET    5 AB2 6 ARG F 194  ALA F 199  1  O  LEU F 195   N  TYR F 100           
SHEET    6 AB2 6 ALA F 222  LEU F 226  1  O  ALA F 222   N  TYR F 196           
SHEET    1 AB3 3 ILE F 132  VAL F 135  0                                        
SHEET    2 AB3 3 GLY F 140  ALA F 143 -1  O  GLY F 140   N  VAL F 135           
SHEET    3 AB3 3 GLN F 174  SER F 175 -1  O  GLN F 174   N  LEU F 141           
LINK         C   ASP A  53                 N   MSE A  54     1555   1555  1.33  
LINK         C   MSE A  54                 N   GLU A  55     1555   1555  1.33  
LINK         C   PHE A 155                 N   MSE A 156     1555   1555  1.34  
LINK         C   MSE A 156                 N   GLY A 157     1555   1555  1.33  
LINK         C   GLY A 163                 N   MSE A 164     1555   1555  1.32  
LINK         C   MSE A 164                 N   PRO A 165     1555   1555  1.33  
LINK         C   PRO A 184                 N   MSE A 185     1555   1555  1.33  
LINK         C   MSE A 185                 N   GLU A 186     1555   1555  1.33  
LINK         C   GLN A 212                 N   MSE A 213     1555   1555  1.33  
LINK         C   MSE A 213                 N   GLN A 214     1555   1555  1.33  
LINK         C   SER A 235                 N   MSE A 236     1555   1555  1.34  
LINK         C   MSE A 236                 N   PRO A 237     1555   1555  1.33  
LINK         C   ASP B  53                 N   MSE B  54     1555   1555  1.33  
LINK         C   MSE B  54                 N   GLU B  55     1555   1555  1.35  
LINK         C   PHE B 155                 N   MSE B 156     1555   1555  1.34  
LINK         C   MSE B 156                 N   GLY B 157     1555   1555  1.33  
LINK         C   GLY B 163                 N   MSE B 164     1555   1555  1.31  
LINK         C   MSE B 164                 N   PRO B 165     1555   1555  1.33  
LINK         C   PRO B 184                 N   MSE B 185     1555   1555  1.34  
LINK         C   MSE B 185                 N   GLU B 186     1555   1555  1.33  
LINK         C   GLN B 212                 N   MSE B 213     1555   1555  1.33  
LINK         C   MSE B 213                 N   GLN B 214     1555   1555  1.34  
LINK         C   SER B 235                 N   MSE B 236     1555   1555  1.33  
LINK         C   MSE B 236                 N   PRO B 237     1555   1555  1.33  
LINK         C   ASP C  53                 N   MSE C  54     1555   1555  1.32  
LINK         C   MSE C  54                 N   GLU C  55     1555   1555  1.33  
LINK         C   PHE C 155                 N   MSE C 156     1555   1555  1.33  
LINK         C   MSE C 156                 N   GLY C 157     1555   1555  1.33  
LINK         C   GLY C 163                 N   MSE C 164     1555   1555  1.33  
LINK         C   MSE C 164                 N   PRO C 165     1555   1555  1.33  
LINK         C   PRO C 184                 N   MSE C 185     1555   1555  1.33  
LINK         C   MSE C 185                 N   GLU C 186     1555   1555  1.33  
LINK         C   GLN C 212                 N   MSE C 213     1555   1555  1.32  
LINK         C   MSE C 213                 N   GLN C 214     1555   1555  1.35  
LINK         C   SER C 235                 N   MSE C 236     1555   1555  1.33  
LINK         C   MSE C 236                 N   PRO C 237     1555   1555  1.33  
LINK         C   ASP D  53                 N   MSE D  54     1555   1555  1.32  
LINK         C   MSE D  54                 N   GLU D  55     1555   1555  1.34  
LINK         C   PHE D 155                 N   MSE D 156     1555   1555  1.32  
LINK         C   MSE D 156                 N   GLY D 157     1555   1555  1.33  
LINK         C   GLY D 163                 N   MSE D 164     1555   1555  1.32  
LINK         C   MSE D 164                 N   PRO D 165     1555   1555  1.33  
LINK         C   PRO D 184                 N   MSE D 185     1555   1555  1.33  
LINK         C   MSE D 185                 N   GLU D 186     1555   1555  1.33  
LINK         C   GLN D 212                 N   MSE D 213     1555   1555  1.33  
LINK         C   MSE D 213                 N   GLN D 214     1555   1555  1.33  
LINK         C   SER D 235                 N   MSE D 236     1555   1555  1.33  
LINK         C   MSE D 236                 N   PRO D 237     1555   1555  1.34  
LINK         C   ASP E  53                 N   MSE E  54     1555   1555  1.34  
LINK         C   MSE E  54                 N   GLU E  55     1555   1555  1.33  
LINK         C   PHE E 155                 N   MSE E 156     1555   1555  1.33  
LINK         C   MSE E 156                 N   GLY E 157     1555   1555  1.33  
LINK         C   MSE E 164                 N   PRO E 165     1555   1555  1.38  
LINK         C   PRO E 184                 N   MSE E 185     1555   1555  1.33  
LINK         C   MSE E 185                 N   GLU E 186     1555   1555  1.33  
LINK         C   GLN E 212                 N   MSE E 213     1555   1555  1.32  
LINK         C   MSE E 213                 N   GLN E 214     1555   1555  1.34  
LINK         C   SER E 235                 N   MSE E 236     1555   1555  1.32  
LINK         C   MSE E 236                 N   PRO E 237     1555   1555  1.34  
LINK         C   ASP F  53                 N   MSE F  54     1555   1555  1.32  
LINK         C   MSE F  54                 N   GLU F  55     1555   1555  1.31  
LINK         C   PHE F 155                 N   MSE F 156     1555   1555  1.32  
LINK         C   MSE F 156                 N   GLY F 157     1555   1555  1.33  
LINK         C   GLY F 163                 N   MSE F 164     1555   1555  1.32  
LINK         C   MSE F 164                 N   PRO F 165     1555   1555  1.33  
LINK         C   PRO F 184                 N   MSE F 185     1555   1555  1.31  
LINK         C   MSE F 185                 N   GLU F 186     1555   1555  1.34  
LINK         C   GLN F 212                 N   MSE F 213     1555   1555  1.34  
LINK         C   MSE F 213                 N   GLN F 214     1555   1555  1.33  
LINK         C   SER F 235                 N   MSE F 236     1555   1555  1.33  
LINK         C   MSE F 236                 N   PRO F 237     1555   1555  1.34  
LINK         CE  MSE E 164                SE   MSE F 164     1555   8554  1.81  
CISPEP   1 GLU A  120    PRO A  121          0        -3.79                     
CISPEP   2 GLU B  120    PRO B  121          0        -2.19                     
CISPEP   3 GLU C  120    PRO C  121          0        -2.35                     
CISPEP   4 GLU D  120    PRO D  121          0         0.09                     
CISPEP   5 GLU E  120    PRO E  121          0        -2.45                     
CISPEP   6 GLU F  120    PRO F  121          0        -5.53                     
SITE     1 AC1 12 ALA A  12  ASN A  14  SER A  78  LEU A  79                    
SITE     2 AC1 12 VAL A 116  THR A 125  ALA A 128  ALA A 143                    
SITE     3 AC1 12 PHE A 155  PHE A 179  VAL A 204  HIS A 230                    
SITE     1 AC2  5 SER A 235  MSE A 236  PRO A 237  GLU A 238                    
SITE     2 AC2  5 ARG A 239                                                     
SITE     1 AC3 10 ALA B  12  ASN B  14  SER B  78  LEU B  79                    
SITE     2 AC3 10 ALA B 128  ILE B 132  PHE B 155  PHE B 170                    
SITE     3 AC3 10 PHE B 179  HIS B 230                                          
SITE     1 AC4  5 SER B 235  MSE B 236  PRO B 237  GLU B 238                    
SITE     2 AC4  5 ARG B 239                                                     
SITE     1 AC5 11 ALA C  12  ASN C  14  SER C  78  LEU C  79                    
SITE     2 AC5 11 ALA C 128  ILE C 132  PHE C 155  PHE C 170                    
SITE     3 AC5 11 PHE C 179  VAL C 204  HIS C 230                               
SITE     1 AC6  5 SER C 235  MSE C 236  PRO C 237  GLU C 238                    
SITE     2 AC6  5 ARG C 239                                                     
SITE     1 AC7 13 ALA D  12  LEU D  13  ASN D  14  SER D  78                    
SITE     2 AC7 13 LEU D  79  VAL D 116  THR D 125  ALA D 128                    
SITE     3 AC7 13 ILE D 132  ALA D 143  PHE D 155  PHE D 179                    
SITE     4 AC7 13 HIS D 230                                                     
SITE     1 AC8  5 SER D 235  MSE D 236  PRO D 237  GLU D 238                    
SITE     2 AC8  5 ARG D 239                                                     
SITE     1 AC9 17 ALA E  12  LEU E  13  ASN E  14  SER E  78                    
SITE     2 AC9 17 LEU E  79  VAL E 116  THR E 125  ALA E 128                    
SITE     3 AC9 17 LEU E 129  ILE E 132  LEU E 141  ALA E 143                    
SITE     4 AC9 17 LEU E 151  PHE E 155  MSE E 156  PHE E 179                    
SITE     5 AC9 17 HIS E 230                                                     
SITE     1 AD1  6 SER E 235  MSE E 236  PRO E 237  GLU E 238                    
SITE     2 AD1  6 ARG E 239  HOH E 425                                          
SITE     1 AD2 14 GLY F  11  ALA F  12  ASN F  14  SER F  78                    
SITE     2 AD2 14 LEU F  79  VAL F 116  THR F 125  ALA F 128                    
SITE     3 AD2 14 ALA F 143  PHE F 155  MSE F 156  PHE F 170                    
SITE     4 AD2 14 PHE F 179  HIS F 230                                          
SITE     1 AD3  4 MSE F 236  PRO F 237  GLU F 238  ARG F 239                    
CRYST1  168.857  168.857  123.864  90.00  90.00  90.00 P 42 21 2    48          
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      0.005922  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005922  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008073        0.00000                         
TER    1915      TYR A 254                                                      
TER    3830      TYR B 254                                                      
TER    5739      TYR C 254                                                      
TER    7657      TYR D 254                                                      
TER    9545      TYR E 254                                                      
TER   11373      GLU F 253                                                      
MASTER      703    0   48   92   54    0   33    612042    6  563  138          
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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