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Database: PDB
Entry: 3TZM
LinkDB: 3TZM
Original site: 3TZM 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       27-SEP-11   3TZM              
TITLE     TGF-BETA RECEPTOR TYPE 1 IN COMPLEX WITH SB431542                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TGF-BETA RECEPTOR TYPE-1;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: KINASE DOMAIN, UNP RESIDUES 200-503;                       
COMPND   5 SYNONYM: TGFR-1, ACTIVIN A RECEPTOR TYPE II-LIKE PROTEIN KINASE OF   
COMPND   6 53KD, ACTIVIN RECEPTOR-LIKE KINASE 5, ALK-5, ALK5, SERINE/THREONINE- 
COMPND   7 PROTEIN KINASE RECEPTOR R4, SKR4, TGF-BETA TYPE I RECEPTOR,          
COMPND   8 TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I, TGF-BETA RECEPTOR   
COMPND   9 TYPE I, TBETAR-I;                                                    
COMPND  10 EC: 2.7.11.30;                                                       
COMPND  11 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;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC                                  
KEYWDS    ALK5, SB431542, KINASE DOMAIN, TRANSFERASE-TRANSFERASE INHIBITOR      
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.A.OGUNJIMI,E.ZEQIRAJ,D.F.CECCARELLI,F.SICHERI                       
REVDAT   1   23-MAY-12 3TZM    0                                                
JRNL        AUTH   A.A.OGUNJIMI,E.ZEQIRAJ,D.F.CECCARELLI,F.SICHERI,J.L.WRANA,   
JRNL        AUTH 2 L.DAVID                                                      
JRNL        TITL   STRUCTURAL BASIS FOR SPECIFICITY OF TGFBETA FAMILY RECEPTOR  
JRNL        TITL 2 SMALL MOLECULE INHIBITORS                                    
JRNL        REF    CELL SIGNAL                   V.  24   476 2012              
JRNL        REFN                                                                
JRNL        PMID   21983015                                                     
JRNL        DOI    10.1016/J.CELLSIG.2011.09.027                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.45                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 30296                          
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) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.205                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1616                            
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) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.75                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2255                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.37                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2170                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 129                          
REMARK   3   BIN FREE R VALUE                    : 0.2490                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2368                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 29                                      
REMARK   3   SOLVENT ATOMS            : 158                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.32                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.87000                                             
REMARK   3    B22 (A**2) : 0.82000                                              
REMARK   3    B33 (A**2) : 0.05000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.104         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.060         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.948         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2454 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3316 ; 1.232 ; 1.957       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   295 ; 5.876 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   112 ;31.326 ;22.768       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   439 ;14.135 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    23 ;13.260 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   358 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1845 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  1465 ; 0.955 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2359 ; 1.708 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   989 ; 2.621 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   956 ; 4.143 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2454 ; 1.224 ; 3.000       
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  : NULL                                       
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                                                           
REMARK   4                                                                      
REMARK   4 3TZM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-OCT-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB068119.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-JUN-07                          
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                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : CRYO-SI                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31955                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.38300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 1PY5                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.73                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM IMIDAZOLE  10% PEG 8000, PH       
REMARK 280  8.0, 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       20.88550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.03500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.86300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.03500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       20.88550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.86300            
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     GLY A   195                                                      
REMARK 465     ALA A   196                                                      
REMARK 465     MET A   197                                                      
REMARK 465     GLY A   198                                                      
REMARK 465     SER A   199                                                      
REMARK 465     ASN A   370                                                      
REMARK 465     HIS A   371                                                      
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 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      -84.89   -101.77                                   
REMARK 500    GLN A 324       64.23   -106.65                                   
REMARK 500    ARG A 332       -5.96     80.10                                   
REMARK 500    ASP A 333       44.67   -152.68                                   
REMARK 500    ALA A 350     -169.81   -122.58                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL A 252        24.8      L          L   OUTSIDE RANGE           
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 085 A 1                   
DBREF  3TZM A  200   503  UNP    P36897   TGFR1_HUMAN    200    503             
SEQADV 3TZM GLY A  195  UNP  P36897              EXPRESSION TAG                 
SEQADV 3TZM ALA A  196  UNP  P36897              EXPRESSION TAG                 
SEQADV 3TZM MET A  197  UNP  P36897              EXPRESSION TAG                 
SEQADV 3TZM GLY A  198  UNP  P36897              EXPRESSION TAG                 
SEQADV 3TZM SER A  199  UNP  P36897              EXPRESSION TAG                 
SEQRES   1 A  309  GLY ALA MET GLY SER THR ILE ALA ARG THR ILE VAL LEU          
SEQRES   2 A  309  GLN GLU SER ILE GLY LYS GLY ARG PHE GLY GLU VAL TRP          
SEQRES   3 A  309  ARG GLY LYS TRP ARG GLY GLU GLU VAL ALA VAL LYS ILE          
SEQRES   4 A  309  PHE SER SER ARG GLU GLU ARG SER TRP PHE ARG GLU ALA          
SEQRES   5 A  309  GLU ILE TYR GLN THR VAL MET LEU ARG HIS GLU ASN ILE          
SEQRES   6 A  309  LEU GLY PHE ILE ALA ALA ASP ASN LYS ASP ASN GLY THR          
SEQRES   7 A  309  TRP THR GLN LEU TRP LEU VAL SER ASP TYR HIS GLU HIS          
SEQRES   8 A  309  GLY SER LEU PHE ASP TYR LEU ASN ARG TYR THR VAL THR          
SEQRES   9 A  309  VAL GLU GLY MET ILE LYS LEU ALA LEU SER THR ALA SER          
SEQRES  10 A  309  GLY LEU ALA HIS LEU HIS MET GLU ILE VAL GLY THR GLN          
SEQRES  11 A  309  GLY LYS PRO ALA ILE ALA HIS ARG ASP LEU LYS SER LYS          
SEQRES  12 A  309  ASN ILE LEU VAL LYS LYS ASN GLY THR CYS CYS ILE ALA          
SEQRES  13 A  309  ASP LEU GLY LEU ALA VAL ARG HIS ASP SER ALA THR ASP          
SEQRES  14 A  309  THR ILE ASP ILE ALA PRO ASN HIS ARG VAL GLY THR LYS          
SEQRES  15 A  309  ARG TYR MET ALA PRO GLU VAL LEU ASP ASP SER ILE ASN          
SEQRES  16 A  309  MET LYS HIS PHE GLU SER PHE LYS ARG ALA ASP ILE TYR          
SEQRES  17 A  309  ALA MET GLY LEU VAL PHE TRP GLU ILE ALA ARG ARG CYS          
SEQRES  18 A  309  SER ILE GLY GLY ILE HIS GLU ASP TYR GLN LEU PRO TYR          
SEQRES  19 A  309  TYR ASP LEU VAL PRO SER ASP PRO SER VAL GLU GLU MET          
SEQRES  20 A  309  ARG LYS VAL VAL CYS GLU GLN LYS LEU ARG PRO ASN ILE          
SEQRES  21 A  309  PRO ASN ARG TRP GLN SER CYS GLU ALA LEU ARG VAL MET          
SEQRES  22 A  309  ALA LYS ILE MET ARG GLU CYS TRP TYR ALA ASN GLY ALA          
SEQRES  23 A  309  ALA ARG LEU THR ALA LEU ARG ILE LYS LYS THR LEU SER          
SEQRES  24 A  309  GLN LEU SER GLN GLN GLU GLY ILE LYS MET                      
HET    085  A   1      29                                                       
HETNAM     085 4-[5-(1,3-BENZODIOXOL-5-YL)-4-(PYRIDIN-2-YL)-1H-                 
HETNAM   2 085  IMIDAZOL-2-YL]BENZAMIDE                                         
HETSYN     085 SB431542                                                         
FORMUL   2  085    C22 H16 N4 O3                                                
FORMUL   3  HOH   *158(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 LYS A  335  LYS A  337  5                                   3    
HELIX    7   7 THR A  375  MET A  379  5                                   5    
HELIX    8   8 ALA A  380  ASP A  385  1                                   6    
HELIX    9   9 HIS A  392  ARG A  414  1                                  23    
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 ASN A  478  ARG A  482  5                                   5    
HELIX   14  14 THR A  484  SER A  496  1                                  13    
SHEET    1   A 5 ILE A 205  LYS A 213  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  VAL A 229   N  GLY A 222           
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  LYS A 268   O  GLN A 275           
SHEET    1   B 3 ILE A 329  ALA A 330  0                                        
SHEET    2   B 3 VAL A 356  ASP A 359 -1  O  VAL A 356   N  ALA A 330           
SHEET    3   B 3 THR A 364  ILE A 365 -1  O  THR A 364   N  ASP A 359           
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 17 HOH A   2  HOH A  46  HOH A  47  HOH A 153                    
SITE     2 AC1 17 ILE A 211  GLY A 214  ALA A 230  LYS A 232                    
SITE     3 AC1 17 LEU A 278  SER A 280  ASP A 281  TYR A 282                    
SITE     4 AC1 17 HIS A 283  LYS A 335  LYS A 337  LEU A 340                    
SITE     5 AC1 17 ASP A 351                                                     
CRYST1   41.771   77.726   90.070  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      0.023940  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012866  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011102        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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