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Database: PDB
Entry: 3HMM
LinkDB: 3HMM
Original site: 3HMM 
HEADER    TRANSFERASE                             29-MAY-09   3HMM              
TITLE     STRUCTURE OF ALK5 + GW855857                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TGF-BETA RECEPTOR TYPE-1;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: KINASE DOMAIN, RESIDUES 201-503;                           
COMPND   5 SYNONYM: TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I, TGF-BETA   
COMPND   6 RECEPTOR TYPE I, TGF-BETA TYPE I RECEPTOR, TBETAR-I, TGFR-1,         
COMPND   7 SERINE/THREONINE-PROTEIN KINASE RECEPTOR R4, SKR4, ACTIVIN RECEPTOR- 
COMPND   8 LIKE KINASE 5, ALK-5;                                                
COMPND   9 EC: 2.7.11.30;                                                       
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    TGF-BETA, ALK5, KINASE, INHIBITOR, QUINAZOLINE, AORTIC ANEURYSM, ATP- 
KEYWDS   2 BINDING, CRANIOSYNOSTOSIS, DISEASE MUTATION, DISULFIDE BOND,         
KEYWDS   3 GLYCOPROTEIN, MAGNESIUM, MANGANESE, MEMBRANE, METAL-BINDING,         
KEYWDS   4 NUCLEOTIDE-BINDING, PHOSPHOPROTEIN POLYMORPHISM, RECEPTOR,           
KEYWDS   5 SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE, TRANSMEMBRANE          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.SMITH,C.JANSON                                                      
REVDAT   2   01-NOV-17 3HMM    1       REMARK                                   
REVDAT   1   23-JUN-09 3HMM    0                                                
SPRSDE     23-JUN-09 3HMM      3GXJ                                             
JRNL        AUTH   F.GELLIBERT,M.-H.FOUCHET,V.-L.NGUYEN,R.WANG,G.KRYSA,         
JRNL        AUTH 2 A.-C.DE GOUVILLE,S.HUET,N.DODIC                              
JRNL        TITL   DESIGN OF NOVEL QUINAZOLINE DERIVATIVES AND RELATED          
JRNL        TITL 2 ANALOGUES AS POTENT AND SELECTIVE ALK5 INHIBITORS            
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  19  2277 2009              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   19285388                                                     
JRNL        DOI    10.1016/J.BMCL.2009.02.087                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNX                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN,ACCELRYS                   
REMARK   3               : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,            
REMARK   3               : YIP,DZAKULA)                                         
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.73                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 32084                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.223                           
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.241                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1574                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : NULL                 
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE                    (NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : NULL                 
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL                 
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : 32084                
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2354                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 24                                      
REMARK   3   SOLVENT ATOMS            : 214                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.23                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.20900                                              
REMARK   3    B22 (A**2) : -9.88900                                             
REMARK   3    B33 (A**2) : 7.68000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 0.740 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.253 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.188 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 1.863 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3HMM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-JUN-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000053319.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-NOV-02                          
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               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32478                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
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) : 1.73                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.28500                            
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: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1B6C                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION                          
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       21.00450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       44.83900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.67150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       44.83900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.00450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.67150            
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 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     PRO A   169                                                      
REMARK 465     ASN A   170                                                      
REMARK 465     HIS A   171                                                      
REMARK 465     ARG A   172                                                      
REMARK 465     VAL A   173                                                      
REMARK 465     GLU A   299                                                      
REMARK 465     GLY A   300                                                      
REMARK 465     ILE A   301                                                      
REMARK 465     LYS A   302                                                      
REMARK 465     MET A   303                                                      
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    GLN A 124       67.75   -109.12                                   
REMARK 500    ARG A 132       -1.97     76.01                                   
REMARK 500    ASP A 133       41.50   -153.78                                   
REMARK 500    ALA A 150     -168.91   -127.07                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 224         0.08    SIDE CHAIN                              
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 855 A 857                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3GXL   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN WITH GW857175                                       
DBREF  3HMM A    1   303  UNP    P36897   TGFR1_HUMAN    201    503             
SEQRES   1 A  303  ILE ALA ARG THR ILE VAL LEU GLN GLU SER ILE GLY LYS          
SEQRES   2 A  303  GLY ARG PHE GLY GLU VAL TRP ARG GLY LYS TRP ARG GLY          
SEQRES   3 A  303  GLU GLU VAL ALA VAL LYS ILE PHE SER SER ARG GLU GLU          
SEQRES   4 A  303  ARG SER TRP PHE ARG GLU ALA GLU ILE TYR GLN THR VAL          
SEQRES   5 A  303  MET LEU ARG HIS GLU ASN ILE LEU GLY PHE ILE ALA ALA          
SEQRES   6 A  303  ASP ASN LYS ASP ASN GLY THR TRP THR GLN LEU TRP LEU          
SEQRES   7 A  303  VAL SER ASP TYR HIS GLU HIS GLY SER LEU PHE ASP TYR          
SEQRES   8 A  303  LEU ASN ARG TYR THR VAL THR VAL GLU GLY MET ILE LYS          
SEQRES   9 A  303  LEU ALA LEU SER THR ALA SER GLY LEU ALA HIS LEU HIS          
SEQRES  10 A  303  MET GLU ILE VAL GLY THR GLN GLY LYS PRO ALA ILE ALA          
SEQRES  11 A  303  HIS ARG ASP LEU LYS SER LYS ASN ILE LEU VAL LYS LYS          
SEQRES  12 A  303  ASN GLY THR CYS CYS ILE ALA ASP LEU GLY LEU ALA VAL          
SEQRES  13 A  303  ARG HIS ASP SER ALA THR ASP THR ILE ASP ILE ALA PRO          
SEQRES  14 A  303  ASN HIS ARG VAL GLY THR LYS ARG TYR MET ALA PRO GLU          
SEQRES  15 A  303  VAL LEU ASP ASP SER ILE ASN MET LYS HIS PHE GLU SER          
SEQRES  16 A  303  PHE LYS ARG ALA ASP ILE TYR ALA MET GLY LEU VAL PHE          
SEQRES  17 A  303  TRP GLU ILE ALA ARG ARG CYS SER ILE GLY GLY ILE HIS          
SEQRES  18 A  303  GLU ASP TYR GLN LEU PRO TYR TYR ASP LEU VAL PRO SER          
SEQRES  19 A  303  ASP PRO SER VAL GLU GLU MET ARG LYS VAL VAL CYS GLU          
SEQRES  20 A  303  GLN LYS LEU ARG PRO ASN ILE PRO ASN ARG TRP GLN SER          
SEQRES  21 A  303  CYS GLU ALA LEU ARG VAL MET ALA LYS ILE MET ARG GLU          
SEQRES  22 A  303  CYS TRP TYR ALA ASN GLY ALA ALA ARG LEU THR ALA LEU          
SEQRES  23 A  303  ARG ILE LYS LYS THR LEU SER GLN LEU SER GLN GLN GLU          
SEQRES  24 A  303  GLY ILE LYS MET                                              
HET    855  A 857      24                                                       
HETNAM     855 2-(6-METHYLPYRIDIN-2-YL)-N-PYRIDIN-4-YLQUINAZOLIN-4-             
HETNAM   2 855  AMINE                                                           
FORMUL   2  855    C19 H15 N5                                                   
FORMUL   3  HOH   *214(H2 O)                                                    
HELIX    1   1 ILE A    1  ARG A    3  5                                   3    
HELIX    2   2 SER A   35  ARG A   37  5                                   3    
HELIX    3   3 GLU A   38  GLN A   50  1                                  13    
HELIX    4   4 SER A   87  TYR A   95  1                                   9    
HELIX    5   5 THR A   98  MET A  118  1                                  21    
HELIX    6   6 THR A  175  MET A  179  5                                   5    
HELIX    7   7 ALA A  180  ASP A  185  1                                   6    
HELIX    8   8 HIS A  192  ARG A  214  1                                  23    
HELIX    9   9 SER A  237  CYS A  246  1                                  10    
HELIX   10  10 PRO A  255  SER A  260  5                                   6    
HELIX   11  11 CYS A  261  GLU A  273  1                                  13    
HELIX   12  12 ASN A  278  ARG A  282  5                                   5    
HELIX   13  13 THR A  284  GLN A  298  1                                  15    
SHEET    1   A 5 ILE A   5  LYS A  13  0                                        
SHEET    2   A 5 GLU A  18  TRP A  24 -1  O  VAL A  19   N  GLY A  12           
SHEET    3   A 5 GLU A  27  PHE A  34 -1  O  GLU A  27   N  TRP A  24           
SHEET    4   A 5 THR A  74  ASP A  81 -1  O  LEU A  76   N  PHE A  34           
SHEET    5   A 5 PHE A  62  ASP A  69 -1  N  ILE A  63   O  VAL A  79           
SHEET    1   B 3 ILE A 129  ALA A 130  0                                        
SHEET    2   B 3 VAL A 156  ASP A 159 -1  O  VAL A 156   N  ALA A 130           
SHEET    3   B 3 THR A 164  ILE A 165 -1  O  THR A 164   N  ASP A 159           
SHEET    1   C 2 ILE A 139  VAL A 141  0                                        
SHEET    2   C 2 CYS A 147  ILE A 149 -1  O  CYS A 148   N  LEU A 140           
SITE     1 AC1 13 ALA A  30  LYS A  32  TYR A  49  LEU A  60                    
SITE     2 AC1 13 LEU A  78  SER A  80  ASP A  81  TYR A  82                    
SITE     3 AC1 13 HIS A  83  LYS A 137  LEU A 140  ASP A 151                    
SITE     4 AC1 13 HOH A1006                                                     
CRYST1   42.009   75.343   89.678  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      0.023804  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013273  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011151        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system