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Database: PDB
Entry: 1B6C
LinkDB: 1B6C
Original site: 1B6C 
HEADER    COMPLEX (ISOMERASE/PROTEIN KINASE)      13-JAN-99   1B6C              
TITLE     CRYSTAL STRUCTURE OF THE CYTOPLASMIC DOMAIN OF THE TYPE I             
TITLE    2 TGF-BETA RECEPTOR IN COMPLEX WITH FKBP12                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FK506-BINDING PROTEIN;                                     
COMPND   3 CHAIN: A, C, E, G;                                                   
COMPND   4 SYNONYM: FKBP12;                                                     
COMPND   5 EC: 5.2.1.8;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: TGF-B SUPERFAMILY RECEPTOR TYPE I;                         
COMPND   9 CHAIN: B, D, F, H;                                                   
COMPND  10 FRAGMENT: CYTOPLASMIC PORTION;                                       
COMPND  11 SYNONYM: SERINE/THREONINE-PROTEIN KINASE RECEPTOR R4;                
COMPND  12 EC: 2.7.1.37;                                                        
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELL_LINE: PLYS S;                                                   
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE  10 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;                      
SOURCE  11 EXPRESSION_SYSTEM_VECTOR: BACULOVIRUS;                               
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PFASTBAC;                                 
SOURCE  13 MOL_ID: 2;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_COMMON: HUMAN;                                              
SOURCE  16 ORGANISM_TAXID: 9606;                                                
SOURCE  17 CELL_LINE: PLYS S;                                                   
SOURCE  18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  20 EXPRESSION_SYSTEM_CELL_LINE: PLYS S;                                 
SOURCE  21 EXPRESSION_SYSTEM_CELLULAR_LOCATION: CYTOPLASM;                      
SOURCE  22 EXPRESSION_SYSTEM_PLASMID: PET23                                     
KEYWDS    COMPLEX (ISOMERASE/PROTEIN KINASE), RECEPTOR                          
KEYWDS   2 SERINE/THREONINE KINASE                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.HUSE,Y.-G.CHEN,J.MASSAGUE,J.KURIYAN                                 
REVDAT   2   24-FEB-09 1B6C    1       VERSN                                    
REVDAT   1   15-JUN-99 1B6C    0                                                
JRNL        AUTH   M.HUSE,Y.G.CHEN,J.MASSAGUE,J.KURIYAN                         
JRNL        TITL   CRYSTAL STRUCTURE OF THE CYTOPLASMIC DOMAIN OF THE           
JRNL        TITL 2 TYPE I TGF BETA RECEPTOR IN COMPLEX WITH FKBP12.             
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V.  96   425 1999              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   10025408                                                     
JRNL        DOI    10.1016/S0092-8674(00)80555-3                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.3C                                             
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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 57740                          
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) : 0.249                           
REMARK   3   FREE R VALUE                     : 0.269                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 5883                            
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           : 50                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.62                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1138                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3448                       
REMARK   3   BIN FREE R VALUE                    : 0.3114                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.00                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 126                          
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            : 13732                                   
REMARK   3   NUCLEIC ACID ATOMS       : NULL                                    
REMARK   3   HETEROGEN ATOMS          : 20                                      
REMARK   3   SOLVENT ATOMS            : 88                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.29                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.61600                                             
REMARK   3    B22 (A**2) : -2.27100                                             
REMARK   3    B33 (A**2) : 6.88700                                              
REMARK   3    B12 (A**2) : 3.26200                                              
REMARK   3    B13 (A**2) : 4.94200                                              
REMARK   3    B23 (A**2) : 1.01300                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.66                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
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) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : RESTRAINTS                                              
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  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1B6C COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : FEB-98                             
REMARK 200  TEMPERATURE           (KELVIN) : 200                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 6                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X25                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 57740                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.24000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 6.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: CCP4                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.5                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5                                           
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1980 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL                        
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1990 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19640 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1970 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1950 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
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                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11700 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 74980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -142.0 KCAL/MOL                       
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 APPLY THE FOLLOWING TO CHAINS: G, H                                  
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000      -75.58000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   3  1.000000  0.000000  0.000000      -22.81770            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000      -72.45340            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000       89.61722            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000      -48.45441            
REMARK 350   BIOMT2   4  0.000000  1.000000  0.000000      -73.15972            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000      -89.61722            
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     GLU B   162                                                      
REMARK 465     ASP B   163                                                      
REMARK 465     PRO B   164                                                      
REMARK 465     SER B   165                                                      
REMARK 465     LEU B   166                                                      
REMARK 465     ASP B   167                                                      
REMARK 465     ARG B   168                                                      
REMARK 465     PRO B   169                                                      
REMARK 465     PHE B   170                                                      
REMARK 465     ILE B   171                                                      
REMARK 465     SER B   172                                                      
REMARK 465     GLU B   173                                                      
REMARK 465     GLY B   174                                                      
REMARK 465     ILE B   501                                                      
REMARK 465     LYS B   502                                                      
REMARK 465     MET B   503                                                      
REMARK 465     GLU D   162                                                      
REMARK 465     ASP D   163                                                      
REMARK 465     PRO D   164                                                      
REMARK 465     SER D   165                                                      
REMARK 465     LEU D   166                                                      
REMARK 465     ASP D   167                                                      
REMARK 465     ARG D   168                                                      
REMARK 465     PRO D   169                                                      
REMARK 465     PHE D   170                                                      
REMARK 465     ILE D   171                                                      
REMARK 465     SER D   172                                                      
REMARK 465     GLU D   173                                                      
REMARK 465     GLY D   174                                                      
REMARK 465     ILE D   501                                                      
REMARK 465     LYS D   502                                                      
REMARK 465     MET D   503                                                      
REMARK 465     GLU F   162                                                      
REMARK 465     ASP F   163                                                      
REMARK 465     PRO F   164                                                      
REMARK 465     SER F   165                                                      
REMARK 465     LEU F   166                                                      
REMARK 465     ASP F   167                                                      
REMARK 465     ARG F   168                                                      
REMARK 465     PRO F   169                                                      
REMARK 465     PHE F   170                                                      
REMARK 465     ILE F   171                                                      
REMARK 465     SER F   172                                                      
REMARK 465     GLU F   173                                                      
REMARK 465     GLY F   174                                                      
REMARK 465     ILE F   501                                                      
REMARK 465     LYS F   502                                                      
REMARK 465     MET F   503                                                      
REMARK 465     GLU H   162                                                      
REMARK 465     ASP H   163                                                      
REMARK 465     PRO H   164                                                      
REMARK 465     SER H   165                                                      
REMARK 465     LEU H   166                                                      
REMARK 465     ASP H   167                                                      
REMARK 465     ARG H   168                                                      
REMARK 465     PRO H   169                                                      
REMARK 465     PHE H   170                                                      
REMARK 465     ILE H   171                                                      
REMARK 465     SER H   172                                                      
REMARK 465     GLU H   173                                                      
REMARK 465     GLY H   174                                                      
REMARK 465     ILE H   501                                                      
REMARK 465     LYS H   502                                                      
REMARK 465     MET H   503                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLN A    3   CD    OE1   NE2                                     
REMARK 480     LYS A   52   CD    CE    NZ                                      
REMARK 480     ASP B  269   CG    OD1   OD2                                     
REMARK 480     GLN B  324   CG    CD    OE1   NE2                               
REMARK 480     LYS B  343   CE    NZ                                            
REMARK 480     HIS B  371   CG    ND1   CD2   CE1   NE2                         
REMARK 480     LYS B  391   CD    CE    NZ                                      
REMARK 480     GLN C    3   CD    OE1   NE2                                     
REMARK 480     LYS C   52   CD    CE    NZ                                      
REMARK 480     ASP D  269   CG    OD1   OD2                                     
REMARK 480     GLN D  324   CG    CD    OE1   NE2                               
REMARK 480     LYS D  343   CE    NZ                                            
REMARK 480     HIS D  371   CG    ND1   CD2   CE1   NE2                         
REMARK 480     LYS D  391   CD    CE    NZ                                      
REMARK 480     GLN E    3   CD    OE1   NE2                                     
REMARK 480     LYS E   52   CD    CE    NZ                                      
REMARK 480     ASP F  269   CG    OD1   OD2                                     
REMARK 480     GLN F  324   CG    CD    OE1   NE2                               
REMARK 480     LYS F  343   CE    NZ                                            
REMARK 480     HIS F  371   CG    ND1   CD2   CE1   NE2                         
REMARK 480     LYS F  391   CD    CE    NZ                                      
REMARK 480     GLN G    3   CD    OE1   NE2                                     
REMARK 480     LYS G   52   CD    CE    NZ                                      
REMARK 480     ASP H  269   CG    OD1   OD2                                     
REMARK 480     GLN H  324   CG    CD    OE1   NE2                               
REMARK 480     LYS H  343   CE    NZ                                            
REMARK 480     HIS H  371   CG    ND1   CD2   CE1   NE2                         
REMARK 480     LYS H  391   CD    CE    NZ                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE2  GLU D   209     NH1  ARG D   221              2.16            
REMARK 500   OE2  GLU H   209     NH1  ARG H   221              2.16            
REMARK 500   OE2  GLU F   209     NH1  ARG F   221              2.16            
REMARK 500   OE2  GLU B   209     NH1  ARG B   221              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LYS B 391   CG    LYS B 391   CD      0.431                       
REMARK 500    LYS D 391   CG    LYS D 391   CD      0.431                       
REMARK 500    HIS F 283   C     GLU F 284   N      -0.143                       
REMARK 500    LYS F 391   CG    LYS F 391   CD      0.430                       
REMARK 500    LYS H 391   CG    LYS H 391   CD      0.431                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (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,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LYS B 391   CB  -  CG  -  CD  ANGL. DEV. = -19.6 DEGREES          
REMARK 500    LYS D 391   CB  -  CG  -  CD  ANGL. DEV. = -19.6 DEGREES          
REMARK 500    LYS F 391   CB  -  CG  -  CD  ANGL. DEV. = -19.6 DEGREES          
REMARK 500    HIS H 283   O   -  C   -  N   ANGL. DEV. =  10.6 DEGREES          
REMARK 500    LYS H 391   CB  -  CG  -  CD  ANGL. DEV. = -19.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    ASP A  37      144.82   -172.45                                   
REMARK 500    SER A  38      109.02   -163.26                                   
REMARK 500    ALA A  81     -120.24   -126.04                                   
REMARK 500    PRO A  88      112.33    -38.36                                   
REMARK 500    LYS B 213       76.04   -115.54                                   
REMARK 500    PHE B 216       65.88   -107.47                                   
REMARK 500    LYS B 326      131.85    176.55                                   
REMARK 500    ARG B 332       -5.19     85.43                                   
REMARK 500    ASP B 333       44.36   -148.14                                   
REMARK 500    ASP B 351       80.31     52.69                                   
REMARK 500    THR B 362        7.93   -155.99                                   
REMARK 500    GLU B 499       25.74   -145.60                                   
REMARK 500    ASP C  37      144.65   -172.31                                   
REMARK 500    SER C  38      109.07   -163.06                                   
REMARK 500    ALA C  81     -120.37   -126.14                                   
REMARK 500    PRO C  88      112.28    -38.44                                   
REMARK 500    LYS D 213       75.98   -115.47                                   
REMARK 500    PHE D 216       65.87   -107.51                                   
REMARK 500    LYS D 326      131.80    176.38                                   
REMARK 500    ARG D 332       -5.06     85.53                                   
REMARK 500    ASP D 333       44.40   -148.12                                   
REMARK 500    ASP D 351       80.27     52.75                                   
REMARK 500    THR D 362        7.86   -155.91                                   
REMARK 500    GLU D 499       25.68   -145.54                                   
REMARK 500    ASP E  37      144.68   -172.42                                   
REMARK 500    SER E  38      109.03   -163.05                                   
REMARK 500    ALA E  81     -120.42   -126.18                                   
REMARK 500    PRO E  88      112.22    -38.34                                   
REMARK 500    LYS F 213       76.04   -115.51                                   
REMARK 500    PHE F 216       65.97   -107.44                                   
REMARK 500    GLU F 284      -38.08    -36.33                                   
REMARK 500    LYS F 326      131.70    176.46                                   
REMARK 500    ARG F 332       -5.04     85.59                                   
REMARK 500    ASP F 333       44.35   -148.25                                   
REMARK 500    ASP F 351       80.13     52.78                                   
REMARK 500    THR F 362        7.96   -156.00                                   
REMARK 500    GLU F 499       25.75   -145.57                                   
REMARK 500    ASP G  37      144.60   -172.51                                   
REMARK 500    SER G  38      109.06   -163.10                                   
REMARK 500    ALA G  81     -120.47   -126.13                                   
REMARK 500    PRO G  88      112.40    -38.42                                   
REMARK 500    LYS H 213       76.00   -115.57                                   
REMARK 500    PHE H 216       65.93   -107.53                                   
REMARK 500    LYS H 326      131.90    176.68                                   
REMARK 500    ARG H 332       -5.13     85.56                                   
REMARK 500    ASP H 333       44.45   -148.10                                   
REMARK 500    ASP H 351       80.24     52.83                                   
REMARK 500    THR H 362        8.03   -156.01                                   
REMARK 500    GLU H 499       25.71   -145.52                                   
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 B 424         0.07    SIDE_CHAIN                              
REMARK 500    TYR D 424         0.07    SIDE_CHAIN                              
REMARK 500    TYR F 424         0.07    SIDE_CHAIN                              
REMARK 500    TYR H 424         0.07    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 SO4 B 158                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 504                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 504                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 H 504                 
DBREF  1B6C A    1   107  UNP    P62942   FKB1A_HUMAN      1    107             
DBREF  1B6C B  162   503  UNP    P36897   TGFR1_HUMAN    162    503             
DBREF  1B6C C    1   107  UNP    P62942   FKB1A_HUMAN      1    107             
DBREF  1B6C D  162   503  UNP    P36897   TGFR1_HUMAN    162    503             
DBREF  1B6C E    1   107  UNP    P62942   FKB1A_HUMAN      1    107             
DBREF  1B6C F  162   503  UNP    P36897   TGFR1_HUMAN    162    503             
DBREF  1B6C G    1   107  UNP    P62942   FKB1A_HUMAN      1    107             
DBREF  1B6C H  162   503  UNP    P36897   TGFR1_HUMAN    162    503             
SEQRES   1 A  107  GLY VAL GLN VAL GLU THR ILE SER PRO GLY ASP GLY ARG          
SEQRES   2 A  107  THR PHE PRO LYS ARG GLY GLN THR CYS VAL VAL HIS TYR          
SEQRES   3 A  107  THR GLY MET LEU GLU ASP GLY LYS LYS PHE ASP SER SER          
SEQRES   4 A  107  ARG ASP ARG ASN LYS PRO PHE LYS PHE MET LEU GLY LYS          
SEQRES   5 A  107  GLN GLU VAL ILE ARG GLY TRP GLU GLU GLY VAL ALA GLN          
SEQRES   6 A  107  MET SER VAL GLY GLN ARG ALA LYS LEU THR ILE SER PRO          
SEQRES   7 A  107  ASP TYR ALA TYR GLY ALA THR GLY HIS PRO GLY ILE ILE          
SEQRES   8 A  107  PRO PRO HIS ALA THR LEU VAL PHE ASP VAL GLU LEU LEU          
SEQRES   9 A  107  LYS LEU GLU                                                  
SEQRES   1 B  342  GLU ASP PRO SER LEU ASP ARG PRO PHE ILE SER GLU GLY          
SEQRES   2 B  342  THR THR LEU LYS ASP LEU ILE TYR ASP MET THR THR SER          
SEQRES   3 B  342  GLY SER GLY SER GLY LEU PRO LEU LEU VAL GLN ARG THR          
SEQRES   4 B  342  ILE ALA ARG THR ILE VAL LEU GLN GLU SER ILE GLY LYS          
SEQRES   5 B  342  GLY ARG PHE GLY GLU VAL TRP ARG GLY LYS TRP ARG GLY          
SEQRES   6 B  342  GLU GLU VAL ALA VAL LYS ILE PHE SER SER ARG GLU GLU          
SEQRES   7 B  342  ARG SER TRP PHE ARG GLU ALA GLU ILE TYR GLN THR VAL          
SEQRES   8 B  342  MET LEU ARG HIS GLU ASN ILE LEU GLY PHE ILE ALA ALA          
SEQRES   9 B  342  ASP ASN LYS ASP ASN GLY THR TRP THR GLN LEU TRP LEU          
SEQRES  10 B  342  VAL SER ASP TYR HIS GLU HIS GLY SER LEU PHE ASP TYR          
SEQRES  11 B  342  LEU ASN ARG TYR THR VAL THR VAL GLU GLY MET ILE LYS          
SEQRES  12 B  342  LEU ALA LEU SER THR ALA SER GLY LEU ALA HIS LEU HIS          
SEQRES  13 B  342  MET GLU ILE VAL GLY THR GLN GLY LYS PRO ALA ILE ALA          
SEQRES  14 B  342  HIS ARG ASP LEU LYS SER LYS ASN ILE LEU VAL LYS LYS          
SEQRES  15 B  342  ASN GLY THR CYS CYS ILE ALA ASP LEU GLY LEU ALA VAL          
SEQRES  16 B  342  ARG HIS ASP SER ALA THR ASP THR ILE ASP ILE ALA PRO          
SEQRES  17 B  342  ASN HIS ARG VAL GLY THR LYS ARG TYR MET ALA PRO GLU          
SEQRES  18 B  342  VAL LEU ASP ASP SER ILE ASN MET LYS HIS PHE GLU SER          
SEQRES  19 B  342  PHE LYS ARG ALA ASP ILE TYR ALA MET GLY LEU VAL PHE          
SEQRES  20 B  342  TRP GLU ILE ALA ARG ARG CYS SER ILE GLY GLY ILE HIS          
SEQRES  21 B  342  GLU ASP TYR GLN LEU PRO TYR TYR ASP LEU VAL PRO SER          
SEQRES  22 B  342  ASP PRO SER VAL GLU GLU MET ARG LYS VAL VAL CYS GLU          
SEQRES  23 B  342  GLN LYS LEU ARG PRO ASN ILE PRO ASN ARG TRP GLN SER          
SEQRES  24 B  342  CYS GLU ALA LEU ARG VAL MET ALA LYS ILE MET ARG GLU          
SEQRES  25 B  342  CYS TRP TYR ALA ASN GLY ALA ALA ARG LEU THR ALA LEU          
SEQRES  26 B  342  ARG ILE LYS LYS THR LEU SER GLN LEU SER GLN GLN GLU          
SEQRES  27 B  342  GLY ILE LYS MET                                              
SEQRES   1 C  107  GLY VAL GLN VAL GLU THR ILE SER PRO GLY ASP GLY ARG          
SEQRES   2 C  107  THR PHE PRO LYS ARG GLY GLN THR CYS VAL VAL HIS TYR          
SEQRES   3 C  107  THR GLY MET LEU GLU ASP GLY LYS LYS PHE ASP SER SER          
SEQRES   4 C  107  ARG ASP ARG ASN LYS PRO PHE LYS PHE MET LEU GLY LYS          
SEQRES   5 C  107  GLN GLU VAL ILE ARG GLY TRP GLU GLU GLY VAL ALA GLN          
SEQRES   6 C  107  MET SER VAL GLY GLN ARG ALA LYS LEU THR ILE SER PRO          
SEQRES   7 C  107  ASP TYR ALA TYR GLY ALA THR GLY HIS PRO GLY ILE ILE          
SEQRES   8 C  107  PRO PRO HIS ALA THR LEU VAL PHE ASP VAL GLU LEU LEU          
SEQRES   9 C  107  LYS LEU GLU                                                  
SEQRES   1 D  342  GLU ASP PRO SER LEU ASP ARG PRO PHE ILE SER GLU GLY          
SEQRES   2 D  342  THR THR LEU LYS ASP LEU ILE TYR ASP MET THR THR SER          
SEQRES   3 D  342  GLY SER GLY SER GLY LEU PRO LEU LEU VAL GLN ARG THR          
SEQRES   4 D  342  ILE ALA ARG THR ILE VAL LEU GLN GLU SER ILE GLY LYS          
SEQRES   5 D  342  GLY ARG PHE GLY GLU VAL TRP ARG GLY LYS TRP ARG GLY          
SEQRES   6 D  342  GLU GLU VAL ALA VAL LYS ILE PHE SER SER ARG GLU GLU          
SEQRES   7 D  342  ARG SER TRP PHE ARG GLU ALA GLU ILE TYR GLN THR VAL          
SEQRES   8 D  342  MET LEU ARG HIS GLU ASN ILE LEU GLY PHE ILE ALA ALA          
SEQRES   9 D  342  ASP ASN LYS ASP ASN GLY THR TRP THR GLN LEU TRP LEU          
SEQRES  10 D  342  VAL SER ASP TYR HIS GLU HIS GLY SER LEU PHE ASP TYR          
SEQRES  11 D  342  LEU ASN ARG TYR THR VAL THR VAL GLU GLY MET ILE LYS          
SEQRES  12 D  342  LEU ALA LEU SER THR ALA SER GLY LEU ALA HIS LEU HIS          
SEQRES  13 D  342  MET GLU ILE VAL GLY THR GLN GLY LYS PRO ALA ILE ALA          
SEQRES  14 D  342  HIS ARG ASP LEU LYS SER LYS ASN ILE LEU VAL LYS LYS          
SEQRES  15 D  342  ASN GLY THR CYS CYS ILE ALA ASP LEU GLY LEU ALA VAL          
SEQRES  16 D  342  ARG HIS ASP SER ALA THR ASP THR ILE ASP ILE ALA PRO          
SEQRES  17 D  342  ASN HIS ARG VAL GLY THR LYS ARG TYR MET ALA PRO GLU          
SEQRES  18 D  342  VAL LEU ASP ASP SER ILE ASN MET LYS HIS PHE GLU SER          
SEQRES  19 D  342  PHE LYS ARG ALA ASP ILE TYR ALA MET GLY LEU VAL PHE          
SEQRES  20 D  342  TRP GLU ILE ALA ARG ARG CYS SER ILE GLY GLY ILE HIS          
SEQRES  21 D  342  GLU ASP TYR GLN LEU PRO TYR TYR ASP LEU VAL PRO SER          
SEQRES  22 D  342  ASP PRO SER VAL GLU GLU MET ARG LYS VAL VAL CYS GLU          
SEQRES  23 D  342  GLN LYS LEU ARG PRO ASN ILE PRO ASN ARG TRP GLN SER          
SEQRES  24 D  342  CYS GLU ALA LEU ARG VAL MET ALA LYS ILE MET ARG GLU          
SEQRES  25 D  342  CYS TRP TYR ALA ASN GLY ALA ALA ARG LEU THR ALA LEU          
SEQRES  26 D  342  ARG ILE LYS LYS THR LEU SER GLN LEU SER GLN GLN GLU          
SEQRES  27 D  342  GLY ILE LYS MET                                              
SEQRES   1 E  107  GLY VAL GLN VAL GLU THR ILE SER PRO GLY ASP GLY ARG          
SEQRES   2 E  107  THR PHE PRO LYS ARG GLY GLN THR CYS VAL VAL HIS TYR          
SEQRES   3 E  107  THR GLY MET LEU GLU ASP GLY LYS LYS PHE ASP SER SER          
SEQRES   4 E  107  ARG ASP ARG ASN LYS PRO PHE LYS PHE MET LEU GLY LYS          
SEQRES   5 E  107  GLN GLU VAL ILE ARG GLY TRP GLU GLU GLY VAL ALA GLN          
SEQRES   6 E  107  MET SER VAL GLY GLN ARG ALA LYS LEU THR ILE SER PRO          
SEQRES   7 E  107  ASP TYR ALA TYR GLY ALA THR GLY HIS PRO GLY ILE ILE          
SEQRES   8 E  107  PRO PRO HIS ALA THR LEU VAL PHE ASP VAL GLU LEU LEU          
SEQRES   9 E  107  LYS LEU GLU                                                  
SEQRES   1 F  342  GLU ASP PRO SER LEU ASP ARG PRO PHE ILE SER GLU GLY          
SEQRES   2 F  342  THR THR LEU LYS ASP LEU ILE TYR ASP MET THR THR SER          
SEQRES   3 F  342  GLY SER GLY SER GLY LEU PRO LEU LEU VAL GLN ARG THR          
SEQRES   4 F  342  ILE ALA ARG THR ILE VAL LEU GLN GLU SER ILE GLY LYS          
SEQRES   5 F  342  GLY ARG PHE GLY GLU VAL TRP ARG GLY LYS TRP ARG GLY          
SEQRES   6 F  342  GLU GLU VAL ALA VAL LYS ILE PHE SER SER ARG GLU GLU          
SEQRES   7 F  342  ARG SER TRP PHE ARG GLU ALA GLU ILE TYR GLN THR VAL          
SEQRES   8 F  342  MET LEU ARG HIS GLU ASN ILE LEU GLY PHE ILE ALA ALA          
SEQRES   9 F  342  ASP ASN LYS ASP ASN GLY THR TRP THR GLN LEU TRP LEU          
SEQRES  10 F  342  VAL SER ASP TYR HIS GLU HIS GLY SER LEU PHE ASP TYR          
SEQRES  11 F  342  LEU ASN ARG TYR THR VAL THR VAL GLU GLY MET ILE LYS          
SEQRES  12 F  342  LEU ALA LEU SER THR ALA SER GLY LEU ALA HIS LEU HIS          
SEQRES  13 F  342  MET GLU ILE VAL GLY THR GLN GLY LYS PRO ALA ILE ALA          
SEQRES  14 F  342  HIS ARG ASP LEU LYS SER LYS ASN ILE LEU VAL LYS LYS          
SEQRES  15 F  342  ASN GLY THR CYS CYS ILE ALA ASP LEU GLY LEU ALA VAL          
SEQRES  16 F  342  ARG HIS ASP SER ALA THR ASP THR ILE ASP ILE ALA PRO          
SEQRES  17 F  342  ASN HIS ARG VAL GLY THR LYS ARG TYR MET ALA PRO GLU          
SEQRES  18 F  342  VAL LEU ASP ASP SER ILE ASN MET LYS HIS PHE GLU SER          
SEQRES  19 F  342  PHE LYS ARG ALA ASP ILE TYR ALA MET GLY LEU VAL PHE          
SEQRES  20 F  342  TRP GLU ILE ALA ARG ARG CYS SER ILE GLY GLY ILE HIS          
SEQRES  21 F  342  GLU ASP TYR GLN LEU PRO TYR TYR ASP LEU VAL PRO SER          
SEQRES  22 F  342  ASP PRO SER VAL GLU GLU MET ARG LYS VAL VAL CYS GLU          
SEQRES  23 F  342  GLN LYS LEU ARG PRO ASN ILE PRO ASN ARG TRP GLN SER          
SEQRES  24 F  342  CYS GLU ALA LEU ARG VAL MET ALA LYS ILE MET ARG GLU          
SEQRES  25 F  342  CYS TRP TYR ALA ASN GLY ALA ALA ARG LEU THR ALA LEU          
SEQRES  26 F  342  ARG ILE LYS LYS THR LEU SER GLN LEU SER GLN GLN GLU          
SEQRES  27 F  342  GLY ILE LYS MET                                              
SEQRES   1 G  107  GLY VAL GLN VAL GLU THR ILE SER PRO GLY ASP GLY ARG          
SEQRES   2 G  107  THR PHE PRO LYS ARG GLY GLN THR CYS VAL VAL HIS TYR          
SEQRES   3 G  107  THR GLY MET LEU GLU ASP GLY LYS LYS PHE ASP SER SER          
SEQRES   4 G  107  ARG ASP ARG ASN LYS PRO PHE LYS PHE MET LEU GLY LYS          
SEQRES   5 G  107  GLN GLU VAL ILE ARG GLY TRP GLU GLU GLY VAL ALA GLN          
SEQRES   6 G  107  MET SER VAL GLY GLN ARG ALA LYS LEU THR ILE SER PRO          
SEQRES   7 G  107  ASP TYR ALA TYR GLY ALA THR GLY HIS PRO GLY ILE ILE          
SEQRES   8 G  107  PRO PRO HIS ALA THR LEU VAL PHE ASP VAL GLU LEU LEU          
SEQRES   9 G  107  LYS LEU GLU                                                  
SEQRES   1 H  342  GLU ASP PRO SER LEU ASP ARG PRO PHE ILE SER GLU GLY          
SEQRES   2 H  342  THR THR LEU LYS ASP LEU ILE TYR ASP MET THR THR SER          
SEQRES   3 H  342  GLY SER GLY SER GLY LEU PRO LEU LEU VAL GLN ARG THR          
SEQRES   4 H  342  ILE ALA ARG THR ILE VAL LEU GLN GLU SER ILE GLY LYS          
SEQRES   5 H  342  GLY ARG PHE GLY GLU VAL TRP ARG GLY LYS TRP ARG GLY          
SEQRES   6 H  342  GLU GLU VAL ALA VAL LYS ILE PHE SER SER ARG GLU GLU          
SEQRES   7 H  342  ARG SER TRP PHE ARG GLU ALA GLU ILE TYR GLN THR VAL          
SEQRES   8 H  342  MET LEU ARG HIS GLU ASN ILE LEU GLY PHE ILE ALA ALA          
SEQRES   9 H  342  ASP ASN LYS ASP ASN GLY THR TRP THR GLN LEU TRP LEU          
SEQRES  10 H  342  VAL SER ASP TYR HIS GLU HIS GLY SER LEU PHE ASP TYR          
SEQRES  11 H  342  LEU ASN ARG TYR THR VAL THR VAL GLU GLY MET ILE LYS          
SEQRES  12 H  342  LEU ALA LEU SER THR ALA SER GLY LEU ALA HIS LEU HIS          
SEQRES  13 H  342  MET GLU ILE VAL GLY THR GLN GLY LYS PRO ALA ILE ALA          
SEQRES  14 H  342  HIS ARG ASP LEU LYS SER LYS ASN ILE LEU VAL LYS LYS          
SEQRES  15 H  342  ASN GLY THR CYS CYS ILE ALA ASP LEU GLY LEU ALA VAL          
SEQRES  16 H  342  ARG HIS ASP SER ALA THR ASP THR ILE ASP ILE ALA PRO          
SEQRES  17 H  342  ASN HIS ARG VAL GLY THR LYS ARG TYR MET ALA PRO GLU          
SEQRES  18 H  342  VAL LEU ASP ASP SER ILE ASN MET LYS HIS PHE GLU SER          
SEQRES  19 H  342  PHE LYS ARG ALA ASP ILE TYR ALA MET GLY LEU VAL PHE          
SEQRES  20 H  342  TRP GLU ILE ALA ARG ARG CYS SER ILE GLY GLY ILE HIS          
SEQRES  21 H  342  GLU ASP TYR GLN LEU PRO TYR TYR ASP LEU VAL PRO SER          
SEQRES  22 H  342  ASP PRO SER VAL GLU GLU MET ARG LYS VAL VAL CYS GLU          
SEQRES  23 H  342  GLN LYS LEU ARG PRO ASN ILE PRO ASN ARG TRP GLN SER          
SEQRES  24 H  342  CYS GLU ALA LEU ARG VAL MET ALA LYS ILE MET ARG GLU          
SEQRES  25 H  342  CYS TRP TYR ALA ASN GLY ALA ALA ARG LEU THR ALA LEU          
SEQRES  26 H  342  ARG ILE LYS LYS THR LEU SER GLN LEU SER GLN GLN GLU          
SEQRES  27 H  342  GLY ILE LYS MET                                              
HET    SO4  B 158       5                                                       
HET    SO4  D 504       5                                                       
HET    SO4  F 504       5                                                       
HET    SO4  H 504       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   9  SO4    4(O4 S 2-)                                                   
FORMUL  13  HOH   *88(H2 O)                                                     
HELIX    1   1 SER A   39  ARG A   42  1                                   4    
HELIX    2   2 ARG A   57  GLN A   65  1                                   9    
HELIX    3   3 PRO A   78  TYR A   80  5                                   3    
HELIX    4   4 LEU B  177  ASP B  183  1                                   7    
HELIX    5   5 LEU B  195  THR B  204  1                                  10    
HELIX    6   6 SER B  236  THR B  251  5                                  16    
HELIX    7   7 LEU B  288  ARG B  294  1                                   7    
HELIX    8   8 VAL B  299  HIS B  317  1                                  19    
HELIX    9   9 SER B  336  ASN B  338  5                                   3    
HELIX   10  10 LYS B  376  TYR B  378  5                                   3    
HELIX   11  11 PRO B  381  LEU B  384  1                                   4    
HELIX   12  12 PHE B  393  ARG B  414  1                                  22    
HELIX   13  13 VAL B  438  VAL B  445  1                                   8    
HELIX   14  14 ASN B  456  GLN B  459  5                                   4    
HELIX   15  15 GLU B  462  CYS B  474  1                                  13    
HELIX   16  16 GLY B  479  ALA B  481  5                                   3    
HELIX   17  17 ALA B  485  GLN B  497  1                                  13    
HELIX   18  18 SER C   39  ARG C   42  1                                   4    
HELIX   19  19 ARG C   57  GLN C   65  1                                   9    
HELIX   20  20 PRO C   78  TYR C   80  5                                   3    
HELIX   21  21 LEU D  177  ASP D  183  1                                   7    
HELIX   22  22 LEU D  195  THR D  204  1                                  10    
HELIX   23  23 SER D  236  THR D  251  5                                  16    
HELIX   24  24 LEU D  288  ARG D  294  1                                   7    
HELIX   25  25 VAL D  299  HIS D  317  1                                  19    
HELIX   26  26 SER D  336  ASN D  338  5                                   3    
HELIX   27  27 LYS D  376  TYR D  378  5                                   3    
HELIX   28  28 PRO D  381  LEU D  384  1                                   4    
HELIX   29  29 PHE D  393  ARG D  414  1                                  22    
HELIX   30  30 VAL D  438  VAL D  445  1                                   8    
HELIX   31  31 ASN D  456  GLN D  459  5                                   4    
HELIX   32  32 GLU D  462  CYS D  474  1                                  13    
HELIX   33  33 GLY D  479  ALA D  481  5                                   3    
HELIX   34  34 ALA D  485  GLN D  497  1                                  13    
HELIX   35  35 SER E   39  ARG E   42  1                                   4    
HELIX   36  36 ARG E   57  GLN E   65  1                                   9    
HELIX   37  37 PRO E   78  TYR E   80  5                                   3    
HELIX   38  38 LEU F  177  ASP F  183  1                                   7    
HELIX   39  39 LEU F  195  THR F  204  1                                  10    
HELIX   40  40 SER F  236  THR F  251  5                                  16    
HELIX   41  41 LEU F  288  ARG F  294  1                                   7    
HELIX   42  42 VAL F  299  HIS F  317  1                                  19    
HELIX   43  43 SER F  336  ASN F  338  5                                   3    
HELIX   44  44 LYS F  376  TYR F  378  5                                   3    
HELIX   45  45 PRO F  381  LEU F  384  1                                   4    
HELIX   46  46 PHE F  393  ARG F  414  1                                  22    
HELIX   47  47 VAL F  438  VAL F  445  1                                   8    
HELIX   48  48 ASN F  456  GLN F  459  5                                   4    
HELIX   49  49 GLU F  462  CYS F  474  1                                  13    
HELIX   50  50 GLY F  479  ALA F  481  5                                   3    
HELIX   51  51 ALA F  485  GLN F  497  1                                  13    
HELIX   52  52 SER G   39  ARG G   42  1                                   4    
HELIX   53  53 ARG G   57  GLN G   65  1                                   9    
HELIX   54  54 PRO G   78  TYR G   80  5                                   3    
HELIX   55  55 LEU H  177  ASP H  183  1                                   7    
HELIX   56  56 LEU H  195  THR H  204  1                                  10    
HELIX   57  57 SER H  236  THR H  251  5                                  16    
HELIX   58  58 LEU H  288  ARG H  294  1                                   7    
HELIX   59  59 VAL H  299  HIS H  317  1                                  19    
HELIX   60  60 SER H  336  ASN H  338  5                                   3    
HELIX   61  61 LYS H  376  TYR H  378  5                                   3    
HELIX   62  62 PRO H  381  LEU H  384  1                                   4    
HELIX   63  63 PHE H  393  ARG H  414  1                                  22    
HELIX   64  64 VAL H  438  VAL H  445  1                                   8    
HELIX   65  65 ASN H  456  GLN H  459  5                                   4    
HELIX   66  66 GLU H  462  CYS H  474  1                                  13    
HELIX   67  67 GLY H  479  ALA H  481  5                                   3    
HELIX   68  68 ALA H  485  GLN H  497  1                                  13    
SHEET    1   A 5 PHE A  46  MET A  49  0                                        
SHEET    2   A 5 THR A  21  LEU A  30 -1  N  VAL A  24   O  PHE A  46           
SHEET    3   A 5 LEU A  97  GLU A 107 -1  N  GLU A 107   O  THR A  21           
SHEET    4   A 5 ARG A  71  ILE A  76 -1  N  ILE A  76   O  LEU A  97           
SHEET    5   A 5 VAL A   2  SER A   8 -1  N  SER A   8   O  ARG A  71           
SHEET    1   B 2 THR A  27  MET A  29  0                                        
SHEET    2   B 2 LYS A  35  SER A  38 -1  N  ASP A  37   O  GLY A  28           
SHEET    1   C 5 GLY B 212  GLY B 214  0                                        
SHEET    2   C 5 GLY B 217  TRP B 224 -1  N  VAL B 219   O  GLY B 212           
SHEET    3   C 5 GLU B 227  PHE B 234 -1  N  ILE B 233   O  GLU B 218           
SHEET    4   C 5 LEU B 276  SER B 280 -1  N  SER B 280   O  ALA B 230           
SHEET    5   C 5 PHE B 262  ASN B 267 -1  N  ASP B 266   O  TRP B 277           
SHEET    1   D 3 ALA B 328  ALA B 330  0                                        
SHEET    2   D 3 VAL B 356  ASP B 359 -1  N  HIS B 358   O  ALA B 328           
SHEET    3   D 3 THR B 364  ILE B 367 -1  N  ASP B 366   O  ARG B 357           
SHEET    1   E 2 ILE B 339  VAL B 341  0                                        
SHEET    2   E 2 CYS B 347  ILE B 349 -1  N  CYS B 348   O  LEU B 340           
SHEET    1   F 2 VAL B 206  SER B 210  0                                        
SHEET    2   F 2 TRP B 220  LYS B 223 -1  N  LYS B 223   O  VAL B 206           
SHEET    1   G 5 PHE C  46  MET C  49  0                                        
SHEET    2   G 5 THR C  21  LEU C  30 -1  N  VAL C  24   O  PHE C  46           
SHEET    3   G 5 LEU C  97  GLU C 107 -1  N  GLU C 107   O  THR C  21           
SHEET    4   G 5 ARG C  71  ILE C  76 -1  N  ILE C  76   O  LEU C  97           
SHEET    5   G 5 VAL C   2  SER C   8 -1  N  SER C   8   O  ARG C  71           
SHEET    1   H 2 THR C  27  MET C  29  0                                        
SHEET    2   H 2 LYS C  35  SER C  38 -1  N  ASP C  37   O  GLY C  28           
SHEET    1   I 5 GLY D 212  GLY D 214  0                                        
SHEET    2   I 5 GLY D 217  TRP D 224 -1  N  VAL D 219   O  GLY D 212           
SHEET    3   I 5 GLU D 227  PHE D 234 -1  N  ILE D 233   O  GLU D 218           
SHEET    4   I 5 LEU D 276  SER D 280 -1  N  SER D 280   O  ALA D 230           
SHEET    5   I 5 PHE D 262  ASN D 267 -1  N  ASP D 266   O  TRP D 277           
SHEET    1   J 3 ALA D 328  ALA D 330  0                                        
SHEET    2   J 3 VAL D 356  ASP D 359 -1  N  HIS D 358   O  ALA D 328           
SHEET    3   J 3 THR D 364  ILE D 367 -1  N  ASP D 366   O  ARG D 357           
SHEET    1   K 2 ILE D 339  VAL D 341  0                                        
SHEET    2   K 2 CYS D 347  ILE D 349 -1  N  CYS D 348   O  LEU D 340           
SHEET    1   L 2 VAL D 206  SER D 210  0                                        
SHEET    2   L 2 TRP D 220  LYS D 223 -1  N  LYS D 223   O  VAL D 206           
SHEET    1   M 5 PHE E  46  MET E  49  0                                        
SHEET    2   M 5 THR E  21  LEU E  30 -1  N  VAL E  24   O  PHE E  46           
SHEET    3   M 5 LEU E  97  GLU E 107 -1  N  GLU E 107   O  THR E  21           
SHEET    4   M 5 ARG E  71  ILE E  76 -1  N  ILE E  76   O  LEU E  97           
SHEET    5   M 5 VAL E   2  SER E   8 -1  N  SER E   8   O  ARG E  71           
SHEET    1   N 2 THR E  27  MET E  29  0                                        
SHEET    2   N 2 LYS E  35  SER E  38 -1  N  ASP E  37   O  GLY E  28           
SHEET    1   O 5 GLY F 212  GLY F 214  0                                        
SHEET    2   O 5 GLY F 217  TRP F 224 -1  N  VAL F 219   O  GLY F 212           
SHEET    3   O 5 GLU F 227  PHE F 234 -1  N  ILE F 233   O  GLU F 218           
SHEET    4   O 5 LEU F 276  SER F 280 -1  N  SER F 280   O  ALA F 230           
SHEET    5   O 5 PHE F 262  ASN F 267 -1  N  ASP F 266   O  TRP F 277           
SHEET    1   P 3 ALA F 328  ALA F 330  0                                        
SHEET    2   P 3 VAL F 356  ASP F 359 -1  N  HIS F 358   O  ALA F 328           
SHEET    3   P 3 THR F 364  ILE F 367 -1  N  ASP F 366   O  ARG F 357           
SHEET    1   Q 2 ILE F 339  VAL F 341  0                                        
SHEET    2   Q 2 CYS F 347  ILE F 349 -1  N  CYS F 348   O  LEU F 340           
SHEET    1   R 2 VAL F 206  SER F 210  0                                        
SHEET    2   R 2 TRP F 220  LYS F 223 -1  N  LYS F 223   O  VAL F 206           
SHEET    1   S 5 PHE G  46  MET G  49  0                                        
SHEET    2   S 5 THR G  21  LEU G  30 -1  N  VAL G  24   O  PHE G  46           
SHEET    3   S 5 LEU G  97  GLU G 107 -1  N  GLU G 107   O  THR G  21           
SHEET    4   S 5 ARG G  71  ILE G  76 -1  N  ILE G  76   O  LEU G  97           
SHEET    5   S 5 VAL G   2  SER G   8 -1  N  SER G   8   O  ARG G  71           
SHEET    1   T 2 THR G  27  MET G  29  0                                        
SHEET    2   T 2 LYS G  35  SER G  38 -1  N  ASP G  37   O  GLY G  28           
SHEET    1   U 5 GLY H 212  GLY H 214  0                                        
SHEET    2   U 5 GLY H 217  TRP H 224 -1  N  VAL H 219   O  GLY H 212           
SHEET    3   U 5 GLU H 227  PHE H 234 -1  N  ILE H 233   O  GLU H 218           
SHEET    4   U 5 LEU H 276  SER H 280 -1  N  SER H 280   O  ALA H 230           
SHEET    5   U 5 PHE H 262  ASN H 267 -1  N  ASP H 266   O  TRP H 277           
SHEET    1   V 3 ALA H 328  ALA H 330  0                                        
SHEET    2   V 3 VAL H 356  ASP H 359 -1  N  HIS H 358   O  ALA H 328           
SHEET    3   V 3 THR H 364  ILE H 367 -1  N  ASP H 366   O  ARG H 357           
SHEET    1   W 2 ILE H 339  VAL H 341  0                                        
SHEET    2   W 2 CYS H 347  ILE H 349 -1  N  CYS H 348   O  LEU H 340           
SHEET    1   X 2 VAL H 206  SER H 210  0                                        
SHEET    2   X 2 TRP H 220  LYS H 223 -1  N  LYS H 223   O  VAL H 206           
SITE     1 AC1  3 ARG B 377  LEU B 426  ASP B 435                               
SITE     1 AC2  3 ARG D 377  LEU D 426  ASP D 435                               
SITE     1 AC3  3 ARG F 377  LEU F 426  ASP F 435                               
SITE     1 AC4  3 ARG H 377  LEU H 426  ASP H 435                               
CRYST1   75.580   81.060   90.530  86.23  81.86  63.92 P 1           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      0.013231 -0.006476 -0.001867        0.00000                         
SCALE2      0.000000  0.013735 -0.000054        0.00000                         
SCALE3      0.000000  0.000000  0.011159        0.00000                         
MTRIX1   1 -0.999639 -0.026418 -0.004965       -4.30666    1                    
MTRIX2   1 -0.026378  0.999619 -0.008128       -0.72160    1                    
MTRIX3   1  0.005178 -0.007994 -0.999955       -0.03192    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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