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Database: PDB
Entry: 5N63
LinkDB: 5N63
Original site: 5N63 
HEADER    TRANSFERASE                             14-FEB-17   5N63              
TITLE     CRYSTAL STRUCTURE OF P38ALPHA IN COMPLEX WITH LIPID POCKET LIGAND 9C  
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    KINASE, SMALL MOLECULE, LIPID POCKET, P38, QUINAZOLINE, TRANSFERASE   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.BUEHRMANN,M.P.MUELLER,D.RAUH                                        
REVDAT   1   20-SEP-17 5N63    0                                                
JRNL        AUTH   M.BUHRMANN,B.M.WIEDEMANN,M.P.MULLER,J.HARDICK,M.ECKE,D.RAUH  
JRNL        TITL   STRUCTURE-BASED DESIGN, SYNTHESIS AND CRYSTALLIZATION OF     
JRNL        TITL 2 2-ARYLQUINAZOLINES AS LIPID POCKET LIGANDS OF P38 ALPHA      
JRNL        TITL 3 MAPK.                                                        
JRNL        REF    PLOS ONE                      V.  12 84627 2017              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   28892510                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0184627                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10_2155: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.26                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 15592                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 780                             
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 49.2694 -  4.3603    1.00     2590   137  0.1689 0.1820        
REMARK   3     2  4.3603 -  3.4612    1.00     2495   131  0.1751 0.2291        
REMARK   3     3  3.4612 -  3.0237    1.00     2434   128  0.2309 0.2770        
REMARK   3     4  3.0237 -  2.7473    1.00     2445   129  0.2283 0.3051        
REMARK   3     5  2.7473 -  2.5504    1.00     2421   127  0.2477 0.2778        
REMARK   3     6  2.5504 -  2.4000    1.00     2427   128  0.2699 0.2883        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.300            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.440           
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      :  0.008           2727                                  
REMARK   3   ANGLE     :  0.912           3703                                  
REMARK   3   CHIRALITY :  0.051            415                                  
REMARK   3   PLANARITY :  0.006            469                                  
REMARK   3   DIHEDRAL  : 10.669           1640                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESSEQ 5:353)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.5305  -3.7389  15.5731              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4113 T22:   0.3450                                     
REMARK   3      T33:   0.2776 T12:   0.0422                                     
REMARK   3      T13:  -0.0536 T23:  -0.0495                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9034 L22:   2.2198                                     
REMARK   3      L33:   1.4443 L12:   0.0821                                     
REMARK   3      L13:  -0.4045 L23:   0.3909                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0341 S12:  -0.2209 S13:   0.1110                       
REMARK   3      S21:   0.1272 S22:  -0.0435 S23:  -0.1145                       
REMARK   3      S31:   0.0023 S32:   0.0502 S33:   0.0001                       
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 5N63 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 14-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003375.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-SEP-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 90                                 
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) : 0.9779                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15592                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 13.00                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.60                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.760                              
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: 4DLI                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.78                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES PH 5.6-6.2, 20-30 %           
REMARK 280  PEG4000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.15K         
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       32.69500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       39.16000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.45000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       39.16000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.69500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.45000            
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: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 16600 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     GLU A     4                                                      
REMARK 465     GLY A    31                                                      
REMARK 465     SER A    32                                                      
REMARK 465     GLY A    33                                                      
REMARK 465     ALA A    34                                                      
REMARK 465     VAL A   117                                                      
REMARK 465     LYS A   118                                                      
REMARK 465     CYS A   119                                                      
REMARK 465     GLN A   120                                                      
REMARK 465     LYS A   121                                                      
REMARK 465     PHE A   169                                                      
REMARK 465     GLY A   170                                                      
REMARK 465     LEU A   171                                                      
REMARK 465     ALA A   172                                                      
REMARK 465     ARG A   173                                                      
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     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 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    ASP A   168     O    HOH A   501              1.96            
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    ASN A  14       51.47     35.23                                   
REMARK 500    ARG A 149      -15.82     81.55                                   
REMARK 500    ASN A 201     -164.30   -111.29                                   
REMARK 500    PHE A 274       59.72   -106.04                                   
REMARK 500    LEU A 289       52.15    -91.95                                   
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 8OW A 401                 
DBREF  5N63 A    1   360  UNP    Q16539   MK14_HUMAN       1    360             
SEQRES   1 A  360  MET SER GLN GLU ARG PRO THR PHE TYR ARG GLN GLU LEU          
SEQRES   2 A  360  ASN LYS THR ILE TRP GLU VAL PRO GLU ARG TYR GLN ASN          
SEQRES   3 A  360  LEU SER PRO VAL GLY SER GLY ALA TYR GLY SER VAL CYS          
SEQRES   4 A  360  ALA ALA PHE ASP THR LYS THR GLY LEU ARG VAL ALA VAL          
SEQRES   5 A  360  LYS LYS LEU SER ARG PRO PHE GLN SER ILE ILE HIS ALA          
SEQRES   6 A  360  LYS ARG THR TYR ARG GLU LEU ARG LEU LEU LYS HIS MET          
SEQRES   7 A  360  LYS HIS GLU ASN VAL ILE GLY LEU LEU ASP VAL PHE THR          
SEQRES   8 A  360  PRO ALA ARG SER LEU GLU GLU PHE ASN ASP VAL TYR LEU          
SEQRES   9 A  360  VAL THR HIS LEU MET GLY ALA ASP LEU ASN ASN ILE VAL          
SEQRES  10 A  360  LYS CYS GLN LYS LEU THR ASP ASP HIS VAL GLN PHE LEU          
SEQRES  11 A  360  ILE TYR GLN ILE LEU ARG GLY LEU LYS TYR ILE HIS SER          
SEQRES  12 A  360  ALA ASP ILE ILE HIS ARG ASP LEU LYS PRO SER ASN LEU          
SEQRES  13 A  360  ALA VAL ASN GLU ASP CYS GLU LEU LYS ILE LEU ASP PHE          
SEQRES  14 A  360  GLY LEU ALA ARG HIS THR ASP ASP GLU MET THR GLY TYR          
SEQRES  15 A  360  VAL ALA THR ARG TRP TYR ARG ALA PRO GLU ILE MET LEU          
SEQRES  16 A  360  ASN TRP MET HIS TYR ASN GLN THR VAL ASP ILE TRP SER          
SEQRES  17 A  360  VAL GLY CYS ILE MET ALA GLU LEU LEU THR GLY ARG THR          
SEQRES  18 A  360  LEU PHE PRO GLY THR ASP HIS ILE ASP GLN LEU LYS LEU          
SEQRES  19 A  360  ILE LEU ARG LEU VAL GLY THR PRO GLY ALA GLU LEU LEU          
SEQRES  20 A  360  LYS LYS ILE SER SER GLU SER ALA ARG ASN TYR ILE GLN          
SEQRES  21 A  360  SER LEU THR GLN MET PRO LYS MET ASN PHE ALA ASN VAL          
SEQRES  22 A  360  PHE ILE GLY ALA ASN PRO LEU ALA VAL ASP LEU LEU GLU          
SEQRES  23 A  360  LYS MET LEU VAL LEU ASP SER ASP LYS ARG ILE THR ALA          
SEQRES  24 A  360  ALA GLN ALA LEU ALA HIS ALA TYR PHE ALA GLN TYR HIS          
SEQRES  25 A  360  ASP PRO ASP ASP GLU PRO VAL ALA ASP PRO TYR ASP GLN          
SEQRES  26 A  360  SER PHE GLU SER ARG ASP LEU LEU ILE ASP GLU TRP LYS          
SEQRES  27 A  360  SER LEU THR TYR ASP GLU VAL ILE SER PHE VAL PRO PRO          
SEQRES  28 A  360  PRO LEU ASP GLN GLU GLU MET GLU SER                          
HET    8OW  A 401      26                                                       
HETNAM     8OW ~{N}4-[(4-FLUOROPHENYL)METHYL]-2-PHENYL-QUINAZOLINE-4,           
HETNAM   2 8OW  7-DIAMINE                                                       
FORMUL   2  8OW    C21 H17 F N4                                                 
FORMUL   3  HOH   *32(H2 O)                                                     
HELIX    1 AA1 SER A   61  MET A   78  1                                  18    
HELIX    2 AA2 ASN A  114  ILE A  116  5                                   3    
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  184  ARG A  189  5                                   6    
HELIX    6 AA6 ALA A  190  LEU A  195  1                                   6    
HELIX    7 AA7 GLN A  202  GLY A  219  1                                  18    
HELIX    8 AA8 ASP A  227  GLY A  240  1                                  14    
HELIX    9 AA9 GLY A  243  LYS A  248  1                                   6    
HELIX   10 AB1 SER A  252  LEU A  262  1                                  11    
HELIX   11 AB2 ASN A  269  PHE A  274  1                                   6    
HELIX   12 AB3 ASN A  278  LEU A  289  1                                  12    
HELIX   13 AB4 ASP A  292  ARG A  296  5                                   5    
HELIX   14 AB5 THR A  298  ALA A  304  1                                   7    
HELIX   15 AB6 HIS A  305  ALA A  309  5                                   5    
HELIX   16 AB7 ASP A  313  GLU A  317  5                                   5    
HELIX   17 AB8 GLN A  325  ARG A  330  5                                   6    
HELIX   18 AB9 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  PRO A  29  0                                        
SHEET    2 AA2 5 GLY A  36  ASP A  43 -1  O  ALA A  40   N  SER A  28           
SHEET    3 AA2 5 LEU A  48  LEU A  55 -1  O  VAL A  52   N  CYS A  39           
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 3 ALA A 111  ASP A 112  0                                        
SHEET    2 AA3 3 LEU A 156  VAL A 158 -1  O  VAL A 158   N  ALA A 111           
SHEET    3 AA3 3 LEU A 164  ILE A 166 -1  O  LYS A 165   N  ALA A 157           
SITE     1 AC1 11 PRO A 191  GLU A 192  LEU A 195  TRP A 197                    
SITE     2 AC1 11 PRO A 242  LEU A 246  LYS A 249  SER A 252                    
SITE     3 AC1 11 ILE A 259  ASP A 292  ASP A 294                               
CRYST1   65.390   74.900   78.320  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      0.015293  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013351  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012768        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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