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Database: PDB
Entry: 2WOU
LinkDB: 2WOU
Original site: 2WOU 
HEADER    TRANSFERASE                             28-JUL-09   2WOU              
TITLE     ALK5 IN COMPLEX WITH 4-((4-((2,6-DIMETHYL-3-PYRIDYL)OXY)-2-PYRIDYL)   
TITLE    2 AMINO)BENZENESULFONAMIDE                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TGF-BETA RECEPTOR TYPE-1;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 200-503;                        
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_TAXID: 7108;                                       
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    TRANSFERASE, SERINE/THREONINE-PROTEIN KINASE, ALK, ATP-BINDING,       
KEYWDS   2 KINASE INHIBITOR, NUCLEOTIDE-BINDING, TGF BETA TYPE I RECEPTOR       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.E.DEBRECZENI,R.A.NORMAN,F.W.GOLDBERG,R.A.WARD,R.FINLAY,S.J.POWELL,  
AUTHOR   2 N.J.ROBERTS,A.P.DISHINGTON,H.J.GINGELL,K.F.WICKSON,A.L.ROBERTS       
REVDAT   5   08-MAY-19 2WOU    1       REMARK                                   
REVDAT   4   04-APR-18 2WOU    1       REMARK                                   
REVDAT   3   23-NOV-11 2WOU    1       AUTHOR JRNL                              
REVDAT   2   13-JUL-11 2WOU    1       VERSN                                    
REVDAT   1   22-SEP-09 2WOU    0                                                
JRNL        AUTH   F.W.GOLDBERG,R.A.WARD,S.J.POWELL,J.E.DEBRECZENI,R.A.NORMAN,  
JRNL        AUTH 2 N.J.ROBERTS,A.P.DISHINGTON,H.J.GINGELL,K.F.WICKSON,          
JRNL        AUTH 3 A.L.ROBERTS                                                  
JRNL        TITL   RAPID GENERATION OF A HIGH QUALITY LEAD FOR TRANSFORMING     
JRNL        TITL 2 GROWTH FACTOR-BETA (TGF-BETA) TYPE I RECEPTOR (ALK5).        
JRNL        REF    J.MED.CHEM.                   V.  52  7901 2009              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   19736928                                                     
JRNL        DOI    10.1021/JM900807W                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0055                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 12761                          
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) : 0.229                           
REMARK   3   R VALUE            (WORKING SET) : 0.226                           
REMARK   3   FREE R VALUE                     : 0.302                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 654                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 885                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.60                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2110                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 49                           
REMARK   3   BIN FREE R VALUE                    : 0.2750                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2339                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 135                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 25.95                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.45                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.74000                                             
REMARK   3    B22 (A**2) : 0.21000                                              
REMARK   3    B33 (A**2) : 1.52000                                              
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.515         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.315         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.192         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.417        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.922                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.872                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2438 ; 0.009 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  1655 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3299 ; 1.135 ; 1.946       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4002 ; 0.812 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   299 ; 5.851 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   108 ;33.567 ;23.056       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   416 ;13.811 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;13.719 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   359 ; 0.065 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2751 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   527 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1486 ; 0.674 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   612 ; 0.110 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2383 ; 1.146 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   952 ; 0.604 ; 2.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   916 ; 0.971 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   198        A   284                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.0242  15.7778   2.9360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0261 T22:   0.0831                                     
REMARK   3      T33:   0.0178 T12:   0.0038                                     
REMARK   3      T13:   0.0104 T23:   0.0248                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9082 L22:   1.2553                                     
REMARK   3      L33:   1.3137 L12:  -0.2650                                     
REMARK   3      L13:   0.5427 L23:  -0.1624                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0228 S12:  -0.0402 S13:   0.0567                       
REMARK   3      S21:  -0.0250 S22:  -0.0069 S23:   0.0034                       
REMARK   3      S31:   0.0158 S32:  -0.0599 S33:   0.0296                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   285        A   500                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.9790  -5.0829  16.6135              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0306 T22:   0.0340                                     
REMARK   3      T33:   0.0660 T12:   0.0127                                     
REMARK   3      T13:   0.0133 T23:   0.0425                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6731 L22:   1.4983                                     
REMARK   3      L33:   1.9056 L12:   0.3984                                     
REMARK   3      L13:  -0.5380 L23:  -0.8238                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0498 S12:  -0.0498 S13:  -0.1847                       
REMARK   3      S21:  -0.0419 S22:   0.0080 S23:  -0.0361                       
REMARK   3      S31:   0.1197 S32:   0.0501 S33:   0.0418                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. U VALUES RESIDUAL ONLY.                                  
REMARK   4                                                                      
REMARK   4 2WOU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-JUL-09.                  
REMARK 100 THE DEPOSITION ID IS D_1290040589.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-OCT-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E                        
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK                             
REMARK 200  DATA SCALING SOFTWARE          : D*TREK                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15281                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 3.740                              
REMARK 200  R MERGE                    (I) : 0.17000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.74                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SITTING DROP METHOD. DROPS PROTEIN       
REMARK 280  -PRECIPITANT 1-1, PROTEIN: 10MG/ML ALK5, PRECIPITANT: 20-30%        
REMARK 280  PEG8K, 100 MM PCTP BUFFER PH 8.5-9.2, 0.2 M NAAC, VAPOR             
REMARK 280  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       20.94050            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.19350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.52100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.19350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       20.94050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.52100            
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     GLN A   497                                                      
REMARK 465     GLN A   498                                                      
REMARK 465     GLU A   499                                                      
REMARK 465     GLY A   500                                                      
REMARK 465     ILE A   501                                                      
REMARK 465     LYS A   502                                                      
REMARK 465     MET A   503                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 213    CD   CE   NZ                                        
REMARK 470     LYS A 223    CE   NZ                                             
REMARK 470     ARG A 240    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A 343    CG   CD   CE   NZ                                   
REMARK 470     ASP A 363    CG   OD1  OD2                                       
REMARK 470     ASN A 370    CG   OD1  ND2                                       
REMARK 470     HIS A 371    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP A 386    CG   OD1  OD2                                       
REMARK 470     LYS A 391    CG   CD   CE   NZ                                   
REMARK 470     GLU A 439    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 456    CG   OD1  ND2                                       
REMARK 470     LYS A 469    CG   CD   CE   NZ                                   
REMARK 470     ARG A 472    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A 487    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 490    CD   CE   NZ                                        
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    ILE A 201      -92.55   -114.95                                   
REMARK 500    ARG A 332       -3.97     81.95                                   
REMARK 500    ASP A 333       41.72   -147.95                                   
REMARK 500    LYS A 391       31.98    -97.25                                   
REMARK 500    ARG A 457      -39.00    -38.15                                   
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 EDO A 1497                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZZF A 1500                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1PY5   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF TGF-BETA RECEPTOR I KINASE WITHINHIBITOR        
REMARK 900 RELATED ID: 1IAS   RELATED DB: PDB                                   
REMARK 900 CYTOPLASMIC DOMAIN OF UNPHOSPHORYLATED TYPE I TGF-BETARECEPTOR       
REMARK 900 CRYSTALLIZED WITHOUT FKBP12                                          
REMARK 900 RELATED ID: 1B6C   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CYTOPLASMIC DOMAIN OF THE TYPE I TGF-BETA   
REMARK 900 RECEPTOR IN COMPLEX WITH FKBP12                                      
REMARK 900 RELATED ID: 1VJY   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A NAPHTHYRIDINE INHIBITOR OF HUMAN TGF-BETA     
REMARK 900 TYPE I RECEPTOR                                                      
REMARK 900 RELATED ID: 1RW8   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF TGF-BETA RECEPTOR I KINASE WITH ATPSITE         
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 2WOT   RELATED DB: PDB                                   
REMARK 900 ALK5 IN COMPLEX WITH 4-((5,6-DIMETHYL-2 -(2-PYRIDYL)-3-PYRIDYL)OXY)- 
REMARK 900 N-(3,4,5- TRIMETHOXYPHENYL)PYRIDIN-2-AMINE                           
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 G198 AND G199 ARE CLONING ARTIFACTS.                                 
DBREF  2WOU A  198   199  PDB    2WOU     2WOU           198    199             
DBREF  2WOU A  200   503  UNP    P36897   TGFR1_HUMAN    200    503             
SEQRES   1 A  306  GLY GLY THR ILE ALA ARG THR ILE VAL LEU GLN GLU SER          
SEQRES   2 A  306  ILE GLY LYS GLY ARG PHE GLY GLU VAL TRP ARG GLY LYS          
SEQRES   3 A  306  TRP ARG GLY GLU GLU VAL ALA VAL LYS ILE PHE SER SER          
SEQRES   4 A  306  ARG GLU GLU ARG SER TRP PHE ARG GLU ALA GLU ILE TYR          
SEQRES   5 A  306  GLN THR VAL MET LEU ARG HIS GLU ASN ILE LEU GLY PHE          
SEQRES   6 A  306  ILE ALA ALA ASP ASN LYS ASP ASN GLY THR TRP THR GLN          
SEQRES   7 A  306  LEU TRP LEU VAL SER ASP TYR HIS GLU HIS GLY SER LEU          
SEQRES   8 A  306  PHE ASP TYR LEU ASN ARG TYR THR VAL THR VAL GLU GLY          
SEQRES   9 A  306  MET ILE LYS LEU ALA LEU SER THR ALA SER GLY LEU ALA          
SEQRES  10 A  306  HIS LEU HIS MET GLU ILE VAL GLY THR GLN GLY LYS PRO          
SEQRES  11 A  306  ALA ILE ALA HIS ARG ASP LEU LYS SER LYS ASN ILE LEU          
SEQRES  12 A  306  VAL LYS LYS ASN GLY THR CYS CYS ILE ALA ASP LEU GLY          
SEQRES  13 A  306  LEU ALA VAL ARG HIS ASP SER ALA THR ASP THR ILE ASP          
SEQRES  14 A  306  ILE ALA PRO ASN HIS ARG VAL GLY THR LYS ARG TYR MET          
SEQRES  15 A  306  ALA PRO GLU VAL LEU ASP ASP SER ILE ASN MET LYS HIS          
SEQRES  16 A  306  PHE GLU SER PHE LYS ARG ALA ASP ILE TYR ALA MET GLY          
SEQRES  17 A  306  LEU VAL PHE TRP GLU ILE ALA ARG ARG CYS SER ILE GLY          
SEQRES  18 A  306  GLY ILE HIS GLU ASP TYR GLN LEU PRO TYR TYR ASP LEU          
SEQRES  19 A  306  VAL PRO SER ASP PRO SER VAL GLU GLU MET ARG LYS VAL          
SEQRES  20 A  306  VAL CYS GLU GLN LYS LEU ARG PRO ASN ILE PRO ASN ARG          
SEQRES  21 A  306  TRP GLN SER CYS GLU ALA LEU ARG VAL MET ALA LYS ILE          
SEQRES  22 A  306  MET ARG GLU CYS TRP TYR ALA ASN GLY ALA ALA ARG LEU          
SEQRES  23 A  306  THR ALA LEU ARG ILE LYS LYS THR LEU SER GLN LEU SER          
SEQRES  24 A  306  GLN GLN GLU GLY ILE LYS MET                                  
HET    EDO  A1497       4                                                       
HET    ZZF  A1500      26                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     ZZF 4-({4-[(2,6-DIMETHYLPYRIDIN-3-YL)OXY]PYRIDIN-2-                  
HETNAM   2 ZZF  YL}AMINO)BENZENESULFONAMIDE                                     
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  EDO    C2 H6 O2                                                     
FORMUL   3  ZZF    C18 H18 N4 O3 S                                              
FORMUL   4  HOH   *135(H2 O)                                                    
HELIX    1   1 ILE A  201  ARG A  203  5                                   3    
HELIX    2   2 GLU A  238  GLN A  250  1                                  13    
HELIX    3   3 SER A  287  TYR A  295  1                                   9    
HELIX    4   4 MET A  302  SER A  311  1                                  10    
HELIX    5   5 LEU A  313  MET A  318  1                                   6    
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  MET A  404  1                                  13    
HELIX    9   9 LEU A  406  ARG A  413  1                                   8    
HELIX   10  10 SER A  437  CYS A  446  1                                  10    
HELIX   11  11 PRO A  455  SER A  460  5                                   6    
HELIX   12  12 CYS A  461  TRP A  475  1                                  15    
HELIX   13  13 THR A  484  SER A  496  1                                  13    
SHEET    1  AA 5 ILE A 205  SER A 210  0                                        
SHEET    2  AA 5 VAL A 219  TRP A 224 -1  O  ARG A 221   N  GLN A 208           
SHEET    3  AA 5 VAL A 229  SER A 235 -1  O  VAL A 231   N  TRP A 220           
SHEET    4  AA 5 THR A 274  ASP A 281 -1  O  LEU A 276   N  PHE A 234           
SHEET    5  AA 5 ALA A 264  ASP A 269 -1  O  ALA A 264   N  VAL A 279           
SHEET    1  AB 3 ILE A 329  ALA A 330  0                                        
SHEET    2  AB 3 VAL A 356  ASP A 359 -1  O  VAL A 356   N  ALA A 330           
SHEET    3  AB 3 THR A 364  ILE A 365 -1  O  THR A 364   N  ASP A 359           
SHEET    1  AC 2 ILE A 339  VAL A 341  0                                        
SHEET    2  AC 2 CYS A 347  ILE A 349 -1  O  CYS A 348   N  LEU A 340           
SITE     1 AC1  4 MET A 253  ASP A 269  THR A 272  TRP A 273                    
SITE     1 AC2 17 ILE A 211  VAL A 219  ALA A 230  LEU A 260                    
SITE     2 AC2 17 LEU A 278  SER A 280  ASP A 281  TYR A 282                    
SITE     3 AC2 17 HIS A 283  GLY A 286  ASP A 290  GLY A 322                    
SITE     4 AC2 17 THR A 323  LEU A 340  ASP A 351  HOH A2024                    
SITE     5 AC2 17 HOH A2135                                                     
CRYST1   41.881   77.042   90.387  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      0.023877  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012980  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011064        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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