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Database: PDB
Entry: 1VJY
LinkDB: 1VJY
Original site: 1VJY 
HEADER    TRANSFERASE                             07-APR-04   1VJY              
TITLE     CRYSTAL STRUCTURE OF A NAPHTHYRIDINE INHIBITOR OF HUMAN TGF-          
TITLE    2 BETA TYPE I RECEPTOR                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TGF-BETA RECEPTOR TYPE I;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: PROTEIN KINASE;                                            
COMPND   5 SYNONYM: TGFR-1, TGF-BETA TYPE I RECEPTOR,                           
COMPND   6 SERINE/THREONINE-PROTEIN KINASE RECEPTOR R4, SKR4, ACTIVIN           
COMPND   7 RECEPTOR-LIKE KINASE 5, ALK-5;                                       
COMPND   8 EC: 2.7.1.37;                                                        
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 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    TRANSFERASE, PROTEIN KINASE, INHIBITOR COMPLEX                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.GELLIBERT,J.WOOLVEN,M.-H.FOUCHET,N.MATHEWS,H.GOODLAND,              
AUTHOR   2 V.LOVEGROVE,A.LAROZE,V.-L.NGUYEN,S.SAUTET,R.WANG,C.JANSON,           
AUTHOR   3 W.SMITH,G.KRYSA,V.BOULLAY,A.-C.DE GOUVILLE,S.HUET,D.HARTLEY          
REVDAT   2   24-FEB-09 1VJY    1       VERSN                                    
REVDAT   1   31-AUG-04 1VJY    0                                                
JRNL        AUTH   F.GELLIBERT,J.WOOLVEN,M.-H.FOUCHET,N.MATHEWS,                
JRNL        AUTH 2 H.GOODLAND,V.LOVEGROVE,A.LAROZE,V.-L.NGUYEN,                 
JRNL        AUTH 3 S.SAUTET,R.WANG,C.JANSON,W.SMITH,G.KRYSA,V.BOULLAY,          
JRNL        AUTH 4 A.-C.DE GOUVILLE,S.HUET,D.HARTLEY                            
JRNL        TITL   IDENTIFICATION OF 1,5-NAPHTHYRIDINE DERIVATIVES AS           
JRNL        TITL 2 A NOVEL SERIES OF POTENT AND SELECTIVE TGF-BETA              
JRNL        TITL 3 TYPE I RECEPTOR INHIBITORS.                                  
JRNL        REF    J.MED.CHEM.                   V.  47  4494 2004              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   15317461                                                     
JRNL        DOI    10.1021/JM0400247                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 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                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 88.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 17608                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 854                             
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) : 20019                
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            : 2406                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 22                                      
REMARK   3   SOLVENT ATOMS            : 114                                     
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  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) : 2.000                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.50                            
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) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
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                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1VJY COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-APR-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB001933.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17608                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
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     (%) : 88.0                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.05100                            
REMARK 200  R SYM                      (I) : NULL                               
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) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.04                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.20900                            
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: NULL                         
REMARK 200 SOFTWARE USED: CNX                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.06                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 4000, 0.1M TRIS HCL, 0.2 M       
REMARK 280  MAGNESIUM CHLORIDE, PH 8.0, VAPOR DIFFUSION/SITTING DROP,           
REMARK 280  TEMPERATURE 278K, VAPOR DIFFUSION, SITTING DROP                     
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       21.03450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       44.79450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.88750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       44.79450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.03450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.88750            
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 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     ALA A   368                                                      
REMARK 465     PRO A   369                                                      
REMARK 465     ASN A   370                                                      
REMARK 465     HIS A   371                                                      
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 324       50.76   -100.88                                   
REMARK 500    ASP A 333       43.72   -158.12                                   
REMARK 500    ASP A 351       72.16     46.73                                   
REMARK 500    GLN A 498      -71.65    -70.88                                   
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 424         0.07    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1087        DISTANCE =  5.02 ANGSTROMS                       
REMARK 525    HOH A1099        DISTANCE =  5.41 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 460 A 999                 
DBREF  1VJY A  201   503  UNP    P36897   TGFR1_HUMAN      1    303             
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    460  A 999      22                                                       
HETNAM     460 2-[5-(6-METHYLPYRIDIN-2-YL)-2,3-DIHYDRO-1H-PYRAZOL-4-            
HETNAM   2 460  YL]-1,5-NAPHTHYRIDINE                                           
HETSYN     460 NAPHTHYRIDINE INHIBITOR                                          
FORMUL   2  460    C17 H15 N5                                                   
FORMUL   3  HOH   *114(H2 O)                                                    
HELIX    1   1 ILE A  201  ARG A  203  5                                   3    
HELIX    2   2 SER A  235  ARG A  237  5                                   3    
HELIX    3   3 GLU A  238  GLN A  250  1                                  13    
HELIX    4   4 SER A  287  TYR A  295  1                                   9    
HELIX    5   5 THR A  298  MET A  318  1                                  21    
HELIX    6   6 THR A  375  MET A  379  5                                   5    
HELIX    7   7 ALA A  380  ASP A  385  1                                   6    
HELIX    8   8 HIS A  392  ARG A  414  1                                  23    
HELIX    9   9 SER A  437  CYS A  446  1                                  10    
HELIX   10  10 PRO A  455  SER A  460  5                                   6    
HELIX   11  11 CYS A  461  GLU A  473  1                                  13    
HELIX   12  12 ASN A  478  ARG A  482  5                                   5    
HELIX   13  13 THR A  484  GLY A  500  1                                  17    
SHEET    1   A 5 ILE A 205  GLY A 212  0                                        
SHEET    2   A 5 GLU A 218  TRP A 224 -1  O  VAL A 219   N  GLY A 212           
SHEET    3   A 5 GLU A 227  PHE A 234 -1  O  GLU A 227   N  TRP A 224           
SHEET    4   A 5 THR A 274  ASP A 281 -1  O  LEU A 278   N  LYS A 232           
SHEET    5   A 5 PHE A 262  ASP A 269 -1  N  ASP A 266   O  TRP A 277           
SHEET    1   B 2 ALA A 328  ALA A 330  0                                        
SHEET    2   B 2 VAL A 356  HIS A 358 -1  O  HIS A 358   N  ALA A 328           
SHEET    1   C 2 ILE A 339  VAL A 341  0                                        
SHEET    2   C 2 CYS A 347  ILE A 349 -1  O  CYS A 348   N  LEU A 340           
SITE     1 AC1 12 ALA A 230  LYS A 232  TYR A 249  LEU A 260                    
SITE     2 AC1 12 LEU A 278  SER A 280  ASP A 281  TYR A 282                    
SITE     3 AC1 12 HIS A 283  LEU A 340  ASP A 351  HOH A1001                    
CRYST1   42.069   75.775   89.589  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      0.023770  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013197  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011162        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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