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Database: PDB
Entry: 4X2J
LinkDB: 4X2J
Original site: 4X2J 
HEADER    TRANSFERASE                             26-NOV-14   4X2J              
TITLE     SELECTION OF FRAGMENTS FOR KINASE INHIBITOR DESIGN: DECORATION IS KEY 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TGF-BETA RECEPTOR TYPE-1;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: TGFR-1,ACTIVIN A RECEPTOR TYPE II-LIKE PROTEIN KINASE OF    
COMPND   5 53KD,ACTIVIN RECEPTOR-LIKE KINASE 5,ALK5,SERINE/THREONINE-PROTEIN    
COMPND   6 KINASE RECEPTOR R4,SKR4,TGF-BETA TYPE I RECEPTOR,TRANSFORMING GROWTH 
COMPND   7 FACTOR-BETA RECEPTOR TYPE I,TBETAR-I;                                
COMPND   8 EC: 2.7.11.30;                                                       
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: TGFBR1, ALK5, SKR4;                                            
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    TRANSFERASE, PROTEIN KINASE, INHIBITOR COMPLEX                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.CZODROWSKI,G.HOELZEMANN,G.BARNICKEL,H.GREINER,D.MUSIL               
REVDAT   2   21-JAN-15 4X2J    1       JRNL                                     
REVDAT   1   24-DEC-14 4X2J    0                                                
JRNL        AUTH   P.CZODROWSKI,G.HOLZEMANN,G.BARNICKEL,H.GREINER,D.MUSIL       
JRNL        TITL   SELECTION OF FRAGMENTS FOR KINASE INHIBITOR DESIGN:          
JRNL        TITL 2 DECORATION IS KEY.                                           
JRNL        REF    J.MED.CHEM.                   V.  58   457 2015              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   25437144                                                     
JRNL        DOI    10.1021/JM501597J                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.69 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.4                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.69                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 22.54                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 33214                          
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)  : 0.167                          
REMARK   3   R VALUE            (WORKING SET)  : 0.154                          
REMARK   3   FREE R VALUE                      : 0.184                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 43.220                         
REMARK   3   FREE R VALUE TEST SET COUNT       : 14356                          
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 17                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.69                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.74                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 97.79                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2321                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.1851                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 1292                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.1562                   
REMARK   3   BIN FREE R VALUE                        : 0.2224                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 44.33                    
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 1029                     
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            : 2429                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 24                                      
REMARK   3   SOLVENT ATOMS            : 250                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.15                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.71                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.55650                                              
REMARK   3    B22 (A**2) : -2.90370                                             
REMARK   3    B33 (A**2) : 2.34720                                              
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) : 0.177               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.097               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.093               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.092               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.090               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.945                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 2566   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 3477   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 921    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 61     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 380    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 2566   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 328    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 3264   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.02                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.60                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 14.17                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   12.1070   76.5297   12.1773           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0324 T22:   -0.0347                                    
REMARK   3     T33:   -0.0190 T12:    0.0011                                    
REMARK   3     T13:   -0.0007 T23:    0.0004                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.2852 L22:    0.5007                                    
REMARK   3     L33:    0.6610 L12:    0.2185                                    
REMARK   3     L13:    0.1731 L23:    0.3986                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0188 S12:   -0.0097 S13:    0.0458                     
REMARK   3     S21:   -0.0414 S22:    0.0009 S23:    0.0252                     
REMARK   3     S31:   -0.0842 S32:    0.0038 S33:    0.0179                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4X2J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-NOV-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000204962.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-DEC-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 33372                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.690                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.080                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL, 240 MM LI2SO4, 24% PEG   
REMARK 280  4000, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       21.15500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.10000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.75500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.10000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.15500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.75500            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 220 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 14490 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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     LYS A   502                                                      
REMARK 465     MET A   503                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 332       -2.13     73.15                                   
REMARK 500    ASP A 333       44.66   -150.40                                   
REMARK 500    ALA A 368       66.54     39.05                                   
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 3WN A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 602                 
DBREF  4X2J A  200   503  UNP    P36897   TGFR1_HUMAN    200    503             
SEQADV 4X2J GLY A  199  UNP  P36897              EXPRESSION TAG                 
SEQRES   1 A  305  GLY THR ILE ALA ARG THR ILE VAL LEU GLN GLU SER ILE          
SEQRES   2 A  305  GLY LYS GLY ARG PHE GLY GLU VAL TRP ARG GLY LYS TRP          
SEQRES   3 A  305  ARG GLY GLU GLU VAL ALA VAL LYS ILE PHE SER SER ARG          
SEQRES   4 A  305  GLU GLU ARG SER TRP PHE ARG GLU ALA GLU ILE TYR GLN          
SEQRES   5 A  305  THR VAL MET LEU ARG HIS GLU ASN ILE LEU GLY PHE ILE          
SEQRES   6 A  305  ALA ALA ASP ASN LYS ASP ASN GLY THR TRP THR GLN LEU          
SEQRES   7 A  305  TRP LEU VAL SER ASP TYR HIS GLU HIS GLY SER LEU PHE          
SEQRES   8 A  305  ASP TYR LEU ASN ARG TYR THR VAL THR VAL GLU GLY MET          
SEQRES   9 A  305  ILE LYS LEU ALA LEU SER THR ALA SER GLY LEU ALA HIS          
SEQRES  10 A  305  LEU HIS MET GLU ILE VAL GLY THR GLN GLY LYS PRO ALA          
SEQRES  11 A  305  ILE ALA HIS ARG ASP LEU LYS SER LYS ASN ILE LEU VAL          
SEQRES  12 A  305  LYS LYS ASN GLY THR CYS CYS ILE ALA ASP LEU GLY LEU          
SEQRES  13 A  305  ALA VAL ARG HIS ASP SER ALA THR ASP THR ILE ASP ILE          
SEQRES  14 A  305  ALA PRO ASN HIS ARG VAL GLY THR LYS ARG TYR MET ALA          
SEQRES  15 A  305  PRO GLU VAL LEU ASP ASP SER ILE ASN MET LYS HIS PHE          
SEQRES  16 A  305  GLU SER PHE LYS ARG ALA ASP ILE TYR ALA MET GLY LEU          
SEQRES  17 A  305  VAL PHE TRP GLU ILE ALA ARG ARG CYS SER ILE GLY GLY          
SEQRES  18 A  305  ILE HIS GLU ASP TYR GLN LEU PRO TYR TYR ASP LEU VAL          
SEQRES  19 A  305  PRO SER ASP PRO SER VAL GLU GLU MET ARG LYS VAL VAL          
SEQRES  20 A  305  CYS GLU GLN LYS LEU ARG PRO ASN ILE PRO ASN ARG TRP          
SEQRES  21 A  305  GLN SER CYS GLU ALA LEU ARG VAL MET ALA LYS ILE MET          
SEQRES  22 A  305  ARG GLU CYS TRP TYR ALA ASN GLY ALA ALA ARG LEU THR          
SEQRES  23 A  305  ALA LEU ARG ILE LYS LYS THR LEU SER GLN LEU SER GLN          
SEQRES  24 A  305  GLN GLU GLY ILE LYS MET                                      
HET    3WN  A 601      26                                                       
HET    SO4  A 602       5                                                       
HETNAM     3WN 4-[(3-AMINOPHENYL)AMINO]PYRIDO[2,3-D]PYRIMIDIN-5(8H)-            
HETNAM   2 3WN  ONE                                                             
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  3WN    C13 H11 N5 O                                                 
FORMUL   3  SO4    O4 S 2-                                                      
FORMUL   4  HOH   *250(H2 O)                                                    
HELIX    1 AA1 ILE A  201  ARG A  203  5                                   3    
HELIX    2 AA2 GLU A  238  GLN A  250  1                                  13    
HELIX    3 AA3 SER A  287  TYR A  295  1                                   9    
HELIX    4 AA4 THR A  298  MET A  318  1                                  21    
HELIX    5 AA5 LYS A  335  LYS A  337  5                                   3    
HELIX    6 AA6 ASP A  351  ALA A  355  5                                   5    
HELIX    7 AA7 THR A  375  MET A  379  5                                   5    
HELIX    8 AA8 ALA A  380  ASP A  385  1                                   6    
HELIX    9 AA9 HIS A  392  ARG A  414  1                                  23    
HELIX   10 AB1 SER A  437  CYS A  446  1                                  10    
HELIX   11 AB2 PRO A  455  SER A  460  5                                   6    
HELIX   12 AB3 CYS A  461  TRP A  475  1                                  15    
HELIX   13 AB4 ASN A  478  ARG A  482  5                                   5    
HELIX   14 AB5 THR A  484  GLY A  500  1                                  17    
SHEET    1 AA1 5 ILE A 205  LYS A 213  0                                        
SHEET    2 AA1 5 GLU A 218  TRP A 224 -1  O  ARG A 221   N  GLN A 208           
SHEET    3 AA1 5 GLU A 227  SER A 235 -1  O  GLU A 227   N  TRP A 224           
SHEET    4 AA1 5 THR A 274  ASP A 281 -1  O  LEU A 278   N  LYS A 232           
SHEET    5 AA1 5 PHE A 262  ASP A 269 -1  N  ALA A 264   O  VAL A 279           
SHEET    1 AA2 3 ILE A 329  ALA A 330  0                                        
SHEET    2 AA2 3 VAL A 356  ASP A 359 -1  O  VAL A 356   N  ALA A 330           
SHEET    3 AA2 3 THR A 364  ILE A 365 -1  O  THR A 364   N  ASP A 359           
SHEET    1 AA3 2 ILE A 339  VAL A 341  0                                        
SHEET    2 AA3 2 CYS A 347  ILE A 349 -1  O  CYS A 348   N  LEU A 340           
SITE     1 AC1 14 VAL A 219  ALA A 230  LYS A 232  GLU A 245                    
SITE     2 AC1 14 TYR A 249  LEU A 260  LEU A 278  SER A 280                    
SITE     3 AC1 14 ASP A 281  TYR A 282  HIS A 283  GLY A 286                    
SITE     4 AC1 14 LEU A 340  ASP A 351                                          
SITE     1 AC2  8 LYS A 337  ARG A 377  ASP A 435  HOH A 718                    
SITE     2 AC2  8 HOH A 733  HOH A 768  HOH A 813  HOH A 863                    
CRYST1   42.310   77.510   90.200  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      0.023635  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012902  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011086        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system