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Database: PDB
Entry: 2PJY
LinkDB: 2PJY
Original site: 2PJY 
HEADER    CYTOKINE/CYTOKINE RECEPTOR              16-APR-07   2PJY              
TITLE     STRUCTURAL BASIS FOR COOPERATIVE ASSEMBLY OF THE TGF-BETA SIGNALING   
TITLE    2 COMPLEX                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRANSFORMING GROWTH FACTOR BETA-3;                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: TGF-BETA-3;                                                 
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: TGF-BETA RECEPTOR TYPE-2;                                  
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: EXTRACELLULAR DOMAIN;                                      
COMPND  10 SYNONYM: TGF-BETA RECEPTOR TYPE II, TGFR-2, TGF-BETA TYPE II         
COMPND  11 RECEPTOR, TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE II, TBETAR-  
COMPND  12 II;                                                                  
COMPND  13 EC: 2.7.11.30;                                                       
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MUTATION: YES;                                                       
COMPND  16 MOL_ID: 3;                                                           
COMPND  17 MOLECULE: TGF-BETA RECEPTOR TYPE-1;                                  
COMPND  18 CHAIN: C;                                                            
COMPND  19 FRAGMENT: EXTRACELLULAR DOMAIN;                                      
COMPND  20 SYNONYM: TGF-BETA RECEPTOR TYPE I, TGFR-1, TGF-BETA TYPE I RECEPTOR, 
COMPND  21 TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I, TBETAR-I,           
COMPND  22 SERINE/THREONINE-PROTEIN KINASE RECEPTOR R4, SKR4, ACTIVIN RECEPTOR- 
COMPND  23 LIKE KINASE 5, ALK-5;                                                
COMPND  24 EC: 2.7.11.30;                                                       
COMPND  25 ENGINEERED: YES;                                                     
COMPND  26 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: TGFB3;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: TGFBR2;                                                        
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 GENE: TGFBR1;                                                        
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TERNARY COMPLEX, THREE FINGER TOXIN, CYTOKINE-CYTOKINE RECEPTOR       
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.GROPPE,C.ZUBIETA                                                    
REVDAT   4   13-JUL-11 2PJY    1       VERSN                                    
REVDAT   3   16-MAR-10 2PJY    1       JRNL                                     
REVDAT   2   24-FEB-09 2PJY    1       VERSN                                    
REVDAT   1   05-FEB-08 2PJY    0                                                
JRNL        AUTH   J.GROPPE,C.S.HINCK,P.SAMAVARCHI-TEHRANI,C.ZUBIETA,           
JRNL        AUTH 2 J.P.SCHUERMANN,A.B.TAYLOR,P.M.SCHWARZ,J.L.WRANA,A.P.HINCK    
JRNL        TITL   COOPERATIVE ASSEMBLY OF TGF-BETA SUPERFAMILY SIGNALING       
JRNL        TITL 2 COMPLEXES IS MEDIATED BY TWO DISPARATE MECHANISMS AND        
JRNL        TITL 3 DISTINCT MODES OF RECEPTOR BINDING.                          
JRNL        REF    MOL.CELL                      V.  29   157 2008              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   18243111                                                     
JRNL        DOI    10.1016/J.MOLCEL.2007.11.039                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 6701                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.244                           
REMARK   3   R VALUE            (WORKING SET) : 0.242                           
REMARK   3   FREE R VALUE                     : 0.297                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 312                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.08                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 491                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3530                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 38                           
REMARK   3   BIN FREE R VALUE                    : 0.3870                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2328                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 9                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 75.06                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.65                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.14000                                              
REMARK   3    B22 (A**2) : 0.14000                                              
REMARK   3    B33 (A**2) : -0.21000                                             
REMARK   3    B12 (A**2) : 0.07000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.566         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.508         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 63.761        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.924                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.906                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2396 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3264 ; 0.809 ; 1.958       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   296 ; 4.640 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   103 ;36.337 ;25.146       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   399 ;14.569 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ; 9.433 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   367 ; 0.055 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1798 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   934 ; 0.152 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1616 ; 0.290 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    67 ; 0.089 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    70 ; 0.243 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     4 ; 0.158 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1549 ; 0.101 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2456 ; 0.186 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   958 ; 0.140 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   808 ; 0.247 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 11                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A    48                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.4930   9.7510 -12.8850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6171 T22:   0.2455                                     
REMARK   3      T33:   0.1784 T12:   0.2118                                     
REMARK   3      T13:  -0.0047 T23:   0.0111                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4425 L22:  10.7537                                     
REMARK   3      L33:   2.2316 L12:   1.2650                                     
REMARK   3      L13:   1.9817 L23:  -1.2043                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1158 S12:  -0.0723 S13:  -0.0596                       
REMARK   3      S21:   0.0088 S22:  -0.1452 S23:   0.6767                       
REMARK   3      S31:   0.3098 S32:  -0.2540 S33:   0.0294                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    49        A    68                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.8120 -12.9400   0.0340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8137 T22:   0.3055                                     
REMARK   3      T33:   0.4862 T12:  -0.0939                                     
REMARK   3      T13:  -0.1604 T23:   0.1050                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4893 L22:   4.0170                                     
REMARK   3      L33:   8.7582 L12:  -2.5712                                     
REMARK   3      L13:   5.4940 L23:  -1.8893                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.9639 S12:   0.3982 S13:   0.7434                       
REMARK   3      S21:  -1.2105 S22:  -0.2916 S23:   0.8684                       
REMARK   3      S31:   0.9989 S32:  -0.6442 S33:  -0.6723                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    69        A   112                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.1460  10.1720  -7.3740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6407 T22:   0.3068                                     
REMARK   3      T33:   0.2161 T12:   0.1525                                     
REMARK   3      T13:  -0.1015 T23:  -0.0014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2251 L22:  12.4868                                     
REMARK   3      L33:   3.3905 L12:   4.3224                                     
REMARK   3      L13:  -1.2514 L23:  -4.5541                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2704 S12:  -0.3088 S13:  -0.1348                       
REMARK   3      S21:   0.5077 S22:  -0.4210 S23:  -0.1804                       
REMARK   3      S31:   0.1896 S32:   0.1215 S33:   0.1506                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    20        B    27                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.5810  33.0680   4.3600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5191 T22:   0.4529                                     
REMARK   3      T33:  -0.1206 T12:   0.2416                                     
REMARK   3      T13:  -0.1891 T23:   0.2673                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  32.2498 L22:   4.1842                                     
REMARK   3      L33:  50.4218 L12:  11.6164                                     
REMARK   3      L13:  40.3248 L23:  14.5250                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.1703 S12:  -0.1358 S13:  -1.0442                       
REMARK   3      S21:   0.2902 S22:   0.4981 S23:   0.7361                       
REMARK   3      S31:   1.5223 S32:  -0.5878 S33:  -1.6684                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    28        B    38                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.6290  43.4360 -16.9710              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8230 T22:   0.1985                                     
REMARK   3      T33:   0.2947 T12:   0.1196                                     
REMARK   3      T13:  -0.0445 T23:  -0.1679                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3247 L22:   0.2860                                     
REMARK   3      L33:  12.1226 L12:   0.6007                                     
REMARK   3      L13:   2.8884 L23:  -1.0358                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8441 S12:   0.0329 S13:   1.1909                       
REMARK   3      S21:  -0.2763 S22:   0.7373 S23:  -0.8082                       
REMARK   3      S31:  -0.1922 S32:   0.6543 S33:   0.1068                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    39        B    77                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.6990  45.8350 -13.1720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5682 T22:   0.1791                                     
REMARK   3      T33:   0.3147 T12:   0.0502                                     
REMARK   3      T13:  -0.0917 T23:  -0.2306                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.5661 L22:   9.2049                                     
REMARK   3      L33:   6.2362 L12:  -2.2751                                     
REMARK   3      L13:  -1.7418 L23:  -1.0621                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2882 S12:   0.3082 S13:   0.6632                       
REMARK   3      S21:  -0.4569 S22:  -0.1139 S23:  -0.2627                       
REMARK   3      S31:  -0.6499 S32:   0.2581 S33:  -0.1743                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    78        B   110                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.7120  52.9310  -4.9690              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9755 T22:   0.2329                                     
REMARK   3      T33:   0.5319 T12:   0.0192                                     
REMARK   3      T13:  -0.1969 T23:  -0.4263                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.2720 L22:   8.6272                                     
REMARK   3      L33:   9.3798 L12:  -6.0855                                     
REMARK   3      L13:  -3.7774 L23:  -3.5481                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1598 S12:  -0.2762 S13:   1.8376                       
REMARK   3      S21:   0.1334 S22:   0.6143 S23:  -0.7614                       
REMARK   3      S31:  -0.9436 S32:   0.5289 S33:  -0.4544                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   111        B   126                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.8040  44.3930  -7.5650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4331 T22:   0.1886                                     
REMARK   3      T33:   0.1238 T12:   0.1840                                     
REMARK   3      T13:  -0.1339 T23:  -0.2116                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2152 L22:  21.4467                                     
REMARK   3      L33:   9.8327 L12:  -9.1170                                     
REMARK   3      L13:  -0.9324 L23:  -7.7462                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3552 S12:  -0.8809 S13:   0.1949                       
REMARK   3      S21:   0.4920 S22:   0.3181 S23:   1.2350                       
REMARK   3      S31:  -0.1545 S32:  -0.6778 S33:   0.0371                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    10        C    37                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.2550  16.2750  15.5920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5362 T22:   0.3144                                     
REMARK   3      T33:   0.2339 T12:  -0.1161                                     
REMARK   3      T13:  -0.0571 T23:  -0.0533                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6044 L22:   9.6792                                     
REMARK   3      L33:  10.2700 L12:  -1.4146                                     
REMARK   3      L13:   3.2712 L23:  -3.6654                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1809 S12:  -0.1712 S13:  -0.5597                       
REMARK   3      S21:  -0.0648 S22:  -0.1878 S23:  -0.0237                       
REMARK   3      S31:   0.4261 S32:  -0.3068 S33:   0.3687                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    38        C    60                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.8330  19.9380   7.0430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5877 T22:   0.1121                                     
REMARK   3      T33:   0.1802 T12:  -0.0490                                     
REMARK   3      T13:  -0.1900 T23:  -0.1031                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  15.9666 L22:  11.7998                                     
REMARK   3      L33:   4.5157 L12:   2.0303                                     
REMARK   3      L13:   3.5089 L23:  -4.8323                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5592 S12:  -0.1942 S13:  -0.1448                       
REMARK   3      S21:  -0.3345 S22:  -0.6657 S23:   0.4811                       
REMARK   3      S31:   0.3409 S32:   0.1212 S33:   0.1065                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    61        C    87                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.2160  24.2880  12.7230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9700 T22:   0.4977                                     
REMARK   3      T33:   0.5083 T12:   0.2304                                     
REMARK   3      T13:   0.1124 T23:  -0.1018                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5823 L22:   7.3465                                     
REMARK   3      L33:  10.6964 L12:  -0.2449                                     
REMARK   3      L13:   2.2890 L23:  -4.4703                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2156 S12:  -0.7391 S13:   0.6437                       
REMARK   3      S21:   0.2815 S22:   0.2659 S23:   1.5607                       
REMARK   3      S31:  -1.4530 S32:  -2.0077 S33:  -0.4816                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2PJY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-APR-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB042460.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-AUG-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL11-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 325 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6710                               
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     (%) : 90.3                               
REMARK 200  DATA REDUNDANCY                : 8.700                              
REMARK 200  R MERGE                    (I) : 0.07400                            
REMARK 200  R SYM                      (I) : 0.07800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.2000                            
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) : 3.29                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.30                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.59800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.63000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: SOLVE   ;   MOLREP                                    
REMARK 200 STARTING MODEL: PDB ENTRY 1KTZ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-20% PEG 3350, 0.4-0.65 M CALCIUM      
REMARK 280  ACETATE, 0.1-0.25M NACL, PH 7.5, VAPOR DIFFUSION, HANGING DROP,     
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      169.57333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       84.78667            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      127.18000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       42.39333            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      211.96667            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      169.57333            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       84.78667            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       42.39333            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000      127.18000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      211.96667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8880 ANGSTROM**2                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A   9    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  37    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    ASN A  42      176.84     64.06                                   
REMARK 500    SER A  53       57.95     33.19                                   
REMARK 500    THR A  56     -168.92   -119.49                                   
REMARK 500    ASP B  32     -148.82     57.99                                   
REMARK 500    ASN B  68     -145.97   -106.47                                   
REMARK 500    GLU B  70      -81.11    -92.68                                   
REMARK 500    LYS B  82       48.10    -88.70                                   
REMARK 500    SER B 116       70.23   -112.36                                   
REMARK 500    THR C  38       78.03     63.43                                   
REMARK 500    ARG C  58       87.01   -157.22                                   
REMARK 500    PRO C  64     -179.65    -66.83                                   
REMARK 500    HIS C  81       24.50     47.96                                   
REMARK 500    ASN C  83       29.12    -79.09                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  2PJY A    1   112  UNP    P10600   TGFB3_HUMAN    301    412             
DBREF  2PJY B   19   126  UNP    P37173   TGFR2_HUMAN     42    149             
DBREF  2PJY C    9    87  UNP    P36897   TGFR1_HUMAN     33    111             
SEQADV 2PJY ALA B   19  UNP  P37173    ASN    42 ENGINEERED                     
SEQADV 2PJY SER C   46  UNP  P36897    MET    70 ENGINEERED                     
SEQRES   1 A  112  ALA LEU ASP THR ASN TYR CYS PHE ARG ASN LEU GLU GLU          
SEQRES   2 A  112  ASN CYS CYS VAL ARG PRO LEU TYR ILE ASP PHE ARG GLN          
SEQRES   3 A  112  ASP LEU GLY TRP LYS TRP VAL HIS GLU PRO LYS GLY TYR          
SEQRES   4 A  112  TYR ALA ASN PHE CYS SER GLY PRO CYS PRO TYR LEU ARG          
SEQRES   5 A  112  SER ALA ASP THR THR HIS SER THR VAL LEU GLY LEU TYR          
SEQRES   6 A  112  ASN THR LEU ASN PRO GLU ALA SER ALA SER PRO CYS CYS          
SEQRES   7 A  112  VAL PRO GLN ASP LEU GLU PRO LEU THR ILE LEU TYR TYR          
SEQRES   8 A  112  VAL GLY ARG THR PRO LYS VAL GLU GLN LEU SER ASN MET          
SEQRES   9 A  112  VAL VAL LYS SER CYS LYS CYS SER                              
SEQRES   1 B  108  ALA GLY ALA VAL LYS PHE PRO GLN LEU CYS LYS PHE CYS          
SEQRES   2 B  108  ASP VAL ARG PHE SER THR CYS ASP ASN GLN LYS SER CYS          
SEQRES   3 B  108  MET SER ASN CYS SER ILE THR SER ILE CYS GLU LYS PRO          
SEQRES   4 B  108  GLN GLU VAL CYS VAL ALA VAL TRP ARG LYS ASN ASP GLU          
SEQRES   5 B  108  ASN ILE THR LEU GLU THR VAL CYS HIS ASP PRO LYS LEU          
SEQRES   6 B  108  PRO TYR HIS ASP PHE ILE LEU GLU ASP ALA ALA SER PRO          
SEQRES   7 B  108  LYS CYS ILE MET LYS GLU LYS LYS LYS PRO GLY GLU THR          
SEQRES   8 B  108  PHE PHE MET CYS SER CYS SER SER ASP GLU CYS ASN ASP          
SEQRES   9 B  108  ASN ILE ILE PHE                                              
SEQRES   1 C   79  ALA LEU GLN CYS PHE CYS HIS LEU CYS THR LYS ASP ASN          
SEQRES   2 C   79  PHE THR CYS VAL THR ASP GLY LEU CYS PHE VAL SER VAL          
SEQRES   3 C   79  THR GLU THR THR ASP LYS VAL ILE HIS ASN SER SER CYS          
SEQRES   4 C   79  ILE ALA GLU ILE ASP LEU ILE PRO ARG ASP ARG PRO PHE          
SEQRES   5 C   79  VAL CYS ALA PRO SER SER LYS THR GLY SER VAL THR THR          
SEQRES   6 C   79  THR TYR CYS CYS ASN GLN ASP HIS CYS ASN LYS ILE GLU          
SEQRES   7 C   79  LEU                                                          
FORMUL   4  HOH   *9(H2 O)                                                      
HELIX    1   1 THR A    4  PHE A    8  1                                   5    
HELIX    2   2 PHE A   24  LEU A   28  1                                   5    
HELIX    3   3 THR A   56  ASN A   69  1                                  14    
HELIX    4   4 GLU B  119  ASN B  121  5                                   3    
HELIX    5   5 PRO C   59  ALA C   63  5                                   5    
HELIX    6   6 PRO C   64  GLY C   69  1                                   6    
SHEET    1   A 3 LEU A   2  ASP A   3  0                                        
SHEET    2   A 3 SER A 108  SER A 112 -1  O  CYS A 109   N  LEU A   2           
SHEET    3   A 3 CYS A  77  PRO A  80 -1  N  VAL A  79   O  LYS A 110           
SHEET    1   B 2 CYS A  16  ARG A  18  0                                        
SHEET    2   B 2 PHE A  43  SER A  45 -1  O  PHE A  43   N  ARG A  18           
SHEET    1   C 2 TYR A  21  ASP A  23  0                                        
SHEET    2   C 2 GLY A  38  TYR A  40 -1  O  TYR A  39   N  ILE A  22           
SHEET    1   D 3 VAL A  33  GLU A  35  0                                        
SHEET    2   D 3 LEU A  83  VAL A  92 -1  O  LEU A  89   N  GLU A  35           
SHEET    3   D 3 THR A  95  VAL A 106 -1  O  LYS A  97   N  TYR A  90           
SHEET    1   E 4 VAL A  33  GLU A  35  0                                        
SHEET    2   E 4 LEU A  83  VAL A  92 -1  O  LEU A  89   N  GLU A  35           
SHEET    3   E 4 THR B  51  ILE B  53  1  O  ILE B  53   N  TYR A  91           
SHEET    4   E 4 LEU B  27  LYS B  29 -1  N  CYS B  28   O  SER B  52           
SHEET    1   F 5 ASP B  32  PHE B  35  0                                        
SHEET    2   F 5 ILE B  72  HIS B  79 -1  O  LEU B  74   N  ARG B  34           
SHEET    3   F 5 VAL B  60  LYS B  67 -1  N  ARG B  66   O  THR B  73           
SHEET    4   F 5 GLU B 108  CYS B 115 -1  O  PHE B 111   N  TRP B  65           
SHEET    5   F 5 LYS B 101  LYS B 105 -1  N  LYS B 103   O  PHE B 110           
SHEET    1   G 3 SER B  43  MET B  45  0                                        
SHEET    2   G 3 ASN B 123  ILE B 125 -1  O  ILE B 124   N  CYS B  44           
SHEET    3   G 3 CYS B  98  ILE B  99  1  N  CYS B  98   O  ILE B 125           
SHEET    1   H 2 LEU C  10  PHE C  13  0                                        
SHEET    2   H 2 THR C  23  THR C  26 -1  O  THR C  26   N  LEU C  10           
SHEET    1   I 3 ILE C  42  ILE C  48  0                                        
SHEET    2   I 3 LEU C  29  THR C  35 -1  N  LEU C  29   O  ILE C  48           
SHEET    3   I 3 THR C  72  CYS C  77 -1  O  CYS C  77   N  CYS C  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 A   77                          1555   8555  2.05  
SSBOND   6 CYS B   28    CYS B   61                          1555   1555  2.03  
SSBOND   7 CYS B   31    CYS B   48                          1555   1555  2.03  
SSBOND   8 CYS B   38    CYS B   44                          1555   1555  2.03  
SSBOND   9 CYS B   54    CYS B   78                          1555   1555  2.03  
SSBOND  10 CYS B   98    CYS B  113                          1555   1555  2.03  
SSBOND  11 CYS B  115    CYS B  120                          1555   1555  2.03  
SSBOND  12 CYS C   12    CYS C   30                          1555   1555  2.03  
SSBOND  13 CYS C   14    CYS C   17                          1555   1555  2.03  
SSBOND  14 CYS C   24    CYS C   47                          1555   1555  2.03  
SSBOND  15 CYS C   62    CYS C   76                          1555   1555  2.03  
SSBOND  16 CYS C   77    CYS C   82                          1555   1555  2.02  
CISPEP   1 GLU A   35    PRO A   36          0        -2.67                     
CISPEP   2 ILE C   54    PRO C   55          0       -12.16                     
CRYST1   66.920   66.920  254.360  90.00  90.00 120.00 P 65 2 2     12          
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      0.014943  0.008627  0.000000        0.00000                         
SCALE2      0.000000  0.017255  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003931        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system