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Database: PDB
Entry: 5E8U
LinkDB: 5E8U
Original site: 5E8U 
HEADER    TRANSFERASE                             14-OCT-15   5E8U              
TITLE     TGF-BETA RECEPTOR TYPE 1 KINASE DOMAIN (T204D,I211V,Y249F,S280T,      
TITLE    2 Y282F,S287N,A350C,L352F)                                             
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,ALK5,SERINE/THREONINE-PROTEIN    
COMPND   7 KINASE RECEPTOR R4,SKR4,TGF-BETA TYPE I RECEPTOR,TRANSFORMING GROWTH 
COMPND   8 FACTOR-BETA RECEPTOR TYPE I,TBETAR-I;                                
COMPND   9 EC: 2.7.11.30;                                                       
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MUTATION: 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: PFASTBAC1                                 
KEYWDS    ALK5, KINASE DOMAIN, TRANSFERASE                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.SHERIFF                                                             
REVDAT   2   18-APR-18 5E8U    1       JRNL   REMARK                            
REVDAT   1   11-MAY-16 5E8U    0                                                
JRNL        AUTH   A.J.TEBBEN,M.RUZANOV,M.GAO,D.XIE,S.E.KIEFER,C.YAN,           
JRNL        AUTH 2 J.A.NEWITT,L.ZHANG,K.KIM,H.LU,L.M.KOPCHO,S.SHERIFF           
JRNL        TITL   CRYSTAL STRUCTURES OF APO AND INHIBITOR-BOUND TGF BETA R2    
JRNL        TITL 2 KINASE DOMAIN: INSIGHTS INTO TGF BETA R ISOFORM SELECTIVITY. 
JRNL        REF    ACTA CRYSTALLOGR D STRUCT     V.  72   658 2016              
JRNL        REF  2 BIOL                                                         
JRNL        REFN                   ISSN 2059-7983                               
JRNL        PMID   27139629                                                     
JRNL        DOI    10.1107/S2059798316003624                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.03 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER-TNT BUSTER 2.11.6                             
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) : 2.03                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 19117                          
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)  : 0.182                          
REMARK   3   R VALUE            (WORKING SET)  : 0.179                          
REMARK   3   FREE R VALUE                      : 0.223                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.070                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 970                            
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               : 10                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.03                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.14                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.15                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2615                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.1883                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2485                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.1855                   
REMARK   3   BIN FREE R VALUE                        : 0.2359                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.97                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 130                      
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            : 2433                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 18                                      
REMARK   3   SOLVENT ATOMS            : 125                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.27                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.48550                                             
REMARK   3    B22 (A**2) : -9.22190                                             
REMARK   3    B33 (A**2) : 10.70740                                             
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) : 0.216               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.207               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.168               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.197               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.166               
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      : 0.933                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.911                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 2500   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 3371   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 889    ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 56     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 365    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 2500   ; 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   : 322    ; 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   : 2946   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.01                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.33                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 16.44                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5E8U COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-OCT-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000214548.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-SEP-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CLSI                               
REMARK 200  BEAMLINE                       : 08ID-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.980                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-300                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19168                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.010                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.01                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
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: 3TZM                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.69                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 23%(W/V) PEG3350, 3%(V/V) GLCYEROL, PH   
REMARK 280  5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                
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       20.80000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       44.80000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.55000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       44.80000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       20.80000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.55000            
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 TOTAL BURIED SURFACE AREA: 570 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 14610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 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     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    CG   CD   CE   NZ                                   
REMARK 470     HIS A 371    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 391    CE   NZ                                             
REMARK 470     ASN A 456    CG   OD1  ND2                                       
REMARK 470     GLN A 459    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 498    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 499    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 502    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    GLN A 324       69.87   -103.98                                   
REMARK 500    ASP A 333       38.82   -153.73                                   
REMARK 500    ASP A 351       81.95     56.13                                   
REMARK 500    ASP A 386       16.21     58.33                                   
REMARK 500    ASP A 435       75.86   -119.50                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 424         0.06    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 603                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5E8S   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5E8T   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5E8V   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5E8W   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5E8X   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5E8Y   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5E8Z   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5E90   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5E91   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5E92   RELATED DB: PDB                                   
DBREF  5E8U A  200   503  UNP    P36897   TGFR1_HUMAN    200    503             
SEQADV 5E8U GLY A  197  UNP  P36897              EXPRESSION TAG                 
SEQADV 5E8U HIS A  198  UNP  P36897              EXPRESSION TAG                 
SEQADV 5E8U MET A  199  UNP  P36897              EXPRESSION TAG                 
SEQADV 5E8U ASP A  204  UNP  P36897    THR   204 ENGINEERED MUTATION            
SEQADV 5E8U VAL A  211  UNP  P36897    ILE   211 ENGINEERED MUTATION            
SEQADV 5E8U PHE A  249  UNP  P36897    TYR   249 ENGINEERED MUTATION            
SEQADV 5E8U THR A  280  UNP  P36897    SER   280 ENGINEERED MUTATION            
SEQADV 5E8U PHE A  282  UNP  P36897    TYR   282 ENGINEERED MUTATION            
SEQADV 5E8U ASN A  287  UNP  P36897    SER   287 ENGINEERED MUTATION            
SEQADV 5E8U CYS A  350  UNP  P36897    ALA   350 ENGINEERED MUTATION            
SEQADV 5E8U PHE A  352  UNP  P36897    LEU   352 ENGINEERED MUTATION            
SEQRES   1 A  307  GLY HIS MET THR ILE ALA ARG ASP ILE VAL LEU GLN GLU          
SEQRES   2 A  307  SER VAL GLY LYS GLY ARG PHE GLY GLU VAL TRP ARG GLY          
SEQRES   3 A  307  LYS TRP ARG GLY GLU GLU VAL ALA VAL LYS ILE PHE SER          
SEQRES   4 A  307  SER ARG GLU GLU ARG SER TRP PHE ARG GLU ALA GLU ILE          
SEQRES   5 A  307  PHE GLN THR VAL MET LEU ARG HIS GLU ASN ILE LEU GLY          
SEQRES   6 A  307  PHE ILE ALA ALA ASP ASN LYS ASP ASN GLY THR TRP THR          
SEQRES   7 A  307  GLN LEU TRP LEU VAL THR ASP PHE HIS GLU HIS GLY ASN          
SEQRES   8 A  307  LEU PHE ASP TYR LEU ASN ARG TYR THR VAL THR VAL GLU          
SEQRES   9 A  307  GLY MET ILE LYS LEU ALA LEU SER THR ALA SER GLY LEU          
SEQRES  10 A  307  ALA HIS LEU HIS MET GLU ILE VAL GLY THR GLN GLY LYS          
SEQRES  11 A  307  PRO ALA ILE ALA HIS ARG ASP LEU LYS SER LYS ASN ILE          
SEQRES  12 A  307  LEU VAL LYS LYS ASN GLY THR CYS CYS ILE CYS ASP PHE          
SEQRES  13 A  307  GLY LEU ALA VAL ARG HIS ASP SER ALA THR ASP THR ILE          
SEQRES  14 A  307  ASP ILE ALA PRO ASN HIS ARG VAL GLY THR LYS ARG TYR          
SEQRES  15 A  307  MET ALA PRO GLU VAL LEU ASP ASP SER ILE ASN MET LYS          
SEQRES  16 A  307  HIS PHE GLU SER PHE LYS ARG ALA ASP ILE TYR ALA MET          
SEQRES  17 A  307  GLY LEU VAL PHE TRP GLU ILE ALA ARG ARG CYS SER ILE          
SEQRES  18 A  307  GLY GLY ILE HIS GLU ASP TYR GLN LEU PRO TYR TYR ASP          
SEQRES  19 A  307  LEU VAL PRO SER ASP PRO SER VAL GLU GLU MET ARG LYS          
SEQRES  20 A  307  VAL VAL CYS GLU GLN LYS LEU ARG PRO ASN ILE PRO ASN          
SEQRES  21 A  307  ARG TRP GLN SER CYS GLU ALA LEU ARG VAL MET ALA LYS          
SEQRES  22 A  307  ILE MET ARG GLU CYS TRP TYR ALA ASN GLY ALA ALA ARG          
SEQRES  23 A  307  LEU THR ALA LEU ARG ILE LYS LYS THR LEU SER GLN LEU          
SEQRES  24 A  307  SER GLN GLN GLU GLY ILE LYS MET                              
HET    GOL  A 601       6                                                       
HET    GOL  A 602       6                                                       
HET    GOL  A 603       6                                                       
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  GOL    3(C3 H8 O3)                                                  
FORMUL   5  HOH   *125(H2 O)                                                    
HELIX    1 AA1 ILE A  201  ARG A  203  5                                   3    
HELIX    2 AA2 SER A  235  ARG A  237  5                                   3    
HELIX    3 AA3 GLU A  238  GLN A  250  1                                  13    
HELIX    4 AA4 ASN A  287  TYR A  295  1                                   9    
HELIX    5 AA5 THR A  298  MET A  318  1                                  21    
HELIX    6 AA6 LYS A  335  LYS A  337  5                                   3    
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  GLU A  473  1                                  13    
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  GLU A 209           
SHEET    3 AA1 5 GLU A 227  PHE A 234 -1  O  VAL A 229   N  GLY A 222           
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 ALA A 328  ALA A 330  0                                        
SHEET    2 AA2 3 VAL A 356  ASP A 359 -1  O  HIS A 358   N  ALA A 328           
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  5 ASP A 269  GLY A 271  THR A 272  TRP A 273                    
SITE     2 AC1  5 HOH A 716                                                     
SITE     1 AC2  6 ARG A 225  LYS A 449  ARG A 451  TYR A 476                    
SITE     2 AC2  6 ALA A 477  HOH A 765                                          
SITE     1 AC3  7 MET A 199  LEU A 207  ILE A 263  ASN A 270                    
SITE     2 AC3  7 GLN A 275  HOH A 703  HOH A 775                               
CRYST1   41.600   77.100   89.600  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      0.024038  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012970  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011161        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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