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LongText Report for: 5tnh-pdb

Name Class
5tnh-pdb
HEADER    HYDROLASE                               14-OCT-16   5TNH              
TITLE     CRYSTAL STRUCTURE OF THE E153Q MUTANT OF THE CFTR INHIBITORY FACTOR   
TITLE    2 CIF CONTAINING THE ADDUCTED 17,18-EPETE 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   11-OCT-17 5TNH    0                                                
JRNL        AUTH   K.L.HVORECNY,C.D.BAHL,S.KITAMURA,K.S.S.LEE,B.D.HAMMOCK,      
JRNL        AUTH 2 C.MORISSEAU,D.R.MADDEN                                       
JRNL        TITL   ACTIVE-SITE FLEXIBILITY AND SUBSTRATE SPECIFICITY IN A       
JRNL        TITL 2 BACTERIAL VIRULENCE FACTOR: CRYSTALLOGRAPHIC SNAPSHOTS OF AN 
JRNL        TITL 3 EPOXIDE HYDROLASE.                                           
JRNL        REF    STRUCTURE                     V.  25   697 2017              
JRNL        REFN                   ISSN 1878-4186                               
JRNL        PMID   28392259                                                     
JRNL        DOI    10.1016/J.STR.2017.03.002                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.84                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 71620                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3576                            
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 19.8411 -  6.1610    1.00     2676   179  0.1869 0.2105        
REMARK   3     2  6.1610 -  4.9146    1.00     2598   179  0.1819 0.2000        
REMARK   3     3  4.9146 -  4.3006    1.00     2784     0  0.1525 0.0000        
REMARK   3     4  4.3006 -  3.9107    1.00     2564   179  0.1657 0.1961        
REMARK   3     5  3.9107 -  3.6322    1.00     2620   179  0.1761 0.2157        
REMARK   3     6  3.6322 -  3.4192    1.00     2561   179  0.1718 0.2316        
REMARK   3     7  3.4192 -  3.2487    1.00     2759     0  0.1788 0.0000        
REMARK   3     8  3.2487 -  3.1079    1.00     2567   179  0.1799 0.2063        
REMARK   3     9  3.1079 -  2.9886    1.00     2595   179  0.1903 0.2625        
REMARK   3    10  2.9886 -  2.8858    1.00     2592   179  0.1970 0.2331        
REMARK   3    11  2.8858 -  2.7958    1.00     2540   156  0.1916 0.2504        
REMARK   3    12  2.7958 -  2.7161    1.00     2757    23  0.1890 0.2522        
REMARK   3    13  2.7161 -  2.6448    1.00     2569   179  0.2004 0.2464        
REMARK   3    14  2.6448 -  2.5804    1.00     2591   179  0.1888 0.2376        
REMARK   3    15  2.5804 -  2.5219    1.00     2573   179  0.1969 0.2620        
REMARK   3    16  2.5219 -  2.4683    1.00     2725     0  0.1986 0.0000        
REMARK   3    17  2.4683 -  2.4190    1.00     2548   179  0.2032 0.2691        
REMARK   3    18  2.4190 -  2.3734    1.00     2580   179  0.2003 0.2835        
REMARK   3    19  2.3734 -  2.3311    1.00     2544   179  0.1939 0.2422        
REMARK   3    20  2.3311 -  2.2917    1.00     2724     0  0.1974 0.0000        
REMARK   3    21  2.2917 -  2.2547    1.00     2616   178  0.2003 0.2554        
REMARK   3    22  2.2547 -  2.2201    1.00     2547   179  0.1955 0.2583        
REMARK   3    23  2.2201 -  2.1875    1.00     2530   179  0.1937 0.2494        
REMARK   3    24  2.1875 -  2.1567    1.00     2767     0  0.2014 0.0000        
REMARK   3    25  2.1567 -  2.1276    1.00     2547   176  0.2126 0.2716        
REMARK   3    26  2.1276 -  2.1000    1.00     2570   179  0.2210 0.2988        
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)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.000           
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           9778                                  
REMARK   3   ANGLE     :  0.821          13266                                  
REMARK   3   CHIRALITY :  0.049           1362                                  
REMARK   3   PLANARITY :  0.006           1734                                  
REMARK   3   DIHEDRAL  : 15.764           5766                                  
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):  -5.9935  29.7947 -27.0027              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1047 T22:   0.1183                                     
REMARK   3      T33:   0.1546 T12:  -0.0074                                     
REMARK   3      T13:  -0.0028 T23:  -0.0030                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0926 L22:   1.0829                                     
REMARK   3      L33:   0.8551 L12:  -0.1455                                     
REMARK   3      L13:  -0.0874 L23:  -0.1766                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0020 S12:   0.0429 S13:   0.1517                       
REMARK   3      S21:  -0.0468 S22:  -0.0227 S23:   0.0264                       
REMARK   3      S31:  -0.1181 S32:  -0.0354 S33:   0.0240                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: ( CHAIN D AND RESID 25:317 )                           
REMARK   3    ORIGIN FOR THE GROUP (A): -14.7316  -9.4892 -15.7260              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1220 T22:   0.1413                                     
REMARK   3      T33:   0.1142 T12:  -0.0258                                     
REMARK   3      T13:   0.0049 T23:   0.0136                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1106 L22:   1.3005                                     
REMARK   3      L33:   0.4958 L12:   0.4319                                     
REMARK   3      L13:  -0.1454 L23:  -0.0929                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0098 S12:  -0.0431 S13:  -0.0861                       
REMARK   3      S21:   0.0489 S22:   0.0154 S23:   0.0970                       
REMARK   3      S31:   0.0902 S32:  -0.0124 S33:  -0.0066                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 25:318 )                           
REMARK   3    ORIGIN FOR THE GROUP (A):  22.0116  -2.7354 -27.1755              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0955 T22:   0.1173                                     
REMARK   3      T33:   0.1419 T12:  -0.0095                                     
REMARK   3      T13:   0.0024 T23:  -0.0054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1543 L22:   1.0551                                     
REMARK   3      L33:   0.8432 L12:  -0.0132                                     
REMARK   3      L13:   0.1883 L23:   0.0252                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0044 S12:   0.0799 S13:  -0.1040                       
REMARK   3      S21:  -0.0602 S22:  -0.0062 S23:  -0.0304                       
REMARK   3      S31:   0.0999 S32:   0.0238 S33:   0.0040                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: ( CHAIN B AND RESID 25:318 )                           
REMARK   3    ORIGIN FOR THE GROUP (A):  30.7894  36.5750 -15.6674              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1084 T22:   0.1310                                     
REMARK   3      T33:   0.1551 T12:  -0.0243                                     
REMARK   3      T13:  -0.0164 T23:  -0.0112                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3075 L22:   1.4665                                     
REMARK   3      L33:   0.7739 L12:   0.5832                                     
REMARK   3      L13:   0.0821 L23:   0.2553                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0132 S12:  -0.0121 S13:   0.1224                       
REMARK   3      S21:   0.0603 S22:   0.0214 S23:  -0.0724                       
REMARK   3      S31:  -0.0824 S32:   0.0003 S33:  -0.0058                       
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 5TNH 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_1000222803.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-MAR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X6A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8856                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS NOVEMBER 1, 2011               
REMARK 200  DATA SCALING SOFTWARE          : XDS NOVEMBER 1, 2011               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 71625                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.840                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 7.650                              
REMARK 200  R MERGE                    (I) : 0.14900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 12.2100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.69                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.63400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.760                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX (1.10_2155: ???)                               
REMARK 200 STARTING MODEL: 3KD2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM ACETATE, PH5 CALCIUM CHLORIDE     
REMARK 280  PEG 8000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -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        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       84.06600            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.04150            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       84.06600            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       42.04150            
REMARK 290   SMTRY3   4  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: 20400 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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: 2850 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY 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     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     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: 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     -128.52     58.58                                   
REMARK 500    ALA C 154      147.80   -170.28                                   
REMARK 500    CYS C 303       59.25   -142.34                                   
REMARK 500    ASP D 129     -127.96     58.15                                   
REMARK 500    ALA D 154      138.58    178.98                                   
REMARK 500    ASP D 185       16.63     59.89                                   
REMARK 500    TRP D 298       56.44    -90.96                                   
REMARK 500    ASP A 129     -128.85     57.10                                   
REMARK 500    ASN A 142       58.06   -140.29                                   
REMARK 500    ALA A 154      146.72   -170.20                                   
REMARK 500    ASP B 129     -129.24     63.67                                   
REMARK 500    ALA B 154      142.58    176.91                                   
REMARK 500    LYS B 195       28.48   -142.43                                   
REMARK 500    TRP B 298       59.17    -92.20                                   
REMARK 500    CYS B 303       52.56   -142.45                                   
REMARK 500    ARG B 317       96.45    -63.07                                   
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 659        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH C 660        DISTANCE =  6.16 ANGSTROMS                       
REMARK 525    HOH C 661        DISTANCE =  7.76 ANGSTROMS                       
REMARK 525    HOH D 650        DISTANCE =  5.85 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7MS C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide 7MS 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 7MS 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 7MS D 401 and ASP D    
REMARK 800  129                                                                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3KD2, 4DMC   RELATED DB: PDB                             
REMARK 900 3KD2 - WILD TYPE VERSION OF THE CURRENT SUBMISSION 4DMC - APO        
REMARK 900 VERSION OF SAME PROTEIN AS CURRENT SUBMISSION (CIF WITH E153Q        
REMARK 900 MUTATION)                                                            
DBREF1 5TNH C   25   325  UNP                  A0A0M3KL26_PSEAB                 
DBREF2 5TNH C     A0A0M3KL26                          1         301             
DBREF1 5TNH D   25   325  UNP                  A0A0M3KL26_PSEAB                 
DBREF2 5TNH D     A0A0M3KL26                          1         301             
DBREF1 5TNH A   25   325  UNP                  A0A0M3KL26_PSEAB                 
DBREF2 5TNH A     A0A0M3KL26                          1         301             
DBREF1 5TNH B   25   325  UNP                  A0A0M3KL26_PSEAB                 
DBREF2 5TNH B     A0A0M3KL26                          1         301             
SEQADV 5TNH GLN C  153  UNP  A0A0M3KL2 GLU   129 ENGINEERED MUTATION            
SEQADV 5TNH GLN D  153  UNP  A0A0M3KL2 GLU   129 ENGINEERED MUTATION            
SEQADV 5TNH GLN A  153  UNP  A0A0M3KL2 GLU   129 ENGINEERED MUTATION            
SEQADV 5TNH 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    7MS  C 401      23                                                       
HET    7MS  D 401      23                                                       
HET    7MS  A 401      23                                                       
HET    7MS  B 401      23                                                       
HETNAM     7MS (5Z,8Z,11Z,14Z,17R,18R)-17,18-DIHYDROXYICOSA-5,8,11,14-          
HETNAM   2 7MS  TETRAENOIC ACID                                                 
FORMUL   5  7MS    4(C20 H32 O4)                                                
FORMUL   9  HOH   *600(H2 O)                                                    
HELIX    1 AA1 THR C   66  HIS C   71  5                                   6    
HELIX    2 AA2 GLN C   72  LYS C   79  1                                   8    
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  PHE C  164  5                                   7    
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  282  1                                   9    
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  284  1                                  11    
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 SER B  215  ALA B  227  1                                  13    
HELIX   59 AG5 LYS B  228  ALA B  241  1                                  14    
HELIX   60 AG6 ALA B  241  ALA B  253  1                                  13    
HELIX   61 AG7 THR B  274  ALA B  282  1                                   9    
HELIX   62 AG8 TRP B  298  CYS B  303  1                                   6    
HELIX   63 AG9 CYS B  303  ARG B  317  1                                  15    
SHEET    1 AA1 8 PHE C  34  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  MET C  58           
SHEET    6 AA1 8 ILE C 146  MET C 152  1  O  ALA C 147   N  PHE C 123           
SHEET    7 AA1 8 THR C 261  GLY C 266  1  O  MET C 262   N  TYR C 151           
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  VAL D  57   O  THR D  82           
SHEET    5 AA2 8 PHE D 123  HIS D 128  1  O  ASP D 124   N  LEU D  56           
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 PHE A  34  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  ASP A 124   N  MET A  58           
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 2 PHE A 167  THR A 168  0                                        
SHEET    2 AA5 2 GLY A 171  GLU A 172 -1  O  GLY A 171   N  THR A 168           
SHEET    1 AA6 8 GLU B  35  VAL B  41  0                                        
SHEET    2 AA6 8 VAL B  44  GLY B  52 -1  O  LYS B  50   N  GLU B  35           
SHEET    3 AA6 8 THR B  82  PRO B  86 -1  O  VAL B  83   N  GLY B  51           
SHEET    4 AA6 8 LEU B  56  VAL B  60  1  N  VAL B  57   O  THR B  82           
SHEET    5 AA6 8 PHE B 123  HIS B 128  1  O  VAL B 126   N  VAL B  60           
SHEET    6 AA6 8 ILE B 146  MET B 152  1  O  VAL B 150   N  LEU B 125           
SHEET    7 AA6 8 THR B 261  GLY B 266  1  O  MET B 262   N  LEU B 149           
SHEET    8 AA6 8 VAL B 287  LEU B 292  1  O  LEU B 292   N  ALA B 265           
SHEET    1 AA7 2 PHE B 167  THR B 168  0                                        
SHEET    2 AA7 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  2.01  
SSBOND   2 CYS D  295    CYS D  303                          1555   1555  2.01  
SSBOND   3 CYS A  295    CYS A  303                          1555   1555  2.02  
SSBOND   4 CYS B  295    CYS B  303                          1555   1555  2.00  
LINK         OD1 ASP C 129                 C3  7MS C 401     1555   1555  1.41  
LINK         OD1 ASP D 129                 C3  7MS D 401     1555   1555  1.41  
LINK         OD1 ASP A 129                 C3  7MS A 401     1555   1555  1.41  
LINK         OD1 ASP B 129                 C3  7MS B 401     1555   1555  1.41  
SITE     1 AC1 13 ASP C 129  GLN C 153  PHE C 164  PRO C 165                    
SITE     2 AC1 13 LEU C 174  HIS C 177  PHE C 178  PHE C 203                    
SITE     3 AC1 13 TYR C 239  GLY C 270  GLY C 271  MET C 272                    
SITE     4 AC1 13 HIS C 297                                                     
SITE     1 AC2 19 GLY A  62  PHE A  63  HIS A 128  ILE A 130                    
SITE     2 AC2 19 GLY A 131  ILE A 132  MET A 152  GLN A 153                    
SITE     3 AC2 19 ALA A 154  LEU A 174  HIS A 177  PHE A 178                    
SITE     4 AC2 19 PHE A 203  HIS A 207  TYR A 239  GLY A 270                    
SITE     5 AC2 19 MET A 272  HIS A 297  HOH A 581                               
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 PHE B 164  LEU B 174  VAL B 175  HIS B 177                    
SITE     4 AC3 20 PHE B 178  PHE B 203  TYR B 239  GLY B 270                    
SITE     5 AC3 20 MET B 272  PHE B 275  HIS B 297  HOH B 606                    
SITE     1 AC4 17 PHE D  63  HIS D 128  ILE D 130  GLY D 131                    
SITE     2 AC4 17 ILE D 132  MET D 152  GLN D 153  ALA D 154                    
SITE     3 AC4 17 PRO D 165  SER D 173  LEU D 174  HIS D 177                    
SITE     4 AC4 17 PHE D 178  PHE D 203  TYR D 239  GLY D 270                    
SITE     5 AC4 17 HIS D 297                                                     
CRYST1  168.132   84.083   89.564  90.00 100.28  90.00 C 1 2 1      16          
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      0.005948  0.000000  0.001078        0.00000                         
SCALE2      0.000000  0.011893  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011347        0.00000                         
TER    2351      ARG C 317                                                      
TER    4702      ARG D 317                                                      
TER    7045      GLY A 318                                                      
TER    9395      GLY B 318                                                      
MASTER      401    0    4   63   38    0   19    610052    4  104   96          
END                                                                             

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Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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