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LongText Report for: 5tnr-pdb

Name Class
5tnr-pdb
HEADER    HYDROLASE                               14-OCT-16   5TNR              
TITLE     CRYSTAL STRUCTURE OF THE E153Q MUTANT OF THE CFTR INHIBITORY FACTOR   
TITLE    2 CIF CONTAINING THE ADDUCTED 16,17-EPDPE HYDROLYSIS INTERMEDIATE      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CFTR INHIBITORY FACTOR;                                    
COMPND   3 CHAIN: C, D, A, B;                                                   
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA (STRAIN UCBPP-PA14);     
SOURCE   3 ORGANISM_TAXID: 208963;                                              
SOURCE   4 STRAIN: UCBPP-PA14;                                                  
SOURCE   5 GENE: PA14_26090;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: TOP10                                      
KEYWDS    EPOXIDE HYDROLASE, HYDROXYALKYL-ENZYME INTERMEDIATE, HYDROLASE        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.L.HVORECNY,D.R.MADDEN                                               
REVDAT   1   18-OCT-17 5TNR    0                                                
JRNL        AUTH   K.L.HVORECNY,D.R.MADDEN                                      
JRNL        TITL   CRYSTAL STRUCTURE OF THE E153Q MUTANT OF THE CFTR INHIBITORY 
JRNL        TITL 2 FACTOR CIF CONTAINING THE ADDUCTED 16,17-EPDPE HYDROLYSIS    
JRNL        TITL 3 INTERMEDIATE                                                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10_2155: ???)                              
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.74                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 115459                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.163                           
REMARK   3   R VALUE            (WORKING SET) : 0.161                           
REMARK   3   FREE R VALUE                     : 0.189                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5759                            
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 46.7588 -  5.5899    0.99     3756   288  0.1638 0.1865        
REMARK   3     2  5.5899 -  4.4380    1.00     3951     0  0.1306 0.0000        
REMARK   3     3  4.4380 -  3.8773    1.00     3638   288  0.1307 0.1334        
REMARK   3     4  3.8773 -  3.5229    1.00     3601   288  0.1393 0.1496        
REMARK   3     5  3.5229 -  3.2705    1.00     3873     0  0.1418 0.0000        
REMARK   3     6  3.2705 -  3.0777    1.00     3591   288  0.1567 0.1795        
REMARK   3     7  3.0777 -  2.9236    1.00     3590   288  0.1652 0.1802        
REMARK   3     8  2.9236 -  2.7964    1.00     3841     0  0.1575 0.0000        
REMARK   3     9  2.7964 -  2.6887    1.00     3566   288  0.1565 0.1935        
REMARK   3    10  2.6887 -  2.5960    1.00     3571   288  0.1618 0.1895        
REMARK   3    11  2.5960 -  2.5148    1.00     3870     0  0.1553 0.0000        
REMARK   3    12  2.5148 -  2.4429    0.99     3507   288  0.1595 0.1913        
REMARK   3    13  2.4429 -  2.3786    1.00     3558   288  0.1619 0.1938        
REMARK   3    14  2.3786 -  2.3206    1.00     3842     0  0.1563 0.0000        
REMARK   3    15  2.3206 -  2.2678    1.00     3541   288  0.1612 0.1793        
REMARK   3    16  2.2678 -  2.2196    1.00     3542   288  0.1572 0.1915        
REMARK   3    17  2.2196 -  2.1752    1.00     3838     0  0.1672 0.0000        
REMARK   3    18  2.1752 -  2.1341    1.00     3523   288  0.1627 0.2254        
REMARK   3    19  2.1341 -  2.0960    1.00     3524   288  0.1650 0.2075        
REMARK   3    20  2.0960 -  2.0605    0.99     3841     0  0.1764 0.0000        
REMARK   3    21  2.0605 -  2.0272    0.99     3520   288  0.1809 0.2211        
REMARK   3    22  2.0272 -  1.9960    1.00     3483   288  0.1865 0.2238        
REMARK   3    23  1.9960 -  1.9667    1.00     3813     0  0.1860 0.0000        
REMARK   3    24  1.9667 -  1.9390    1.00     3556   288  0.1950 0.2240        
REMARK   3    25  1.9390 -  1.9128    1.00     3519   287  0.1932 0.2376        
REMARK   3    26  1.9128 -  1.8879    1.00     3811     0  0.2070 0.0000        
REMARK   3    27  1.8879 -  1.8643    1.00     3558   288  0.2133 0.2507        
REMARK   3    28  1.8643 -  1.8419    1.00     3512   288  0.2209 0.2430        
REMARK   3    29  1.8419 -  1.8205    1.00     3782     0  0.2260 0.0000        
REMARK   3    30  1.8205 -  1.8000    1.00     3582   288  0.2486 0.2825        
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)     : 0.170            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.300           
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      :  0.007           9853                                  
REMARK   3   ANGLE     :  0.856          13373                                  
REMARK   3   CHIRALITY :  0.054           1370                                  
REMARK   3   PLANARITY :  0.006           1773                                  
REMARK   3   DIHEDRAL  : 16.088           5803                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ( CHAIN C AND RESID 25:317 )                           
REMARK   3    ORIGIN FOR THE GROUP (A): -16.0845  -5.9703 -27.0516              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0806 T22:   0.0836                                     
REMARK   3      T33:   0.1022 T12:   0.0012                                     
REMARK   3      T13:  -0.0160 T23:   0.0059                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8333 L22:   0.8478                                     
REMARK   3      L33:   0.7371 L12:   0.0076                                     
REMARK   3      L13:   0.0613 L23:  -0.0413                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0191 S12:   0.0447 S13:  -0.0931                       
REMARK   3      S21:  -0.0781 S22:   0.0249 S23:   0.1383                       
REMARK   3      S31:   0.0555 S32:  -0.0997 S33:  -0.0045                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: ( CHAIN D AND RESID 25:317 )                           
REMARK   3    ORIGIN FOR THE GROUP (A):  22.8969 -14.9980 -15.6400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0827 T22:   0.0842                                     
REMARK   3      T33:   0.0618 T12:   0.0218                                     
REMARK   3      T13:  -0.0049 T23:   0.0104                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7214 L22:   0.9625                                     
REMARK   3      L33:   0.4032 L12:  -0.2209                                     
REMARK   3      L13:   0.0499 L23:  -0.0698                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0122 S12:  -0.0066 S13:  -0.0531                       
REMARK   3      S21:   0.0365 S22:   0.0052 S23:  -0.0586                       
REMARK   3      S31:  -0.0019 S32:   0.0477 S33:   0.0082                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 25:317 )                           
REMARK   3    ORIGIN FOR THE GROUP (A):  16.2749  21.9881 -27.3300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0849 T22:   0.0865                                     
REMARK   3      T33:   0.0655 T12:   0.0003                                     
REMARK   3      T13:   0.0156 T23:   0.0068                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6926 L22:   0.8363                                     
REMARK   3      L33:   0.6800 L12:   0.0114                                     
REMARK   3      L13:   0.0104 L23:   0.1584                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0052 S12:   0.0830 S13:   0.0546                       
REMARK   3      S21:  -0.1161 S22:   0.0172 S23:  -0.0887                       
REMARK   3      S31:  -0.0500 S32:   0.0988 S33:  -0.0046                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: ( CHAIN B AND RESID 25:317 )                           
REMARK   3    ORIGIN FOR THE GROUP (A): -22.9907  30.8803 -15.6512              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0727 T22:   0.0877                                     
REMARK   3      T33:   0.1046 T12:   0.0141                                     
REMARK   3      T13:   0.0054 T23:  -0.0125                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1611 L22:   1.1781                                     
REMARK   3      L33:   0.5864 L12:  -0.4043                                     
REMARK   3      L13:  -0.1289 L23:  -0.0105                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0253 S12:  -0.0147 S13:   0.0191                       
REMARK   3      S21:   0.0082 S22:  -0.0232 S23:   0.1778                       
REMARK   3      S31:  -0.0180 S32:  -0.0944 S33:  -0.0013                       
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 5TNR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-OCT-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000223249.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-JUL-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL9-2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS MAY 1, 2016                    
REMARK 200  DATA SCALING SOFTWARE          : XDS MAY 1, 2016                    
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 115528                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.743                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.750                              
REMARK 200  R MERGE                    (I) : 0.14500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 13.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.83                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.59700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.980                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.6.0                                          
REMARK 200 STARTING MODEL: 3KD2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM ACETATE, PH5 CALCIUM CHLORIDE     
REMARK 280  PEG 8000, PH 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       88.21200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       88.21200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       41.92300            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       84.45600            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       41.92300            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       84.45600            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       88.21200            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       41.92300            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       84.45600            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       88.21200            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       41.92300            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       84.45600            
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                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20490 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20550 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH D 501  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH D 801  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH D 831  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY C   318                                                      
REMARK 465     ARG C   319                                                      
REMARK 465     HIS C   320                                                      
REMARK 465     HIS C   321                                                      
REMARK 465     HIS C   322                                                      
REMARK 465     HIS C   323                                                      
REMARK 465     HIS C   324                                                      
REMARK 465     HIS C   325                                                      
REMARK 465     GLY D   318                                                      
REMARK 465     ARG D   319                                                      
REMARK 465     HIS D   320                                                      
REMARK 465     HIS D   321                                                      
REMARK 465     HIS D   322                                                      
REMARK 465     HIS D   323                                                      
REMARK 465     HIS D   324                                                      
REMARK 465     HIS D   325                                                      
REMARK 465     GLY A   318                                                      
REMARK 465     ARG A   319                                                      
REMARK 465     HIS A   320                                                      
REMARK 465     HIS A   321                                                      
REMARK 465     HIS A   322                                                      
REMARK 465     HIS A   323                                                      
REMARK 465     HIS A   324                                                      
REMARK 465     HIS A   325                                                      
REMARK 465     GLY B   318                                                      
REMARK 465     ARG B   319                                                      
REMARK 465     HIS B   320                                                      
REMARK 465     HIS B   321                                                      
REMARK 465     HIS B   322                                                      
REMARK 465     HIS B   323                                                      
REMARK 465     HIS B   324                                                      
REMARK 465     HIS B   325                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH D   509     O    HOH D   772              1.81            
REMARK 500   O    HOH D   635     O    HOH D   724              1.85            
REMARK 500   O    HOH D   713     O    HOH D   768              1.89            
REMARK 500   O    HOH C   700     O    HOH C   726              1.92            
REMARK 500   O    HOH D   621     O    HOH D   777              2.00            
REMARK 500   OE1  GLU A   172     O    HOH A   501              2.02            
REMARK 500   O    HOH A   540     O    HOH A   771              2.02            
REMARK 500   O    HOH C   756     O    HOH C   760              2.03            
REMARK 500   O    HOH C   508     O    HOH C   515              2.04            
REMARK 500   O    HOH A   748     O    HOH A   776              2.04            
REMARK 500   O    HOH C   676     O    HOH C   756              2.06            
REMARK 500   O    HOH A   676     O    HOH A   756              2.07            
REMARK 500   O    HOH B   605     O    HOH B   736              2.07            
REMARK 500   O    HOH A   570     O    HOH A   655              2.09            
REMARK 500   O    HOH B   736     O    HOH B   771              2.12            
REMARK 500   O    HOH A   508     O    HOH A   765              2.13            
REMARK 500   O    HOH B   521     O    HOH B   609              2.13            
REMARK 500   O    HOH C   647     O    HOH C   769              2.14            
REMARK 500   O    HOH D   519     O    HOH D   676              2.15            
REMARK 500   O    HOH D   756     O    HOH D   810              2.16            
REMARK 500   O    HOH A   681     O    HOH A   723              2.16            
REMARK 500   O    HOH B   717     O    HOH B   743              2.16            
REMARK 500   O    HOH C   510     O    HOH C   746              2.17            
REMARK 500   O    HOH D   700     O    HOH D   789              2.18            
REMARK 500   O    HOH C   565     O    HOH C   724              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   O    HOH D   743     O    HOH B   694     5545     2.10            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP C 129     -131.30     60.46                                   
REMARK 500    CYS C 303       57.93   -142.25                                   
REMARK 500    THR D  99      -64.01    -97.14                                   
REMARK 500    ASP D 129     -130.19     56.93                                   
REMARK 500    ALA D 154      146.25   -171.32                                   
REMARK 500    ASP D 184     -159.57    -84.90                                   
REMARK 500    ASP A 129     -131.79     60.90                                   
REMARK 500    CYS A 303       58.10   -140.43                                   
REMARK 500    THR B  99      -62.93    -93.65                                   
REMARK 500    ASP B 129     -132.04     57.89                                   
REMARK 500    ALA B 154      142.83   -173.35                                   
REMARK 500    CYS B 303       51.71   -141.98                                   
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 C 795        DISTANCE =  6.13 ANGSTROMS                       
REMARK 525    HOH D 829        DISTANCE =  5.87 ANGSTROMS                       
REMARK 525    HOH D 830        DISTANCE =  5.90 ANGSTROMS                       
REMARK 525    HOH D 831        DISTANCE =  5.98 ANGSTROMS                       
REMARK 525    HOH D 832        DISTANCE =  6.61 ANGSTROMS                       
REMARK 525    HOH D 833        DISTANCE =  6.75 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7EZ C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 7EZ A 401 and ASP A    
REMARK 800  129                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 7EZ B 401 and ASP B    
REMARK 800  129                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 7EZ D 401 and ASP D    
REMARK 800  129                                                                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5TNF   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5TNG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5TNH   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5TNL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5TNM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5TNN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5TNS   RELATED DB: PDB                                   
DBREF1 5TNR C   25   325  UNP                  A0A0M3KL26_PSEAB                 
DBREF2 5TNR C     A0A0M3KL26                          1         301             
DBREF1 5TNR D   25   325  UNP                  A0A0M3KL26_PSEAB                 
DBREF2 5TNR D     A0A0M3KL26                          1         301             
DBREF1 5TNR A   25   325  UNP                  A0A0M3KL26_PSEAB                 
DBREF2 5TNR A     A0A0M3KL26                          1         301             
DBREF1 5TNR B   25   325  UNP                  A0A0M3KL26_PSEAB                 
DBREF2 5TNR B     A0A0M3KL26                          1         301             
SEQADV 5TNR GLN C  153  UNP  A0A0M3KL2 GLU   129 ENGINEERED MUTATION            
SEQADV 5TNR GLN D  153  UNP  A0A0M3KL2 GLU   129 ENGINEERED MUTATION            
SEQADV 5TNR GLN A  153  UNP  A0A0M3KL2 GLU   129 ENGINEERED MUTATION            
SEQADV 5TNR GLN B  153  UNP  A0A0M3KL2 GLU   129 ENGINEERED MUTATION            
SEQRES   1 C  301  ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA          
SEQRES   2 C  301  TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS          
SEQRES   3 C  301  GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE          
SEQRES   4 C  301  GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU          
SEQRES   5 C  301  LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO          
SEQRES   6 C  301  GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER          
SEQRES   7 C  301  GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG          
SEQRES   8 C  301  GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS          
SEQRES   9 C  301  ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS          
SEQRES  10 C  301  ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLN ALA          
SEQRES  11 C  301  PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE          
SEQRES  12 C  301  THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE          
SEQRES  13 C  301  PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA          
SEQRES  14 C  301  GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER          
SEQRES  15 C  301  HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU          
SEQRES  16 C  301  ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU          
SEQRES  17 C  301  ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER          
SEQRES  18 C  301  VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN          
SEQRES  19 C  301  MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY          
SEQRES  20 C  301  MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA          
SEQRES  21 C  301  GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS          
SEQRES  22 C  301  TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU          
SEQRES  23 C  301  VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS          
SEQRES  24 C  301  HIS HIS                                                      
SEQRES   1 D  301  ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA          
SEQRES   2 D  301  TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS          
SEQRES   3 D  301  GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE          
SEQRES   4 D  301  GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU          
SEQRES   5 D  301  LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO          
SEQRES   6 D  301  GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER          
SEQRES   7 D  301  GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG          
SEQRES   8 D  301  GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS          
SEQRES   9 D  301  ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS          
SEQRES  10 D  301  ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLN ALA          
SEQRES  11 D  301  PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE          
SEQRES  12 D  301  THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE          
SEQRES  13 D  301  PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA          
SEQRES  14 D  301  GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER          
SEQRES  15 D  301  HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU          
SEQRES  16 D  301  ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU          
SEQRES  17 D  301  ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER          
SEQRES  18 D  301  VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN          
SEQRES  19 D  301  MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY          
SEQRES  20 D  301  MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA          
SEQRES  21 D  301  GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS          
SEQRES  22 D  301  TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU          
SEQRES  23 D  301  VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS          
SEQRES  24 D  301  HIS HIS                                                      
SEQRES   1 A  301  ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA          
SEQRES   2 A  301  TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS          
SEQRES   3 A  301  GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE          
SEQRES   4 A  301  GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU          
SEQRES   5 A  301  LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO          
SEQRES   6 A  301  GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER          
SEQRES   7 A  301  GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG          
SEQRES   8 A  301  GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS          
SEQRES   9 A  301  ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS          
SEQRES  10 A  301  ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLN ALA          
SEQRES  11 A  301  PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE          
SEQRES  12 A  301  THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE          
SEQRES  13 A  301  PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA          
SEQRES  14 A  301  GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER          
SEQRES  15 A  301  HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU          
SEQRES  16 A  301  ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU          
SEQRES  17 A  301  ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER          
SEQRES  18 A  301  VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN          
SEQRES  19 A  301  MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY          
SEQRES  20 A  301  MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA          
SEQRES  21 A  301  GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS          
SEQRES  22 A  301  TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU          
SEQRES  23 A  301  VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS          
SEQRES  24 A  301  HIS HIS                                                      
SEQRES   1 B  301  ALA GLU GLU PHE PRO VAL PRO ASN GLY PHE GLU SER ALA          
SEQRES   2 B  301  TYR ARG GLU VAL ASP GLY VAL LYS LEU HIS TYR VAL LYS          
SEQRES   3 B  301  GLY GLY GLN GLY PRO LEU VAL MET LEU VAL HIS GLY PHE          
SEQRES   4 B  301  GLY GLN THR TRP TYR GLU TRP HIS GLN LEU MET PRO GLU          
SEQRES   5 B  301  LEU ALA LYS ARG PHE THR VAL ILE ALA PRO ASP LEU PRO          
SEQRES   6 B  301  GLY LEU GLY GLN SER GLU PRO PRO LYS THR GLY TYR SER          
SEQRES   7 B  301  GLY GLU GLN VAL ALA VAL TYR LEU HIS LYS LEU ALA ARG          
SEQRES   8 B  301  GLN PHE SER PRO ASP ARG PRO PHE ASP LEU VAL ALA HIS          
SEQRES   9 B  301  ASP ILE GLY ILE TRP ASN THR TYR PRO MET VAL VAL LYS          
SEQRES  10 B  301  ASN GLN ALA ASP ILE ALA ARG LEU VAL TYR MET GLN ALA          
SEQRES  11 B  301  PRO ILE PRO ASP ALA ARG ILE TYR ARG PHE PRO ALA PHE          
SEQRES  12 B  301  THR ALA GLN GLY GLU SER LEU VAL TRP HIS PHE SER PHE          
SEQRES  13 B  301  PHE ALA ALA ASP ASP ARG LEU ALA GLU THR LEU ILE ALA          
SEQRES  14 B  301  GLY LYS GLU ARG PHE PHE LEU GLU HIS PHE ILE LYS SER          
SEQRES  15 B  301  HIS ALA SER ASN THR GLU VAL PHE SER GLU ARG LEU LEU          
SEQRES  16 B  301  ASP LEU TYR ALA ARG SER TYR ALA LYS PRO HIS SER LEU          
SEQRES  17 B  301  ASN ALA SER PHE GLU TYR TYR ARG ALA LEU ASN GLU SER          
SEQRES  18 B  301  VAL ARG GLN ASN ALA GLU LEU ALA LYS THR ARG LEU GLN          
SEQRES  19 B  301  MET PRO THR MET THR LEU ALA GLY GLY GLY HIS GLY GLY          
SEQRES  20 B  301  MET GLY THR PHE GLN LEU GLU GLN MET LYS ALA TYR ALA          
SEQRES  21 B  301  GLU ASP VAL GLU GLY HIS VAL LEU PRO GLY CYS GLY HIS          
SEQRES  22 B  301  TRP LEU PRO GLU GLU CYS ALA ALA PRO MET ASN ARG LEU          
SEQRES  23 B  301  VAL ILE ASP PHE LEU SER ARG GLY ARG HIS HIS HIS HIS          
SEQRES  24 B  301  HIS HIS                                                      
HET    7EZ  C 401      25                                                       
HET    7EZ  D 401      25                                                       
HET    7EZ  A 401      25                                                       
HET    7EZ  B 401      25                                                       
HETNAM     7EZ (4Z,7Z,10Z,13Z,16R,17R,19Z)-16,17-DIHYDROXYDOCOSA-4,7,           
HETNAM   2 7EZ  10,13,19-PENTAENOIC ACID                                        
FORMUL   5  7EZ    4(C22 H34 O4)                                                
FORMUL   9  HOH   *1226(H2 O)                                                   
HELIX    1 AA1 THR C   66  HIS C   71  5                                   6    
HELIX    2 AA2 GLN C   72  ALA C   78  1                                   7    
HELIX    3 AA3 SER C  102  SER C  118  1                                  17    
HELIX    4 AA4 ASP C  129  ASN C  134  1                                   6    
HELIX    5 AA5 THR C  135  ASN C  142  1                                   8    
HELIX    6 AA6 ASP C  158  ARG C  163  5                                   6    
HELIX    7 AA7 TRP C  176  ALA C  183  1                                   8    
HELIX    8 AA8 ARG C  186  ALA C  193  1                                   8    
HELIX    9 AA9 LYS C  195  HIS C  207  1                                  13    
HELIX   10 AB1 ASN C  210  PHE C  214  5                                   5    
HELIX   11 AB2 SER C  215  ALA C  227  1                                  13    
HELIX   12 AB3 LYS C  228  ALA C  241  1                                  14    
HELIX   13 AB4 ALA C  241  ALA C  253  1                                  13    
HELIX   14 AB5 THR C  274  ALA C  284  1                                  11    
HELIX   15 AB6 TRP C  298  CYS C  303  1                                   6    
HELIX   16 AB7 CYS C  303  SER C  316  1                                  14    
HELIX   17 AB8 THR D   66  HIS D   71  5                                   6    
HELIX   18 AB9 GLN D   72  ALA D   78  1                                   7    
HELIX   19 AC1 SER D  102  SER D  118  1                                  17    
HELIX   20 AC2 ASP D  129  ASN D  134  1                                   6    
HELIX   21 AC3 THR D  135  ASN D  142  1                                   8    
HELIX   22 AC4 ASP D  158  PHE D  164  5                                   7    
HELIX   23 AC5 TRP D  176  ALA D  183  1                                   8    
HELIX   24 AC6 ARG D  186  ALA D  193  1                                   8    
HELIX   25 AC7 LYS D  195  HIS D  207  1                                  13    
HELIX   26 AC8 ASN D  210  PHE D  214  5                                   5    
HELIX   27 AC9 SER D  215  ALA D  227  1                                  13    
HELIX   28 AD1 LYS D  228  ALA D  241  1                                  14    
HELIX   29 AD2 ALA D  241  ALA D  253  1                                  13    
HELIX   30 AD3 THR D  274  ALA D  284  1                                  11    
HELIX   31 AD4 TRP D  298  CYS D  303  1                                   6    
HELIX   32 AD5 CYS D  303  ARG D  317  1                                  15    
HELIX   33 AD6 THR A   66  HIS A   71  5                                   6    
HELIX   34 AD7 LEU A   73  ALA A   78  1                                   6    
HELIX   35 AD8 SER A  102  SER A  118  1                                  17    
HELIX   36 AD9 ASP A  129  ASN A  134  1                                   6    
HELIX   37 AE1 THR A  135  ASN A  142  1                                   8    
HELIX   38 AE2 ASP A  158  ARG A  163  5                                   6    
HELIX   39 AE3 TRP A  176  ALA A  183  1                                   8    
HELIX   40 AE4 ARG A  186  ALA A  193  1                                   8    
HELIX   41 AE5 LYS A  195  HIS A  207  1                                  13    
HELIX   42 AE6 ASN A  210  PHE A  214  5                                   5    
HELIX   43 AE7 SER A  215  ALA A  227  1                                  13    
HELIX   44 AE8 LYS A  228  ALA A  241  1                                  14    
HELIX   45 AE9 ALA A  241  ALA A  253  1                                  13    
HELIX   46 AF1 THR A  274  ALA A  282  1                                   9    
HELIX   47 AF2 TRP A  298  CYS A  303  1                                   6    
HELIX   48 AF3 CYS A  303  SER A  316  1                                  14    
HELIX   49 AF4 THR B   66  HIS B   71  5                                   6    
HELIX   50 AF5 GLN B   72  ALA B   78  1                                   7    
HELIX   51 AF6 SER B  102  SER B  118  1                                  17    
HELIX   52 AF7 ASP B  129  ASN B  134  1                                   6    
HELIX   53 AF8 THR B  135  ASN B  142  1                                   8    
HELIX   54 AF9 ASP B  158  PHE B  164  5                                   7    
HELIX   55 AG1 TRP B  176  ALA B  183  1                                   8    
HELIX   56 AG2 ARG B  186  ALA B  193  1                                   8    
HELIX   57 AG3 LYS B  195  HIS B  207  1                                  13    
HELIX   58 AG4 ASN B  210  PHE B  214  5                                   5    
HELIX   59 AG5 SER B  215  ALA B  227  1                                  13    
HELIX   60 AG6 LYS B  228  ALA B  241  1                                  14    
HELIX   61 AG7 ALA B  241  ALA B  253  1                                  13    
HELIX   62 AG8 THR B  274  ALA B  284  1                                  11    
HELIX   63 AG9 TRP B  298  CYS B  303  1                                   6    
HELIX   64 AH1 CYS B  303  ARG B  317  1                                  15    
SHEET    1 AA1 8 GLU C  35  VAL C  41  0                                        
SHEET    2 AA1 8 VAL C  44  GLY C  52 -1  O  VAL C  44   N  VAL C  41           
SHEET    3 AA1 8 THR C  82  PRO C  86 -1  O  VAL C  83   N  GLY C  51           
SHEET    4 AA1 8 LEU C  56  VAL C  60  1  N  VAL C  57   O  THR C  82           
SHEET    5 AA1 8 PHE C 123  HIS C 128  1  O  VAL C 126   N  VAL C  60           
SHEET    6 AA1 8 ILE C 146  MET C 152  1  O  VAL C 150   N  LEU C 125           
SHEET    7 AA1 8 THR C 261  GLY C 266  1  O  MET C 262   N  LEU C 149           
SHEET    8 AA1 8 VAL C 287  LEU C 292  1  O  LEU C 292   N  ALA C 265           
SHEET    1 AA2 8 GLU D  35  VAL D  41  0                                        
SHEET    2 AA2 8 VAL D  44  GLY D  52 -1  O  LEU D  46   N  ARG D  39           
SHEET    3 AA2 8 THR D  82  PRO D  86 -1  O  VAL D  83   N  GLY D  51           
SHEET    4 AA2 8 LEU D  56  VAL D  60  1  N  LEU D  59   O  ILE D  84           
SHEET    5 AA2 8 PHE D 123  HIS D 128  1  O  VAL D 126   N  VAL D  60           
SHEET    6 AA2 8 ILE D 146  MET D 152  1  O  VAL D 150   N  LEU D 125           
SHEET    7 AA2 8 THR D 261  GLY D 266  1  O  MET D 262   N  LEU D 149           
SHEET    8 AA2 8 VAL D 287  LEU D 292  1  O  LEU D 292   N  ALA D 265           
SHEET    1 AA3 2 PHE D 167  THR D 168  0                                        
SHEET    2 AA3 2 GLY D 171  GLU D 172 -1  O  GLY D 171   N  THR D 168           
SHEET    1 AA4 8 GLU A  35  VAL A  41  0                                        
SHEET    2 AA4 8 VAL A  44  GLY A  52 -1  O  VAL A  44   N  VAL A  41           
SHEET    3 AA4 8 THR A  82  PRO A  86 -1  O  VAL A  83   N  GLY A  51           
SHEET    4 AA4 8 LEU A  56  VAL A  60  1  N  VAL A  57   O  THR A  82           
SHEET    5 AA4 8 PHE A 123  HIS A 128  1  O  VAL A 126   N  VAL A  60           
SHEET    6 AA4 8 ILE A 146  MET A 152  1  O  ALA A 147   N  PHE A 123           
SHEET    7 AA4 8 THR A 261  GLY A 266  1  O  MET A 262   N  TYR A 151           
SHEET    8 AA4 8 VAL A 287  LEU A 292  1  O  LEU A 292   N  ALA A 265           
SHEET    1 AA5 8 PHE B  34  VAL B  41  0                                        
SHEET    2 AA5 8 VAL B  44  GLY B  52 -1  O  VAL B  44   N  VAL B  41           
SHEET    3 AA5 8 THR B  82  PRO B  86 -1  O  VAL B  83   N  GLY B  51           
SHEET    4 AA5 8 LEU B  56  VAL B  60  1  N  VAL B  57   O  THR B  82           
SHEET    5 AA5 8 PHE B 123  HIS B 128  1  O  ASP B 124   N  MET B  58           
SHEET    6 AA5 8 ILE B 146  MET B 152  1  O  VAL B 150   N  LEU B 125           
SHEET    7 AA5 8 THR B 261  GLY B 266  1  O  MET B 262   N  LEU B 149           
SHEET    8 AA5 8 VAL B 287  LEU B 292  1  O  LEU B 292   N  ALA B 265           
SHEET    1 AA6 2 PHE B 167  THR B 168  0                                        
SHEET    2 AA6 2 GLY B 171  GLU B 172 -1  O  GLY B 171   N  THR B 168           
SSBOND   1 CYS C  295    CYS C  303                          1555   1555  2.00  
SSBOND   2 CYS D  295    CYS D  303                          1555   1555  1.98  
SSBOND   3 CYS A  295    CYS A  303                          1555   1555  2.00  
SSBOND   4 CYS B  295    CYS B  303                          1555   1555  2.00  
LINK         OD1 ASP C 129                 C6  7EZ C 401     1555   1555  1.42  
LINK         OD1 ASP D 129                 C6  7EZ D 401     1555   1555  1.42  
LINK         OD1 ASP A 129                 C6  7EZ A 401     1555   1555  1.43  
LINK         OD1 ASP B 129                 C6  7EZ B 401     1555   1555  1.42  
SITE     1 AC1 11 ASP C 129  GLN C 153  PHE C 164  PRO C 165                    
SITE     2 AC1 11 HIS C 177  PHE C 178  HIS C 207  TYR C 239                    
SITE     3 AC1 11 MET C 272  HIS C 297  HOH C 535                               
SITE     1 AC2 15 PHE A  63  HIS A 128  ILE A 130  GLY A 131                    
SITE     2 AC2 15 ILE A 132  MET A 152  GLN A 153  ALA A 154                    
SITE     3 AC2 15 PHE A 164  HIS A 177  TYR A 239  MET A 272                    
SITE     4 AC2 15 HIS A 297  HOH A 652  HOH A 782                               
SITE     1 AC3 20 PHE B  63  HIS B 128  ILE B 130  GLY B 131                    
SITE     2 AC3 20 ILE B 132  MET B 152  GLN B 153  ALA B 154                    
SITE     3 AC3 20 VAL B 175  HIS B 177  PHE B 178  HIS B 207                    
SITE     4 AC3 20 TYR B 239  GLY B 270  MET B 272  HIS B 297                    
SITE     5 AC3 20 HOH B 550  HOH B 577  HOH B 594  HOH B 680                    
SITE     1 AC4 19 PHE D  63  HIS D 128  ILE D 130  GLY D 131                    
SITE     2 AC4 19 ILE D 132  MET D 152  GLN D 153  ALA D 154                    
SITE     3 AC4 19 VAL D 175  HIS D 177  PHE D 178  HIS D 207                    
SITE     4 AC4 19 TYR D 239  GLY D 270  MET D 272  HIS D 297                    
SITE     5 AC4 19 HOH D 564  HOH D 648  HOH D 702                               
CRYST1   83.846  168.912  176.424  90.00  90.00  90.00 C 2 2 21     32          
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      0.011927  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005920  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005668        0.00000                         
TER    2371      ARG C 317                                                      
TER    4741      ARG D 317                                                      
TER    7094      ARG A 317                                                      
TER    9456      ARG B 317                                                      
MASTER      487    0    4   64   36    0   17    610678    4  112   96          
END                                                                             

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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:
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