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LongText Report for: 5hka-pdb

Name Class
5hka-pdb
HEADER    HYDROLASE/HYDROLASE INHIBITOR           13-JAN-16   5HKA              
TITLE     CRYSTAL STRUCTURE OF THE CFTR INHIBITORY FACTOR CIF BOUND TO AN AMIDE 
TITLE    2 INHIBITOR                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CFTR INHIBITORY FACTOR;                                    
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: 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;                                     
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PDPM73                                    
KEYWDS    BACTERIAL EPOXIDE HYDROLASE, INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR 
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.L.HVORECNY,D.R.MADDEN                                               
REVDAT   1   18-MAY-16 5HKA    0                                                
JRNL        AUTH   S.KITAMURA,K.L.HVORECNY,J.NIU,B.D.HAMMOCK,D.R.MADDEN,        
JRNL        AUTH 2 C.MORISSEAU                                                  
JRNL        TITL   RATIONAL DESIGN OF POTENT AND SELECTIVE INHIBITORS OF AN     
JRNL        TITL 2 EPOXIDE HYDROLASE VIRULENCE FACTOR FROM PSEUDOMONAS          
JRNL        TITL 3 AERUGINOSA.                                                  
JRNL        REF    J.MED.CHEM.                                2016              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   27120257                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.6B00173                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.7.3_928                                     
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) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.97                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 75318                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.164                           
REMARK   3   R VALUE            (WORKING SET) : 0.162                           
REMARK   3   FREE R VALUE                     : 0.197                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3764                            
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 19.9677 -  6.0934    1.00     2723   191  0.1754 0.2026        
REMARK   3     2  6.0934 -  4.8595    0.99     2662   190  0.1686 0.1429        
REMARK   3     3  4.8595 -  4.2520    0.99     2822     0  0.1223 0.0000        
REMARK   3     4  4.2520 -  3.8663    0.99     2645   190  0.1401 0.1549        
REMARK   3     5  3.8663 -  3.5909    0.99     2614   191  0.1553 0.1841        
REMARK   3     6  3.5909 -  3.3802    0.99     2678   136  0.1567 0.1991        
REMARK   3     7  3.3802 -  3.2117    0.99     2755    53  0.1546 0.1805        
REMARK   3     8  3.2117 -  3.0724    0.99     2627   190  0.1588 0.2168        
REMARK   3     9  3.0724 -  2.9545    0.99     2580   189  0.1754 0.2149        
REMARK   3    10  2.9545 -  2.8529    0.99     2800     0  0.1675 0.0000        
REMARK   3    11  2.8529 -  2.7639    0.99     2614   190  0.1592 0.1888        
REMARK   3    12  2.7639 -  2.6851    0.99     2590   189  0.1491 0.1757        
REMARK   3    13  2.6851 -  2.6145    0.99     2578   189  0.1588 0.2188        
REMARK   3    14  2.6145 -  2.5509    0.99     2801     0  0.1685 0.0000        
REMARK   3    15  2.5509 -  2.4930    0.99     2607   187  0.1750 0.1993        
REMARK   3    16  2.4930 -  2.4400    0.99     2601   188  0.1633 0.1976        
REMARK   3    17  2.4400 -  2.3913    0.98     2578   188  0.1655 0.2075        
REMARK   3    18  2.3913 -  2.3463    0.99     2775     0  0.1743 0.0000        
REMARK   3    19  2.3463 -  2.3044    0.98     2581   187  0.1716 0.2296        
REMARK   3    20  2.3044 -  2.2654    0.98     2576   188  0.1771 0.2539        
REMARK   3    21  2.2654 -  2.2289    0.98     2577   183  0.1687 0.2249        
REMARK   3    22  2.2289 -  2.1947    0.98     2764     0  0.1767 0.0000        
REMARK   3    23  2.1947 -  2.1624    0.98     2592   186  0.1835 0.2518        
REMARK   3    24  2.1624 -  2.1320    0.98     2550   186  0.1855 0.2583        
REMARK   3    25  2.1320 -  2.1032    0.98     2563   189  0.1859 0.2268        
REMARK   3    26  2.1032 -  2.0759    0.98     2760     0  0.1978 0.0000        
REMARK   3    27  2.0759 -  2.0500    0.97     2541   184  0.2005 0.2168        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.98                                          
REMARK   3   K_SOL              : 0.40                                          
REMARK   3   B_SOL              : 33.27                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.220            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.660           
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) : -0.68540                                             
REMARK   3    B22 (A**2) : -2.31750                                             
REMARK   3    B33 (A**2) : 3.00290                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.39620                                              
REMARK   3    B23 (A**2) : 0.00000                                              
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           9914                                  
REMARK   3   ANGLE     :  1.129          13473                                  
REMARK   3   CHIRALITY :  0.076           1367                                  
REMARK   3   PLANARITY :  0.005           1771                                  
REMARK   3   DIHEDRAL  : 14.602           3631                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 25:321)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -22.0448  11.6744  27.1790              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1041 T22:   0.0941                                     
REMARK   3      T33:   0.0812 T12:   0.0109                                     
REMARK   3      T13:   0.0154 T23:   0.0033                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7711 L22:   1.0027                                     
REMARK   3      L33:   0.9645 L12:   0.1765                                     
REMARK   3      L13:  -0.0021 L23:  -0.0038                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0294 S12:  -0.0811 S13:  -0.0789                       
REMARK   3      S21:   0.0883 S22:  -0.0199 S23:   0.0297                       
REMARK   3      S31:   0.1180 S32:   0.0016 S33:   0.0487                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 25:317)                             
REMARK   3    ORIGIN FOR THE GROUP (A): -31.0945  50.9938  15.4655              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0826 T22:   0.0938                                     
REMARK   3      T33:   0.1192 T12:   0.0118                                     
REMARK   3      T13:  -0.0226 T23:   0.0004                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0197 L22:   1.2219                                     
REMARK   3      L33:   0.6266 L12:  -0.3592                                     
REMARK   3      L13:  -0.1670 L23:  -0.0694                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0021 S12:   0.0142 S13:   0.1522                       
REMARK   3      S21:  -0.0316 S22:   0.0160 S23:   0.0347                       
REMARK   3      S31:  -0.0830 S32:  -0.0358 S33:  -0.0100                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN C AND RESID 25:317)                             
REMARK   3    ORIGIN FOR THE GROUP (A):   5.6445  44.4982  26.8302              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0936 T22:   0.0924                                     
REMARK   3      T33:   0.1061 T12:   0.0099                                     
REMARK   3      T13:  -0.0040 T23:   0.0097                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6972 L22:   1.2829                                     
REMARK   3      L33:   1.0194 L12:   0.0848                                     
REMARK   3      L13:   0.0746 L23:   0.1661                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0110 S12:  -0.0315 S13:   0.0880                       
REMARK   3      S21:   0.0733 S22:  -0.0279 S23:  -0.0828                       
REMARK   3      S31:  -0.1020 S32:   0.0221 S33:   0.0387                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN D AND RESID 25:321)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  14.8356   5.1093  15.5722              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0889 T22:   0.0991                                     
REMARK   3      T33:   0.0741 T12:   0.0220                                     
REMARK   3      T13:   0.0157 T23:   0.0018                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8146 L22:   0.9897                                     
REMARK   3      L33:   0.5766 L12:  -0.1202                                     
REMARK   3      L13:   0.1212 L23:   0.1698                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0270 S12:   0.0256 S13:  -0.0638                       
REMARK   3      S21:  -0.0522 S22:  -0.0051 S23:  -0.0867                       
REMARK   3      S31:   0.0352 S32:   0.0109 S33:  -0.0173                       
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 5HKA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-APR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000217150.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-DEC-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
REMARK 200  PH                             : 5                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9770                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS JANUARY 10, 2014               
REMARK 200  DATA SCALING SOFTWARE          : XSCALE JANUARY 10, 2014            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 75324                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.09300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 15.2500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.530                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX 1.7.3_928                                      
REMARK 200 STARTING MODEL: 3KD2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, CALCIUM CHLORIDE, SODIUM       
REMARK 280  ACETATE, DIMETHYLSULFOXIDE, PH 5, VAPOR DIFFUSION, HANGING DROP,    
REMARK 280  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       84.48550            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.85550            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       84.48550            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       41.85550            
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: 2770 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2780 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     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 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     HIS D   322                                                      
REMARK 465     HIS D   323                                                      
REMARK 465     HIS D   324                                                      
REMARK 465     HIS D   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 A 129     -132.77     60.09                                   
REMARK 500    ALA A 154      149.16   -172.24                                   
REMARK 500    ASP B 129     -136.58     62.64                                   
REMARK 500    ALA B 154      142.09   -171.94                                   
REMARK 500    ASP B 184     -159.19    -86.83                                   
REMARK 500    ASP C 129     -131.52     58.90                                   
REMARK 500    ALA C 154      146.65   -175.86                                   
REMARK 500    ASP C 184     -178.42    -68.65                                   
REMARK 500    CYS C 303       51.88   -140.31                                   
REMARK 500    ASP D 129     -136.08     61.60                                   
REMARK 500    ALA D 154      142.60   -174.23                                   
REMARK 500    ARG D 319      120.95    -33.35                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 64N A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 64N B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 64N C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 64N D 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3KD2   RELATED DB: PDB                                   
REMARK 900 3KD2 CONTAINS THE SAME PROTEIN IN ITS APO STATE                      
REMARK 900 RELATED ID: 4YX9   RELATED DB: PDB                                   
REMARK 900 4YX9 CONTAINS THE SAME PROTEIN COMPLEXED WITH TIRATRICOL             
REMARK 900 RELATED ID: 5HKB   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5HK9   RELATED DB: PDB                                   
DBREF1 5HKA A   25   325  UNP                  A0A0M3KL26_PSEAB                 
DBREF2 5HKA A     A0A0M3KL26                          1         301             
DBREF1 5HKA B   25   325  UNP                  A0A0M3KL26_PSEAB                 
DBREF2 5HKA B     A0A0M3KL26                          1         301             
DBREF1 5HKA C   25   325  UNP                  A0A0M3KL26_PSEAB                 
DBREF2 5HKA C     A0A0M3KL26                          1         301             
DBREF1 5HKA D   25   325  UNP                  A0A0M3KL26_PSEAB                 
DBREF2 5HKA D     A0A0M3KL26                          1         301             
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 GLU 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 GLU 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                                                      
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 GLU 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 GLU 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                                                      
HET    64N  A 401      30                                                       
HET    64N  B 401      30                                                       
HET    64N  C 401      30                                                       
HET    64N  D 401      30                                                       
HETNAM     64N 5'-[2,6-DICHLORO-4-(PROPANOYLAMINO)PHENOXY]-2'-                  
HETNAM   2 64N  HYDROXYBIPHENYL-4-CARBOXAMIDE                                   
FORMUL   5  64N    4(C22 H18 CL2 N2 O4)                                         
FORMUL   9  HOH   *753(H2 O)                                                    
HELIX    1 AA1 THR A   66  HIS A   71  5                                   6    
HELIX    2 AA2 LEU A   73  ALA A   78  1                                   6    
HELIX    3 AA3 SER A  102  SER A  118  1                                  17    
HELIX    4 AA4 ASP A  129  ASN A  134  1                                   6    
HELIX    5 AA5 THR A  135  ASN A  142  1                                   8    
HELIX    6 AA6 ASP A  158  PHE A  164  5                                   7    
HELIX    7 AA7 TRP A  176  ALA A  183  1                                   8    
HELIX    8 AA8 ARG A  186  ALA A  193  1                                   8    
HELIX    9 AA9 LYS A  195  HIS A  207  1                                  13    
HELIX   10 AB1 ASN A  210  PHE A  214  5                                   5    
HELIX   11 AB2 SER A  215  ALA A  227  1                                  13    
HELIX   12 AB3 LYS A  228  ALA A  241  1                                  14    
HELIX   13 AB4 ALA A  241  ALA A  253  1                                  13    
HELIX   14 AB5 THR A  274  ALA A  282  1                                   9    
HELIX   15 AB6 TRP A  298  CYS A  303  1                                   6    
HELIX   16 AB7 CYS A  303  SER A  316  1                                  14    
HELIX   17 AB8 THR B   66  HIS B   71  5                                   6    
HELIX   18 AB9 GLN B   72  ALA B   78  1                                   7    
HELIX   19 AC1 SER B  102  SER B  118  1                                  17    
HELIX   20 AC2 ASP B  129  ASN B  134  1                                   6    
HELIX   21 AC3 THR B  135  ASN B  142  1                                   8    
HELIX   22 AC4 ASP B  158  PHE B  164  5                                   7    
HELIX   23 AC5 TRP B  176  ALA B  183  1                                   8    
HELIX   24 AC6 ARG B  186  ALA B  193  1                                   8    
HELIX   25 AC7 LYS B  195  HIS B  207  1                                  13    
HELIX   26 AC8 ASN B  210  PHE B  214  5                                   5    
HELIX   27 AC9 SER B  215  ALA B  227  1                                  13    
HELIX   28 AD1 LYS B  228  ALA B  241  1                                  14    
HELIX   29 AD2 ALA B  241  ALA B  253  1                                  13    
HELIX   30 AD3 THR B  274  ALA B  284  1                                  11    
HELIX   31 AD4 TRP B  298  CYS B  303  1                                   6    
HELIX   32 AD5 CYS B  303  ARG B  317  1                                  15    
HELIX   33 AD6 THR C   66  HIS C   71  5                                   6    
HELIX   34 AD7 GLN C   72  ALA C   78  1                                   7    
HELIX   35 AD8 SER C  102  SER C  118  1                                  17    
HELIX   36 AD9 ASP C  129  ASN C  134  1                                   6    
HELIX   37 AE1 THR C  135  ASN C  142  1                                   8    
HELIX   38 AE2 ASP C  158  PHE C  164  5                                   7    
HELIX   39 AE3 TRP C  176  ALA C  183  1                                   8    
HELIX   40 AE4 ARG C  186  ALA C  193  1                                   8    
HELIX   41 AE5 LYS C  195  HIS C  207  1                                  13    
HELIX   42 AE6 ASN C  210  PHE C  214  5                                   5    
HELIX   43 AE7 SER C  215  ALA C  227  1                                  13    
HELIX   44 AE8 LYS C  228  ALA C  241  1                                  14    
HELIX   45 AE9 ALA C  241  ALA C  253  1                                  13    
HELIX   46 AF1 THR C  274  ALA C  282  1                                   9    
HELIX   47 AF2 TRP C  298  CYS C  303  1                                   6    
HELIX   48 AF3 CYS C  303  ARG C  317  1                                  15    
HELIX   49 AF4 THR D   66  HIS D   71  5                                   6    
HELIX   50 AF5 LEU D   73  ALA D   78  1                                   6    
HELIX   51 AF6 SER D  102  SER D  118  1                                  17    
HELIX   52 AF7 ASP D  129  ASN D  134  1                                   6    
HELIX   53 AF8 THR D  135  ASN D  142  1                                   8    
HELIX   54 AF9 ASP D  158  PHE D  164  5                                   7    
HELIX   55 AG1 TRP D  176  ALA D  183  1                                   8    
HELIX   56 AG2 ARG D  186  ALA D  193  1                                   8    
HELIX   57 AG3 LYS D  195  HIS D  207  1                                  13    
HELIX   58 AG4 ASN D  210  PHE D  214  5                                   5    
HELIX   59 AG5 SER D  215  ALA D  227  1                                  13    
HELIX   60 AG6 LYS D  228  ALA D  241  1                                  14    
HELIX   61 AG7 ALA D  241  ALA D  253  1                                  13    
HELIX   62 AG8 THR D  274  ALA D  284  1                                  11    
HELIX   63 AG9 TRP D  298  CYS D  303  1                                   6    
HELIX   64 AH1 CYS D  303  ARG D  317  1                                  15    
SHEET    1 AA1 8 GLU A  35  VAL A  41  0                                        
SHEET    2 AA1 8 VAL A  44  GLY A  52 -1  O  LYS A  50   N  GLU A  35           
SHEET    3 AA1 8 THR A  82  PRO A  86 -1  O  VAL A  83   N  GLY A  51           
SHEET    4 AA1 8 LEU A  56  VAL A  60  1  N  LEU A  59   O  ILE A  84           
SHEET    5 AA1 8 PHE A 123  HIS A 128  1  O  ASP A 124   N  LEU A  56           
SHEET    6 AA1 8 ILE A 146  MET A 152  1  O  VAL A 150   N  LEU A 125           
SHEET    7 AA1 8 THR A 261  GLY A 266  1  O  MET A 262   N  LEU A 149           
SHEET    8 AA1 8 VAL A 287  LEU A 292  1  O  LEU A 292   N  ALA A 265           
SHEET    1 AA2 2 PHE A 167  THR A 168  0                                        
SHEET    2 AA2 2 GLY A 171  GLU A 172 -1  O  GLY A 171   N  THR A 168           
SHEET    1 AA3 8 GLU B  35  VAL B  41  0                                        
SHEET    2 AA3 8 VAL B  44  GLY B  52 -1  O  LEU B  46   N  ARG B  39           
SHEET    3 AA3 8 THR B  82  PRO B  86 -1  O  VAL B  83   N  GLY B  51           
SHEET    4 AA3 8 LEU B  56  VAL B  60  1  N  LEU B  59   O  ILE B  84           
SHEET    5 AA3 8 PHE B 123  HIS B 128  1  O  VAL B 126   N  VAL B  60           
SHEET    6 AA3 8 ILE B 146  MET B 152  1  O  VAL B 150   N  LEU B 125           
SHEET    7 AA3 8 THR B 261  GLY B 266  1  O  MET B 262   N  LEU B 149           
SHEET    8 AA3 8 VAL B 287  LEU B 292  1  O  LEU B 292   N  ALA B 265           
SHEET    1 AA4 2 PHE B 167  THR B 168  0                                        
SHEET    2 AA4 2 GLY B 171  GLU B 172 -1  O  GLY B 171   N  THR B 168           
SHEET    1 AA5 8 GLU C  35  VAL C  41  0                                        
SHEET    2 AA5 8 VAL C  44  GLY C  52 -1  O  TYR C  48   N  ALA C  37           
SHEET    3 AA5 8 THR C  82  PRO C  86 -1  O  VAL C  83   N  GLY C  51           
SHEET    4 AA5 8 LEU C  56  VAL C  60  1  N  LEU C  59   O  ILE C  84           
SHEET    5 AA5 8 PHE C 123  HIS C 128  1  O  ASP C 124   N  LEU C  56           
SHEET    6 AA5 8 ILE C 146  MET C 152  1  O  VAL C 150   N  LEU C 125           
SHEET    7 AA5 8 THR C 261  GLY C 266  1  O  MET C 262   N  TYR C 151           
SHEET    8 AA5 8 VAL C 287  LEU C 292  1  O  LEU C 292   N  ALA C 265           
SHEET    1 AA6 2 PHE C 167  THR C 168  0                                        
SHEET    2 AA6 2 GLY C 171  GLU C 172 -1  O  GLY C 171   N  THR C 168           
SHEET    1 AA7 8 GLU D  35  VAL D  41  0                                        
SHEET    2 AA7 8 VAL D  44  GLY D  52 -1  O  LEU D  46   N  ARG D  39           
SHEET    3 AA7 8 THR D  82  PRO D  86 -1  O  VAL D  83   N  GLY D  51           
SHEET    4 AA7 8 LEU D  56  VAL D  60  1  N  VAL D  57   O  THR D  82           
SHEET    5 AA7 8 PHE D 123  HIS D 128  1  O  ASP D 124   N  LEU D  56           
SHEET    6 AA7 8 ILE D 146  MET D 152  1  O  VAL D 150   N  ALA D 127           
SHEET    7 AA7 8 THR D 261  GLY D 266  1  O  MET D 262   N  LEU D 149           
SHEET    8 AA7 8 VAL D 287  LEU D 292  1  O  LEU D 292   N  ALA D 265           
SHEET    1 AA8 2 PHE D 167  THR D 168  0                                        
SHEET    2 AA8 2 GLY D 171  GLU D 172 -1  O  GLY D 171   N  THR D 168           
SSBOND   1 CYS A  295    CYS A  303                          1555   1555  2.01  
SSBOND   2 CYS B  295    CYS B  303                          1555   1555  2.01  
SSBOND   3 CYS C  295    CYS C  303                          1555   1555  2.01  
SSBOND   4 CYS D  295    CYS D  303                          1555   1555  2.00  
SITE     1 AC1 16 ASP A 129  ILE A 130  TRP A 133  GLU A 153                    
SITE     2 AC1 16 PHE A 164  PRO A 165  LEU A 174  VAL A 175                    
SITE     3 AC1 16 HIS A 177  TYR A 239  GLY A 270  GLY A 271                    
SITE     4 AC1 16 MET A 272  HIS A 297  HOH A 586  HOH A 601                    
SITE     1 AC2 15 ASP B 129  PHE B 164  LEU B 174  VAL B 175                    
SITE     2 AC2 15 HIS B 177  PHE B 178  HIS B 207  TYR B 239                    
SITE     3 AC2 15 GLY B 270  GLY B 271  MET B 272  PHE B 275                    
SITE     4 AC2 15 HIS B 297  HOH B 612  HOH B 677                               
SITE     1 AC3 16 GLU A 278  ASP C 129  ILE C 130  TRP C 133                    
SITE     2 AC3 16 GLU C 153  PHE C 164  LEU C 174  VAL C 175                    
SITE     3 AC3 16 HIS C 177  TYR C 239  GLY C 270  GLY C 271                    
SITE     4 AC3 16 MET C 272  PHE C 275  HIS C 297  HOH C 602                    
SITE     1 AC4 13 ASP D 129  PHE D 164  LEU D 174  VAL D 175                    
SITE     2 AC4 13 HIS D 177  PHE D 178  HIS D 207  TYR D 239                    
SITE     3 AC4 13 GLY D 270  GLY D 271  MET D 272  PHE D 275                    
SITE     4 AC4 13 HIS D 297                                                     
CRYST1  168.971   83.711   88.879  90.00 100.68  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      0.005918  0.000000  0.001116        0.00000                         
SCALE2      0.000000  0.011946  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011449        0.00000                         
TER    2395      HIS A 321                                                      
TER    4738      ARG B 317                                                      
TER    7111      ARG C 317                                                      
TER    9485      HIS D 321                                                      
MASTER      376    0    4   64   40    0   16    610295    4  128   96          
END                                                                             

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