GenomeNet

Database: PDB
Entry: 6HWT
LinkDB: 6HWT
Original site: 6HWT 
HEADER    TRANSFERASE                             15-OCT-18   6HWT              
TITLE     CRYSTAL STRUCTURE OF P38ALPHA IN COMPLEX WITH A REDUCED               
TITLE    2 PHOTOSWITCHABLE 2-AZOTHIAZOL-BASED INHIBITOR (COMPOUND 31)           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 14;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MAPK 14,CYTOKINE SUPPRESSIVE ANTI-INFLAMMATORY DRUG-BINDING 
COMPND   5 PROTEIN,CSBP,MAP KINASE MXI2,MAX-INTERACTING PROTEIN 2,MITOGEN-      
COMPND   6 ACTIVATED PROTEIN KINASE P38 ALPHA,MAP KINASE P38 ALPHA,STRESS-      
COMPND   7 ACTIVATED PROTEIN KINASE 2A,SAPK2A;                                  
COMPND   8 EC: 2.7.11.24;                                                       
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MAPK14, CSBP, CSBP1, CSBP2, CSPB1, MXI2, SAPK2A;               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    P38ALPHA, MAPK14, PHOTOSWITCHABLE, AZOTHIAZOL, TRANSFERASE            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.P.MUELLER,D.RAUH                                                    
REVDAT   2   19-JUN-19 6HWT    1       JRNL                                     
REVDAT   1   17-APR-19 6HWT    0                                                
JRNL        AUTH   M.SCHEHR,C.IANES,J.WEISNER,L.HEINTZE,M.P.MULLER,C.PICHLO,    
JRNL        AUTH 2 J.CHARL,E.BRUNSTEIN,J.EWERT,M.LEHR,U.BAUMANN,D.RAUH,         
JRNL        AUTH 3 U.KNIPPSCHILD,C.PEIFER,R.HERGES                              
JRNL        TITL   2-AZO-, 2-DIAZOCINE-THIAZOLS AND 2-AZO-IMIDAZOLES AS         
JRNL        TITL 2 PHOTOSWITCHABLE KINASE INHIBITORS: LIMITATIONS AND PITFALLS  
JRNL        TITL 3 OF THE PHOTOSWITCHABLE INHIBITOR APPROACH.                   
JRNL        REF    PHOTOCHEM. PHOTOBIOL. SCI.    V.  18  1398 2019              
JRNL        REFN                   ISSN 1474-9092                               
JRNL        PMID   30924488                                                     
JRNL        DOI    10.1039/C9PP00010K                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.26                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 39952                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
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 49.2774 -  4.0966    1.00     2924   154  0.1628 0.1816        
REMARK   3     2  4.0966 -  3.2518    1.00     2812   148  0.1678 0.2067        
REMARK   3     3  3.2518 -  2.8408    1.00     2777   147  0.2026 0.2400        
REMARK   3     4  2.8408 -  2.5810    1.00     2761   145  0.1900 0.2127        
REMARK   3     5  2.5810 -  2.3960    1.00     2738   144  0.1953 0.2430        
REMARK   3     6  2.3960 -  2.2548    0.97     2669   140  0.2276 0.2781        
REMARK   3     7  2.2548 -  2.1419    0.94     2594   137  0.2776 0.2953        
REMARK   3     8  2.1419 -  2.0486    1.00     2722   143  0.1976 0.2461        
REMARK   3     9  2.0486 -  1.9698    1.00     2717   144  0.2311 0.2483        
REMARK   3    10  1.9698 -  1.9018    0.97     2657   140  0.4173 0.4582        
REMARK   3    11  1.9018 -  1.8423    0.91     2468   130  0.3453 0.4159        
REMARK   3    12  1.8423 -  1.7897    1.00     2675   141  0.2685 0.2829        
REMARK   3    13  1.7897 -  1.7425    1.00     2741   145  0.2796 0.3349        
REMARK   3    14  1.7425 -  1.7000    1.00     2697   142  0.3127 0.3254        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.200            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.930           
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      :  0.005           2919                                  
REMARK   3   ANGLE     :  0.965           3965                                  
REMARK   3   CHIRALITY :  0.048            449                                  
REMARK   3   PLANARITY :  0.004            495                                  
REMARK   3   DIHEDRAL  : 12.525           1791                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 5 THROUGH 102 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -31.1075  -4.9235  19.1214              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2553 T22:   0.2481                                     
REMARK   3      T33:   0.2585 T12:   0.0543                                     
REMARK   3      T13:   0.0271 T23:   0.0005                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8301 L22:   1.2349                                     
REMARK   3      L33:   0.9695 L12:   0.2391                                     
REMARK   3      L13:   0.0390 L23:   0.6040                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0398 S12:   0.0049 S13:   0.0145                       
REMARK   3      S21:   0.0024 S22:  -0.0128 S23:   0.3159                       
REMARK   3      S31:  -0.2662 S32:  -0.2558 S33:   0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 103 THROUGH 201 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.3579  -1.6402  21.2993              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2425 T22:   0.1851                                     
REMARK   3      T33:   0.1933 T12:   0.0289                                     
REMARK   3      T13:  -0.0111 T23:  -0.0061                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4736 L22:   0.6631                                     
REMARK   3      L33:   0.7564 L12:   0.3580                                     
REMARK   3      L13:  -0.0076 L23:  -0.1894                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0255 S12:  -0.0163 S13:   0.1629                       
REMARK   3      S21:   0.0722 S22:  -0.0186 S23:   0.0083                       
REMARK   3      S31:  -0.2176 S32:  -0.0212 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 202 THROUGH 352 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.6156  -5.8535  15.3381              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2186 T22:   0.1769                                     
REMARK   3      T33:   0.1752 T12:   0.0171                                     
REMARK   3      T13:  -0.0113 T23:  -0.0195                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3116 L22:   0.7929                                     
REMARK   3      L33:   0.5447 L12:   0.1455                                     
REMARK   3      L13:   0.0150 L23:  -0.1099                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0327 S12:   0.1034 S13:  -0.0232                       
REMARK   3      S21:   0.0430 S22:  -0.0236 S23:  -0.1066                       
REMARK   3      S31:  -0.0583 S32:   0.0792 S33:   0.0000                       
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 6HWT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-OCT-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200012294.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-SEP-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.977928                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39982                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 8.400                              
REMARK 200  R MERGE                    (I) : 0.06500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.80300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 5N63                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.19                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES PH 5.6-6.2, 20-30 %           
REMARK 280  PEG4000, 40MM BOG, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE       
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       34.75500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       37.28500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.90500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       37.28500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       34.75500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.90500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1560 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17110 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 15.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     HIS A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     GLY A    33                                                      
REMARK 465     HIS A   174                                                      
REMARK 465     THR A   175                                                      
REMARK 465     ASP A   176                                                      
REMARK 465     ASP A   177                                                      
REMARK 465     GLU A   178                                                      
REMARK 465     MET A   179                                                      
REMARK 465     THR A   180                                                      
REMARK 465     GLY A   181                                                      
REMARK 465     TYR A   182                                                      
REMARK 465     VAL A   183                                                      
REMARK 465     ALA A   184                                                      
REMARK 465     LEU A   353                                                      
REMARK 465     ASP A   354                                                      
REMARK 465     GLN A   355                                                      
REMARK 465     GLU A   356                                                      
REMARK 465     GLU A   357                                                      
REMARK 465     MET A   358                                                      
REMARK 465     GLU A   359                                                      
REMARK 465     SER A   360                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     TYR A  35    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG A 173    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   506     O    HOH A   582              2.18            
REMARK 500   O    HOH A   547     O    HOH A   652              2.19            
REMARK 500   O    ASN A   272     O    HOH A   501              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   573     O    HOH A   617     4545     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 149      -12.38     78.69                                   
REMARK 500    ARG A 149      -17.13     82.41                                   
REMARK 500    ASP A 150       44.84   -141.96                                   
REMARK 500    MET A 198     -170.61     61.36                                   
REMARK 500    PHE A 274       61.90   -101.51                                   
REMARK 500    LEU A 289       58.89    -97.86                                   
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 BOG A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BOG A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BOG A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GXH A 404                 
DBREF  6HWT A    2   360  UNP    Q16539   MK14_HUMAN       2    360             
SEQADV 6HWT GLY A   -1  UNP  Q16539              EXPRESSION TAG                 
SEQADV 6HWT SER A    0  UNP  Q16539              EXPRESSION TAG                 
SEQADV 6HWT HIS A    1  UNP  Q16539              EXPRESSION TAG                 
SEQRES   1 A  362  GLY SER HIS SER GLN GLU ARG PRO THR PHE TYR ARG GLN          
SEQRES   2 A  362  GLU LEU ASN LYS THR ILE TRP GLU VAL PRO GLU ARG TYR          
SEQRES   3 A  362  GLN ASN LEU SER PRO VAL GLY SER GLY ALA TYR GLY SER          
SEQRES   4 A  362  VAL CYS ALA ALA PHE ASP THR LYS THR GLY LEU ARG VAL          
SEQRES   5 A  362  ALA VAL LYS LYS LEU SER ARG PRO PHE GLN SER ILE ILE          
SEQRES   6 A  362  HIS ALA LYS ARG THR TYR ARG GLU LEU ARG LEU LEU LYS          
SEQRES   7 A  362  HIS MET LYS HIS GLU ASN VAL ILE GLY LEU LEU ASP VAL          
SEQRES   8 A  362  PHE THR PRO ALA ARG SER LEU GLU GLU PHE ASN ASP VAL          
SEQRES   9 A  362  TYR LEU VAL THR HIS LEU MET GLY ALA ASP LEU ASN ASN          
SEQRES  10 A  362  ILE VAL LYS CYS GLN LYS LEU THR ASP ASP HIS VAL GLN          
SEQRES  11 A  362  PHE LEU ILE TYR GLN ILE LEU ARG GLY LEU LYS TYR ILE          
SEQRES  12 A  362  HIS SER ALA ASP ILE ILE HIS ARG ASP LEU LYS PRO SER          
SEQRES  13 A  362  ASN LEU ALA VAL ASN GLU ASP CYS GLU LEU LYS ILE LEU          
SEQRES  14 A  362  ASP PHE GLY LEU ALA ARG HIS THR ASP ASP GLU MET THR          
SEQRES  15 A  362  GLY TYR VAL ALA THR ARG TRP TYR ARG ALA PRO GLU ILE          
SEQRES  16 A  362  MET LEU ASN TRP MET HIS TYR ASN GLN THR VAL ASP ILE          
SEQRES  17 A  362  TRP SER VAL GLY CYS ILE MET ALA GLU LEU LEU THR GLY          
SEQRES  18 A  362  ARG THR LEU PHE PRO GLY THR ASP HIS ILE ASP GLN LEU          
SEQRES  19 A  362  LYS LEU ILE LEU ARG LEU VAL GLY THR PRO GLY ALA GLU          
SEQRES  20 A  362  LEU LEU LYS LYS ILE SER SER GLU SER ALA ARG ASN TYR          
SEQRES  21 A  362  ILE GLN SER LEU THR GLN MET PRO LYS MET ASN PHE ALA          
SEQRES  22 A  362  ASN VAL PHE ILE GLY ALA ASN PRO LEU ALA VAL ASP LEU          
SEQRES  23 A  362  LEU GLU LYS MET LEU VAL LEU ASP SER ASP LYS ARG ILE          
SEQRES  24 A  362  THR ALA ALA GLN ALA LEU ALA HIS ALA TYR PHE ALA GLN          
SEQRES  25 A  362  TYR HIS ASP PRO ASP ASP GLU PRO VAL ALA ASP PRO TYR          
SEQRES  26 A  362  ASP GLN SER PHE GLU SER ARG ASP LEU LEU ILE ASP GLU          
SEQRES  27 A  362  TRP LYS SER LEU THR TYR ASP GLU VAL ILE SER PHE VAL          
SEQRES  28 A  362  PRO PRO PRO LEU ASP GLN GLU GLU MET GLU SER                  
HET    BOG  A 401      20                                                       
HET    BOG  A 402      20                                                       
HET    BOG  A 403      20                                                       
HET    GXH  A 404      41                                                       
HETNAM     BOG B-OCTYLGLUCOSIDE                                                 
HETNAM     GXH 3-(2,5-DIMETHOXYPHENYL)-~{N}-[4-[4-(4-FLUOROPHENYL)-2-           
HETNAM   2 GXH  (2-PHENYLHYDRAZINYL)-1,3-THIAZOL-5-YL]PYRIDIN-2-                
HETNAM   3 GXH  YL]PROPANAMIDE                                                  
FORMUL   2  BOG    3(C14 H28 O6)                                                
FORMUL   5  GXH    C31 H28 F N5 O3 S                                            
FORMUL   6  HOH   *205(H2 O)                                                    
HELIX    1 AA1 SER A   61  MET A   78  1                                  18    
HELIX    2 AA2 ASP A  112  LYS A  118  1                                   7    
HELIX    3 AA3 THR A  123  ALA A  144  1                                  22    
HELIX    4 AA4 LYS A  152  SER A  154  5                                   3    
HELIX    5 AA5 ALA A  190  LEU A  195  1                                   6    
HELIX    6 AA6 THR A  203  GLY A  219  1                                  17    
HELIX    7 AA7 ASP A  227  GLY A  240  1                                  14    
HELIX    8 AA8 GLY A  243  LYS A  248  1                                   6    
HELIX    9 AA9 SER A  252  LEU A  262  1                                  11    
HELIX   10 AB1 ASN A  269  VAL A  273  5                                   5    
HELIX   11 AB2 ASN A  278  LEU A  289  1                                  12    
HELIX   12 AB3 ASP A  292  ARG A  296  5                                   5    
HELIX   13 AB4 THR A  298  ALA A  304  1                                   7    
HELIX   14 AB5 HIS A  305  ALA A  309  5                                   5    
HELIX   15 AB6 GLN A  325  ARG A  330  5                                   6    
HELIX   16 AB7 LEU A  333  SER A  347  1                                  15    
SHEET    1 AA1 2 PHE A   8  LEU A  13  0                                        
SHEET    2 AA1 2 THR A  16  PRO A  21 -1  O  TRP A  18   N  GLN A  11           
SHEET    1 AA2 5 TYR A  24  GLY A  31  0                                        
SHEET    2 AA2 5 GLY A  36  ASP A  43 -1  O  VAL A  38   N  GLY A  31           
SHEET    3 AA2 5 LEU A  48  LEU A  55 -1  O  LEU A  48   N  ASP A  43           
SHEET    4 AA2 5 TYR A 103  HIS A 107 -1  O  LEU A 104   N  LYS A  53           
SHEET    5 AA2 5 ASP A  88  PHE A  90 -1  N  ASP A  88   O  VAL A 105           
SHEET    1 AA3 2 LEU A 156  VAL A 158  0                                        
SHEET    2 AA3 2 LEU A 164  ILE A 166 -1  O  LYS A 165   N  ALA A 157           
SITE     1 AC1  6 ILE A  84  ILE A 141  ILE A 146  ILE A 147                    
SITE     2 AC1  6 ARG A 149  ASP A 168                                          
SITE     1 AC2 15 GLU A 192  TRP A 197  MET A 198  HIS A 199                    
SITE     2 AC2 15 TYR A 200  ASN A 201  LEU A 246  ILE A 259                    
SITE     3 AC2 15 LEU A 291  ASP A 292  SER A 293  ASP A 294                    
SITE     4 AC2 15 HOH A 518  HOH A 541  HOH A 565                               
SITE     1 AC3  3 GLN A  25  THR A  44  TYR A 258                               
SITE     1 AC4 15 VAL A  30  GLY A  31  ALA A  40  ALA A  51                    
SITE     2 AC4 15 LYS A  53  LEU A 104  VAL A 105  THR A 106                    
SITE     3 AC4 15 HIS A 107  MET A 109  PHE A 169  GLY A 170                    
SITE     4 AC4 15 LEU A 171  ALA A 172  ARG A 173                               
CRYST1   69.510   69.810   74.570  90.00  90.00  90.00 P 21 21 21    4          
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      0.014386  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014325  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013410        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system