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Database: PDB
Entry: 3KFD
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HEADER    CYTOKINE/CYTOKINE RECEPTOR              27-OCT-09   3KFD              
TITLE     TERNARY COMPLEX OF TGF-B1 REVEALS ISOFORM-SPECIFIC LIGAND RECOGNITION 
TITLE    2 AND RECEPTOR RECRUITMENT IN THE SUPERFAMILY                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRANSFORMING GROWTH FACTOR BETA-1;                         
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: TGF-BETA-1, LATENCY-ASSOCIATED PEPTIDE, LAP;                
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: TGF-BETA RECEPTOR TYPE-2;                                  
COMPND   8 CHAIN: E, F, G, H;                                                   
COMPND   9 FRAGMENT: EXTRACELLULAR DOMAIN;                                      
COMPND  10 SYNONYM: TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE II, TGF-BETA  
COMPND  11 RECEPTOR TYPE II, TGF-BETA TYPE II RECEPTOR, TBETAR-II, TGFR-2;      
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: TGF-BETA RECEPTOR TYPE-1;                                  
COMPND  15 CHAIN: I, J, K, L;                                                   
COMPND  16 FRAGMENT: EXTRACELLULAR DOMAIN;                                      
COMPND  17 SYNONYM: TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I, TGF-BETA   
COMPND  18 RECEPTOR TYPE I, TGF-BETA TYPE I RECEPTOR, TBETAR-I, TGFR-1,         
COMPND  19 SERINE/THREONINE-PROTEIN KINASE RECEPTOR R4, SKR4, ACTIVIN RECEPTOR- 
COMPND  20 LIKE KINASE 5, ALK-5;                                                
COMPND  21 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: TGFB1, TGFB;                                                   
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: CHO-LEC3.2.8.1;                            
SOURCE  10 EXPRESSION_SYSTEM_ORGAN: OVARY CELLS;                                
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: TGFBR2;                                                        
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 MOL_ID: 3;                                                           
SOURCE  19 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  20 ORGANISM_COMMON: HUMAN;                                              
SOURCE  21 ORGANISM_TAXID: 9606;                                                
SOURCE  22 GENE: TGFBR1;                                                        
SOURCE  23 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  24 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TGF-BETA, TGF-B1, TGF-BETA RECEPTOR TYPE-1, TGF-BETA RECEPTOR TYPE-2, 
KEYWDS   2 TBRII, TBRI, GROWTH FACTOR, RECEPTOR, SERINE/THREONINE-PROTEIN       
KEYWDS   3 KINASE, CYTOKINE-CYTOKINE RECEPTOR COMPLEX                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.RADAEV,P.D.SUN                                                      
REVDAT   2   19-MAY-10 3KFD    1       JRNL                                     
REVDAT   1   02-MAR-10 3KFD    0                                                
JRNL        AUTH   S.RADAEV,Z.ZOU,T.HUANG,E.M.LAFER,A.P.HINCK,P.D.SUN           
JRNL        TITL   TERNARY COMPLEX OF TRANSFORMING GROWTH FACTOR-BETA1 REVEALS  
JRNL        TITL 2 ISOFORM-SPECIFIC LIGAND RECOGNITION AND RECEPTOR             
JRNL        TITL 3 RECRUITMENT IN THE SUPERFAMILY.                              
JRNL        REF    J.BIOL.CHEM.                  V. 285 14806 2010              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   20207738                                                     
JRNL        DOI    10.1074/JBC.M109.079921                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.08                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.060                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 82.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 22125                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.220                           
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1062                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 46.0854 -  5.9861    0.96     3064   151  0.2328 0.2557        
REMARK   3     2  5.9861 -  4.7529    0.96     3048   161  0.1819 0.2193        
REMARK   3     3  4.7529 -  4.1526    0.95     3048   159  0.1638 0.2223        
REMARK   3     4  4.1526 -  3.7731    0.94     2968   164  0.2021 0.2482        
REMARK   3     5  3.7731 -  3.5027    0.93     3016   131  0.2222 0.3165        
REMARK   3     6  3.5027 -  3.2963    0.85     2695   138  0.2605 0.3392        
REMARK   3     7  3.2963 -  3.1312    0.63     1990    96  0.2890 0.3283        
REMARK   3     8  3.1312 -  2.9950    0.38     1234    62  0.3001 0.3876        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.32                                          
REMARK   3   B_SOL              : 41.91                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.410            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.610           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 73.45                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.63500                                              
REMARK   3    B22 (A**2) : -6.66200                                             
REMARK   3    B33 (A**2) : -31.29000                                            
REMARK   3    B12 (A**2) : -2.72800                                             
REMARK   3    B13 (A**2) : 0.20600                                              
REMARK   3    B23 (A**2) : 8.38400                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           9334                                  
REMARK   3   ANGLE     :  0.631          12563                                  
REMARK   3   CHIRALITY :  0.044           1396                                  
REMARK   3   PLANARITY :  0.003           1613                                  
REMARK   3   DIHEDRAL  : 20.035           3375                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3KFD COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-OCT-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB055922.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-OCT-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23426                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 1.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.24500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER, EPMR                                          
REMARK 200 STARTING MODEL: PDB ENTRIES  2TGI, 1M9Z, 1REW                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 8-15% PEG 4000-8000, PH 7.0, VAPOR       
REMARK 280  DIFFUSION, TEMPERATURE 298K                                         
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                                                 
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: HEXAMER                                                      
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9310 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28420 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F, I, J                      
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: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9400 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -66.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, G, H, K, L                      
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC                
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 20380 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 55220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -131.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E, F, I, J, C, D, G,            
REMARK 350                    AND CHAINS: H, K, L                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     VAL E    15                                                      
REMARK 465     THR E    16                                                      
REMARK 465     ASP E    17                                                      
REMARK 465     ASN E    18                                                      
REMARK 465     ASN E    19                                                      
REMARK 465     GLY E    20                                                      
REMARK 465     GLU E   129                                                      
REMARK 465     TYR E   130                                                      
REMARK 465     VAL F    15                                                      
REMARK 465     THR F    16                                                      
REMARK 465     ASP F    17                                                      
REMARK 465     ASN F    18                                                      
REMARK 465     ASN F    19                                                      
REMARK 465     GLY F    20                                                      
REMARK 465     SER F   127                                                      
REMARK 465     GLU F   128                                                      
REMARK 465     GLU F   129                                                      
REMARK 465     TYR F   130                                                      
REMARK 465     ALA I     7                                                      
REMARK 465     THR I     8                                                      
REMARK 465     GLU I    36                                                      
REMARK 465     THR I    37                                                      
REMARK 465     THR I    38                                                      
REMARK 465     PRO I    64                                                      
REMARK 465     SER I    65                                                      
REMARK 465     SER I    66                                                      
REMARK 465     LYS I    67                                                      
REMARK 465     THR I    68                                                      
REMARK 465     GLY I    69                                                      
REMARK 465     SER I    70                                                      
REMARK 465     VAL I    71                                                      
REMARK 465     GLU I    86                                                      
REMARK 465     LEU I    87                                                      
REMARK 465     PRO I    88                                                      
REMARK 465     THR I    89                                                      
REMARK 465     THR I    90                                                      
REMARK 465     VAL I    91                                                      
REMARK 465     ALA J     7                                                      
REMARK 465     THR J     8                                                      
REMARK 465     ASP J    39                                                      
REMARK 465     LYS J    40                                                      
REMARK 465     LYS J    67                                                      
REMARK 465     THR J    68                                                      
REMARK 465     GLY J    69                                                      
REMARK 465     SER J    70                                                      
REMARK 465     ILE J    85                                                      
REMARK 465     GLU J    86                                                      
REMARK 465     LEU J    87                                                      
REMARK 465     PRO J    88                                                      
REMARK 465     THR J    89                                                      
REMARK 465     THR J    90                                                      
REMARK 465     VAL J    91                                                      
REMARK 465     VAL G    15                                                      
REMARK 465     THR G    16                                                      
REMARK 465     ASP G    17                                                      
REMARK 465     ASN G    18                                                      
REMARK 465     ASN G    19                                                      
REMARK 465     GLU G   129                                                      
REMARK 465     TYR G   130                                                      
REMARK 465     VAL H    15                                                      
REMARK 465     THR H    16                                                      
REMARK 465     ASP H    17                                                      
REMARK 465     ASN H    18                                                      
REMARK 465     ASN H    19                                                      
REMARK 465     GLY H    20                                                      
REMARK 465     SER H   127                                                      
REMARK 465     GLU H   128                                                      
REMARK 465     GLU H   129                                                      
REMARK 465     TYR H   130                                                      
REMARK 465     ALA K     7                                                      
REMARK 465     THR K     8                                                      
REMARK 465     GLU K    36                                                      
REMARK 465     THR K    37                                                      
REMARK 465     THR K    38                                                      
REMARK 465     PRO K    64                                                      
REMARK 465     SER K    65                                                      
REMARK 465     SER K    66                                                      
REMARK 465     LYS K    67                                                      
REMARK 465     THR K    68                                                      
REMARK 465     GLY K    69                                                      
REMARK 465     SER K    70                                                      
REMARK 465     VAL K    71                                                      
REMARK 465     GLU K    86                                                      
REMARK 465     LEU K    87                                                      
REMARK 465     PRO K    88                                                      
REMARK 465     THR K    89                                                      
REMARK 465     THR K    90                                                      
REMARK 465     VAL K    91                                                      
REMARK 465     ALA L     7                                                      
REMARK 465     THR L     8                                                      
REMARK 465     ASP L    39                                                      
REMARK 465     LYS L    40                                                      
REMARK 465     LYS L    67                                                      
REMARK 465     THR L    68                                                      
REMARK 465     GLY L    69                                                      
REMARK 465     SER L    70                                                      
REMARK 465     ILE L    85                                                      
REMARK 465     GLU L    86                                                      
REMARK 465     LEU L    87                                                      
REMARK 465     PRO L    88                                                      
REMARK 465     THR L    89                                                      
REMARK 465     THR L    90                                                      
REMARK 465     VAL L    91                                                      
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     SER A  112   OXT                                                 
REMARK 480     SER B  112   OXT                                                 
REMARK 480     GLU E   55   CG                                                  
REMARK 480     LYS E  101   CE   NZ                                             
REMARK 480     LYS E  103   CE   NZ                                             
REMARK 480     LYS E  104   CG   CD   CE   NZ                                   
REMARK 480     GLU F   55   CG                                                  
REMARK 480     LYS F  101   CE   NZ                                             
REMARK 480     LYS F  103   CE   NZ                                             
REMARK 480     LYS F  104   CG   CD   CE   NZ                                   
REMARK 480     SER C  112   OXT                                                 
REMARK 480     SER D  112   OXT                                                 
REMARK 480     GLU G   55   CG                                                  
REMARK 480     LYS G  101   CE   NZ                                             
REMARK 480     LYS G  103   CE   NZ                                             
REMARK 480     LYS G  104   CG   CD   CE   NZ                                   
REMARK 480     GLU H   55   CG                                                  
REMARK 480     LYS H  101   CE   NZ                                             
REMARK 480     LYS H  103   CE   NZ                                             
REMARK 480     LYS H  104   CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  20      101.18   -165.57                                   
REMARK 500    ASN A  42     -179.55     65.48                                   
REMARK 500    ASP A  55      -74.54    -43.54                                   
REMARK 500    GLN A  81      -50.25   -139.09                                   
REMARK 500    SER B  10     -152.39   -116.75                                   
REMARK 500    LYS B  13       25.62     42.24                                   
REMARK 500    CYS B  15      118.93    -33.12                                   
REMARK 500    CYS B  16      168.78    179.65                                   
REMARK 500    ASN B  42     -172.69     69.91                                   
REMARK 500    ILE B  51       75.58     51.75                                   
REMARK 500    TRP B  52       80.84   -150.94                                   
REMARK 500    SER B  73       -2.21     70.38                                   
REMARK 500    ASP E  32     -136.47     61.95                                   
REMARK 500    SER E  46      -49.32    -13.02                                   
REMARK 500    ASN E  68     -116.61    -60.48                                   
REMARK 500    ASP E  69      -67.18    -99.23                                   
REMARK 500    ASP E  87       36.97     85.22                                   
REMARK 500    GLU E 108      163.58    178.94                                   
REMARK 500    SER E 127     -137.30   -123.11                                   
REMARK 500    PRO F  25      171.55    -59.26                                   
REMARK 500    ASP F  32     -156.01     63.11                                   
REMARK 500    CYS F  38      107.57    -48.84                                   
REMARK 500    ASN F  47       43.92     29.65                                   
REMARK 500    ASN F  68      -73.44    -59.34                                   
REMARK 500    ASP F  69      -59.08   -141.70                                   
REMARK 500    LEU F  74      104.49   -162.08                                   
REMARK 500    HIS F  79      122.86   -175.56                                   
REMARK 500    LEU F  90      106.67    -54.28                                   
REMARK 500    ASP F  92       48.67    -98.40                                   
REMARK 500    MET F 100       90.71    -62.78                                   
REMARK 500    LEU I  10     -160.72    -74.73                                   
REMARK 500    GLN I  11      107.30   -174.39                                   
REMARK 500    THR I  18      -79.23    -43.30                                   
REMARK 500    LYS I  19       43.89    -76.41                                   
REMARK 500    ASP I  20       36.93   -145.83                                   
REMARK 500    THR I  26     -155.54   -124.19                                   
REMARK 500    LYS I  40     -153.15    -71.33                                   
REMARK 500    ARG I  58       81.26   -163.93                                   
REMARK 500    CYS I  77      152.95    -45.52                                   
REMARK 500    ASN I  78       65.96   -119.03                                   
REMARK 500    GLN I  79     -143.37   -152.30                                   
REMARK 500    CYS I  82       57.47   -105.83                                   
REMARK 500    LYS I  84     -167.49    -63.68                                   
REMARK 500    THR J  18      -83.26    -54.93                                   
REMARK 500    LYS J  19       32.40    -72.17                                   
REMARK 500    ASN J  21       -4.15     69.53                                   
REMARK 500    THR J  37      -95.41   -105.50                                   
REMARK 500    ARG J  58       75.68   -161.30                                   
REMARK 500    PRO J  64      152.75    -46.82                                   
REMARK 500    SER J  65     -169.93   -100.50                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     102 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 113        DISTANCE =  6.40 ANGSTROMS                       
REMARK 525    HOH D 115        DISTANCE =  5.06 ANGSTROMS                       
REMARK 525    HOH C 117        DISTANCE =  5.95 ANGSTROMS                       
REMARK 525    HOH B 120        DISTANCE =  5.28 ANGSTROMS                       
REMARK 525    HOH A 131        DISTANCE =  5.55 ANGSTROMS                       
REMARK 525    HOH A 133        DISTANCE =  6.86 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1M9Z   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2PJY   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2TGI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1REW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1TGK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1TGJ   RELATED DB: PDB                                   
DBREF  3KFD A    1   112  UNP    P01137   TGFB1_HUMAN    279    390             
DBREF  3KFD B    1   112  UNP    P01137   TGFB1_HUMAN    279    390             
DBREF  3KFD E   15   130  UNP    P37173   TGFR2_HUMAN     38    153             
DBREF  3KFD F   15   130  UNP    P37173   TGFR2_HUMAN     38    153             
DBREF  3KFD I    7    91  UNP    P36897   TGFR1_HUMAN     31    115             
DBREF  3KFD J    7    91  UNP    P36897   TGFR1_HUMAN     31    115             
DBREF  3KFD C    1   112  UNP    P01137   TGFB1_HUMAN    279    390             
DBREF  3KFD D    1   112  UNP    P01137   TGFB1_HUMAN    279    390             
DBREF  3KFD G   15   130  UNP    P37173   TGFR2_HUMAN     38    153             
DBREF  3KFD H   15   130  UNP    P37173   TGFR2_HUMAN     38    153             
DBREF  3KFD K    7    91  UNP    P36897   TGFR1_HUMAN     31    115             
DBREF  3KFD L    7    91  UNP    P36897   TGFR1_HUMAN     31    115             
SEQRES   1 A  112  ALA LEU ASP THR ASN TYR CYS PHE SER SER THR GLU LYS          
SEQRES   2 A  112  ASN CYS CYS VAL ARG GLN LEU TYR ILE ASP PHE ARG LYS          
SEQRES   3 A  112  ASP LEU GLY TRP LYS TRP ILE HIS GLU PRO LYS GLY TYR          
SEQRES   4 A  112  HIS ALA ASN PHE CYS LEU GLY PRO CYS PRO TYR ILE TRP          
SEQRES   5 A  112  SER LEU ASP THR GLN TYR SER LYS VAL LEU ALA LEU TYR          
SEQRES   6 A  112  ASN GLN HIS ASN PRO GLY ALA SER ALA ALA PRO CYS CYS          
SEQRES   7 A  112  VAL PRO GLN ALA LEU GLU PRO LEU PRO ILE VAL TYR TYR          
SEQRES   8 A  112  VAL GLY ARG LYS PRO LYS VAL GLU GLN LEU SER ASN MET          
SEQRES   9 A  112  ILE VAL ARG SER CYS LYS CYS SER                              
SEQRES   1 B  112  ALA LEU ASP THR ASN TYR CYS PHE SER SER THR GLU LYS          
SEQRES   2 B  112  ASN CYS CYS VAL ARG GLN LEU TYR ILE ASP PHE ARG LYS          
SEQRES   3 B  112  ASP LEU GLY TRP LYS TRP ILE HIS GLU PRO LYS GLY TYR          
SEQRES   4 B  112  HIS ALA ASN PHE CYS LEU GLY PRO CYS PRO TYR ILE TRP          
SEQRES   5 B  112  SER LEU ASP THR GLN TYR SER LYS VAL LEU ALA LEU TYR          
SEQRES   6 B  112  ASN GLN HIS ASN PRO GLY ALA SER ALA ALA PRO CYS CYS          
SEQRES   7 B  112  VAL PRO GLN ALA LEU GLU PRO LEU PRO ILE VAL TYR TYR          
SEQRES   8 B  112  VAL GLY ARG LYS PRO LYS VAL GLU GLN LEU SER ASN MET          
SEQRES   9 B  112  ILE VAL ARG SER CYS LYS CYS SER                              
SEQRES   1 E  116  VAL THR ASP ASN ASN GLY ALA VAL LYS PHE PRO GLN LEU          
SEQRES   2 E  116  CYS LYS PHE CYS ASP VAL ARG PHE SER THR CYS ASP ASN          
SEQRES   3 E  116  GLN LYS SER CYS MET SER ASN CYS SER ILE THR SER ILE          
SEQRES   4 E  116  CYS GLU LYS PRO GLN GLU VAL CYS VAL ALA VAL TRP ARG          
SEQRES   5 E  116  LYS ASN ASP GLU ASN ILE THR LEU GLU THR VAL CYS HIS          
SEQRES   6 E  116  ASP PRO LYS LEU PRO TYR HIS ASP PHE ILE LEU GLU ASP          
SEQRES   7 E  116  ALA ALA SER PRO LYS CYS ILE MET LYS GLU LYS LYS LYS          
SEQRES   8 E  116  PRO GLY GLU THR PHE PHE MET CYS SER CYS SER SER ASP          
SEQRES   9 E  116  GLU CYS ASN ASP ASN ILE ILE PHE SER GLU GLU TYR              
SEQRES   1 F  116  VAL THR ASP ASN ASN GLY ALA VAL LYS PHE PRO GLN LEU          
SEQRES   2 F  116  CYS LYS PHE CYS ASP VAL ARG PHE SER THR CYS ASP ASN          
SEQRES   3 F  116  GLN LYS SER CYS MET SER ASN CYS SER ILE THR SER ILE          
SEQRES   4 F  116  CYS GLU LYS PRO GLN GLU VAL CYS VAL ALA VAL TRP ARG          
SEQRES   5 F  116  LYS ASN ASP GLU ASN ILE THR LEU GLU THR VAL CYS HIS          
SEQRES   6 F  116  ASP PRO LYS LEU PRO TYR HIS ASP PHE ILE LEU GLU ASP          
SEQRES   7 F  116  ALA ALA SER PRO LYS CYS ILE MET LYS GLU LYS LYS LYS          
SEQRES   8 F  116  PRO GLY GLU THR PHE PHE MET CYS SER CYS SER SER ASP          
SEQRES   9 F  116  GLU CYS ASN ASP ASN ILE ILE PHE SER GLU GLU TYR              
SEQRES   1 I   85  ALA THR ALA LEU GLN CYS PHE CYS HIS LEU CYS THR LYS          
SEQRES   2 I   85  ASP ASN PHE THR CYS VAL THR ASP GLY LEU CYS PHE VAL          
SEQRES   3 I   85  SER VAL THR GLU THR THR ASP LYS VAL ILE HIS ASN SER          
SEQRES   4 I   85  MET CYS ILE ALA GLU ILE ASP LEU ILE PRO ARG ASP ARG          
SEQRES   5 I   85  PRO PHE VAL CYS ALA PRO SER SER LYS THR GLY SER VAL          
SEQRES   6 I   85  THR THR THR TYR CYS CYS ASN GLN ASP HIS CYS ASN LYS          
SEQRES   7 I   85  ILE GLU LEU PRO THR THR VAL                                  
SEQRES   1 J   85  ALA THR ALA LEU GLN CYS PHE CYS HIS LEU CYS THR LYS          
SEQRES   2 J   85  ASP ASN PHE THR CYS VAL THR ASP GLY LEU CYS PHE VAL          
SEQRES   3 J   85  SER VAL THR GLU THR THR ASP LYS VAL ILE HIS ASN SER          
SEQRES   4 J   85  MET CYS ILE ALA GLU ILE ASP LEU ILE PRO ARG ASP ARG          
SEQRES   5 J   85  PRO PHE VAL CYS ALA PRO SER SER LYS THR GLY SER VAL          
SEQRES   6 J   85  THR THR THR TYR CYS CYS ASN GLN ASP HIS CYS ASN LYS          
SEQRES   7 J   85  ILE GLU LEU PRO THR THR VAL                                  
SEQRES   1 C  112  ALA LEU ASP THR ASN TYR CYS PHE SER SER THR GLU LYS          
SEQRES   2 C  112  ASN CYS CYS VAL ARG GLN LEU TYR ILE ASP PHE ARG LYS          
SEQRES   3 C  112  ASP LEU GLY TRP LYS TRP ILE HIS GLU PRO LYS GLY TYR          
SEQRES   4 C  112  HIS ALA ASN PHE CYS LEU GLY PRO CYS PRO TYR ILE TRP          
SEQRES   5 C  112  SER LEU ASP THR GLN TYR SER LYS VAL LEU ALA LEU TYR          
SEQRES   6 C  112  ASN GLN HIS ASN PRO GLY ALA SER ALA ALA PRO CYS CYS          
SEQRES   7 C  112  VAL PRO GLN ALA LEU GLU PRO LEU PRO ILE VAL TYR TYR          
SEQRES   8 C  112  VAL GLY ARG LYS PRO LYS VAL GLU GLN LEU SER ASN MET          
SEQRES   9 C  112  ILE VAL ARG SER CYS LYS CYS SER                              
SEQRES   1 D  112  ALA LEU ASP THR ASN TYR CYS PHE SER SER THR GLU LYS          
SEQRES   2 D  112  ASN CYS CYS VAL ARG GLN LEU TYR ILE ASP PHE ARG LYS          
SEQRES   3 D  112  ASP LEU GLY TRP LYS TRP ILE HIS GLU PRO LYS GLY TYR          
SEQRES   4 D  112  HIS ALA ASN PHE CYS LEU GLY PRO CYS PRO TYR ILE TRP          
SEQRES   5 D  112  SER LEU ASP THR GLN TYR SER LYS VAL LEU ALA LEU TYR          
SEQRES   6 D  112  ASN GLN HIS ASN PRO GLY ALA SER ALA ALA PRO CYS CYS          
SEQRES   7 D  112  VAL PRO GLN ALA LEU GLU PRO LEU PRO ILE VAL TYR TYR          
SEQRES   8 D  112  VAL GLY ARG LYS PRO LYS VAL GLU GLN LEU SER ASN MET          
SEQRES   9 D  112  ILE VAL ARG SER CYS LYS CYS SER                              
SEQRES   1 G  116  VAL THR ASP ASN ASN GLY ALA VAL LYS PHE PRO GLN LEU          
SEQRES   2 G  116  CYS LYS PHE CYS ASP VAL ARG PHE SER THR CYS ASP ASN          
SEQRES   3 G  116  GLN LYS SER CYS MET SER ASN CYS SER ILE THR SER ILE          
SEQRES   4 G  116  CYS GLU LYS PRO GLN GLU VAL CYS VAL ALA VAL TRP ARG          
SEQRES   5 G  116  LYS ASN ASP GLU ASN ILE THR LEU GLU THR VAL CYS HIS          
SEQRES   6 G  116  ASP PRO LYS LEU PRO TYR HIS ASP PHE ILE LEU GLU ASP          
SEQRES   7 G  116  ALA ALA SER PRO LYS CYS ILE MET LYS GLU LYS LYS LYS          
SEQRES   8 G  116  PRO GLY GLU THR PHE PHE MET CYS SER CYS SER SER ASP          
SEQRES   9 G  116  GLU CYS ASN ASP ASN ILE ILE PHE SER GLU GLU TYR              
SEQRES   1 H  116  VAL THR ASP ASN ASN GLY ALA VAL LYS PHE PRO GLN LEU          
SEQRES   2 H  116  CYS LYS PHE CYS ASP VAL ARG PHE SER THR CYS ASP ASN          
SEQRES   3 H  116  GLN LYS SER CYS MET SER ASN CYS SER ILE THR SER ILE          
SEQRES   4 H  116  CYS GLU LYS PRO GLN GLU VAL CYS VAL ALA VAL TRP ARG          
SEQRES   5 H  116  LYS ASN ASP GLU ASN ILE THR LEU GLU THR VAL CYS HIS          
SEQRES   6 H  116  ASP PRO LYS LEU PRO TYR HIS ASP PHE ILE LEU GLU ASP          
SEQRES   7 H  116  ALA ALA SER PRO LYS CYS ILE MET LYS GLU LYS LYS LYS          
SEQRES   8 H  116  PRO GLY GLU THR PHE PHE MET CYS SER CYS SER SER ASP          
SEQRES   9 H  116  GLU CYS ASN ASP ASN ILE ILE PHE SER GLU GLU TYR              
SEQRES   1 K   85  ALA THR ALA LEU GLN CYS PHE CYS HIS LEU CYS THR LYS          
SEQRES   2 K   85  ASP ASN PHE THR CYS VAL THR ASP GLY LEU CYS PHE VAL          
SEQRES   3 K   85  SER VAL THR GLU THR THR ASP LYS VAL ILE HIS ASN SER          
SEQRES   4 K   85  MET CYS ILE ALA GLU ILE ASP LEU ILE PRO ARG ASP ARG          
SEQRES   5 K   85  PRO PHE VAL CYS ALA PRO SER SER LYS THR GLY SER VAL          
SEQRES   6 K   85  THR THR THR TYR CYS CYS ASN GLN ASP HIS CYS ASN LYS          
SEQRES   7 K   85  ILE GLU LEU PRO THR THR VAL                                  
SEQRES   1 L   85  ALA THR ALA LEU GLN CYS PHE CYS HIS LEU CYS THR LYS          
SEQRES   2 L   85  ASP ASN PHE THR CYS VAL THR ASP GLY LEU CYS PHE VAL          
SEQRES   3 L   85  SER VAL THR GLU THR THR ASP LYS VAL ILE HIS ASN SER          
SEQRES   4 L   85  MET CYS ILE ALA GLU ILE ASP LEU ILE PRO ARG ASP ARG          
SEQRES   5 L   85  PRO PHE VAL CYS ALA PRO SER SER LYS THR GLY SER VAL          
SEQRES   6 L   85  THR THR THR TYR CYS CYS ASN GLN ASP HIS CYS ASN LYS          
SEQRES   7 L   85  ILE GLU LEU PRO THR THR VAL                                  
FORMUL  13  HOH   *93(H2 O)                                                     
HELIX    1   1 ASP A    3  PHE A    8  1                                   6    
HELIX    2   2 THR A   56  ASN A   69  1                                  14    
HELIX    3   3 ASP B    3  PHE B    8  1                                   6    
HELIX    4   4 THR B   56  ASN B   69  1                                  14    
HELIX    5   5 GLU E  119  ASP E  122  5                                   4    
HELIX    6   6 GLU F  119  ASP F  122  5                                   4    
HELIX    7   7 ALA J   49  LEU J   53  5                                   5    
HELIX    8   8 PRO J   59  ALA J   63  5                                   5    
HELIX    9   9 ASP C    3  PHE C    8  1                                   6    
HELIX   10  10 THR C   56  ASN C   69  1                                  14    
HELIX   11  11 THR D    4  PHE D    8  1                                   5    
HELIX   12  12 THR D   56  ASN D   69  1                                  14    
HELIX   13  13 GLU G  119  ASN G  121  5                                   3    
HELIX   14  14 GLU H  119  ASN H  121  5                                   3    
HELIX   15  15 ALA L   49  LEU L   53  5                                   5    
HELIX   16  16 PRO L   59  ALA L   63  5                                   5    
SHEET    1   A 2 CYS A  16  ARG A  18  0                                        
SHEET    2   A 2 PHE A  43  LEU 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  HIS A  40 -1  O  TYR A  39   N  ILE A  22           
SHEET    1   C 3 ILE A  33  GLU A  35  0                                        
SHEET    2   C 3 CYS A  78  VAL A  92 -1  O  VAL A  89   N  GLU A  35           
SHEET    3   C 3 LYS A  95  CYS A 111 -1  O  ARG A 107   N  ALA A  82           
SHEET    1   D 2 CYS B  16  ARG B  18  0                                        
SHEET    2   D 2 PHE B  43  LEU B  45 -1  O  PHE B  43   N  ARG B  18           
SHEET    1   E 2 TYR B  21  ASP B  23  0                                        
SHEET    2   E 2 GLY B  38  HIS B  40 -1  O  TYR B  39   N  ILE B  22           
SHEET    1   F 2 CYS B  78  VAL B  92  0                                        
SHEET    2   F 2 LYS B  95  CYS B 111 -1  O  ARG B 107   N  ALA B  82           
SHEET    1   G 2 LEU E  27  LYS E  29  0                                        
SHEET    2   G 2 THR E  51  ILE E  53 -1  O  SER E  52   N  CYS E  28           
SHEET    1   H 5 ASP E  32  PHE E  35  0                                        
SHEET    2   H 5 ILE E  72  HIS E  79 -1  O  LEU E  74   N  ARG E  34           
SHEET    3   H 5 VAL E  60  LYS E  67 -1  N  VAL E  60   O  HIS E  79           
SHEET    4   H 5 GLU E 108  CYS E 115 -1  O  PHE E 111   N  TRP E  65           
SHEET    5   H 5 LYS E 103  LYS E 105 -1  N  LYS E 103   O  PHE E 110           
SHEET    1   I 3 SER E  43  CYS E  44  0                                        
SHEET    2   I 3 ILE E 124  ILE E 125 -1  O  ILE E 124   N  CYS E  44           
SHEET    3   I 3 CYS E  98  ILE E  99  1  N  CYS E  98   O  ILE E 125           
SHEET    1   J 2 LEU F  27  LYS F  29  0                                        
SHEET    2   J 2 THR F  51  ILE F  53 -1  O  SER F  52   N  CYS F  28           
SHEET    1   K 5 ASP F  32  PHE F  35  0                                        
SHEET    2   K 5 THR F  73  HIS F  79 -1  O  THR F  76   N  ASP F  32           
SHEET    3   K 5 VAL F  60  LYS F  67 -1  N  ARG F  66   O  THR F  73           
SHEET    4   K 5 THR F 109  CYS F 115 -1  O  PHE F 111   N  TRP F  65           
SHEET    5   K 5 LYS F 101  GLU F 102 -1  N  LYS F 101   O  MET F 112           
SHEET    1   L 2 CYS F  98  ILE F  99  0                                        
SHEET    2   L 2 ILE F 124  ILE F 125  1  O  ILE F 125   N  CYS F  98           
SHEET    1   M 2 CYS I  12  PHE I  13  0                                        
SHEET    2   M 2 THR I  23  CYS I  24 -1  O  CYS I  24   N  CYS I  12           
SHEET    1   N 3 SER I  45  ILE I  48  0                                        
SHEET    2   N 3 LEU I  29  SER I  33 -1  N  PHE I  31   O  MET I  46           
SHEET    3   N 3 THR I  74  TYR I  75 -1  O  TYR I  75   N  VAL I  32           
SHEET    1   O 2 GLN J  11  PHE J  13  0                                        
SHEET    2   O 2 THR J  23  VAL J  25 -1  O  CYS J  24   N  CYS J  12           
SHEET    1   P 3 ILE J  42  ILE J  48  0                                        
SHEET    2   P 3 LEU J  29  THR J  35 -1  N  PHE J  31   O  MET J  46           
SHEET    3   P 3 THR J  72  CYS J  77 -1  O  CYS J  77   N  CYS J  30           
SHEET    1   Q 2 CYS C  16  ARG C  18  0                                        
SHEET    2   Q 2 PHE C  43  LEU C  45 -1  O  PHE C  43   N  ARG C  18           
SHEET    1   R 2 TYR C  21  ASP C  23  0                                        
SHEET    2   R 2 GLY C  38  HIS C  40 -1  O  TYR C  39   N  ILE C  22           
SHEET    1   S 3 ILE C  33  GLU C  35  0                                        
SHEET    2   S 3 CYS C  78  VAL C  92 -1  O  VAL C  89   N  GLU C  35           
SHEET    3   S 3 LYS C  95  CYS C 111 -1  O  ILE C 105   N  GLU C  84           
SHEET    1   T 3 LEU D   2  ASP D   3  0                                        
SHEET    2   T 3 LYS D  95  CYS D 111 -1  O  CYS D 109   N  LEU D   2           
SHEET    3   T 3 CYS D  78  VAL D  92 -1  N  VAL D  79   O  LYS D 110           
SHEET    1   U 2 CYS D  16  ARG D  18  0                                        
SHEET    2   U 2 PHE D  43  LEU D  45 -1  O  PHE D  43   N  ARG D  18           
SHEET    1   V 2 TYR D  21  ASP D  23  0                                        
SHEET    2   V 2 GLY D  38  HIS D  40 -1  O  TYR D  39   N  ILE D  22           
SHEET    1   W 2 LEU G  27  LYS G  29  0                                        
SHEET    2   W 2 THR G  51  ILE G  53 -1  O  SER G  52   N  CYS G  28           
SHEET    1   X 5 ASP G  32  PHE G  35  0                                        
SHEET    2   X 5 ILE G  72  HIS G  79 -1  O  THR G  76   N  ASP G  32           
SHEET    3   X 5 VAL G  60  LYS G  67 -1  N  VAL G  64   O  GLU G  75           
SHEET    4   X 5 GLU G 108  CYS G 115 -1  O  PHE G 111   N  TRP G  65           
SHEET    5   X 5 LYS G 103  LYS G 105 -1  N  LYS G 103   O  PHE G 110           
SHEET    1   Y 3 SER G  43  MET G  45  0                                        
SHEET    2   Y 3 ASN G 123  ILE G 125 -1  O  ILE G 124   N  CYS G  44           
SHEET    3   Y 3 CYS G  98  ILE G  99  1  N  CYS G  98   O  ILE G 125           
SHEET    1   Z 2 LEU H  27  LYS H  29  0                                        
SHEET    2   Z 2 THR H  51  ILE H  53 -1  O  SER H  52   N  CYS H  28           
SHEET    1  AA 5 ARG H  34  PHE H  35  0                                        
SHEET    2  AA 5 THR H  73  HIS H  79 -1  O  LEU H  74   N  ARG H  34           
SHEET    3  AA 5 VAL H  60  LYS H  67 -1  N  ARG H  66   O  THR H  73           
SHEET    4  AA 5 THR H 109  CYS H 115 -1  O  PHE H 111   N  TRP H  65           
SHEET    5  AA 5 LYS H 101  GLU H 102 -1  N  LYS H 101   O  MET H 112           
SHEET    1  AB 3 SER H  43  MET H  45  0                                        
SHEET    2  AB 3 ASN H 123  ILE H 125 -1  O  ILE H 124   N  CYS H  44           
SHEET    3  AB 3 CYS H  98  ILE H  99  1  N  CYS H  98   O  ILE H 125           
SHEET    1  AC 2 CYS K  12  PHE K  13  0                                        
SHEET    2  AC 2 THR K  23  CYS K  24 -1  O  CYS K  24   N  CYS K  12           
SHEET    1  AD 3 SER K  45  ILE K  48  0                                        
SHEET    2  AD 3 LEU K  29  SER K  33 -1  N  PHE K  31   O  MET K  46           
SHEET    3  AD 3 THR K  74  CYS K  77 -1  O  TYR K  75   N  VAL K  32           
SHEET    1  AE 2 GLN L  11  PHE L  13  0                                        
SHEET    2  AE 2 THR L  23  VAL L  25 -1  O  CYS L  24   N  CYS L  12           
SHEET    1  AF 3 ILE L  42  ILE L  48  0                                        
SHEET    2  AF 3 LEU L  29  THR L  35 -1  N  THR L  35   O  ILE L  42           
SHEET    3  AF 3 THR L  72  CYS L  77 -1  O  CYS L  77   N  CYS L  30           
SSBOND   1 CYS A    7    CYS A   16                          1555   1555  2.03  
SSBOND   2 CYS A   15    CYS A   78                          1555   1555  2.03  
SSBOND   3 CYS A   44    CYS A  109                          1555   1555  2.03  
SSBOND   4 CYS A   48    CYS A  111                          1555   1555  2.03  
SSBOND   5 CYS A   77    CYS B   77                          1555   1555  2.03  
SSBOND   6 CYS B    7    CYS B   16                          1555   1555  2.03  
SSBOND   7 CYS B   15    CYS B   78                          1555   1555  2.03  
SSBOND   8 CYS B   44    CYS B  109                          1555   1555  2.03  
SSBOND   9 CYS B   48    CYS B  111                          1555   1555  2.03  
SSBOND  10 CYS E   28    CYS E   61                          1555   1555  2.03  
SSBOND  11 CYS E   31    CYS E   48                          1555   1555  2.01  
SSBOND  12 CYS E   38    CYS E   44                          1555   1555  2.03  
SSBOND  13 CYS E   54    CYS E   78                          1555   1555  2.03  
SSBOND  14 CYS E   98    CYS E  113                          1555   1555  2.03  
SSBOND  15 CYS E  115    CYS E  120                          1555   1555  2.03  
SSBOND  16 CYS F   28    CYS F   61                          1555   1555  2.03  
SSBOND  17 CYS F   31    CYS F   48                          1555   1555  2.03  
SSBOND  18 CYS F   38    CYS F   44                          1555   1555  2.03  
SSBOND  19 CYS F   54    CYS F   78                          1555   1555  2.03  
SSBOND  20 CYS F   98    CYS F  113                          1555   1555  2.03  
SSBOND  21 CYS F  115    CYS F  120                          1555   1555  2.03  
SSBOND  22 CYS I   12    CYS I   30                          1555   1555  2.03  
SSBOND  23 CYS I   14    CYS I   17                          1555   1555  2.03  
SSBOND  24 CYS I   24    CYS I   47                          1555   1555  2.03  
SSBOND  25 CYS I   62    CYS I   76                          1555   1555  2.03  
SSBOND  26 CYS I   77    CYS I   82                          1555   1555  2.03  
SSBOND  27 CYS J   12    CYS J   30                          1555   1555  2.03  
SSBOND  28 CYS J   14    CYS J   17                          1555   1555  2.03  
SSBOND  29 CYS J   24    CYS J   47                          1555   1555  2.03  
SSBOND  30 CYS J   62    CYS J   76                          1555   1555  2.03  
SSBOND  31 CYS J   77    CYS J   82                          1555   1555  2.03  
SSBOND  32 CYS C    7    CYS C   16                          1555   1555  2.03  
SSBOND  33 CYS C   15    CYS C   78                          1555   1555  2.03  
SSBOND  34 CYS C   44    CYS C  109                          1555   1555  2.03  
SSBOND  35 CYS C   48    CYS C  111                          1555   1555  2.03  
SSBOND  36 CYS C   77    CYS D   77                          1555   1555  2.03  
SSBOND  37 CYS D    7    CYS D   16                          1555   1555  2.02  
SSBOND  38 CYS D   15    CYS D   78                          1555   1555  2.03  
SSBOND  39 CYS D   44    CYS D  109                          1555   1555  2.03  
SSBOND  40 CYS D   48    CYS D  111                          1555   1555  2.03  
SSBOND  41 CYS G   28    CYS G   61                          1555   1555  2.03  
SSBOND  42 CYS G   31    CYS G   48                          1555   1555  2.03  
SSBOND  43 CYS G   38    CYS G   44                          1555   1555  2.03  
SSBOND  44 CYS G   54    CYS G   78                          1555   1555  2.03  
SSBOND  45 CYS G   98    CYS G  113                          1555   1555  2.03  
SSBOND  46 CYS G  115    CYS G  120                          1555   1555  2.03  
SSBOND  47 CYS H   28    CYS H   61                          1555   1555  2.03  
SSBOND  48 CYS H   31    CYS H   48                          1555   1555  2.03  
SSBOND  49 CYS H   38    CYS H   44                          1555   1555  2.03  
SSBOND  50 CYS H   54    CYS H   78                          1555   1555  2.03  
SSBOND  51 CYS H   98    CYS H  113                          1555   1555  2.03  
SSBOND  52 CYS H  115    CYS H  120                          1555   1555  2.03  
SSBOND  53 CYS K   12    CYS K   30                          1555   1555  2.03  
SSBOND  54 CYS K   14    CYS K   17                          1555   1555  2.03  
SSBOND  55 CYS K   24    CYS K   47                          1555   1555  2.03  
SSBOND  56 CYS K   62    CYS K   76                          1555   1555  2.03  
SSBOND  57 CYS K   77    CYS K   82                          1555   1555  2.03  
SSBOND  58 CYS L   12    CYS L   30                          1555   1555  2.03  
SSBOND  59 CYS L   14    CYS L   17                          1555   1555  2.03  
SSBOND  60 CYS L   24    CYS L   47                          1555   1555  2.03  
SSBOND  61 CYS L   62    CYS L   76                          1555   1555  2.03  
SSBOND  62 CYS L   77    CYS L   82                          1555   1555  2.03  
CISPEP   1 GLU A   35    PRO A   36          0        -4.04                     
CISPEP   2 GLU B   35    PRO B   36          0         1.58                     
CISPEP   3 ILE I   54    PRO I   55          0        -4.15                     
CISPEP   4 ILE J   54    PRO J   55          0        -2.02                     
CISPEP   5 GLU C   35    PRO C   36          0        -4.94                     
CISPEP   6 GLU D   35    PRO D   36          0         0.68                     
CISPEP   7 ILE K   54    PRO K   55          0        -4.29                     
CISPEP   8 ILE L   54    PRO L   55          0        -2.27                     
CRYST1   37.700   99.350  102.700  64.01  84.47  84.34 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      0.026527 -0.002629 -0.001587        0.00000                         
SCALE2      0.000000  0.010114 -0.004856        0.00000                         
SCALE3      0.000000  0.000000  0.010851        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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