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Entry: 6BVI
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HEADER    SIGNALING PROTEIN                       13-DEC-17   6BVI              
TITLE     RAS:SOS:RAS IN COMPLEX WITH A SMALL MOLECULE ACTIVATOR                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GTPASE HRAS;                                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: H-RAS-1,HA-RAS,TRANSFORMING PROTEIN P21,C-H-RAS,P21RAS;     
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: SON OF SEVENLESS HOMOLOG 1;                                
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: SOS-1;                                                      
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: GTPASE HRAS;                                               
COMPND  14 CHAIN: C;                                                            
COMPND  15 SYNONYM: H-RAS-1,HA-RAS,TRANSFORMING PROTEIN P21,C-H-RAS,P21RAS;     
COMPND  16 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: HRAS, HRAS1;                                                   
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: SOS1;                                                          
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: HRAS, HRAS1;                                                   
SOURCE  20 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    RAS, SOS, INHIBITOR, ONCOPROTEIN, PROTEIN-PROTEIN COMPLEX, MAPK,      
KEYWDS   2 SIGNALING PROTEIN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.PHAN,J.ABBOTT,S.W.FESIK                                             
REVDAT   2   01-MAY-19 6BVI    1       JRNL                                     
REVDAT   1   24-OCT-18 6BVI    0                                                
JRNL        AUTH   J.R.ABBOTT,T.R.HODGES,R.N.DANIELS,P.A.PATEL,J.P.KENNEDY,     
JRNL        AUTH 2 J.E.HOWES,D.T.AKAN,M.C.BURNS,J.SAI,T.SOBOLIK,Y.BEESETTY,     
JRNL        AUTH 3 T.LEE,O.W.ROSSANESE,J.PHAN,A.G.WATERSON,S.W.FESIK            
JRNL        TITL   DISCOVERY OF AMINOPIPERIDINE INDOLES THAT ACTIVATE THE       
JRNL        TITL 2 GUANINE NUCLEOTIDE EXCHANGE FACTOR SOS1 AND MODULATE RAS     
JRNL        TITL 3 SIGNALING.                                                   
JRNL        REF    J. MED. CHEM.                 V.  61  6002 2018              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   29856609                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.8B00360                                 
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.C.BURNS,Q.SUN,R.N.DANIELS,D.CAMPER,J.P.KENNEDY,J.PHAN,     
REMARK   1  AUTH 2 E.T.OLEJNICZAK,T.LEE,A.G.WATERSON,O.W.ROSSANESE,S.W.FESIK    
REMARK   1  TITL   APPROACH FOR TARGETING RAS WITH SMALL MOLECULES THAT         
REMARK   1  TITL 2 ACTIVATE SOS-MEDIATED NUCLEOTIDE EXCHANGE.                   
REMARK   1  REF    PROC. NATL. ACAD. SCI.        V. 111  3401 2014              
REMARK   1  REF  2 U.S.A.                                                       
REMARK   1  REFN                   ESSN 1091-6490                               
REMARK   1  PMID   24550516                                                     
REMARK   1  DOI    10.1073/PNAS.1315798111                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.12RC1_2801: ???)                           
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) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.82                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 154062                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.157                           
REMARK   3   R VALUE            (WORKING SET) : 0.156                           
REMARK   3   FREE R VALUE                     : 0.169                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7754                            
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 42.8283 -  5.4220    0.99     5218   233  0.1671 0.1590        
REMARK   3     2  5.4220 -  4.3049    1.00     4990   292  0.1331 0.1384        
REMARK   3     3  4.3049 -  3.7611    1.00     4919   295  0.1268 0.1240        
REMARK   3     4  3.7611 -  3.4174    1.00     4967   263  0.1361 0.1447        
REMARK   3     5  3.4174 -  3.1725    1.00     4930   231  0.1499 0.1681        
REMARK   3     6  3.1725 -  2.9855    1.00     4939   249  0.1579 0.1724        
REMARK   3     7  2.9855 -  2.8360    1.00     4879   280  0.1579 0.1792        
REMARK   3     8  2.8360 -  2.7126    1.00     4890   258  0.1618 0.1750        
REMARK   3     9  2.7126 -  2.6082    1.00     4912   244  0.1608 0.1980        
REMARK   3    10  2.6082 -  2.5182    1.00     4838   303  0.1532 0.1721        
REMARK   3    11  2.5182 -  2.4395    1.00     4876   259  0.1577 0.1661        
REMARK   3    12  2.4395 -  2.3697    1.00     4891   254  0.1564 0.1744        
REMARK   3    13  2.3697 -  2.3074    1.00     4861   275  0.1561 0.1840        
REMARK   3    14  2.3074 -  2.2511    1.00     4855   257  0.1565 0.1774        
REMARK   3    15  2.2511 -  2.1999    1.00     4838   278  0.1544 0.1717        
REMARK   3    16  2.1999 -  2.1531    1.00     4880   257  0.1488 0.1604        
REMARK   3    17  2.1531 -  2.1100    1.00     4829   261  0.1497 0.1684        
REMARK   3    18  2.1100 -  2.0702    1.00     4880   249  0.1559 0.1891        
REMARK   3    19  2.0702 -  2.0332    1.00     4834   260  0.1641 0.1745        
REMARK   3    20  2.0332 -  1.9988    1.00     4915   227  0.1642 0.1912        
REMARK   3    21  1.9988 -  1.9665    1.00     4857   245  0.1702 0.1966        
REMARK   3    22  1.9665 -  1.9363    1.00     4807   273  0.1806 0.1955        
REMARK   3    23  1.9363 -  1.9078    1.00     4829   290  0.1830 0.1954        
REMARK   3    24  1.9078 -  1.8809    1.00     4779   288  0.1820 0.2184        
REMARK   3    25  1.8809 -  1.8555    1.00     4892   248  0.1892 0.2163        
REMARK   3    26  1.8555 -  1.8314    1.00     4863   225  0.1924 0.2076        
REMARK   3    27  1.8314 -  1.8085    1.00     4862   238  0.1959 0.2279        
REMARK   3    28  1.8085 -  1.7867    1.00     4853   232  0.2103 0.2321        
REMARK   3    29  1.7867 -  1.7659    1.00     4862   269  0.2149 0.2396        
REMARK   3    30  1.7659 -  1.7461    0.94     4563   221  0.2342 0.2636        
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)     : 0.140            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.430           
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      :  0.007           7124                                  
REMARK   3   ANGLE     :  0.843           9678                                  
REMARK   3   CHIRALITY :  0.053           1048                                  
REMARK   3   PLANARITY :  0.005           1305                                  
REMARK   3   DIHEDRAL  : 14.742           4399                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 17                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 36 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  19.5705  50.3067  62.3869              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1382 T22:   0.1504                                     
REMARK   3      T33:   0.1403 T12:  -0.0271                                     
REMARK   3      T13:   0.0136 T23:  -0.0109                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0642 L22:   0.0755                                     
REMARK   3      L33:   0.0846 L12:   0.0658                                     
REMARK   3      L13:   0.0162 L23:   0.0494                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0341 S12:   0.0114 S13:  -0.0058                       
REMARK   3      S21:  -0.0230 S22:   0.0184 S23:   0.0784                       
REMARK   3      S31:   0.0789 S32:  -0.0347 S33:  -0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 37 THROUGH 52 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  29.2099  45.1622  56.7858              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1510 T22:   0.1705                                     
REMARK   3      T33:   0.1292 T12:  -0.0460                                     
REMARK   3      T13:   0.0180 T23:  -0.0115                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0259 L22:  -0.0023                                     
REMARK   3      L33:   0.0510 L12:   0.0092                                     
REMARK   3      L13:   0.0673 L23:   0.0016                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0096 S12:  -0.1093 S13:  -0.0074                       
REMARK   3      S21:   0.0610 S22:   0.0374 S23:  -0.0310                       
REMARK   3      S31:  -0.0587 S32:   0.1007 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 53 THROUGH 76 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  24.0570  46.1061  73.3857              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2030 T22:   0.1707                                     
REMARK   3      T33:   0.1284 T12:  -0.0377                                     
REMARK   3      T13:   0.0254 T23:   0.0105                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0323 L22:   0.0107                                     
REMARK   3      L33:   0.0261 L12:   0.0238                                     
REMARK   3      L13:   0.0467 L23:   0.0015                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0125 S12:  -0.0688 S13:  -0.1303                       
REMARK   3      S21:   0.1226 S22:  -0.0358 S23:   0.0643                       
REMARK   3      S31:   0.1640 S32:  -0.0536 S33:  -0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 77 THROUGH 116 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  27.2248  57.1853  74.6427              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1567 T22:   0.1659                                     
REMARK   3      T33:   0.1238 T12:  -0.0414                                     
REMARK   3      T13:   0.0185 T23:  -0.0316                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0438 L22:   0.0754                                     
REMARK   3      L33:  -0.0029 L12:   0.0513                                     
REMARK   3      L13:   0.0276 L23:   0.0168                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0950 S12:  -0.1787 S13:   0.0775                       
REMARK   3      S21:   0.1070 S22:  -0.0281 S23:   0.0264                       
REMARK   3      S31:  -0.0350 S32:   0.0392 S33:   0.0000                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 117 THROUGH 151 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  24.6778  66.1821  65.8379              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1716 T22:   0.1200                                     
REMARK   3      T33:   0.1889 T12:  -0.0254                                     
REMARK   3      T13:   0.0326 T23:  -0.0207                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0382 L22:   0.0855                                     
REMARK   3      L33:   0.0584 L12:   0.1324                                     
REMARK   3      L13:  -0.0831 L23:  -0.0743                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0724 S12:  -0.0059 S13:   0.1597                       
REMARK   3      S21:  -0.0098 S22:  -0.0221 S23:   0.1012                       
REMARK   3      S31:  -0.1092 S32:   0.0782 S33:  -0.0000                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 152 THROUGH 166 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  34.6171  54.1505  60.7577              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1543 T22:   0.1870                                     
REMARK   3      T33:   0.1341 T12:  -0.0483                                     
REMARK   3      T13:   0.0131 T23:  -0.0140                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0147 L22:  -0.0066                                     
REMARK   3      L33:   0.0182 L12:  -0.0307                                     
REMARK   3      L13:  -0.0218 L23:  -0.0000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0407 S12:   0.0188 S13:   0.0882                       
REMARK   3      S21:  -0.0061 S22:  -0.0682 S23:  -0.0323                       
REMARK   3      S31:  -0.1231 S32:   0.1808 S33:  -0.0000                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 565 THROUGH 699 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  15.4042  30.6756  80.2422              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1357 T22:   0.1378                                     
REMARK   3      T33:   0.1018 T12:  -0.0156                                     
REMARK   3      T13:   0.0007 T23:   0.0035                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0515 L22:   0.1249                                     
REMARK   3      L33:   0.2077 L12:  -0.1089                                     
REMARK   3      L13:  -0.1871 L23:   0.0556                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0138 S12:  -0.0171 S13:   0.0180                       
REMARK   3      S21:   0.0120 S22:   0.0343 S23:  -0.0030                       
REMARK   3      S31:   0.0054 S32:   0.0851 S33:  -0.0000                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 700 THROUGH 818 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   9.3851  40.2530  49.1384              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1021 T22:   0.1133                                     
REMARK   3      T33:   0.1151 T12:  -0.0053                                     
REMARK   3      T13:   0.0057 T23:   0.0050                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1067 L22:  -0.0319                                     
REMARK   3      L33:   0.3345 L12:   0.1278                                     
REMARK   3      L13:  -0.0519 L23:  -0.0400                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0033 S12:   0.0075 S13:   0.0115                       
REMARK   3      S21:  -0.0126 S22:   0.0112 S23:   0.0381                       
REMARK   3      S31:  -0.0439 S32:  -0.0721 S33:   0.0000                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 819 THROUGH 1046 )                
REMARK   3    ORIGIN FOR THE GROUP (A):  24.0510  33.1123  32.0262              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0663 T22:   0.0693                                     
REMARK   3      T33:   0.0631 T12:  -0.0255                                     
REMARK   3      T13:   0.0138 T23:  -0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1764 L22:   0.2141                                     
REMARK   3      L33:   0.5241 L12:   0.0102                                     
REMARK   3      L13:  -0.0807 L23:  -0.0571                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0372 S12:   0.0287 S13:  -0.0017                       
REMARK   3      S21:  -0.0268 S22:   0.0225 S23:  -0.0257                       
REMARK   3      S31:   0.0141 S32:   0.0358 S33:  -0.0103                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 0 THROUGH 24 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  31.5623  12.1609  41.7635              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1168 T22:   0.1211                                     
REMARK   3      T33:   0.2087 T12:   0.0150                                     
REMARK   3      T13:   0.0030 T23:   0.0032                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0028 L22:   0.0829                                     
REMARK   3      L33:   0.0020 L12:  -0.0184                                     
REMARK   3      L13:   0.0265 L23:  -0.0467                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0641 S12:   0.0359 S13:   0.1782                       
REMARK   3      S21:   0.0774 S22:   0.0285 S23:  -0.1290                       
REMARK   3      S31:   0.0471 S32:   0.0068 S33:  -0.0000                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 25 THROUGH 34 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  32.2157  12.6716  55.8789              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2635 T22:   0.1648                                     
REMARK   3      T33:   0.4087 T12:   0.0095                                     
REMARK   3      T13:  -0.1055 T23:   0.0661                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0054 L22:   0.0030                                     
REMARK   3      L33:  -0.0001 L12:  -0.0073                                     
REMARK   3      L13:  -0.0001 L23:  -0.0101                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0604 S12:   0.0805 S13:  -0.1168                       
REMARK   3      S21:   0.0951 S22:   0.0838 S23:   0.0237                       
REMARK   3      S31:   0.0984 S32:  -0.0069 S33:   0.0000                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 35 THROUGH 48 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  39.9603  14.3438  46.0613              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2125 T22:   0.2500                                     
REMARK   3      T33:   0.3990 T12:   0.0622                                     
REMARK   3      T13:  -0.0987 T23:   0.0049                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0058 L22:   0.0115                                     
REMARK   3      L33:   0.0071 L12:   0.0093                                     
REMARK   3      L13:  -0.0246 L23:  -0.0050                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0098 S12:  -0.0628 S13:   0.0346                       
REMARK   3      S21:   0.0057 S22:  -0.1405 S23:  -0.1031                       
REMARK   3      S31:  -0.0705 S32:   0.1595 S33:   0.0046                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 49 THROUGH 74 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  29.4083  19.0519  36.2470              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1103 T22:   0.0922                                     
REMARK   3      T33:   0.1764 T12:  -0.0013                                     
REMARK   3      T13:   0.0129 T23:   0.0175                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0141 L22:   0.1189                                     
REMARK   3      L33:   0.0435 L12:   0.0422                                     
REMARK   3      L13:   0.1016 L23:   0.0833                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0651 S12:   0.0018 S13:  -0.0412                       
REMARK   3      S21:  -0.0182 S22:  -0.0302 S23:  -0.1724                       
REMARK   3      S31:  -0.0129 S32:  -0.0175 S33:  -0.0031                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 75 THROUGH 117 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  23.4273   8.9356  31.5689              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1320 T22:   0.1153                                     
REMARK   3      T33:   0.1314 T12:   0.0235                                     
REMARK   3      T13:   0.0210 T23:   0.0060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0314 L22:   0.1712                                     
REMARK   3      L33:   0.0256 L12:  -0.0070                                     
REMARK   3      L13:  -0.0907 L23:   0.0004                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0953 S12:   0.0545 S13:  -0.0143                       
REMARK   3      S21:  -0.1197 S22:  -0.0416 S23:   0.0139                       
REMARK   3      S31:   0.0050 S32:   0.0142 S33:  -0.0000                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 118 THROUGH 137 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  18.0800  -1.8122  36.4687              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1482 T22:   0.1286                                     
REMARK   3      T33:   0.2070 T12:   0.0098                                     
REMARK   3      T13:   0.0121 T23:  -0.0301                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0246 L22:   0.0185                                     
REMARK   3      L33:   0.0292 L12:  -0.0070                                     
REMARK   3      L13:   0.0341 L23:  -0.0049                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1025 S12:  -0.0449 S13:   0.0366                       
REMARK   3      S21:  -0.1267 S22:  -0.0367 S23:   0.2310                       
REMARK   3      S31:   0.0601 S32:   0.0420 S33:   0.0000                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 138 THROUGH 151 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  26.3776   1.1343  43.3065              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1380 T22:   0.1251                                     
REMARK   3      T33:   0.1385 T12:   0.0218                                     
REMARK   3      T13:   0.0009 T23:  -0.0098                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0146 L22:   0.0333                                     
REMARK   3      L33:   0.0049 L12:  -0.0015                                     
REMARK   3      L13:   0.0173 L23:  -0.0058                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0064 S12:  -0.0495 S13:   0.0082                       
REMARK   3      S21:   0.0139 S22:  -0.0151 S23:  -0.0346                       
REMARK   3      S31:  -0.0622 S32:   0.0273 S33:   0.0000                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 152 THROUGH 166 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  37.0196   3.4219  37.0246              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1369 T22:   0.1262                                     
REMARK   3      T33:   0.2146 T12:   0.0362                                     
REMARK   3      T13:   0.0264 T23:  -0.0033                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0166 L22:   0.0253                                     
REMARK   3      L33:   0.0029 L12:  -0.0166                                     
REMARK   3      L13:  -0.0025 L23:  -0.0035                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0832 S12:  -0.0293 S13:   0.0550                       
REMARK   3      S21:  -0.0312 S22:  -0.0603 S23:  -0.2243                       
REMARK   3      S31:   0.1673 S32:   0.0432 S33:   0.0000                       
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 6BVI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-DEC-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000231306.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-JUL-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-F                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
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 : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 154073                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.746                              
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     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 11.80                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.8900                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4NYI                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.43                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE, 2.0 M SODIUM       
REMARK 280  FORMATE, PH 4.0, VAPOR DIFFUSION, TEMPERATURE 292K                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z                                                 
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      11555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290      12555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290      13555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      14555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      15555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       92.16150            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       92.16150            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       89.54550            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       92.16150            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       92.16150            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       89.54550            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       92.16150            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       92.16150            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       89.54550            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       92.16150            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       92.16150            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       89.54550            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       92.16150            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       92.16150            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       89.54550            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       92.16150            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       92.16150            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       89.54550            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       92.16150            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       92.16150            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       89.54550            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       92.16150            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       92.16150            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       89.54550            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8870 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 35970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL                        
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B2832  LIES ON A SPECIAL POSITION.                          
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     0                                                      
REMARK 465     ASN B   591                                                      
REMARK 465     MET B   592                                                      
REMARK 465     GLN B   593                                                      
REMARK 465     PRO B   594                                                      
REMARK 465     LYS B   595                                                      
REMARK 465     ALA B   596                                                      
REMARK 465     ARG B   744                                                      
REMARK 465     ASP B   745                                                      
REMARK 465     ASN B   746                                                      
REMARK 465     GLY B   747                                                      
REMARK 465     PRO B   748                                                      
REMARK 465     GLY B   749                                                      
REMARK 465     HIS B   750                                                      
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   O    HOH B  2239     O    HOH B  2658              1.87            
REMARK 500   O    HOH B  2282     O    HOH B  2732              1.88            
REMARK 500   O    HOH B  2454     O    HOH B  2590              1.88            
REMARK 500   O    HOH B  2118     O    HOH B  2607              1.90            
REMARK 500   O    HOH B  2320     O    HOH B  2646              1.90            
REMARK 500   O    HOH B  2261     O    HOH B  2280              1.90            
REMARK 500   O    HOH C   301     O    HOH C   440              1.92            
REMARK 500   O    HOH A   306     O    HOH A   476              1.94            
REMARK 500   O    HOH C   395     O    HOH C   410              1.96            
REMARK 500   O    HOH A   413     O    HOH A   463              1.99            
REMARK 500   O    HOH C   326     O    HOH C   460              2.00            
REMARK 500   OE1  GLN A   129     O    HOH A   301              2.02            
REMARK 500   O    HOH B  2740     O    HOH B  2813              2.03            
REMARK 500   O    HOH C   375     O    HOH C   418              2.03            
REMARK 500   O    HOH B  2199     O    HOH B  2636              2.04            
REMARK 500   NH2  ARG C    68     O    HOH C   301              2.06            
REMARK 500   NH1  ARG C    68     O    HOH C   302              2.07            
REMARK 500   O    HOH C   399     O    HOH C   521              2.08            
REMARK 500   OD1  ASP B   620     O    HOH B  2101              2.09            
REMARK 500   O    HOH B  2708     O    HOH B  2758              2.10            
REMARK 500   O    HOH C   418     O    HOH C   467              2.11            
REMARK 500   O    HOH C   464     O    HOH C   505              2.11            
REMARK 500   O    HOH B  2407     O    HOH B  2677              2.11            
REMARK 500   O    HOH B  2152     O    HOH C   467              2.11            
REMARK 500   O    HOH B  2710     O    HOH B  2735              2.12            
REMARK 500   O    HOH B  2352     O    HOH B  2738              2.12            
REMARK 500   O    HOH C   391     O    HOH C   448              2.12            
REMARK 500   O    HOH B  2145     O    HOH B  2747              2.13            
REMARK 500   O    HOH A   409     O    HOH A   476              2.14            
REMARK 500   OE2  GLU B   654     O    HOH B  2102              2.14            
REMARK 500   O    HOH B  2256     O    HOH B  2649              2.16            
REMARK 500   O    HOH B  2368     O    HOH B  2519              2.17            
REMARK 500   O2   FMT C   201     O    HOH C   303              2.17            
REMARK 500   O    HOH B  2482     O    HOH B  2688              2.17            
REMARK 500   ND1  HIS B   905     O    HOH B  2103              2.18            
REMARK 500   O    HOH B  2299     O    HOH B  2329              2.18            
REMARK 500   O    HOH B  2332     O    HOH B  2735              2.18            
REMARK 500   O    HOH A   315     O    HOH A   426              2.18            
REMARK 500   O    HOH A   393     O    HOH A   397              2.18            
REMARK 500   O    HOH A   471     O    HOH B  2218              2.19            
REMARK 500   O    HOH B  2359     O    HOH B  2553              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B  2767     O    HOH B  2833     7556     2.02            
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    ILE A  36      -64.30    -99.40                                   
REMARK 500    ARG A 149       -4.41     82.56                                   
REMARK 500    HIS B 764     -119.19   -127.11                                   
REMARK 500    HIS B 770       62.70   -102.68                                   
REMARK 500    ASN C  26       99.12    -42.78                                   
REMARK 500    GLU C  37      110.75    -24.46                                   
REMARK 500    ASP C  38       45.09     70.40                                   
REMARK 500    ASP C  38       45.20     70.40                                   
REMARK 500    ASP C 119     -169.93   -160.17                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLN C   25     ASN C   26                  143.76                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 202  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A  17   OG                                                     
REMARK 620 2 THR A  35   OG1  84.5                                              
REMARK 620 3 GNP A 201   O1G 173.7  89.8                                        
REMARK 620 4 GNP A 201   O1B  92.9 176.6  92.9                                  
REMARK 620 5 HOH A 318   O    86.9  90.6  90.6  91.5                            
REMARK 620 6 HOH A 352   O    89.0  89.0  93.5  88.7 175.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA C 202  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C  87   OG1                                                    
REMARK 620 2 HOH C 477   O    66.7                                              
REMARK 620 3 HOH C 476   O   131.5 120.1                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GNP A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EC4 B 2001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 2002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 2003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 2004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 2005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 2006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 2007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 2008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT C 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA C 202                  
DBREF  6BVI A    1   166  UNP    P01112   RASH_HUMAN       1    166             
DBREF  6BVI B  566  1046  UNP    Q07889   SOS1_HUMAN     566   1046             
DBREF  6BVI C    1   166  UNP    P01112   RASH_HUMAN       1    166             
SEQADV 6BVI GLY A    0  UNP  P01112              EXPRESSION TAG                 
SEQADV 6BVI ALA A   64  UNP  P01112    TYR    64 ENGINEERED MUTATION            
SEQADV 6BVI GLY B  565  UNP  Q07889              EXPRESSION TAG                 
SEQADV 6BVI GLY C    0  UNP  P01112              EXPRESSION TAG                 
SEQRES   1 A  167  GLY MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA GLY          
SEQRES   2 A  167  GLY VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN          
SEQRES   3 A  167  ASN HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP          
SEQRES   4 A  167  SER TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CSO          
SEQRES   5 A  167  LEU LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU ALA          
SEQRES   6 A  167  SER ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY          
SEQRES   7 A  167  PHE LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE          
SEQRES   8 A  167  GLU ASP ILE HIS GLN TYR ARG GLU GLN ILE LYS ARG VAL          
SEQRES   9 A  167  LYS ASP SER ASP ASP VAL PRO MET VAL LEU VAL GLY ASN          
SEQRES  10 A  167  LYS CYS ASP LEU ALA ALA ARG THR VAL GLU SER ARG GLN          
SEQRES  11 A  167  ALA GLN ASP LEU ALA ARG SER TYR GLY ILE PRO TYR ILE          
SEQRES  12 A  167  GLU THR SER ALA LYS THR ARG GLN GLY VAL GLU ASP ALA          
SEQRES  13 A  167  PHE TYR THR LEU VAL ARG GLU ILE ARG GLN HIS                  
SEQRES   1 B  482  GLY GLN MET ARG LEU PRO SER ALA ASP VAL TYR ARG PHE          
SEQRES   2 B  482  ALA GLU PRO ASP SER GLU GLU ASN ILE ILE PHE GLU GLU          
SEQRES   3 B  482  ASN MET GLN PRO LYS ALA GLY ILE PRO ILE ILE LYS ALA          
SEQRES   4 B  482  GLY THR VAL ILE LYS LEU ILE GLU ARG LEU THR TYR HIS          
SEQRES   5 B  482  MET TYR ALA ASP PRO ASN PHE VAL ARG THR PHE LEU THR          
SEQRES   6 B  482  THR TYR ARG SER PHE CYS LYS PRO GLN GLU LEU LEU SER          
SEQRES   7 B  482  LEU ILE ILE GLU ARG PHE GLU ILE PRO GLU PRO GLU PRO          
SEQRES   8 B  482  THR GLU ALA ASP ARG ILE ALA ILE GLU ASN GLY ASP GLN          
SEQRES   9 B  482  PRO LEU SER ALA GLU LEU LYS ARG PHE ARG LYS GLU TYR          
SEQRES  10 B  482  ILE GLN PRO VAL GLN LEU ARG VAL LEU ASN VAL CYS ARG          
SEQRES  11 B  482  HIS TRP VAL GLU HIS HIS PHE TYR ASP PHE GLU ARG ASP          
SEQRES  12 B  482  ALA TYR LEU LEU GLN ARG MET GLU GLU PHE ILE GLY THR          
SEQRES  13 B  482  VAL ARG GLY LYS ALA MET LYS LYS TRP VAL GLU SER ILE          
SEQRES  14 B  482  THR LYS ILE ILE GLN ARG LYS LYS ILE ALA ARG ASP ASN          
SEQRES  15 B  482  GLY PRO GLY HIS ASN ILE THR PHE GLN SER SER PRO PRO          
SEQRES  16 B  482  THR VAL GLU TRP HIS ILE SER ARG PRO GLY HIS ILE GLU          
SEQRES  17 B  482  THR PHE ASP LEU LEU THR LEU HIS PRO ILE GLU ILE ALA          
SEQRES  18 B  482  ARG GLN LEU THR LEU LEU GLU SER ASP LEU TYR ARG ALA          
SEQRES  19 B  482  VAL GLN PRO SER GLU LEU VAL GLY SER VAL TRP THR LYS          
SEQRES  20 B  482  GLU ASP LYS GLU ILE ASN SER PRO ASN LEU LEU LYS MET          
SEQRES  21 B  482  ILE ARG HIS THR THR ASN LEU THR LEU TRP PHE GLU LYS          
SEQRES  22 B  482  CYS ILE VAL GLU THR GLU ASN LEU GLU GLU ARG VAL ALA          
SEQRES  23 B  482  VAL VAL SER ARG ILE ILE GLU ILE LEU GLN VAL PHE GLN          
SEQRES  24 B  482  GLU LEU ASN ASN PHE ASN GLY VAL LEU GLU VAL VAL SER          
SEQRES  25 B  482  ALA MET ASN SER SER PRO VAL TYR ARG LEU ASP HIS THR          
SEQRES  26 B  482  PHE GLU GLN ILE PRO SER ARG GLN LYS LYS ILE LEU GLU          
SEQRES  27 B  482  GLU ALA HIS GLU LEU SER GLU ASP HIS TYR LYS LYS TYR          
SEQRES  28 B  482  LEU ALA LYS LEU ARG SER ILE ASN PRO PRO CYS VAL PRO          
SEQRES  29 B  482  PHE PHE GLY ILE TYR LEU THR ASN ILE LEU LYS THR GLU          
SEQRES  30 B  482  GLU GLY ASN PRO GLU VAL LEU LYS ARG HIS GLY LYS GLU          
SEQRES  31 B  482  LEU ILE ASN PHE SER LYS ARG ARG LYS VAL ALA GLU ILE          
SEQRES  32 B  482  THR GLY GLU ILE GLN GLN TYR GLN ASN GLN PRO TYR CYS          
SEQRES  33 B  482  LEU ARG VAL GLU SER ASP ILE LYS ARG PHE PHE GLU ASN          
SEQRES  34 B  482  LEU ASN PRO MET GLY ASN SER MET GLU LYS GLU PHE THR          
SEQRES  35 B  482  ASP TYR LEU PHE ASN LYS SER LEU GLU ILE GLU PRO ARG          
SEQRES  36 B  482  ASN PRO LYS PRO LEU PRO ARG PHE PRO LYS LYS TYR SER          
SEQRES  37 B  482  TYR PRO LEU LYS SER PRO GLY VAL ARG PRO SER ASN PRO          
SEQRES  38 B  482  ARG                                                          
SEQRES   1 C  167  GLY MET THR GLU TYR LYS LEU VAL VAL VAL GLY ALA GLY          
SEQRES   2 C  167  GLY VAL GLY LYS SER ALA LEU THR ILE GLN LEU ILE GLN          
SEQRES   3 C  167  ASN HIS PHE VAL ASP GLU TYR ASP PRO THR ILE GLU ASP          
SEQRES   4 C  167  SER TYR ARG LYS GLN VAL VAL ILE ASP GLY GLU THR CYS          
SEQRES   5 C  167  LEU LEU ASP ILE LEU ASP THR ALA GLY GLN GLU GLU TYR          
SEQRES   6 C  167  SER ALA MET ARG ASP GLN TYR MET ARG THR GLY GLU GLY          
SEQRES   7 C  167  PHE LEU CYS VAL PHE ALA ILE ASN ASN THR LYS SER PHE          
SEQRES   8 C  167  GLU ASP ILE HIS GLN TYR ARG GLU GLN ILE LYS ARG VAL          
SEQRES   9 C  167  LYS ASP SER ASP ASP VAL PRO MET VAL LEU VAL GLY ASN          
SEQRES  10 C  167  LYS CYS ASP LEU ALA ALA ARG THR VAL GLU SER ARG GLN          
SEQRES  11 C  167  ALA GLN ASP LEU ALA ARG SER TYR GLY ILE PRO TYR ILE          
SEQRES  12 C  167  GLU THR SER ALA LYS THR ARG GLN GLY VAL GLU ASP ALA          
SEQRES  13 C  167  PHE TYR THR LEU VAL ARG GLU ILE ARG GLN HIS                  
MODRES 6BVI CSO A   51  CYS  MODIFIED RESIDUE                                   
HET    CSO  A  51       7                                                       
HET    GNP  A 201      32                                                       
HET     MG  A 202       1                                                       
HET    EC4  B2001      33                                                       
HET    FMT  B2002       3                                                       
HET    FMT  B2003       3                                                       
HET    FMT  B2004       3                                                       
HET    FMT  B2005       3                                                       
HET    FMT  B2006       3                                                       
HET    GOL  B2007       6                                                       
HET    GOL  B2008       6                                                       
HET    FMT  C 201       3                                                       
HET     NA  C 202       1                                                       
HETNAM     CSO S-HYDROXYCYSTEINE                                                
HETNAM     GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     EC4 6-CHLORO-N-{1-[(5-CHLORO-1H-INDOL-3-YL)                          
HETNAM   2 EC4  METHYL]PIPERIDIN-4-YL}-L-TRYPTOPHANAMIDE                        
HETNAM     FMT FORMIC ACID                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM      NA SODIUM ION                                                       
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  CSO    C3 H7 N O3 S                                                 
FORMUL   4  GNP    C10 H17 N6 O13 P3                                            
FORMUL   5   MG    MG 2+                                                        
FORMUL   6  EC4    C25 H27 CL2 N5 O                                             
FORMUL   7  FMT    6(C H2 O2)                                                   
FORMUL  12  GOL    2(C3 H8 O3)                                                  
FORMUL  15   NA    NA 1+                                                        
FORMUL  16  HOH   *1161(H2 O)                                                   
HELIX    1 AA1 GLY A   15  ASN A   26  1                                  12    
HELIX    2 AA2 GLN A   61  SER A   65  5                                   5    
HELIX    3 AA3 ARG A   68  GLY A   75  1                                   8    
HELIX    4 AA4 ASN A   86  ASP A   92  1                                   7    
HELIX    5 AA5 ASP A   92  ASP A  105  1                                  14    
HELIX    6 AA6 GLU A  126  GLY A  138  1                                  13    
HELIX    7 AA7 GLY A  151  GLN A  165  1                                  15    
HELIX    8 AA8 TYR B  575  GLU B  579  5                                   5    
HELIX    9 AA9 THR B  605  THR B  614  1                                  10    
HELIX   10 AB1 ASP B  620  TYR B  631  1                                  12    
HELIX   11 AB2 ARG B  632  PHE B  634  5                                   3    
HELIX   12 AB3 LYS B  636  GLU B  649  1                                  14    
HELIX   13 AB4 THR B  656  ASN B  665  1                                  10    
HELIX   14 AB5 SER B  671  TYR B  681  1                                  11    
HELIX   15 AB6 TYR B  681  HIS B  700  1                                  20    
HELIX   16 AB7 PHE B  701  ASP B  707  1                                   7    
HELIX   17 AB8 ASP B  707  THR B  720  1                                  14    
HELIX   18 AB9 MET B  726  ALA B  743  1                                  18    
HELIX   19 AC1 HIS B  770  PHE B  774  5                                   5    
HELIX   20 AC2 HIS B  780  ALA B  798  1                                  19    
HELIX   21 AC3 GLN B  800  LYS B  811  5                                  12    
HELIX   22 AC4 ASP B  813  SER B  818  1                                   6    
HELIX   23 AC5 SER B  818  GLU B  841  1                                  24    
HELIX   24 AC6 ASN B  844  LEU B  865  1                                  22    
HELIX   25 AC7 ASN B  867  ASN B  879  1                                  13    
HELIX   26 AC8 SER B  880  ARG B  885  1                                   6    
HELIX   27 AC9 LEU B  886  GLU B  891  1                                   6    
HELIX   28 AD1 PRO B  894  LEU B  907  1                                  14    
HELIX   29 AD2 SER B  908  ARG B  920  1                                  13    
HELIX   30 AD3 PHE B  930  GLY B  943  1                                  14    
HELIX   31 AD4 PHE B  958  GLN B  975  1                                  18    
HELIX   32 AD5 GLU B  984  ASN B  993  1                                  10    
HELIX   33 AD6 MET B 1001  GLU B 1017  1                                  17    
HELIX   34 AD7 SER C   17  GLN C   25  1                                   9    
HELIX   35 AD8 TYR C   64  ALA C   66  5                                   3    
HELIX   36 AD9 MET C   67  THR C   74  1                                   8    
HELIX   37 AE1 ASN C   86  ASP C   92  1                                   7    
HELIX   38 AE2 ASP C   92  ASP C  105  1                                  14    
HELIX   39 AE3 GLU C  126  GLY C  138  1                                  13    
HELIX   40 AE4 GLY C  151  GLN C  165  1                                  15    
SHEET    1 AA1 6 GLU A  37  ILE A  46  0                                        
SHEET    2 AA1 6 GLU A  49  THR A  58 -1  O  LEU A  53   N  LYS A  42           
SHEET    3 AA1 6 THR A   2  GLY A  10  1  N  TYR A   4   O  ASP A  54           
SHEET    4 AA1 6 GLY A  77  ALA A  83  1  O  VAL A  81   N  VAL A   9           
SHEET    5 AA1 6 MET A 111  ASN A 116  1  O  ASN A 116   N  PHE A  82           
SHEET    6 AA1 6 TYR A 141  GLU A 143  1  O  ILE A 142   N  LEU A 113           
SHEET    1 AA2 4 ILE B 586  PHE B 588  0                                        
SHEET    2 AA2 4 ILE B 601  GLY B 604 -1  O  ALA B 603   N  ILE B 587           
SHEET    3 AA2 4 LYS B 953  ASN B 957 -1  O  ILE B 956   N  GLY B 604           
SHEET    4 AA2 4 VAL B 947  ARG B 950 -1  N  LEU B 948   O  LEU B 955           
SHEET    1 AA3 6 ARG C  41  ILE C  46  0                                        
SHEET    2 AA3 6 GLU C  49  ASP C  57 -1  O  LEU C  53   N  LYS C  42           
SHEET    3 AA3 6 THR C   2  GLY C  10  1  N  LEU C   6   O  LEU C  56           
SHEET    4 AA3 6 GLY C  77  ALA C  83  1  O  VAL C  81   N  VAL C   9           
SHEET    5 AA3 6 MET C 111  LYS C 117  1  O  ASN C 116   N  PHE C  82           
SHEET    6 AA3 6 TYR C 141  SER C 145  1  O  THR C 144   N  LYS C 117           
LINK         OG  SER A  17                MG    MG A 202     1555   1555  2.08  
LINK         OG1 THR A  35                MG    MG A 202     1555   1555  2.08  
LINK         C   THR A  50                 N   CSO A  51     1555   1555  1.32  
LINK         C   CSO A  51                 N   LEU A  52     1555   1555  1.32  
LINK         OG1BTHR C  87                NA    NA C 202     1555   1555  3.17  
LINK         O1G GNP A 201                MG    MG A 202     1555   1555  2.02  
LINK         O1B GNP A 201                MG    MG A 202     1555   1555  2.08  
LINK        MG    MG A 202                 O   HOH A 318     1555   1555  2.12  
LINK        MG    MG A 202                 O   HOH A 352     1555   1555  2.10  
LINK        NA    NA C 202                 O   HOH C 477     1555   1555  2.74  
LINK        NA    NA C 202                 O   HOH C 476     1555   1555  2.30  
CISPEP   1 PRO B  924    PRO B  925          0        11.30                     
CISPEP   2 ASN B 1020    PRO B 1021          0         6.87                     
SITE     1 AC1 31 GLY A  12  GLY A  13  VAL A  14  GLY A  15                    
SITE     2 AC1 31 LYS A  16  SER A  17  ALA A  18  PHE A  28                    
SITE     3 AC1 31 VAL A  29  ASP A  30  GLU A  31  TYR A  32                    
SITE     4 AC1 31 PRO A  34  THR A  35  GLY A  60  GLN A  61                    
SITE     5 AC1 31 ASN A 116  LYS A 117  ASP A 119  LEU A 120                    
SITE     6 AC1 31 SER A 145  ALA A 146  LYS A 147   MG A 202                    
SITE     7 AC1 31 HOH A 318  HOH A 347  HOH A 352  HOH A 371                    
SITE     8 AC1 31 HOH A 386  HOH A 398  HOH A 427                               
SITE     1 AC2  5 SER A  17  THR A  35  GNP A 201  HOH A 318                    
SITE     2 AC2  5 HOH A 352                                                     
SITE     1 AC3 10 MET B 878  ASN B 879  TYR B 884  PHE B 890                    
SITE     2 AC3 10 LYS B 898  LEU B 901  GLU B 902  HOH B2227                    
SITE     3 AC3 10 HOH B2502  HOH B2560                                          
SITE     1 AC4  7 GLN B 566  MET B 567  HIS B 616  MET B 617                    
SITE     2 AC4  7 HOH B2169  HOH B2322  HOH B2336                               
SITE     1 AC5  3 ARG A 128  ARG B 767  PRO B 768                               
SITE     1 AC6  7 GLU A  37  MET A  67  GLN A  70  ALA B 619                    
SITE     2 AC6  7 ARG B 688  HOH B2148  HOH B2260                               
SITE     1 AC7  6 GLU B 611  TYR B 615  HIS B 616  ARG B 647                    
SITE     2 AC7  6 TYR B 681  HOH B2273                                          
SITE     1 AC8  1 TYR B1031                                                     
SITE     1 AC9  5 SER B 793  ASP B 794  PRO B 978  TYR B 979                    
SITE     2 AC9  5 HOH B2275                                                     
SITE     1 AD1  5 ARG B 786  GLU B 864  VAL B1040  HOH B2113                    
SITE     2 AD1  5 HOH B2215                                                     
SITE     1 AD2  6 LEU B 938  LYS C  16  SER C  17  ALA C  59                    
SITE     2 AD2  6 HOH C 303  HOH C 400                                          
SITE     1 AD3  6 ASN C  85  ASN C  86  THR C  87  THR C 124                    
SITE     2 AD3  6 HOH C 476  HOH C 477                                          
CRYST1  184.323  184.323  179.091  90.00  90.00  90.00 I 4 2 2      16          
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      0.005425  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005425  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005584        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system