GenomeNet

Database: PDB
Entry: 5VQF
LinkDB: 5VQF
Original site: 5VQF 
HEADER    PROTEIN BINDING                         08-MAY-17   5VQF              
TITLE     CRYSTAL STRUCTURE OF PRO-TGF-BETA 1                                   
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;                                                 
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIG;                                                
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 GENE: TGFB1;                                                         
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: CHO-LEC3.2.8.1;                         
SOURCE   9 EXPRESSION_SYSTEM_TISSUE: OVARY;                                     
SOURCE  10 EXPRESSION_SYSTEM_CELL: EPITHELIAL;                                  
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PEF1-PURO                                 
KEYWDS    PRO-COMPLEX, LATENCY, HOMODIMER, PROTEIN BINDING                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.ZHAO,S.XU,X.DONG,C.LU,T.A.SPRINGER                                  
REVDAT   5   29-JUL-20 5VQF    1       COMPND REMARK HETNAM LINK                
REVDAT   5 2                   1       SITE   ATOM                              
REVDAT   4   11-DEC-19 5VQF    1       REMARK                                   
REVDAT   3   14-FEB-18 5VQF    1       JRNL                                     
REVDAT   2   22-NOV-17 5VQF    1       COMPND JRNL   SEQADV                     
REVDAT   1   15-NOV-17 5VQF    0                                                
JRNL        AUTH   B.ZHAO,S.XU,X.DONG,C.LU,T.A.SPRINGER                         
JRNL        TITL   PRODOMAIN-GROWTH FACTOR SWAPPING IN THE STRUCTURE OF         
JRNL        TITL 2 PRO-TGF-BETA 1.                                              
JRNL        REF    J. BIOL. CHEM.                V. 293  1579 2018              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   29109152                                                     
JRNL        DOI    10.1074/JBC.M117.809657                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.SHI,J.ZHU,R.WANG,X.CHEN,L.MI,T.WALZ,T.A.SPRINGER           
REMARK   1  TITL   LATENT TGF-BETA STRUCTURE AND ACTIVATION.                    
REMARK   1  REF    NATURE                        V. 474   343 2011              
REMARK   1  REFN                   ESSN 1476-4687                               
REMARK   1  PMID   21677751                                                     
REMARK   1  DOI    10.1038/NATURE10152                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11.1_2575: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.14                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 39887                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.241                           
REMARK   3   R VALUE            (WORKING SET) : 0.239                           
REMARK   3   FREE R VALUE                     : 0.280                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.390                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1354                            
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 37.1448 -  6.2390    0.78     3182   111  0.2486 0.2705        
REMARK   3     2  6.2390 -  4.9558    0.98     3952   135  0.2241 0.2591        
REMARK   3     3  4.9558 -  4.3304    0.98     3955   143  0.1863 0.2375        
REMARK   3     4  4.3304 -  3.9350    0.99     3951   132  0.2165 0.2888        
REMARK   3     5  3.9350 -  3.6532    0.99     3907   142  0.2443 0.2791        
REMARK   3     6  3.6532 -  3.4380    0.98     3959   135  0.2639 0.3142        
REMARK   3     7  3.4380 -  3.2659    0.98     3949   136  0.2825 0.2956        
REMARK   3     8  3.2659 -  3.1238    0.98     3892   137  0.3413 0.3986        
REMARK   3     9  3.1238 -  3.0036    0.98     3909   138  0.4023 0.4584        
REMARK   3    10  3.0036 -  2.9000    0.98     3877   145  0.4519 0.5197        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.640            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 38.270           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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      :  0.005          11030                                  
REMARK   3   ANGLE     :  0.849          14978                                  
REMARK   3   CHIRALITY :  0.051           1663                                  
REMARK   3   PLANARITY :  0.005           1903                                  
REMARK   3   DIHEDRAL  :  9.282           6792                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 2 THROUGH 107 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -85.0097  53.6164 -15.6740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.6423 T22:   1.7500                                     
REMARK   3      T33:   1.7126 T12:   0.3241                                     
REMARK   3      T13:  -0.1471 T23:  -0.2397                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8492 L22:   2.1614                                     
REMARK   3      L33:   6.5853 L12:   0.2537                                     
REMARK   3      L13:   0.9208 L23:   0.0185                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0969 S12:  -0.8758 S13:   0.8775                       
REMARK   3      S21:   0.0534 S22:  -0.0971 S23:   0.4503                       
REMARK   3      S31:  -2.6584 S32:  -0.5848 S33:   0.1582                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 108 THROUGH 252 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -78.8058  43.9596   0.0816              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.2834 T22:   1.5254                                     
REMARK   3      T33:   0.9765 T12:  -0.0590                                     
REMARK   3      T13:  -0.0852 T23:  -0.1249                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1379 L22:   3.2183                                     
REMARK   3      L33:   7.6055 L12:  -1.6634                                     
REMARK   3      L13:   2.6587 L23:   1.8780                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8923 S12:  -0.8864 S13:   0.3917                       
REMARK   3      S21:   0.3928 S22:   0.7185 S23:   0.2254                       
REMARK   3      S31:  -0.2094 S32:   0.0492 S33:  -0.0556                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 253 THROUGH 361 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -78.7686  25.0745 -32.7156              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4783 T22:   1.3076                                     
REMARK   3      T33:   1.1602 T12:  -0.4343                                     
REMARK   3      T13:  -0.1204 T23:  -0.1737                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2173 L22:   8.0009                                     
REMARK   3      L33:   7.3535 L12:  -1.9727                                     
REMARK   3      L13:   2.5294 L23:   0.0019                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1261 S12:   0.2334 S13:  -0.4110                       
REMARK   3      S21:  -0.1863 S22:  -0.0578 S23:   1.5209                       
REMARK   3      S31:   0.1363 S32:  -0.6661 S33:   0.4025                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 77 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -68.5518  18.0155 -34.2654              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8789 T22:   1.0231                                     
REMARK   3      T33:   0.9061 T12:   0.0493                                     
REMARK   3      T13:   0.0488 T23:  -0.0650                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0559 L22:   2.2064                                     
REMARK   3      L33:   6.3289 L12:   1.2047                                     
REMARK   3      L13:   5.7082 L23:  -0.2164                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4977 S12:   0.0027 S13:  -0.4307                       
REMARK   3      S21:  -0.2363 S22:   0.0511 S23:  -0.1445                       
REMARK   3      S31:   0.5469 S32:   0.2607 S33:  -0.7758                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 78 THROUGH 192 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -57.3829  24.1730  -5.8299              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7665 T22:   1.8264                                     
REMARK   3      T33:   1.0485 T12:  -0.2213                                     
REMARK   3      T13:  -0.3523 T23:  -0.2044                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.9068 L22:   7.2031                                     
REMARK   3      L33:   3.8479 L12:  -0.4457                                     
REMARK   3      L13:  -2.5721 L23:  -0.9665                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2092 S12:  -1.1894 S13:  -0.2372                       
REMARK   3      S21:   1.6232 S22:  -0.0313 S23:  -1.1227                       
REMARK   3      S31:  -0.3599 S32:   0.6658 S33:  -0.3653                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 193 THROUGH 361 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -74.2263  43.0598 -22.9025              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7846 T22:   1.0602                                     
REMARK   3      T33:   1.0398 T12:  -0.2752                                     
REMARK   3      T13:  -0.0888 T23:   0.0055                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.0694 L22:   4.9882                                     
REMARK   3      L33:   7.7267 L12:  -3.1094                                     
REMARK   3      L13:   2.9583 L23:   0.9565                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3579 S12:   0.3520 S13:   0.9592                       
REMARK   3      S21:   0.1873 S22:  -0.1000 S23:  -0.5407                       
REMARK   3      S31:  -1.9688 S32:  -0.1832 S33:   0.4026                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 107 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -41.9567  51.3566  54.5132              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1194 T22:   0.8877                                     
REMARK   3      T33:   1.5993 T12:  -0.0176                                     
REMARK   3      T13:  -0.1201 T23:   0.0701                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0107 L22:   5.1484                                     
REMARK   3      L33:   9.0317 L12:  -0.8434                                     
REMARK   3      L13:   1.1726 L23:  -0.9942                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5247 S12:  -0.0513 S13:   0.7996                       
REMARK   3      S21:  -0.1257 S22:  -0.2391 S23:  -0.9747                       
REMARK   3      S31:  -1.1233 S32:   0.1518 S33:   0.8529                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 108 THROUGH 192 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -46.2832  42.8066  37.5682              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4176 T22:   0.9478                                     
REMARK   3      T33:   0.9949 T12:   0.1389                                     
REMARK   3      T13:   0.0996 T23:   0.0844                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.5220 L22:   7.7420                                     
REMARK   3      L33:   9.8382 L12:   2.8604                                     
REMARK   3      L13:   4.3719 L23:  -1.6206                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1139 S12:   1.0160 S13:   0.4401                       
REMARK   3      S21:  -1.3080 S22:  -0.0024 S23:  -0.6845                       
REMARK   3      S31:   0.2845 S32:  -0.0513 S33:   0.1550                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 193 THROUGH 361 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -48.9942  27.7828  59.5251              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8616 T22:   0.6261                                     
REMARK   3      T33:   0.8665 T12:   0.2392                                     
REMARK   3      T13:  -0.0020 T23:  -0.0643                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2845 L22:   4.9559                                     
REMARK   3      L33:   4.9176 L12:   1.6272                                     
REMARK   3      L13:  -1.0155 L23:  -1.9044                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2859 S12:   0.0384 S13:  -0.2177                       
REMARK   3      S21:  -0.5414 S22:   0.0910 S23:  -0.7843                       
REMARK   3      S31:   0.1867 S32:   0.2354 S33:   0.2474                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 0 THROUGH 77 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -58.3037  14.5640  70.0237              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1660 T22:   0.7934                                     
REMARK   3      T33:   0.9347 T12:   0.1300                                     
REMARK   3      T13:   0.1488 T23:   0.2152                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.1386 L22:   9.3517                                     
REMARK   3      L33:   6.1231 L12:   1.6404                                     
REMARK   3      L13:   2.4477 L23:   0.7802                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4719 S12:  -0.9653 S13:  -0.7990                       
REMARK   3      S21:   0.0564 S22:  -0.2020 S23:   0.1074                       
REMARK   3      S31:   0.9744 S32:  -0.6307 S33:  -0.4832                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 78 THROUGH 256 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -68.1603  23.8350  41.7961              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2932 T22:   1.1034                                     
REMARK   3      T33:   0.9219 T12:   0.0886                                     
REMARK   3      T13:  -0.3174 T23:  -0.0905                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.4476 L22:   8.1930                                     
REMARK   3      L33:   7.0056 L12:   2.5672                                     
REMARK   3      L13:  -0.8724 L23:  -2.7837                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3465 S12:   1.1574 S13:  -0.4528                       
REMARK   3      S21:  -1.6060 S22:   0.4119 S23:   0.6720                       
REMARK   3      S31:  -0.2279 S32:  -0.5478 S33:  -0.1411                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 257 THROUGH 361 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -49.8592  43.5471  71.6352              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0021 T22:   0.9805                                     
REMARK   3      T33:   1.0500 T12:   0.2629                                     
REMARK   3      T13:  -0.1702 T23:  -0.2530                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0209 L22:   6.9785                                     
REMARK   3      L33:   9.1301 L12:   1.9668                                     
REMARK   3      L13:  -1.5779 L23:  -2.7903                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3144 S12:  -1.0035 S13:   0.9799                       
REMARK   3      S21:   1.2611 S22:  -0.0700 S23:   0.2456                       
REMARK   3      S31:  -1.1477 S32:  -0.4132 S33:   0.2599                       
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 5VQF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAY-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000226876.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-NOV-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97934, 0.97932, 0.97956,         
REMARK 200                                   0.95667                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39918                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.05200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.98                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 2.74000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.550                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: 3RJR                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.86                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 7% PEG 3350, 17% ISOPROPANOL, 0.1M NA    
REMARK 280  CITRATE PH 5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.0K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       63.46000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9340 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 34210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -61.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, E                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9530 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 35750 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -57.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, F, G                            
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     GLY A    -1                                                      
REMARK 465     PRO A     0                                                      
REMARK 465     LEU A     1                                                      
REMARK 465     VAL A    64                                                      
REMARK 465     GLU A    65                                                      
REMARK 465     PRO A    66                                                      
REMARK 465     GLU A    67                                                      
REMARK 465     PRO A    68                                                      
REMARK 465     GLU A    69                                                      
REMARK 465     ASN A   208                                                      
REMARK 465     GLY A   209                                                      
REMARK 465     PHE A   210                                                      
REMARK 465     ASN A   211                                                      
REMARK 465     SER A   212                                                      
REMARK 465     GLY A   213                                                      
REMARK 465     ARG A   214                                                      
REMARK 465     ARG A   215                                                      
REMARK 465     GLY A   216                                                      
REMARK 465     GLN A   240                                                      
REMARK 465     HIS A   241                                                      
REMARK 465     LEU A   242                                                      
REMARK 465     HIS A   243                                                      
REMARK 465     SER A   244                                                      
REMARK 465     SER A   245                                                      
REMARK 465     ARG A   246                                                      
REMARK 465     HIS A   247                                                      
REMARK 465     ARG A   248                                                      
REMARK 465     ARG A   249                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     PRO B     0                                                      
REMARK 465     SER B    63                                                      
REMARK 465     VAL B    64                                                      
REMARK 465     GLU B    65                                                      
REMARK 465     PRO B    66                                                      
REMARK 465     GLU B    67                                                      
REMARK 465     PRO B    68                                                      
REMARK 465     GLU B    69                                                      
REMARK 465     PRO B    70                                                      
REMARK 465     GLY B   209                                                      
REMARK 465     PHE B   210                                                      
REMARK 465     ASN B   211                                                      
REMARK 465     SER B   212                                                      
REMARK 465     GLY B   213                                                      
REMARK 465     ARG B   214                                                      
REMARK 465     ARG B   215                                                      
REMARK 465     GLN B   240                                                      
REMARK 465     HIS B   241                                                      
REMARK 465     LEU B   242                                                      
REMARK 465     HIS B   243                                                      
REMARK 465     SER B   244                                                      
REMARK 465     SER B   245                                                      
REMARK 465     ARG B   246                                                      
REMARK 465     HIS B   247                                                      
REMARK 465     ARG B   248                                                      
REMARK 465     ARG B   249                                                      
REMARK 465     ALA B   250                                                      
REMARK 465     LEU B   251                                                      
REMARK 465     ASP B   252                                                      
REMARK 465     TYR B   299                                                      
REMARK 465     ILE B   300                                                      
REMARK 465     TRP B   301                                                      
REMARK 465     SER B   302                                                      
REMARK 465     LEU B   303                                                      
REMARK 465     ASP B   304                                                      
REMARK 465     THR B   305                                                      
REMARK 465     GLN B   306                                                      
REMARK 465     TYR B   307                                                      
REMARK 465     SER B   308                                                      
REMARK 465     LYS B   309                                                      
REMARK 465     VAL B   310                                                      
REMARK 465     LEU B   311                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     PRO C     0                                                      
REMARK 465     GLU C    62                                                      
REMARK 465     SER C    63                                                      
REMARK 465     VAL C    64                                                      
REMARK 465     GLU C    65                                                      
REMARK 465     PRO C    66                                                      
REMARK 465     GLU C    67                                                      
REMARK 465     PRO C    68                                                      
REMARK 465     GLY C   209                                                      
REMARK 465     PHE C   210                                                      
REMARK 465     ASN C   211                                                      
REMARK 465     SER C   212                                                      
REMARK 465     GLY C   213                                                      
REMARK 465     ARG C   214                                                      
REMARK 465     LEU C   242                                                      
REMARK 465     HIS C   243                                                      
REMARK 465     SER C   244                                                      
REMARK 465     SER C   245                                                      
REMARK 465     ARG C   246                                                      
REMARK 465     HIS C   247                                                      
REMARK 465     ARG C   248                                                      
REMARK 465     ARG C   249                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     SER D    63                                                      
REMARK 465     VAL D    64                                                      
REMARK 465     GLU D    65                                                      
REMARK 465     PRO D    66                                                      
REMARK 465     GLU D    67                                                      
REMARK 465     PRO D    68                                                      
REMARK 465     GLU D    69                                                      
REMARK 465     PRO D    70                                                      
REMARK 465     GLU D    71                                                      
REMARK 465     ALA D    72                                                      
REMARK 465     GLY D   209                                                      
REMARK 465     PHE D   210                                                      
REMARK 465     ASN D   211                                                      
REMARK 465     SER D   212                                                      
REMARK 465     GLY D   213                                                      
REMARK 465     ARG D   214                                                      
REMARK 465     ARG D   215                                                      
REMARK 465     HIS D   243                                                      
REMARK 465     SER D   244                                                      
REMARK 465     SER D   245                                                      
REMARK 465     ARG D   246                                                      
REMARK 465     HIS D   247                                                      
REMARK 465     ARG D   248                                                      
REMARK 465     ARG D   249                                                      
REMARK 465     ALA D   250                                                      
REMARK 465     LEU D   251                                                      
REMARK 465     ASP D   252                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE2  GLU A    86     ND1  HIS A   222              2.11            
REMARK 500   ND2  ASN A   155     OH   TYR B   152              2.16            
REMARK 500   C4   NAG G     1     C1   NAG G     2              2.17            
REMARK 500   ND2  ASN C    53     O5   NAG F     1              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A 265   CA  -  CB  -  SG  ANGL. DEV. =  12.2 DEGREES          
REMARK 500    CYS B 265   CA  -  CB  -  SG  ANGL. DEV. =  11.1 DEGREES          
REMARK 500    CYS C 265   CA  -  CB  -  SG  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    CYS D 265   CA  -  CB  -  SG  ANGL. DEV. =  16.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A  90      -37.30     76.48                                   
REMARK 500    LEU A 153      -63.44   -108.66                                   
REMARK 500    LYS A 199      112.95   -160.36                                   
REMARK 500    ASP A 304      171.66    -59.75                                   
REMARK 500    ALA A 323      -37.09     64.25                                   
REMARK 500    GLN A 330      -67.52   -108.37                                   
REMARK 500    GLN B  90      -40.47     76.14                                   
REMARK 500    LEU B 153      -61.69   -109.95                                   
REMARK 500    LYS B 199      112.83   -160.66                                   
REMARK 500    ASN B 201       12.31     57.98                                   
REMARK 500    LEU B 313       49.09   -145.88                                   
REMARK 500    GLN B 330      -66.65   -107.87                                   
REMARK 500    SER C   2        0.07    -63.57                                   
REMARK 500    GLN C  90      -41.21     75.93                                   
REMARK 500    PHE C  95       71.89   -119.43                                   
REMARK 500    LEU C 153      -62.68   -106.91                                   
REMARK 500    LYS C 199      111.33   -160.83                                   
REMARK 500    ASN C 201       10.71     58.76                                   
REMARK 500    ALA C 323      -37.37     67.26                                   
REMARK 500    GLN C 330      -64.88   -108.58                                   
REMARK 500    SER D   4       35.82    -96.43                                   
REMARK 500    GLN D  90      -37.38     73.04                                   
REMARK 500    LEU D 153      -63.78   -108.17                                   
REMARK 500    ASP D 200      -99.58     57.20                                   
REMARK 500    HIS D 241       78.48   -104.21                                   
REMARK 500    ASN D 254        0.22    -68.25                                   
REMARK 500    TYR D 314        0.45    -68.30                                   
REMARK 500    GLN D 330      -66.85   -108.54                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3RJR   RELATED DB: PDB                                   
REMARK 900 THE RAW REFLECTION IMAGES ARE THE SAME AS THE ONES WE USED FOR THE   
REMARK 900 PREVIOUS ENTRY 3RJR. WE HAVE USED XDS TO REPROCESS TO A HIGHER       
REMARK 900 RESOLUTION, AND THEN USED MOLECULAR REPLACEMENT TO DETERMINE THE     
REMARK 900 STRUCTURE, THE STARTING MODEL IS 3RJR.                               
DBREF  5VQF A    1   361  UNP    P07200   TGFB1_PIG       30    390             
DBREF  5VQF B    1   361  UNP    P07200   TGFB1_PIG       30    390             
DBREF  5VQF C    1   361  UNP    P07200   TGFB1_PIG       30    390             
DBREF  5VQF D    1   361  UNP    P07200   TGFB1_PIG       30    390             
SEQADV 5VQF GLY A   -1  UNP  P07200              EXPRESSION TAG                 
SEQADV 5VQF PRO A    0  UNP  P07200              EXPRESSION TAG                 
SEQADV 5VQF SER A    4  UNP  P07200    CYS    33 ENGINEERED MUTATION            
SEQADV 5VQF VAL A   85  UNP  P07200    LEU   114 VARIANT                        
SEQADV 5VQF GLN A  147  UNP  P07200    ASN   176 ENGINEERED MUTATION            
SEQADV 5VQF GLY B   -1  UNP  P07200              EXPRESSION TAG                 
SEQADV 5VQF PRO B    0  UNP  P07200              EXPRESSION TAG                 
SEQADV 5VQF SER B    4  UNP  P07200    CYS    33 ENGINEERED MUTATION            
SEQADV 5VQF VAL B   85  UNP  P07200    LEU   114 VARIANT                        
SEQADV 5VQF GLN B  147  UNP  P07200    ASN   176 ENGINEERED MUTATION            
SEQADV 5VQF GLY C   -1  UNP  P07200              EXPRESSION TAG                 
SEQADV 5VQF PRO C    0  UNP  P07200              EXPRESSION TAG                 
SEQADV 5VQF SER C    4  UNP  P07200    CYS    33 ENGINEERED MUTATION            
SEQADV 5VQF VAL C   85  UNP  P07200    LEU   114 VARIANT                        
SEQADV 5VQF GLN C  147  UNP  P07200    ASN   176 ENGINEERED MUTATION            
SEQADV 5VQF GLY D   -1  UNP  P07200              EXPRESSION TAG                 
SEQADV 5VQF PRO D    0  UNP  P07200              EXPRESSION TAG                 
SEQADV 5VQF SER D    4  UNP  P07200    CYS    33 ENGINEERED MUTATION            
SEQADV 5VQF VAL D   85  UNP  P07200    LEU   114 VARIANT                        
SEQADV 5VQF GLN D  147  UNP  P07200    ASN   176 ENGINEERED MUTATION            
SEQRES   1 A  363  GLY PRO LEU SER THR SER LYS THR ILE ASP MET GLU LEU          
SEQRES   2 A  363  VAL LYS ARG LYS ARG ILE GLU ALA ILE ARG GLY GLN ILE          
SEQRES   3 A  363  LEU SER LYS LEU ARG LEU ALA SER PRO PRO SER GLN GLY          
SEQRES   4 A  363  ASP VAL PRO PRO GLY PRO LEU PRO GLU ALA VAL LEU ALA          
SEQRES   5 A  363  LEU TYR ASN SER THR ARG ASP ARG VAL ALA GLY GLU SER          
SEQRES   6 A  363  VAL GLU PRO GLU PRO GLU PRO GLU ALA ASP TYR TYR ALA          
SEQRES   7 A  363  LYS GLU VAL THR ARG VAL LEU MET VAL GLU SER GLY ASN          
SEQRES   8 A  363  GLN ILE TYR ASP LYS PHE LYS GLY THR PRO HIS SER LEU          
SEQRES   9 A  363  TYR MET LEU PHE ASN THR SER GLU LEU ARG GLU ALA VAL          
SEQRES  10 A  363  PRO GLU PRO VAL LEU LEU SER ARG ALA GLU LEU ARG LEU          
SEQRES  11 A  363  LEU ARG LEU LYS LEU LYS VAL GLU GLN HIS VAL GLU LEU          
SEQRES  12 A  363  TYR GLN LYS TYR SER GLN ASP SER TRP ARG TYR LEU SER          
SEQRES  13 A  363  ASN ARG LEU LEU ALA PRO SER ASP SER PRO GLU TRP LEU          
SEQRES  14 A  363  SER PHE ASP VAL THR GLY VAL VAL ARG GLN TRP LEU THR          
SEQRES  15 A  363  ARG ARG GLU ALA ILE GLU GLY PHE ARG LEU SER ALA HIS          
SEQRES  16 A  363  CYS SER CYS ASP SER LYS ASP ASN THR LEU HIS VAL GLU          
SEQRES  17 A  363  ILE ASN GLY PHE ASN SER GLY ARG ARG GLY ASP LEU ALA          
SEQRES  18 A  363  THR ILE HIS GLY MET ASN ARG PRO PHE LEU LEU LEU MET          
SEQRES  19 A  363  ALA THR PRO LEU GLU ARG ALA GLN HIS LEU HIS SER SER          
SEQRES  20 A  363  ARG HIS ARG ARG ALA LEU ASP THR ASN TYR CYS PHE SER          
SEQRES  21 A  363  SER THR GLU LYS ASN CYS CYS VAL ARG GLN LEU TYR ILE          
SEQRES  22 A  363  ASP PHE ARG LYS ASP LEU GLY TRP LYS TRP ILE HIS GLU          
SEQRES  23 A  363  PRO LYS GLY TYR HIS ALA ASN PHE CYS LEU GLY PRO CYS          
SEQRES  24 A  363  PRO TYR ILE TRP SER LEU ASP THR GLN TYR SER LYS VAL          
SEQRES  25 A  363  LEU ALA LEU TYR ASN GLN HIS ASN PRO GLY ALA SER ALA          
SEQRES  26 A  363  ALA PRO CYS CYS VAL PRO GLN ALA LEU GLU PRO LEU PRO          
SEQRES  27 A  363  ILE VAL TYR TYR VAL GLY ARG LYS PRO LYS VAL GLU GLN          
SEQRES  28 A  363  LEU SER ASN MET ILE VAL ARG SER CYS LYS CYS SER              
SEQRES   1 B  363  GLY PRO LEU SER THR SER LYS THR ILE ASP MET GLU LEU          
SEQRES   2 B  363  VAL LYS ARG LYS ARG ILE GLU ALA ILE ARG GLY GLN ILE          
SEQRES   3 B  363  LEU SER LYS LEU ARG LEU ALA SER PRO PRO SER GLN GLY          
SEQRES   4 B  363  ASP VAL PRO PRO GLY PRO LEU PRO GLU ALA VAL LEU ALA          
SEQRES   5 B  363  LEU TYR ASN SER THR ARG ASP ARG VAL ALA GLY GLU SER          
SEQRES   6 B  363  VAL GLU PRO GLU PRO GLU PRO GLU ALA ASP TYR TYR ALA          
SEQRES   7 B  363  LYS GLU VAL THR ARG VAL LEU MET VAL GLU SER GLY ASN          
SEQRES   8 B  363  GLN ILE TYR ASP LYS PHE LYS GLY THR PRO HIS SER LEU          
SEQRES   9 B  363  TYR MET LEU PHE ASN THR SER GLU LEU ARG GLU ALA VAL          
SEQRES  10 B  363  PRO GLU PRO VAL LEU LEU SER ARG ALA GLU LEU ARG LEU          
SEQRES  11 B  363  LEU ARG LEU LYS LEU LYS VAL GLU GLN HIS VAL GLU LEU          
SEQRES  12 B  363  TYR GLN LYS TYR SER GLN ASP SER TRP ARG TYR LEU SER          
SEQRES  13 B  363  ASN ARG LEU LEU ALA PRO SER ASP SER PRO GLU TRP LEU          
SEQRES  14 B  363  SER PHE ASP VAL THR GLY VAL VAL ARG GLN TRP LEU THR          
SEQRES  15 B  363  ARG ARG GLU ALA ILE GLU GLY PHE ARG LEU SER ALA HIS          
SEQRES  16 B  363  CYS SER CYS ASP SER LYS ASP ASN THR LEU HIS VAL GLU          
SEQRES  17 B  363  ILE ASN GLY PHE ASN SER GLY ARG ARG GLY ASP LEU ALA          
SEQRES  18 B  363  THR ILE HIS GLY MET ASN ARG PRO PHE LEU LEU LEU MET          
SEQRES  19 B  363  ALA THR PRO LEU GLU ARG ALA GLN HIS LEU HIS SER SER          
SEQRES  20 B  363  ARG HIS ARG ARG ALA LEU ASP THR ASN TYR CYS PHE SER          
SEQRES  21 B  363  SER THR GLU LYS ASN CYS CYS VAL ARG GLN LEU TYR ILE          
SEQRES  22 B  363  ASP PHE ARG LYS ASP LEU GLY TRP LYS TRP ILE HIS GLU          
SEQRES  23 B  363  PRO LYS GLY TYR HIS ALA ASN PHE CYS LEU GLY PRO CYS          
SEQRES  24 B  363  PRO TYR ILE TRP SER LEU ASP THR GLN TYR SER LYS VAL          
SEQRES  25 B  363  LEU ALA LEU TYR ASN GLN HIS ASN PRO GLY ALA SER ALA          
SEQRES  26 B  363  ALA PRO CYS CYS VAL PRO GLN ALA LEU GLU PRO LEU PRO          
SEQRES  27 B  363  ILE VAL TYR TYR VAL GLY ARG LYS PRO LYS VAL GLU GLN          
SEQRES  28 B  363  LEU SER ASN MET ILE VAL ARG SER CYS LYS CYS SER              
SEQRES   1 C  363  GLY PRO LEU SER THR SER LYS THR ILE ASP MET GLU LEU          
SEQRES   2 C  363  VAL LYS ARG LYS ARG ILE GLU ALA ILE ARG GLY GLN ILE          
SEQRES   3 C  363  LEU SER LYS LEU ARG LEU ALA SER PRO PRO SER GLN GLY          
SEQRES   4 C  363  ASP VAL PRO PRO GLY PRO LEU PRO GLU ALA VAL LEU ALA          
SEQRES   5 C  363  LEU TYR ASN SER THR ARG ASP ARG VAL ALA GLY GLU SER          
SEQRES   6 C  363  VAL GLU PRO GLU PRO GLU PRO GLU ALA ASP TYR TYR ALA          
SEQRES   7 C  363  LYS GLU VAL THR ARG VAL LEU MET VAL GLU SER GLY ASN          
SEQRES   8 C  363  GLN ILE TYR ASP LYS PHE LYS GLY THR PRO HIS SER LEU          
SEQRES   9 C  363  TYR MET LEU PHE ASN THR SER GLU LEU ARG GLU ALA VAL          
SEQRES  10 C  363  PRO GLU PRO VAL LEU LEU SER ARG ALA GLU LEU ARG LEU          
SEQRES  11 C  363  LEU ARG LEU LYS LEU LYS VAL GLU GLN HIS VAL GLU LEU          
SEQRES  12 C  363  TYR GLN LYS TYR SER GLN ASP SER TRP ARG TYR LEU SER          
SEQRES  13 C  363  ASN ARG LEU LEU ALA PRO SER ASP SER PRO GLU TRP LEU          
SEQRES  14 C  363  SER PHE ASP VAL THR GLY VAL VAL ARG GLN TRP LEU THR          
SEQRES  15 C  363  ARG ARG GLU ALA ILE GLU GLY PHE ARG LEU SER ALA HIS          
SEQRES  16 C  363  CYS SER CYS ASP SER LYS ASP ASN THR LEU HIS VAL GLU          
SEQRES  17 C  363  ILE ASN GLY PHE ASN SER GLY ARG ARG GLY ASP LEU ALA          
SEQRES  18 C  363  THR ILE HIS GLY MET ASN ARG PRO PHE LEU LEU LEU MET          
SEQRES  19 C  363  ALA THR PRO LEU GLU ARG ALA GLN HIS LEU HIS SER SER          
SEQRES  20 C  363  ARG HIS ARG ARG ALA LEU ASP THR ASN TYR CYS PHE SER          
SEQRES  21 C  363  SER THR GLU LYS ASN CYS CYS VAL ARG GLN LEU TYR ILE          
SEQRES  22 C  363  ASP PHE ARG LYS ASP LEU GLY TRP LYS TRP ILE HIS GLU          
SEQRES  23 C  363  PRO LYS GLY TYR HIS ALA ASN PHE CYS LEU GLY PRO CYS          
SEQRES  24 C  363  PRO TYR ILE TRP SER LEU ASP THR GLN TYR SER LYS VAL          
SEQRES  25 C  363  LEU ALA LEU TYR ASN GLN HIS ASN PRO GLY ALA SER ALA          
SEQRES  26 C  363  ALA PRO CYS CYS VAL PRO GLN ALA LEU GLU PRO LEU PRO          
SEQRES  27 C  363  ILE VAL TYR TYR VAL GLY ARG LYS PRO LYS VAL GLU GLN          
SEQRES  28 C  363  LEU SER ASN MET ILE VAL ARG SER CYS LYS CYS SER              
SEQRES   1 D  363  GLY PRO LEU SER THR SER LYS THR ILE ASP MET GLU LEU          
SEQRES   2 D  363  VAL LYS ARG LYS ARG ILE GLU ALA ILE ARG GLY GLN ILE          
SEQRES   3 D  363  LEU SER LYS LEU ARG LEU ALA SER PRO PRO SER GLN GLY          
SEQRES   4 D  363  ASP VAL PRO PRO GLY PRO LEU PRO GLU ALA VAL LEU ALA          
SEQRES   5 D  363  LEU TYR ASN SER THR ARG ASP ARG VAL ALA GLY GLU SER          
SEQRES   6 D  363  VAL GLU PRO GLU PRO GLU PRO GLU ALA ASP TYR TYR ALA          
SEQRES   7 D  363  LYS GLU VAL THR ARG VAL LEU MET VAL GLU SER GLY ASN          
SEQRES   8 D  363  GLN ILE TYR ASP LYS PHE LYS GLY THR PRO HIS SER LEU          
SEQRES   9 D  363  TYR MET LEU PHE ASN THR SER GLU LEU ARG GLU ALA VAL          
SEQRES  10 D  363  PRO GLU PRO VAL LEU LEU SER ARG ALA GLU LEU ARG LEU          
SEQRES  11 D  363  LEU ARG LEU LYS LEU LYS VAL GLU GLN HIS VAL GLU LEU          
SEQRES  12 D  363  TYR GLN LYS TYR SER GLN ASP SER TRP ARG TYR LEU SER          
SEQRES  13 D  363  ASN ARG LEU LEU ALA PRO SER ASP SER PRO GLU TRP LEU          
SEQRES  14 D  363  SER PHE ASP VAL THR GLY VAL VAL ARG GLN TRP LEU THR          
SEQRES  15 D  363  ARG ARG GLU ALA ILE GLU GLY PHE ARG LEU SER ALA HIS          
SEQRES  16 D  363  CYS SER CYS ASP SER LYS ASP ASN THR LEU HIS VAL GLU          
SEQRES  17 D  363  ILE ASN GLY PHE ASN SER GLY ARG ARG GLY ASP LEU ALA          
SEQRES  18 D  363  THR ILE HIS GLY MET ASN ARG PRO PHE LEU LEU LEU MET          
SEQRES  19 D  363  ALA THR PRO LEU GLU ARG ALA GLN HIS LEU HIS SER SER          
SEQRES  20 D  363  ARG HIS ARG ARG ALA LEU ASP THR ASN TYR CYS PHE SER          
SEQRES  21 D  363  SER THR GLU LYS ASN CYS CYS VAL ARG GLN LEU TYR ILE          
SEQRES  22 D  363  ASP PHE ARG LYS ASP LEU GLY TRP LYS TRP ILE HIS GLU          
SEQRES  23 D  363  PRO LYS GLY TYR HIS ALA ASN PHE CYS LEU GLY PRO CYS          
SEQRES  24 D  363  PRO TYR ILE TRP SER LEU ASP THR GLN TYR SER LYS VAL          
SEQRES  25 D  363  LEU ALA LEU TYR ASN GLN HIS ASN PRO GLY ALA SER ALA          
SEQRES  26 D  363  ALA PRO CYS CYS VAL PRO GLN ALA LEU GLU PRO LEU PRO          
SEQRES  27 D  363  ILE VAL TYR TYR VAL GLY ARG LYS PRO LYS VAL GLU GLN          
SEQRES  28 D  363  LEU SER ASN MET ILE VAL ARG SER CYS LYS CYS SER              
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET    BMA  E   3      11                                                       
HET    NAG  F   1      14                                                       
HET    NAG  F   2      14                                                       
HET    NAG  G   1      14                                                       
HET    NAG  G   2      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
FORMUL   5  NAG    6(C8 H15 N O6)                                               
FORMUL   5  BMA    C6 H12 O6                                                    
HELIX    1 AA1 SER A    2  LEU A   28  1                                  27    
HELIX    2 AA2 PRO A   45  ASP A   57  1                                  13    
HELIX    3 AA3 THR A  108  VAL A  115  1                                   8    
HELIX    4 AA4 GLU A  117  VAL A  119  5                                   3    
HELIX    5 AA5 VAL A  171  ARG A  181  1                                  11    
HELIX    6 AA6 PRO A  235  ALA A  239  5                                   5    
HELIX    7 AA7 THR A  253  PHE A  257  1                                   5    
HELIX    8 AA8 TYR A  299  LEU A  303  5                                   5    
HELIX    9 AA9 TYR A  307  ALA A  312  1                                   6    
HELIX   10 AB1 LEU A  313  HIS A  317  5                                   5    
HELIX   11 AB2 SER B    2  LEU B   28  1                                  27    
HELIX   12 AB3 PRO B   45  ASP B   57  1                                  13    
HELIX   13 AB4 THR B  108  VAL B  115  1                                   8    
HELIX   14 AB5 GLU B  117  VAL B  119  5                                   3    
HELIX   15 AB6 VAL B  171  ARG B  181  1                                  11    
HELIX   16 AB7 SER C    2  LEU C   28  1                                  27    
HELIX   17 AB8 PRO C   45  ASP C   57  1                                  13    
HELIX   18 AB9 THR C  108  VAL C  115  1                                   8    
HELIX   19 AC1 GLU C  117  VAL C  119  5                                   3    
HELIX   20 AC2 VAL C  171  ARG C  181  1                                  11    
HELIX   21 AC3 THR C  253  PHE C  257  1                                   5    
HELIX   22 AC4 TYR C  307  ALA C  312  1                                   6    
HELIX   23 AC5 LEU C  313  HIS C  317  5                                   5    
HELIX   24 AC6 ASN C  318  SER C  322  5                                   5    
HELIX   25 AC7 SER D    4  LEU D   28  1                                  25    
HELIX   26 AC8 PRO D   45  ASP D   57  1                                  13    
HELIX   27 AC9 THR D  108  VAL D  115  1                                   8    
HELIX   28 AD1 GLU D  117  VAL D  119  5                                   3    
HELIX   29 AD2 VAL D  171  ARG D  181  1                                  11    
HELIX   30 AD3 PRO D  235  ALA D  239  5                                   5    
HELIX   31 AD4 GLN D  306  LEU D  313  1                                   8    
HELIX   32 AD5 TYR D  314  GLN D  316  5                                   3    
SHEET    1 AA1 8 VAL A  59  ALA A  60  0                                        
SHEET    2 AA1 8 GLU A 165  ASP A 170  1  O  TRP A 166   N  ALA A  60           
SHEET    3 AA1 8 LEU A 121  ARG A 130 -1  N  LEU A 128   O  LEU A 167           
SHEET    4 AA1 8 PHE A 228  ALA A 233 -1  O  LEU A 230   N  GLU A 125           
SHEET    5 AA1 8 LYS A  77  LEU A  83 -1  N  THR A  80   O  LEU A 231           
SHEET    6 AA1 8 LYS B 344  VAL B 355 -1  O  GLN B 349   N  LYS A  77           
SHEET    7 AA1 8 LEU B 332  VAL B 341 -1  N  TYR B 339   O  LYS B 346           
SHEET    8 AA1 8 ILE B 282  GLU B 284 -1  N  GLU B 284   O  VAL B 338           
SHEET    1 AA2 4 SER A 101  ASN A 107  0                                        
SHEET    2 AA2 4 ILE A 185  ALA A 192 -1  O  GLU A 186   N  PHE A 106           
SHEET    3 AA2 4 GLN A 137  GLN A 143 -1  N  TYR A 142   O  ARG A 189           
SHEET    4 AA2 4 ARG A 151  LEU A 158 -1  O  LEU A 158   N  GLN A 137           
SHEET    1 AA3 4 SER A 195  LYS A 199  0                                        
SHEET    2 AA3 4 THR A 202  GLU A 206 -1  O  GLU A 206   N  SER A 195           
SHEET    3 AA3 4 THR D 202  ILE D 207 -1  O  LEU D 203   N  VAL A 205           
SHEET    4 AA3 4 CYS D 194  LYS D 199 -1  N  LYS D 199   O  THR D 202           
SHEET    1 AA4 3 LEU A 251  ASP A 252  0                                        
SHEET    2 AA4 3 SER A 357  SER A 361 -1  O  CYS A 358   N  LEU A 251           
SHEET    3 AA4 3 CYS A 326  PRO A 329 -1  N  VAL A 328   O  LYS A 359           
SHEET    1 AA5 2 CYS A 265  ARG A 267  0                                        
SHEET    2 AA5 2 PHE A 292  LEU A 294 -1  O  PHE A 292   N  ARG A 267           
SHEET    1 AA6 2 TYR A 270  ASP A 272  0                                        
SHEET    2 AA6 2 GLY A 287  HIS A 289 -1  O  TYR A 288   N  ILE A 271           
SHEET    1 AA7 7 ILE A 282  GLU A 284  0                                        
SHEET    2 AA7 7 LEU A 332  VAL A 341 -1  O  VAL A 338   N  GLU A 284           
SHEET    3 AA7 7 LYS A 344  VAL A 355 -1  O  GLU A 348   N  ILE A 337           
SHEET    4 AA7 7 LYS B  77  LEU B  83 -1  O  VAL B  79   N  VAL A 347           
SHEET    5 AA7 7 PHE B 228  ALA B 233 -1  O  LEU B 231   N  THR B  80           
SHEET    6 AA7 7 LEU B 121  ARG B 130 -1  N  GLU B 125   O  LEU B 230           
SHEET    7 AA7 7 GLU B 165  ASP B 170 -1  O  LEU B 167   N  LEU B 128           
SHEET    1 AA8 4 SER B 101  ASN B 107  0                                        
SHEET    2 AA8 4 ILE B 185  ALA B 192 -1  O  GLU B 186   N  PHE B 106           
SHEET    3 AA8 4 GLN B 137  GLN B 143 -1  N  TYR B 142   O  ARG B 189           
SHEET    4 AA8 4 ARG B 151  LEU B 158 -1  O  LEU B 158   N  GLN B 137           
SHEET    1 AA9 4 CYS B 194  LYS B 199  0                                        
SHEET    2 AA9 4 THR B 202  ILE B 207 -1  O  GLU B 206   N  SER B 195           
SHEET    3 AA9 4 THR C 202  ILE C 207 -1  O  LEU C 203   N  VAL B 205           
SHEET    4 AA9 4 CYS C 194  LYS C 199 -1  N  SER C 195   O  GLU C 206           
SHEET    1 AB1 2 CYS B 265  ARG B 267  0                                        
SHEET    2 AB1 2 PHE B 292  LEU B 294 -1  O  PHE B 292   N  ARG B 267           
SHEET    1 AB2 2 TYR B 270  ASP B 272  0                                        
SHEET    2 AB2 2 GLY B 287  HIS B 289 -1  O  TYR B 288   N  ILE B 271           
SHEET    1 AB3 2 CYS B 326  PRO B 329  0                                        
SHEET    2 AB3 2 CYS B 358  SER B 361 -1  O  LYS B 359   N  VAL B 328           
SHEET    1 AB4 7 GLU C 165  ASP C 170  0                                        
SHEET    2 AB4 7 LEU C 121  ARG C 130 -1  N  LEU C 128   O  LEU C 167           
SHEET    3 AB4 7 PHE C 228  ALA C 233 -1  O  LEU C 230   N  GLU C 125           
SHEET    4 AB4 7 LYS C  77  LEU C  83 -1  N  THR C  80   O  LEU C 231           
SHEET    5 AB4 7 LYS D 344  VAL D 355 -1  O  VAL D 347   N  VAL C  79           
SHEET    6 AB4 7 LEU D 332  VAL D 341 -1  N  TYR D 339   O  LYS D 346           
SHEET    7 AB4 7 ILE D 282  GLU D 284 -1  N  GLU D 284   O  VAL D 338           
SHEET    1 AB5 4 SER C 101  ASN C 107  0                                        
SHEET    2 AB5 4 ILE C 185  ALA C 192 -1  O  PHE C 188   N  MET C 104           
SHEET    3 AB5 4 GLN C 137  LYS C 144 -1  N  LYS C 144   O  GLY C 187           
SHEET    4 AB5 4 TRP C 150  LEU C 158 -1  O  SER C 154   N  LEU C 141           
SHEET    1 AB6 3 LEU C 251  ASP C 252  0                                        
SHEET    2 AB6 3 SER C 357  CYS C 360 -1  O  CYS C 358   N  LEU C 251           
SHEET    3 AB6 3 CYS C 327  PRO C 329 -1  N  VAL C 328   O  LYS C 359           
SHEET    1 AB7 2 CYS C 265  ARG C 267  0                                        
SHEET    2 AB7 2 PHE C 292  LEU C 294 -1  O  PHE C 292   N  ARG C 267           
SHEET    1 AB8 2 TYR C 270  ASP C 272  0                                        
SHEET    2 AB8 2 GLY C 287  HIS C 289 -1  O  TYR C 288   N  ILE C 271           
SHEET    1 AB9 7 ILE C 282  GLU C 284  0                                        
SHEET    2 AB9 7 LEU C 332  VAL C 341 -1  O  VAL C 338   N  GLU C 284           
SHEET    3 AB9 7 LYS C 344  VAL C 355 -1  O  ILE C 354   N  GLU C 333           
SHEET    4 AB9 7 LYS D  77  LEU D  83 -1  O  VAL D  79   N  VAL C 347           
SHEET    5 AB9 7 PHE D 228  ALA D 233 -1  O  LEU D 231   N  THR D  80           
SHEET    6 AB9 7 LEU D 121  ARG D 130 -1  N  ARG D 123   O  MET D 232           
SHEET    7 AB9 7 GLU D 165  ASP D 170 -1  O  LEU D 167   N  LEU D 128           
SHEET    1 AC1 4 SER D 101  ASN D 107  0                                        
SHEET    2 AC1 4 ILE D 185  ALA D 192 -1  O  GLU D 186   N  PHE D 106           
SHEET    3 AC1 4 GLN D 137  GLN D 143 -1  N  GLU D 140   O  SER D 191           
SHEET    4 AC1 4 ARG D 151  LEU D 158 -1  O  LEU D 158   N  GLN D 137           
SHEET    1 AC2 2 CYS D 265  ARG D 267  0                                        
SHEET    2 AC2 2 PHE D 292  LEU D 294 -1  O  PHE D 292   N  ARG D 267           
SHEET    1 AC3 2 TYR D 270  ASP D 272  0                                        
SHEET    2 AC3 2 GLY D 287  HIS D 289 -1  O  TYR D 288   N  ILE D 271           
SHEET    1 AC4 2 CYS D 327  PRO D 329  0                                        
SHEET    2 AC4 2 CYS D 358  CYS D 360 -1  O  LYS D 359   N  VAL D 328           
SSBOND   1 CYS A  194    CYS B  196                          1555   1555  2.03  
SSBOND   2 CYS A  196    CYS B  194                          1555   1555  2.03  
SSBOND   3 CYS A  256    CYS A  265                          1555   1555  2.04  
SSBOND   4 CYS A  264    CYS A  327                          1555   1555  2.02  
SSBOND   5 CYS A  293    CYS A  358                          1555   1555  2.03  
SSBOND   6 CYS A  297    CYS A  360                          1555   1555  2.03  
SSBOND   7 CYS A  326    CYS B  326                          1555   1555  2.03  
SSBOND   8 CYS B  256    CYS B  265                          1555   1555  2.03  
SSBOND   9 CYS B  264    CYS B  327                          1555   1555  2.03  
SSBOND  10 CYS B  293    CYS B  358                          1555   1555  2.03  
SSBOND  11 CYS B  297    CYS B  360                          1555   1555  2.03  
SSBOND  12 CYS C  194    CYS D  196                          1555   1555  2.03  
SSBOND  13 CYS C  196    CYS D  194                          1555   1555  2.03  
SSBOND  14 CYS C  256    CYS C  265                          1555   1555  2.03  
SSBOND  15 CYS C  264    CYS C  327                          1555   1555  2.02  
SSBOND  16 CYS C  293    CYS C  358                          1555   1555  2.03  
SSBOND  17 CYS C  297    CYS C  360                          1555   1555  2.03  
SSBOND  18 CYS C  326    CYS D  326                          1555   1555  2.04  
SSBOND  19 CYS D  256    CYS D  265                          1555   1555  2.05  
SSBOND  20 CYS D  264    CYS D  327                          1555   1555  2.04  
SSBOND  21 CYS D  293    CYS D  358                          1555   1555  2.03  
SSBOND  22 CYS D  297    CYS D  360                          1555   1555  2.02  
LINK         ND2 ASN B  53                 C1  NAG E   1     1555   1555  1.46  
LINK         ND2 ASN C  53                 C1  NAG F   1     1555   1555  1.42  
LINK         ND2 ASN D  53                 C1  NAG G   1     1555   1555  1.41  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.43  
LINK         O4  NAG E   2                 C1  BMA E   3     1555   1555  1.45  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.42  
LINK         O4  NAG G   1                 C1  NAG G   2     1555   1555  1.48  
CISPEP   1 GLU A  284    PRO A  285          0        -6.00                     
CISPEP   2 GLU B  284    PRO B  285          0        -7.87                     
CISPEP   3 GLU C  284    PRO C  285          0        -5.29                     
CISPEP   4 GLU D  284    PRO D  285          0        -4.68                     
CRYST1   54.660  126.920  137.920  90.00  96.70  90.00 P 1 21 1      8          
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      0.018295  0.000000  0.002148        0.00000                         
SCALE2      0.000000  0.007879  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007300        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system