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Database: PDB
Entry: 1KTZ
LinkDB: 1KTZ
Original site: 1KTZ 
HEADER    CYTOKINE/CYTOKINE RECEPTOR              18-JAN-02   1KTZ              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN TGF-BETA TYPE II RECEPTOR              
TITLE    2 EXTRACELLULAR DOMAIN IN COMPLEX WITH TGF-BETA3                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRANSFORMING GROWTH FACTOR BETA 3;                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: TGF-BETA3;                                                  
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: TGF-BETA TYPE II RECEPTOR;                                 
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: EXTRACELLULAR DOMAIN;                                      
COMPND  10 SYNONYM: TBR-2;                                                      
COMPND  11 EC: 2.7.1.37;                                                        
COMPND  12 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: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CYTOKINE-RECEPTOR COMPLEX, CYTOKINE/CYTOKINE RECEPTOR                 
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.J.HART,S.DEEP,A.B.TAYLOR,Z.SHU,C.S.HINCK,A.P.HINCK                  
REVDAT   3   24-FEB-09 1KTZ    1       VERSN                                    
REVDAT   2   01-APR-03 1KTZ    1       JRNL                                     
REVDAT   1   27-FEB-02 1KTZ    0                                                
JRNL        AUTH   P.J.HART,S.DEEP,A.B.TAYLOR,Z.SHU,C.S.HINCK,                  
JRNL        AUTH 2 A.P.HINCK                                                    
JRNL        TITL   CRYSTAL STRUCTURE OF THE HUMAN TBETAR2                       
JRNL        TITL 2 ECTODOMAIN--TGF-BETA3 COMPLEX.                               
JRNL        REF    NAT.STRUCT.BIOL.              V.   9   203 2002              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   11850637                                                     
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.61                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 3888970.260                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 28916                          
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 SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2002                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.15                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.23                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2632                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2650                       
REMARK   3   BIN FREE R VALUE                    : 0.2880                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 7.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 200                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.020                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1493                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 163                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 29.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.25000                                             
REMARK   3    B22 (A**2) : -2.25000                                             
REMARK   3    B33 (A**2) : 4.51000                                              
REMARK   3    B12 (A**2) : 0.34000                                              
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) : 0.25                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.21                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 26.00                           
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.28                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.24                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.014                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.90                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.74                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.560 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.480 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.970 ; 3.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 5.380 ; 4.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.36                                                 
REMARK   3   BSOL        : 61.04                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1KTZ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JAN-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB015342.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-NOV-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X8C                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29006                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 26.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : 0.05800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.23                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.53300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 75.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROP VAPOR DIFFUSION USING       
REMARK 280  A WELL SOLUTION CONTAINING 20% (V/V) 2-METHYL-2,4-PENTANEDIOL       
REMARK 280  AND 0.1 M CITRATE PH 4.0                                            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z                                               
REMARK 290       6555   -X,-X+Y,-Z                                              
REMARK 290       7555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       8555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       9555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290      10555   Y+2/3,X+1/3,-Z+1/3                                      
REMARK 290      11555   X-Y+2/3,-Y+1/3,-Z+1/3                                   
REMARK 290      12555   -X+2/3,-X+Y+1/3,-Z+1/3                                  
REMARK 290      13555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290      14555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290      15555   -X+Y+1/3,-X+2/3,Z+2/3                                   
REMARK 290      16555   Y+1/3,X+2/3,-Z+2/3                                      
REMARK 290      17555   X-Y+1/3,-Y+2/3,-Z+2/3                                   
REMARK 290      18555   -X+1/3,-X+Y+2/3,-Z+2/3                                  
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000       57.20500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       33.02732            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       69.81000            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000       57.20500            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       33.02732            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       69.81000            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000       57.20500            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       33.02732            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       69.81000            
REMARK 290   SMTRY1  10 -0.500000  0.866025  0.000000       57.20500            
REMARK 290   SMTRY2  10  0.866025  0.500000  0.000000       33.02732            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       69.81000            
REMARK 290   SMTRY1  11  1.000000  0.000000  0.000000       57.20500            
REMARK 290   SMTRY2  11  0.000000 -1.000000  0.000000       33.02732            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       69.81000            
REMARK 290   SMTRY1  12 -0.500000 -0.866025  0.000000       57.20500            
REMARK 290   SMTRY2  12 -0.866025  0.500000  0.000000       33.02732            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       69.81000            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       66.05464            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000      139.62000            
REMARK 290   SMTRY1  14 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  14  0.866025 -0.500000  0.000000       66.05464            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000      139.62000            
REMARK 290   SMTRY1  15 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  15 -0.866025 -0.500000  0.000000       66.05464            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000      139.62000            
REMARK 290   SMTRY1  16 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  16  0.866025  0.500000  0.000000       66.05464            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      139.62000            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  17  0.000000 -1.000000  0.000000       66.05464            
REMARK 290   SMTRY3  17  0.000000  0.000000 -1.000000      139.62000            
REMARK 290   SMTRY1  18 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  18 -0.866025  0.500000  0.000000       66.05464            
REMARK 290   SMTRY3  18  0.000000  0.000000 -1.000000      139.62000            
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 300 REMARK: THE SECOND PART OF THE BIOLOGICAL ASSEMBLY IS GENERATED      
REMARK 300 BY THE CRYSTALLOGRAPHIC SYMMETRY OPERATOR Y, X, -Z AND A             
REMARK 300 TRANSLATION OF ONE UNIT CELL LENGTH ALONG THE Z-AXIS.                
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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 350   BIOMT1   2 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      209.43000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A     1                                                      
REMARK 465     LEU A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     ASN A     5                                                      
REMARK 465     TYR A     6                                                      
REMARK 465     CYS A     7                                                      
REMARK 465     PHE A     8                                                      
REMARK 465     ARG A     9                                                      
REMARK 465     ASN A    10                                                      
REMARK 465     LEU A    11                                                      
REMARK 465     GLU A    12                                                      
REMARK 465     ASP A    55                                                      
REMARK 465     THR A    56                                                      
REMARK 465     THR A    57                                                      
REMARK 465     HIS A    58                                                      
REMARK 465     SER A    59                                                      
REMARK 465     THR A    60                                                      
REMARK 465     VAL A    61                                                      
REMARK 465     LEU A    62                                                      
REMARK 465     GLY A    63                                                      
REMARK 465     LEU A    64                                                      
REMARK 465     TYR A    65                                                      
REMARK 465     ASN A    66                                                      
REMARK 465     THR A    67                                                      
REMARK 465     LEU A    68                                                      
REMARK 465     ASN A    69                                                      
REMARK 465     PRO A    70                                                      
REMARK 465     GLU A    71                                                      
REMARK 465     ALA A    72                                                      
REMARK 465     VAL B    15                                                      
REMARK 465     THR B    16                                                      
REMARK 465     ASP B    17                                                      
REMARK 465     ASN B    18                                                      
REMARK 465     ASN B    19                                                      
REMARK 465     GLY B    20                                                      
REMARK 465     ALA B    21                                                      
REMARK 465     VAL B    22                                                      
REMARK 465     LYS B    23                                                      
REMARK 465     PHE B    24                                                      
REMARK 465     ASN B   131                                                      
REMARK 465     THR B   132                                                      
REMARK 465     SER B   133                                                      
REMARK 465     ASN B   134                                                      
REMARK 465     PRO B   135                                                      
REMARK 465     ASP B   136                                                      
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    ASN A  42      175.06     62.20                                   
REMARK 500    SER A  53       51.44   -119.48                                   
REMARK 500    GLN A  81      -76.05   -114.05                                   
REMARK 500    ASP B  32     -146.68     55.23                                   
REMARK 500    ASN B  68     -168.45   -112.51                                   
REMARK 500    SER B 127      179.59     61.13                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1KTZ A    1   112  UNP    P10600   TGFB3_HUMAN    301    412             
DBREF  1KTZ B   15   136  UNP    P37173   TGFR2_HUMAN     38    159             
SEQRES   1 A  112  ALA LEU ASP THR ASN TYR CYS PHE ARG ASN LEU GLU GLU          
SEQRES   2 A  112  ASN CYS CYS VAL ARG PRO LEU TYR ILE ASP PHE ARG GLN          
SEQRES   3 A  112  ASP LEU GLY TRP LYS TRP VAL HIS GLU PRO LYS GLY TYR          
SEQRES   4 A  112  TYR ALA ASN PHE CYS SER GLY PRO CYS PRO TYR LEU ARG          
SEQRES   5 A  112  SER ALA ASP THR THR HIS SER THR VAL LEU GLY LEU TYR          
SEQRES   6 A  112  ASN THR LEU ASN PRO GLU ALA SER ALA SER PRO CYS CYS          
SEQRES   7 A  112  VAL PRO GLN ASP LEU GLU PRO LEU THR ILE LEU TYR TYR          
SEQRES   8 A  112  VAL GLY ARG THR PRO LYS VAL GLU GLN LEU SER ASN MET          
SEQRES   9 A  112  VAL VAL LYS SER CYS LYS CYS SER                              
SEQRES   1 B  122  VAL THR ASP ASN ASN GLY ALA VAL LYS PHE PRO GLN LEU          
SEQRES   2 B  122  CYS LYS PHE CYS ASP VAL ARG PHE SER THR CYS ASP ASN          
SEQRES   3 B  122  GLN LYS SER CYS MET SER ASN CYS SER ILE THR SER ILE          
SEQRES   4 B  122  CYS GLU LYS PRO GLN GLU VAL CYS VAL ALA VAL TRP ARG          
SEQRES   5 B  122  LYS ASN ASP GLU ASN ILE THR LEU GLU THR VAL CYS HIS          
SEQRES   6 B  122  ASP PRO LYS LEU PRO TYR HIS ASP PHE ILE LEU GLU ASP          
SEQRES   7 B  122  ALA ALA SER PRO LYS CYS ILE MET LYS GLU LYS LYS LYS          
SEQRES   8 B  122  PRO GLY GLU THR PHE PHE MET CYS SER CYS SER SER ASP          
SEQRES   9 B  122  GLU CYS ASN ASP ASN ILE ILE PHE SER GLU GLU TYR ASN          
SEQRES  10 B  122  THR SER ASN PRO ASP                                          
FORMUL   3  HOH   *163(H2 O)                                                    
HELIX    1   1 PHE A   24  GLY A   29  1                                   6    
HELIX    2   2 GLU B  119  ASN B  121  5                                   3    
SHEET    1   A 2 CYS A  16  ARG A  18  0                                        
SHEET    2   A 2 PHE A  43  SER A  45 -1  O  PHE A  43   N  ARG A  18           
SHEET    1   B 2 TYR A  21  ASP A  23  0                                        
SHEET    2   B 2 GLY A  38  TYR A  40 -1  O  TYR A  39   N  ILE A  22           
SHEET    1   C 3 THR A  95  VAL A 106  0                                        
SHEET    2   C 3 LEU A  83  VAL A  92 -1  N  GLU A  84   O  VAL A 105           
SHEET    3   C 3 VAL A  33  GLU A  35 -1  N  GLU A  35   O  LEU A  89           
SHEET    1   D 4 THR A  95  VAL A 106  0                                        
SHEET    2   D 4 LEU A  83  VAL A  92 -1  N  GLU A  84   O  VAL A 105           
SHEET    3   D 4 THR B  51  ILE B  53  1  O  ILE B  53   N  TYR A  91           
SHEET    4   D 4 LEU B  27  LYS B  29 -1  N  CYS B  28   O  SER B  52           
SHEET    1   E 2 CYS A  77  PRO A  80  0                                        
SHEET    2   E 2 CYS A 109  SER A 112 -1  O  SER A 112   N  CYS A  77           
SHEET    1   F 7 ASP B  32  PHE B  35  0                                        
SHEET    2   F 7 ILE B  72  HIS B  79 -1  O  LEU B  74   N  ARG B  34           
SHEET    3   F 7 VAL B  60  LYS B  67 -1  N  VAL B  64   O  GLU B  75           
SHEET    4   F 7 THR B 109  CYS B 115 -1  O  PHE B 111   N  TRP B  65           
SHEET    5   F 7 CYS B  98  LYS B 103 -1  N  LYS B 103   O  PHE B 110           
SHEET    6   F 7 ASN B 123  PHE B 126  1  O  ILE B 125   N  CYS B  98           
SHEET    7   F 7 SER B  43  MET B  45 -1  N  CYS B  44   O  ILE B 124           
SSBOND   1 CYS A   15    CYS A   78                          1555   1555  2.04  
SSBOND   2 CYS A   44    CYS A  109                          1555   1555  2.03  
SSBOND   3 CYS A   48    CYS A  111                          1555   1555  2.04  
SSBOND   4 CYS B   28    CYS B   61                          1555   1555  2.05  
SSBOND   5 CYS B   31    CYS B   48                          1555   1555  2.05  
SSBOND   6 CYS B   38    CYS B   44                          1555   1555  2.05  
SSBOND   7 CYS B   54    CYS B   78                          1555   1555  2.08  
SSBOND   8 CYS B   98    CYS B  113                          1555   1555  2.01  
SSBOND   9 CYS B  115    CYS B  120                          1555   1555  2.03  
CISPEP   1 GLU A   35    PRO A   36          0        -0.86                     
CRYST1  114.410  114.410  209.430  90.00  90.00 120.00 H 3 2        18          
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      0.008740  0.005046  0.000000        0.00000                         
SCALE2      0.000000  0.010092  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004775        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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