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Database: PDB
Entry: 4PBQ
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Original site: 4PBQ 
HEADER    SOLUTE-BINDING PROTEIN                  13-APR-14   4PBQ              
TITLE     CRYSTAL STRUCTURE OF A TRAP PERIPLASMIC SOLUTE BINDING PROTEIN FROM   
TITLE    2 HAEMOPHILUS INFLUENZAE RDAW (HICG_00826, TARGET EFI-510123) WITH     
TITLE    3 BOUND L-GULONATE                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE TRAP PERIPLASMIC SOLUTE BINDING PROTEIN;          
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HAEMOPHILUS INFLUENZAE;                         
SOURCE   3 ORGANISM_TAXID: 656912;                                              
SOURCE   4 STRAIN: RDAW;                                                        
SOURCE   5 GENE: HICG_00826;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET                                       
KEYWDS    TRAP PERIPLASMIC SOLUTE BINDING FAMILY, ENZYME FUNCTION INITIATIVE,   
KEYWDS   2 EFI, STRUCTURAL GENOMICS, SOLUTE-BINDING PROTEIN                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.W.VETTING,N.F.AL OBAIDI,L.L.MORISCO,S.R.WASSERMAN,M.STEAD,          
AUTHOR   2 J.D.ATTONITO,A.SCOTT GLENN,S.CHOWDHURY,B.EVANS,B.HILLERICH,J.LOVE,   
AUTHOR   3 R.D.SEIDEL,K.L.WHALEN,J.A.GERLT,S.C.ALMO,ENZYME FUNCTION INITIATIVE  
AUTHOR   4 (EFI)                                                                
REVDAT   6   25-DEC-19 4PBQ    1       REMARK                                   
REVDAT   5   27-SEP-17 4PBQ    1       REMARK                                   
REVDAT   4   26-AUG-15 4PBQ    1       REMARK                                   
REVDAT   3   25-FEB-15 4PBQ    1       JRNL                                     
REVDAT   2   14-MAY-14 4PBQ    1       REMARK HET    HETNAM FORMUL              
REVDAT   2 2                   1       SITE                                     
REVDAT   1   07-MAY-14 4PBQ    0                                                
JRNL        AUTH   M.W.VETTING,N.AL-OBAIDI,S.ZHAO,B.SAN FRANCISCO,J.KIM,        
JRNL        AUTH 2 D.J.WICHELECKI,J.T.BOUVIER,J.O.SOLBIATI,H.VU,X.ZHANG,        
JRNL        AUTH 3 D.A.RODIONOV,J.D.LOVE,B.S.HILLERICH,R.D.SEIDEL,R.J.QUINN,    
JRNL        AUTH 4 A.L.OSTERMAN,J.E.CRONAN,M.P.JACOBSON,J.A.GERLT,S.C.ALMO      
JRNL        TITL   EXPERIMENTAL STRATEGIES FOR FUNCTIONAL ANNOTATION AND        
JRNL        TITL 2 METABOLISM DISCOVERY: TARGETED SCREENING OF SOLUTE BINDING   
JRNL        TITL 3 PROTEINS AND UNBIASED PANNING OF METABOLOMES.                
JRNL        REF    BIOCHEMISTRY                  V.  54   909 2015              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   25540822                                                     
JRNL        DOI    10.1021/BI501388Y                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.1_1168)                   
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.11                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 237186                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.149                           
REMARK   3   R VALUE            (WORKING SET) : 0.147                           
REMARK   3   FREE R VALUE                     : 0.184                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 11938                           
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 37.1205 -  5.1226    0.96     7434   412  0.1695 0.1983        
REMARK   3     2  5.1226 -  4.0676    0.99     7643   458  0.1139 0.1506        
REMARK   3     3  4.0676 -  3.5539    0.98     7652   416  0.1200 0.1487        
REMARK   3     4  3.5539 -  3.2292    0.98     7653   381  0.1372 0.1599        
REMARK   3     5  3.2292 -  2.9978    0.98     7670   408  0.1409 0.1579        
REMARK   3     6  2.9978 -  2.8211    0.98     7623   401  0.1405 0.1942        
REMARK   3     7  2.8211 -  2.6799    0.98     7596   411  0.1299 0.1630        
REMARK   3     8  2.6799 -  2.5633    0.98     7611   369  0.1246 0.1820        
REMARK   3     9  2.5633 -  2.4646    0.98     7639   406  0.1194 0.1497        
REMARK   3    10  2.4646 -  2.3796    0.97     7560   419  0.1242 0.1736        
REMARK   3    11  2.3796 -  2.3052    0.97     7630   371  0.1232 0.1638        
REMARK   3    12  2.3052 -  2.2393    0.97     7570   416  0.1192 0.1573        
REMARK   3    13  2.2393 -  2.1804    0.97     7493   399  0.1205 0.1604        
REMARK   3    14  2.1804 -  2.1272    0.97     7538   400  0.1325 0.1851        
REMARK   3    15  2.1272 -  2.0788    0.97     7437   420  0.1394 0.1958        
REMARK   3    16  2.0788 -  2.0346    0.97     7630   404  0.1412 0.1844        
REMARK   3    17  2.0346 -  1.9939    0.97     7533   371  0.1518 0.2123        
REMARK   3    18  1.9939 -  1.9563    0.97     7590   339  0.1683 0.2170        
REMARK   3    19  1.9563 -  1.9213    0.96     7361   444  0.1626 0.1890        
REMARK   3    20  1.9213 -  1.8888    0.96     7563   410  0.1687 0.2150        
REMARK   3    21  1.8888 -  1.8583    0.96     7458   372  0.1841 0.2102        
REMARK   3    22  1.8583 -  1.8297    0.95     7323   403  0.1965 0.2460        
REMARK   3    23  1.8297 -  1.8028    0.95     7481   408  0.2029 0.2299        
REMARK   3    24  1.8028 -  1.7774    0.96     7333   402  0.2139 0.2411        
REMARK   3    25  1.7774 -  1.7534    0.94     7411   373  0.2249 0.2680        
REMARK   3    26  1.7534 -  1.7306    0.95     7379   406  0.2278 0.2559        
REMARK   3    27  1.7306 -  1.7090    0.95     7299   390  0.2351 0.2561        
REMARK   3    28  1.7090 -  1.6884    0.95     7470   381  0.2389 0.2467        
REMARK   3    29  1.6884 -  1.6687    0.94     7289   367  0.2561 0.2914        
REMARK   3    30  1.6687 -  1.6500    0.94     7379   381  0.2585 0.2841        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.160            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.110           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 14.08                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.87                          
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      :  0.011           7814                                  
REMARK   3   ANGLE     :  1.179          10560                                  
REMARK   3   CHIRALITY :  0.070           1131                                  
REMARK   3   PLANARITY :  0.006           1347                                  
REMARK   3   DIHEDRAL  : 14.424           3022                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 24                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 25 THROUGH 112 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  22.6668   0.4138  22.4766              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0622 T22:   0.0266                                     
REMARK   3      T33:   0.0687 T12:   0.0121                                     
REMARK   3      T13:   0.0086 T23:  -0.0004                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9930 L22:   0.8658                                     
REMARK   3      L33:   1.0440 L12:  -0.0959                                     
REMARK   3      L13:  -0.2581 L23:   0.0083                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0453 S12:  -0.0080 S13:  -0.0021                       
REMARK   3      S21:  -0.0693 S22:  -0.0234 S23:  -0.1437                       
REMARK   3      S31:   0.0419 S32:   0.0814 S33:  -0.0167                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 113 THROUGH 172 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   7.9353  -4.4875  24.7661              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0820 T22:   0.0291                                     
REMARK   3      T33:   0.0602 T12:  -0.0023                                     
REMARK   3      T13:  -0.0174 T23:   0.0083                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0959 L22:   0.9372                                     
REMARK   3      L33:   0.8264 L12:   0.0348                                     
REMARK   3      L13:  -0.0213 L23:   0.0462                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0179 S12:   0.1007 S13:  -0.1115                       
REMARK   3      S21:  -0.0368 S22:  -0.0215 S23:   0.0704                       
REMARK   3      S31:   0.1393 S32:  -0.1776 S33:   0.0190                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 173 THROUGH 233 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   5.1628   2.3254  35.5809              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0779 T22:   0.0585                                     
REMARK   3      T33:   0.0685 T12:   0.0009                                     
REMARK   3      T13:   0.0026 T23:   0.0181                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7564 L22:   1.1719                                     
REMARK   3      L33:   1.1751 L12:   0.0220                                     
REMARK   3      L13:   0.0562 L23:  -0.0222                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0189 S12:  -0.0995 S13:  -0.0554                       
REMARK   3      S21:   0.1042 S22:   0.0331 S23:   0.0556                       
REMARK   3      S31:  -0.0486 S32:  -0.0523 S33:  -0.0097                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 234 THROUGH 283 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  23.9797  -7.4945  23.1038              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0951 T22:   0.0463                                     
REMARK   3      T33:   0.0858 T12:   0.0212                                     
REMARK   3      T13:  -0.0044 T23:  -0.0027                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8503 L22:   0.6052                                     
REMARK   3      L33:   1.8531 L12:  -0.0743                                     
REMARK   3      L13:  -0.6915 L23:  -0.0271                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0272 S12:  -0.0296 S13:  -0.1408                       
REMARK   3      S21:  -0.0015 S22:   0.0117 S23:  -0.1049                       
REMARK   3      S31:   0.1330 S32:   0.1123 S33:  -0.0292                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 284 THROUGH 313 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.7356  -7.8881  29.6984              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1261 T22:   0.1197                                     
REMARK   3      T33:   0.1914 T12:  -0.0447                                     
REMARK   3      T13:  -0.0209 T23:   0.0468                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1647 L22:   0.6928                                     
REMARK   3      L33:   1.4648 L12:  -0.0458                                     
REMARK   3      L13:   0.4471 L23:   0.7336                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0346 S12:  -0.1218 S13:  -0.2759                       
REMARK   3      S21:   0.0147 S22:  -0.1092 S23:   0.1220                       
REMARK   3      S31:  -0.0031 S32:  -0.3441 S33:   0.0449                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 314 THROUGH 328 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   2.0925 -11.0479  10.8083              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2960 T22:   0.1956                                     
REMARK   3      T33:   0.2195 T12:  -0.0541                                     
REMARK   3      T13:  -0.0741 T23:  -0.0387                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1464 L22:   3.6199                                     
REMARK   3      L33:   0.8235 L12:  -1.2836                                     
REMARK   3      L13:   0.4477 L23:  -1.0324                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0984 S12:   0.0628 S13:  -0.1520                       
REMARK   3      S21:  -0.9425 S22:   0.0973 S23:   0.3575                       
REMARK   3      S31:   0.3681 S32:  -0.3127 S33:   0.0016                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 25 THROUGH 82 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  22.5414  37.9033  13.2696              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0903 T22:   0.0978                                     
REMARK   3      T33:   0.1107 T12:   0.0064                                     
REMARK   3      T13:   0.0122 T23:   0.0267                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0937 L22:   1.0063                                     
REMARK   3      L33:   1.4424 L12:   0.3669                                     
REMARK   3      L13:  -0.3439 L23:  -0.3228                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0081 S12:   0.1646 S13:   0.1367                       
REMARK   3      S21:  -0.0706 S22:   0.1043 S23:   0.1045                       
REMARK   3      S31:  -0.1666 S32:  -0.2263 S33:  -0.0761                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 83 THROUGH 112 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  34.5095  24.6365  20.5067              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0763 T22:   0.0777                                     
REMARK   3      T33:   0.1081 T12:  -0.0111                                     
REMARK   3      T13:   0.0186 T23:  -0.0120                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0986 L22:   0.7187                                     
REMARK   3      L33:   1.2729 L12:   0.1836                                     
REMARK   3      L13:  -0.2161 L23:  -0.3704                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0306 S12:  -0.0187 S13:  -0.0201                       
REMARK   3      S21:  -0.0349 S22:  -0.0164 S23:  -0.1274                       
REMARK   3      S31:   0.0550 S32:   0.1178 S33:  -0.0001                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 113 THROUGH 135 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  41.5071  29.9445  16.9822              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1055 T22:   0.1354                                     
REMARK   3      T33:   0.1489 T12:  -0.0134                                     
REMARK   3      T13:   0.0363 T23:   0.0131                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7935 L22:   0.7288                                     
REMARK   3      L33:   1.4050 L12:   0.4155                                     
REMARK   3      L13:   0.6357 L23:  -0.3456                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0422 S12:   0.1044 S13:   0.0600                       
REMARK   3      S21:  -0.0938 S22:  -0.0557 S23:  -0.2012                       
REMARK   3      S31:   0.0390 S32:   0.4797 S33:   0.0399                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 136 THROUGH 152 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  31.7058  30.2461  25.0065              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0772 T22:   0.0787                                     
REMARK   3      T33:   0.0879 T12:  -0.0267                                     
REMARK   3      T13:   0.0034 T23:  -0.0140                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3451 L22:   0.4533                                     
REMARK   3      L33:   0.6989 L12:   0.0823                                     
REMARK   3      L13:  -0.0745 L23:  -0.1294                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0323 S12:  -0.0675 S13:   0.0665                       
REMARK   3      S21:   0.0720 S22:  -0.0457 S23:  -0.0843                       
REMARK   3      S31:  -0.0994 S32:   0.0794 S33:   0.0165                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 153 THROUGH 190 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  27.5078  16.7444  36.6667              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0914 T22:   0.1120                                     
REMARK   3      T33:   0.0888 T12:   0.0038                                     
REMARK   3      T13:  -0.0219 T23:   0.0138                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3478 L22:   0.9617                                     
REMARK   3      L33:   1.5281 L12:   0.2613                                     
REMARK   3      L13:   0.2140 L23:   0.0462                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0048 S12:  -0.2870 S13:  -0.1850                       
REMARK   3      S21:   0.2027 S22:   0.0463 S23:  -0.0605                       
REMARK   3      S31:   0.0456 S32:  -0.0255 S33:  -0.0551                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 191 THROUGH 233 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  21.9137  27.1728  35.7128              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1060 T22:   0.0850                                     
REMARK   3      T33:   0.0853 T12:  -0.0086                                     
REMARK   3      T13:   0.0036 T23:  -0.0225                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3054 L22:   0.8309                                     
REMARK   3      L33:   0.5984 L12:   0.3192                                     
REMARK   3      L13:  -0.0996 L23:  -0.4041                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0851 S12:  -0.0873 S13:   0.1074                       
REMARK   3      S21:   0.1423 S22:  -0.0111 S23:   0.0340                       
REMARK   3      S31:  -0.1802 S32:  -0.0048 S33:  -0.0518                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 234 THROUGH 283 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  31.2837  39.2447  17.6256              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1136 T22:   0.0560                                     
REMARK   3      T33:   0.1220 T12:  -0.0323                                     
REMARK   3      T13:   0.0338 T23:  -0.0118                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7359 L22:   0.7446                                     
REMARK   3      L33:   1.8286 L12:   0.1149                                     
REMARK   3      L13:  -0.1725 L23:  -0.5197                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0336 S12:  -0.0102 S13:   0.1459                       
REMARK   3      S21:   0.0537 S22:   0.0140 S23:  -0.0079                       
REMARK   3      S31:  -0.3118 S32:   0.0885 S33:  -0.0187                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 284 THROUGH 313 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  37.5516  21.1006  38.5223              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1490 T22:   0.1810                                     
REMARK   3      T33:   0.1609 T12:  -0.0265                                     
REMARK   3      T13:  -0.0609 T23:  -0.0145                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4080 L22:   0.9515                                     
REMARK   3      L33:   1.3370 L12:  -0.1335                                     
REMARK   3      L13:  -0.1227 L23:  -0.7133                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0344 S12:  -0.2627 S13:  -0.0371                       
REMARK   3      S21:   0.1804 S22:  -0.0151 S23:  -0.1649                       
REMARK   3      S31:  -0.0200 S32:   0.2354 S33:   0.0329                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 314 THROUGH 328 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  48.8153  21.5602  22.1588              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1106 T22:   0.2734                                     
REMARK   3      T33:   0.2513 T12:   0.0000                                     
REMARK   3      T13:  -0.0013 T23:   0.0025                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7391 L22:   3.8423                                     
REMARK   3      L33:   1.1716 L12:   2.2209                                     
REMARK   3      L13:   0.8353 L23:   1.2610                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0260 S12:   0.1896 S13:  -0.2894                       
REMARK   3      S21:   0.1000 S22:   0.1892 S23:  -0.5385                       
REMARK   3      S31:   0.1836 S32:   0.3426 S33:  -0.0665                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 25 THROUGH 55 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -11.7227  15.5466  18.4725              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1015 T22:   0.1066                                     
REMARK   3      T33:   0.1019 T12:   0.0137                                     
REMARK   3      T13:  -0.0271 T23:  -0.0025                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2730 L22:   0.9860                                     
REMARK   3      L33:   2.1018 L12:   0.0721                                     
REMARK   3      L13:   0.3762 L23:  -0.0134                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0241 S12:  -0.0214 S13:  -0.0620                       
REMARK   3      S21:  -0.0772 S22:  -0.0722 S23:   0.1906                       
REMARK   3      S31:   0.3371 S32:  -0.0725 S33:   0.0490                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 56 THROUGH 82 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.5010  14.1266  19.6046              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1445 T22:   0.0942                                     
REMARK   3      T33:   0.0731 T12:   0.0458                                     
REMARK   3      T13:  -0.0138 T23:   0.0076                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6098 L22:   0.5545                                     
REMARK   3      L33:   1.6197 L12:  -0.3332                                     
REMARK   3      L13:  -0.1410 L23:  -0.3048                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0266 S12:  -0.0270 S13:  -0.0840                       
REMARK   3      S21:  -0.1834 S22:  -0.0774 S23:  -0.0260                       
REMARK   3      S31:   0.2478 S32:   0.0712 S33:   0.0032                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 83 THROUGH 112 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.0546  32.4380  22.6489              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0628 T22:   0.0896                                     
REMARK   3      T33:   0.1121 T12:   0.0228                                     
REMARK   3      T13:  -0.0114 T23:   0.0106                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8426 L22:   0.5231                                     
REMARK   3      L33:   1.0075 L12:   0.0724                                     
REMARK   3      L13:   0.1015 L23:  -0.3166                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0232 S12:   0.0073 S13:   0.1457                       
REMARK   3      S21:  -0.1466 S22:  -0.0614 S23:  -0.0749                       
REMARK   3      S31:  -0.1110 S32:   0.0353 S33:   0.0508                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 113 THROUGH 152 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.5989  33.2694  18.7179              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0821 T22:   0.1265                                     
REMARK   3      T33:   0.1376 T12:   0.0205                                     
REMARK   3      T13:  -0.0196 T23:   0.0093                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7493 L22:   0.7932                                     
REMARK   3      L33:   0.6786 L12:  -0.2155                                     
REMARK   3      L13:   0.3639 L23:  -0.1465                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0039 S12:   0.1454 S13:   0.2183                       
REMARK   3      S21:  -0.1148 S22:  -0.0811 S23:   0.0345                       
REMARK   3      S31:  -0.1845 S32:  -0.0432 S33:   0.0656                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 153 THROUGH 190 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   1.2442  36.2198  41.3486              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1525 T22:   0.0900                                     
REMARK   3      T33:   0.1376 T12:   0.0199                                     
REMARK   3      T13:  -0.0438 T23:  -0.0693                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8379 L22:   1.4360                                     
REMARK   3      L33:   0.9542 L12:  -0.2564                                     
REMARK   3      L13:   0.3091 L23:   0.0836                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1029 S12:  -0.1639 S13:   0.2614                       
REMARK   3      S21:   0.1883 S22:  -0.0849 S23:  -0.0270                       
REMARK   3      S31:  -0.2666 S32:  -0.0276 S33:  -0.0331                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 191 THROUGH 233 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.7769  27.4962  40.6493              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0777 T22:   0.1519                                     
REMARK   3      T33:   0.1028 T12:   0.0135                                     
REMARK   3      T13:   0.0161 T23:  -0.0526                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6731 L22:   0.8791                                     
REMARK   3      L33:   1.2883 L12:  -0.0101                                     
REMARK   3      L13:   0.3422 L23:   0.0323                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0037 S12:  -0.1387 S13:   0.0375                       
REMARK   3      S21:   0.1237 S22:  -0.0304 S23:   0.1536                       
REMARK   3      S31:   0.0194 S32:  -0.3012 S33:   0.0106                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 234 THROUGH 283 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -11.4777  23.8466  17.2026              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0479 T22:   0.1137                                     
REMARK   3      T33:   0.1054 T12:   0.0369                                     
REMARK   3      T13:  -0.0336 T23:  -0.0099                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0715 L22:   0.9304                                     
REMARK   3      L33:   1.3607 L12:   0.3546                                     
REMARK   3      L13:   0.2141 L23:   0.0109                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0125 S12:  -0.0659 S13:   0.1482                       
REMARK   3      S21:  -0.1503 S22:  -0.0582 S23:   0.1905                       
REMARK   3      S31:  -0.0388 S32:  -0.1169 S33:   0.0105                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 284 THROUGH 313 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.6934  44.2640  36.1571              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2133 T22:   0.0904                                     
REMARK   3      T33:   0.2681 T12:   0.0548                                     
REMARK   3      T13:  -0.0622 T23:  -0.0570                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8535 L22:   1.0524                                     
REMARK   3      L33:   1.8366 L12:   0.1195                                     
REMARK   3      L13:   0.3828 L23:  -0.1932                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1295 S12:  -0.0118 S13:   0.2410                       
REMARK   3      S21:   0.1746 S22:  -0.0598 S23:   0.0292                       
REMARK   3      S31:  -0.5195 S32:  -0.2031 S33:   0.0773                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 314 THROUGH 328 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.0498  46.2313  17.1241              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2685 T22:   0.1447                                     
REMARK   3      T33:   0.3129 T12:  -0.0220                                     
REMARK   3      T13:  -0.0576 T23:   0.0472                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2058 L22:   0.7987                                     
REMARK   3      L33:   0.6869 L12:   0.4197                                     
REMARK   3      L13:   0.3402 L23:   0.0137                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0285 S12:   0.1212 S13:   0.7174                       
REMARK   3      S21:  -0.0887 S22:  -0.0684 S23:  -0.2202                       
REMARK   3      S31:  -0.3133 S32:   0.0752 S33:   0.0379                       
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 4PBQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-APR-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000201116.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-MAR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 31-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.1.27                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 121100                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 103.200                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : 0.10600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.68                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.71900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.40                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN (23.86 MG/ML, 10 MM HEPES PH     
REMARK 280  7.5, 5 MM DTT, 10 MM L-GULONATE); RESERVOIR (0.2 M AMMONIUM         
REMARK 280  SULFATE, 0.1 M MES PH 6.5, 30 %(W/V) PEG 5000 MME);                 
REMARK 280  CRYOPROTECTION (80% RESERVOIR + 20% DIETHYLENE GLYCOL), PH 7.0,     
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       66.72450            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.26850            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       66.72450            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       38.26850            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 B 541  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     MSE A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     HIS A     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 465     HIS A     6                                                      
REMARK 465     HIS A     7                                                      
REMARK 465     HIS A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     GLY A    11                                                      
REMARK 465     VAL A    12                                                      
REMARK 465     ASP A    13                                                      
REMARK 465     LEU A    14                                                      
REMARK 465     GLY A    15                                                      
REMARK 465     THR A    16                                                      
REMARK 465     GLU A    17                                                      
REMARK 465     ASN A    18                                                      
REMARK 465     LEU A    19                                                      
REMARK 465     TYR A    20                                                      
REMARK 465     PHE A    21                                                      
REMARK 465     GLN A    22                                                      
REMARK 465     SER A    23                                                      
REMARK 465     MSE A    24                                                      
REMARK 465     MSE B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     HIS B     4                                                      
REMARK 465     HIS B     5                                                      
REMARK 465     HIS B     6                                                      
REMARK 465     HIS B     7                                                      
REMARK 465     HIS B     8                                                      
REMARK 465     SER B     9                                                      
REMARK 465     SER B    10                                                      
REMARK 465     GLY B    11                                                      
REMARK 465     VAL B    12                                                      
REMARK 465     ASP B    13                                                      
REMARK 465     LEU B    14                                                      
REMARK 465     GLY B    15                                                      
REMARK 465     THR B    16                                                      
REMARK 465     GLU B    17                                                      
REMARK 465     ASN B    18                                                      
REMARK 465     LEU B    19                                                      
REMARK 465     TYR B    20                                                      
REMARK 465     PHE B    21                                                      
REMARK 465     GLN B    22                                                      
REMARK 465     SER B    23                                                      
REMARK 465     MSE B    24                                                      
REMARK 465     MSE C     2                                                      
REMARK 465     HIS C     3                                                      
REMARK 465     HIS C     4                                                      
REMARK 465     HIS C     5                                                      
REMARK 465     HIS C     6                                                      
REMARK 465     HIS C     7                                                      
REMARK 465     HIS C     8                                                      
REMARK 465     SER C     9                                                      
REMARK 465     SER C    10                                                      
REMARK 465     GLY C    11                                                      
REMARK 465     VAL C    12                                                      
REMARK 465     ASP C    13                                                      
REMARK 465     LEU C    14                                                      
REMARK 465     GLY C    15                                                      
REMARK 465     THR C    16                                                      
REMARK 465     GLU C    17                                                      
REMARK 465     ASN C    18                                                      
REMARK 465     LEU C    19                                                      
REMARK 465     TYR C    20                                                      
REMARK 465     PHE C    21                                                      
REMARK 465     GLN C    22                                                      
REMARK 465     SER C    23                                                      
REMARK 465     MSE C    24                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS C 304    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   HE2  HIS C    32     HD1  HIS C    41              1.35            
REMARK 500   HE2  HIS A    32     HD1  HIS A    41              1.35            
REMARK 500   O    HOH A   894     O    HOH C   798              1.96            
REMARK 500   O    HOH C   759     O    HOH C   813              1.98            
REMARK 500   O    HOH C   889     O    HOH C   900              2.02            
REMARK 500   O    HOH C   557     O    HOH C   558              2.02            
REMARK 500   O    HOH A   789     O    HOH A   900              2.03            
REMARK 500   O    HOH A   527     O    HOH A   618              2.05            
REMARK 500   O    HOH A   709     O    HOH A   714              2.05            
REMARK 500   O    HOH C   669     O    HOH C   762              2.05            
REMARK 500   O    HOH B   819     O    HOH B   861              2.06            
REMARK 500   O    HOH B   852     O    HOH B   895              2.06            
REMARK 500   OD1  ASP C   308     O    HOH C   501              2.07            
REMARK 500   O    HOH B   871     O    HOH B   900              2.09            
REMARK 500   O    HOH A   897     O    HOH B   830              2.09            
REMARK 500   O    HOH A   865     O    HOH A   927              2.09            
REMARK 500   O    HOH A   793     O    HOH A   938              2.10            
REMARK 500   O    HOH B   683     O    HOH B   744              2.10            
REMARK 500   O    HOH A   727     O    HOH A   846              2.11            
REMARK 500   O    HOH A   806     O    HOH A   963              2.11            
REMARK 500   O    HOH C   749     O    HOH C   872              2.13            
REMARK 500   OD1  ASN C    67     O    HOH C   765              2.13            
REMARK 500   O    HOH C   696     O    HOH C   842              2.13            
REMARK 500   O    HOH A   927     O    HOH B   738              2.13            
REMARK 500   O    HOH C   799     O    HOH C   840              2.14            
REMARK 500   O    HOH C   819     O    HOH C   883              2.14            
REMARK 500   O    HOH B   787     O    HOH B   902              2.14            
REMARK 500   O    HOH C   799     O    HOH C   856              2.15            
REMARK 500   O    HOH A   770     O    HOH A   775              2.15            
REMARK 500   O    HOH A   864     O    HOH A   927              2.16            
REMARK 500   O    HOH A   783     O    HOH A   884              2.16            
REMARK 500   O    HOH C   831     O    HOH C   844              2.17            
REMARK 500   O    HOH A   971     O    HOH A   988              2.17            
REMARK 500   O    HOH A   911     O    HOH A   937              2.17            
REMARK 500   O    HOH A   808     O    HOH A   887              2.18            
REMARK 500   O    HOH C   818     O    HOH C   825              2.18            
REMARK 500   O    HOH C   841     O    HOH C   891              2.18            
REMARK 500   O    HOH A   849     O    HOH A   965              2.18            
REMARK 500   OH   TYR C   314     O    HOH C   745              2.18            
REMARK 500   O    HOH C   545     O    HOH C   564              2.19            
REMARK 500   NZ   LYS A   127     O    HOH A   872              2.19            
REMARK 500   O    HOH B   785     O    HOH B   800              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 A   559     O    HOH C   562     4546     2.13            
REMARK 500   O    HOH A   547     O    HOH C   529     4546     2.14            
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    ASN A 172      111.84   -160.73                                   
REMARK 500    LEU B  92       31.99    -99.99                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 912        DISTANCE =  6.37 ANGSTROMS                       
REMARK 525    HOH A 935        DISTANCE =  6.24 ANGSTROMS                       
REMARK 525    HOH A 960        DISTANCE =  6.23 ANGSTROMS                       
REMARK 525    HOH A 991        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH A1010        DISTANCE =  6.39 ANGSTROMS                       
REMARK 525    HOH B 879        DISTANCE =  6.65 ANGSTROMS                       
REMARK 525    HOH B 901        DISTANCE =  6.58 ANGSTROMS                       
REMARK 525    HOH B 916        DISTANCE =  6.30 ANGSTROMS                       
REMARK 525    HOH B 918        DISTANCE =  6.00 ANGSTROMS                       
REMARK 525    HOH C 720        DISTANCE =  5.82 ANGSTROMS                       
REMARK 525    HOH C 831        DISTANCE =  6.10 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 2UF A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MES A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 2UF B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 2UF C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 406                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EFI-510123   RELATED DB: TARGETTRACK                     
DBREF  4PBQ A   25   328  UNP    C9MHP2   C9MHP2_HAEIF    25    328             
DBREF  4PBQ B   25   328  UNP    C9MHP2   C9MHP2_HAEIF    25    328             
DBREF  4PBQ C   25   328  UNP    C9MHP2   C9MHP2_HAEIF    25    328             
SEQADV 4PBQ MSE A    2  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ HIS A    3  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ HIS A    4  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ HIS A    5  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ HIS A    6  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ HIS A    7  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ HIS A    8  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ SER A    9  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ SER A   10  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ GLY A   11  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ VAL A   12  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ ASP A   13  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ LEU A   14  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ GLY A   15  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ THR A   16  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ GLU A   17  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ ASN A   18  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ LEU A   19  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ TYR A   20  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ PHE A   21  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ GLN A   22  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ SER A   23  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ MSE A   24  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ MSE B    2  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ HIS B    3  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ HIS B    4  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ HIS B    5  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ HIS B    6  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ HIS B    7  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ HIS B    8  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ SER B    9  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ SER B   10  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ GLY B   11  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ VAL B   12  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ ASP B   13  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ LEU B   14  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ GLY B   15  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ THR B   16  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ GLU B   17  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ ASN B   18  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ LEU B   19  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ TYR B   20  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ PHE B   21  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ GLN B   22  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ SER B   23  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ MSE B   24  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ MSE C    2  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ HIS C    3  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ HIS C    4  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ HIS C    5  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ HIS C    6  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ HIS C    7  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ HIS C    8  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ SER C    9  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ SER C   10  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ GLY C   11  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ VAL C   12  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ ASP C   13  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ LEU C   14  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ GLY C   15  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ THR C   16  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ GLU C   17  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ ASN C   18  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ LEU C   19  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ TYR C   20  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ PHE C   21  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ GLN C   22  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ SER C   23  UNP  C9MHP2              EXPRESSION TAG                 
SEQADV 4PBQ MSE C   24  UNP  C9MHP2              EXPRESSION TAG                 
SEQRES   1 A  327  MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  327  GLY THR GLU ASN LEU TYR PHE GLN SER MSE LYS THR ILE          
SEQRES   3 A  327  ILE LYS LEU GLY HIS TYR ASN SER ASP ILE HIS PRO SER          
SEQRES   4 A  327  HIS ILE ALA LEU GLN GLU TYR PHE LYS LYS THR ILE GLU          
SEQRES   5 A  327  ASN GLU THR ASN HIS LYS TYR GLU ILE ARG LEU TYR PRO          
SEQRES   6 A  327  ASN ASN GLN LEU GLY GLY GLU ASP GLN ILE VAL ASN GLY          
SEQRES   7 A  327  LEU ARG ASN GLY THR ILE GLU ALA GLY ILE THR GLY LEU          
SEQRES   8 A  327  LEU LEU GLN ASN VAL ASP PRO ILE PHE GLY VAL TRP GLU          
SEQRES   9 A  327  TRP PRO TYR LEU PHE LYS ASP ASN GLN GLU ALA LYS LYS          
SEQRES  10 A  327  VAL LEU GLU SER PRO ILE ALA ASN LYS ILE GLY GLN LYS          
SEQRES  11 A  327  MSE GLU LYS TYR GLY ILE LYS LEU LEU ALA TYR GLY MSE          
SEQRES  12 A  327  ASN GLY PHE ARG VAL ILE SER SER ASN LYS LYS LEU GLU          
SEQRES  13 A  327  LYS PHE ASP ASP PHE LYS GLY LEU ARG LEU ARG VAL PRO          
SEQRES  14 A  327  LEU ASN SER LEU PHE VAL ASP TRP ALA LYS ALA MSE ASN          
SEQRES  15 A  327  ILE ASN PRO GLN SER MSE PRO LEU SER GLU VAL PHE THR          
SEQRES  16 A  327  ALA LEU GLU GLN LYS VAL ILE ASP GLY GLN GLU ASN PRO          
SEQRES  17 A  327  TYR MSE LEU ILE LYS ASP SER GLY LEU TYR GLU VAL GLN          
SEQRES  18 A  327  LYS TYR ILE ILE GLN SER ASN HIS ILE PHE SER PRO GLY          
SEQRES  19 A  327  LEU LEU GLN ILE SER LEU LYS THR TRP ASN LYS ILE PRO          
SEQRES  20 A  327  LYS GLU ASP GLN ILE ILE PHE GLU LYS ALA ALA LYS LEU          
SEQRES  21 A  327  TYR GLN GLU LYS GLU TRP GLU LEU ALA ILE LYS THR GLU          
SEQRES  22 A  327  LEU GLU VAL LYS ASP TYR LEU ALA LYS HIS GLY ASN GLU          
SEQRES  23 A  327  ILE ILE VAL PRO SER GLU ALA PHE LYS ASN ASP MSE VAL          
SEQRES  24 A  327  ASN ALA SER LYS VAL LEU TYR ASP SER PHE TYR LYS LYS          
SEQRES  25 A  327  TYR ASP TRP ALA LYS ASP VAL VAL GLN LYS ILE ASN GLU          
SEQRES  26 A  327  ALA LYS                                                      
SEQRES   1 B  327  MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 B  327  GLY THR GLU ASN LEU TYR PHE GLN SER MSE LYS THR ILE          
SEQRES   3 B  327  ILE LYS LEU GLY HIS TYR ASN SER ASP ILE HIS PRO SER          
SEQRES   4 B  327  HIS ILE ALA LEU GLN GLU TYR PHE LYS LYS THR ILE GLU          
SEQRES   5 B  327  ASN GLU THR ASN HIS LYS TYR GLU ILE ARG LEU TYR PRO          
SEQRES   6 B  327  ASN ASN GLN LEU GLY GLY GLU ASP GLN ILE VAL ASN GLY          
SEQRES   7 B  327  LEU ARG ASN GLY THR ILE GLU ALA GLY ILE THR GLY LEU          
SEQRES   8 B  327  LEU LEU GLN ASN VAL ASP PRO ILE PHE GLY VAL TRP GLU          
SEQRES   9 B  327  TRP PRO TYR LEU PHE LYS ASP ASN GLN GLU ALA LYS LYS          
SEQRES  10 B  327  VAL LEU GLU SER PRO ILE ALA ASN LYS ILE GLY GLN LYS          
SEQRES  11 B  327  MSE GLU LYS TYR GLY ILE LYS LEU LEU ALA TYR GLY MSE          
SEQRES  12 B  327  ASN GLY PHE ARG VAL ILE SER SER ASN LYS LYS LEU GLU          
SEQRES  13 B  327  LYS PHE ASP ASP PHE LYS GLY LEU ARG LEU ARG VAL PRO          
SEQRES  14 B  327  LEU ASN SER LEU PHE VAL ASP TRP ALA LYS ALA MSE ASN          
SEQRES  15 B  327  ILE ASN PRO GLN SER MSE PRO LEU SER GLU VAL PHE THR          
SEQRES  16 B  327  ALA LEU GLU GLN LYS VAL ILE ASP GLY GLN GLU ASN PRO          
SEQRES  17 B  327  TYR MSE LEU ILE LYS ASP SER GLY LEU TYR GLU VAL GLN          
SEQRES  18 B  327  LYS TYR ILE ILE GLN SER ASN HIS ILE PHE SER PRO GLY          
SEQRES  19 B  327  LEU LEU GLN ILE SER LEU LYS THR TRP ASN LYS ILE PRO          
SEQRES  20 B  327  LYS GLU ASP GLN ILE ILE PHE GLU LYS ALA ALA LYS LEU          
SEQRES  21 B  327  TYR GLN GLU LYS GLU TRP GLU LEU ALA ILE LYS THR GLU          
SEQRES  22 B  327  LEU GLU VAL LYS ASP TYR LEU ALA LYS HIS GLY ASN GLU          
SEQRES  23 B  327  ILE ILE VAL PRO SER GLU ALA PHE LYS ASN ASP MSE VAL          
SEQRES  24 B  327  ASN ALA SER LYS VAL LEU TYR ASP SER PHE TYR LYS LYS          
SEQRES  25 B  327  TYR ASP TRP ALA LYS ASP VAL VAL GLN LYS ILE ASN GLU          
SEQRES  26 B  327  ALA LYS                                                      
SEQRES   1 C  327  MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 C  327  GLY THR GLU ASN LEU TYR PHE GLN SER MSE LYS THR ILE          
SEQRES   3 C  327  ILE LYS LEU GLY HIS TYR ASN SER ASP ILE HIS PRO SER          
SEQRES   4 C  327  HIS ILE ALA LEU GLN GLU TYR PHE LYS LYS THR ILE GLU          
SEQRES   5 C  327  ASN GLU THR ASN HIS LYS TYR GLU ILE ARG LEU TYR PRO          
SEQRES   6 C  327  ASN ASN GLN LEU GLY GLY GLU ASP GLN ILE VAL ASN GLY          
SEQRES   7 C  327  LEU ARG ASN GLY THR ILE GLU ALA GLY ILE THR GLY LEU          
SEQRES   8 C  327  LEU LEU GLN ASN VAL ASP PRO ILE PHE GLY VAL TRP GLU          
SEQRES   9 C  327  TRP PRO TYR LEU PHE LYS ASP ASN GLN GLU ALA LYS LYS          
SEQRES  10 C  327  VAL LEU GLU SER PRO ILE ALA ASN LYS ILE GLY GLN LYS          
SEQRES  11 C  327  MSE GLU LYS TYR GLY ILE LYS LEU LEU ALA TYR GLY MSE          
SEQRES  12 C  327  ASN GLY PHE ARG VAL ILE SER SER ASN LYS LYS LEU GLU          
SEQRES  13 C  327  LYS PHE ASP ASP PHE LYS GLY LEU ARG LEU ARG VAL PRO          
SEQRES  14 C  327  LEU ASN SER LEU PHE VAL ASP TRP ALA LYS ALA MSE ASN          
SEQRES  15 C  327  ILE ASN PRO GLN SER MSE PRO LEU SER GLU VAL PHE THR          
SEQRES  16 C  327  ALA LEU GLU GLN LYS VAL ILE ASP GLY GLN GLU ASN PRO          
SEQRES  17 C  327  TYR MSE LEU ILE LYS ASP SER GLY LEU TYR GLU VAL GLN          
SEQRES  18 C  327  LYS TYR ILE ILE GLN SER ASN HIS ILE PHE SER PRO GLY          
SEQRES  19 C  327  LEU LEU GLN ILE SER LEU LYS THR TRP ASN LYS ILE PRO          
SEQRES  20 C  327  LYS GLU ASP GLN ILE ILE PHE GLU LYS ALA ALA LYS LEU          
SEQRES  21 C  327  TYR GLN GLU LYS GLU TRP GLU LEU ALA ILE LYS THR GLU          
SEQRES  22 C  327  LEU GLU VAL LYS ASP TYR LEU ALA LYS HIS GLY ASN GLU          
SEQRES  23 C  327  ILE ILE VAL PRO SER GLU ALA PHE LYS ASN ASP MSE VAL          
SEQRES  24 C  327  ASN ALA SER LYS VAL LEU TYR ASP SER PHE TYR LYS LYS          
SEQRES  25 C  327  TYR ASP TRP ALA LYS ASP VAL VAL GLN LYS ILE ASN GLU          
SEQRES  26 C  327  ALA LYS                                                      
MODRES 4PBQ MSE A  132  MET  MODIFIED RESIDUE                                   
MODRES 4PBQ MSE A  144  MET  MODIFIED RESIDUE                                   
MODRES 4PBQ MSE A  182  MET  MODIFIED RESIDUE                                   
MODRES 4PBQ MSE A  189  MET  MODIFIED RESIDUE                                   
MODRES 4PBQ MSE A  211  MET  MODIFIED RESIDUE                                   
MODRES 4PBQ MSE A  299  MET  MODIFIED RESIDUE                                   
MODRES 4PBQ MSE B  132  MET  MODIFIED RESIDUE                                   
MODRES 4PBQ MSE B  144  MET  MODIFIED RESIDUE                                   
MODRES 4PBQ MSE B  182  MET  MODIFIED RESIDUE                                   
MODRES 4PBQ MSE B  189  MET  MODIFIED RESIDUE                                   
MODRES 4PBQ MSE B  211  MET  MODIFIED RESIDUE                                   
MODRES 4PBQ MSE B  299  MET  MODIFIED RESIDUE                                   
MODRES 4PBQ MSE C  132  MET  MODIFIED RESIDUE                                   
MODRES 4PBQ MSE C  144  MET  MODIFIED RESIDUE                                   
MODRES 4PBQ MSE C  182  MET  MODIFIED RESIDUE                                   
MODRES 4PBQ MSE C  189  MET  MODIFIED RESIDUE                                   
MODRES 4PBQ MSE C  211  MET  MODIFIED RESIDUE                                   
MODRES 4PBQ MSE C  299  MET  MODIFIED RESIDUE                                   
HET    MSE  A 132      17                                                       
HET    MSE  A 144      17                                                       
HET    MSE  A 182      17                                                       
HET    MSE  A 189      17                                                       
HET    MSE  A 211      17                                                       
HET    MSE  A 299      17                                                       
HET    MSE  B 132      17                                                       
HET    MSE  B 144      17                                                       
HET    MSE  B 182      17                                                       
HET    MSE  B 189      34                                                       
HET    MSE  B 211      17                                                       
HET    MSE  B 299      17                                                       
HET    MSE  C 132      17                                                       
HET    MSE  C 144      17                                                       
HET    MSE  C 182      17                                                       
HET    MSE  C 189      18                                                       
HET    MSE  C 211      17                                                       
HET    MSE  C 299      17                                                       
HET    2UF  A 401      13                                                       
HET    SO4  A 402       5                                                       
HET    MES  A 403      12                                                       
HET    2UF  B 401      13                                                       
HET    SO4  B 402       5                                                       
HET    2UF  C 401      13                                                       
HET    SO4  C 402       5                                                       
HET    SO4  C 403       5                                                       
HET    PEG  C 404       7                                                       
HET    PEG  C 405       7                                                       
HET    PEG  C 406       7                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     2UF L-GULONATE                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
FORMUL   1  MSE    18(C5 H11 N O2 SE)                                           
FORMUL   4  2UF    3(C6 H12 O7)                                                 
FORMUL   5  SO4    4(O4 S 2-)                                                   
FORMUL   6  MES    C6 H13 N O4 S                                                
FORMUL  12  PEG    3(C4 H10 O3)                                                 
FORMUL  15  HOH   *1371(H2 O)                                                   
HELIX    1 AA1 HIS A   38  TYR A   47  1                                  10    
HELIX    2 AA2 TYR A   47  THR A   56  1                                  10    
HELIX    3 AA3 GLY A   72  GLY A   83  1                                  12    
HELIX    4 AA4 LEU A   92  VAL A   97  5                                   6    
HELIX    5 AA5 ASP A   98  TRP A  106  5                                   9    
HELIX    6 AA6 ASP A  112  GLU A  121  1                                  10    
HELIX    7 AA7 SER A  122  LYS A  131  1                                  10    
HELIX    8 AA8 MSE A  132  TYR A  135  5                                   4    
HELIX    9 AA9 LYS A  158  LYS A  163  5                                   6    
HELIX   10 AB1 ASN A  172  MSE A  182  1                                  11    
HELIX   11 AB2 PRO A  190  SER A  192  5                                   3    
HELIX   12 AB3 GLU A  193  GLN A  200  1                                   8    
HELIX   13 AB4 TYR A  210  SER A  216  1                                   7    
HELIX   14 AB5 GLY A  217  GLN A  222  5                                   6    
HELIX   15 AB6 LEU A  241  ASN A  245  1                                   5    
HELIX   16 AB7 PRO A  248  LYS A  283  1                                  36    
HELIX   17 AB8 SER A  292  TYR A  314  1                                  23    
HELIX   18 AB9 TRP A  316  LYS A  328  1                                  13    
HELIX   19 AC1 HIS B   38  TYR B   47  1                                  10    
HELIX   20 AC2 TYR B   47  THR B   56  1                                  10    
HELIX   21 AC3 GLY B   72  GLY B   83  1                                  12    
HELIX   22 AC4 LEU B   92  VAL B   97  5                                   6    
HELIX   23 AC5 ASP B   98  TRP B  106  5                                   9    
HELIX   24 AC6 ASP B  112  GLU B  121  1                                  10    
HELIX   25 AC7 SER B  122  LYS B  131  1                                  10    
HELIX   26 AC8 MSE B  132  TYR B  135  5                                   4    
HELIX   27 AC9 LYS B  158  LYS B  163  5                                   6    
HELIX   28 AD1 ASN B  172  MSE B  182  1                                  11    
HELIX   29 AD2 PRO B  190  SER B  192  5                                   3    
HELIX   30 AD3 GLU B  193  GLN B  200  1                                   8    
HELIX   31 AD4 TYR B  210  SER B  216  1                                   7    
HELIX   32 AD5 GLY B  217  GLN B  222  5                                   6    
HELIX   33 AD6 LEU B  241  ASN B  245  1                                   5    
HELIX   34 AD7 PRO B  248  HIS B  284  1                                  37    
HELIX   35 AD8 SER B  292  TYR B  314  1                                  23    
HELIX   36 AD9 TRP B  316  LYS B  328  1                                  13    
HELIX   37 AE1 HIS C   38  TYR C   47  1                                  10    
HELIX   38 AE2 TYR C   47  THR C   56  1                                  10    
HELIX   39 AE3 GLY C   72  GLY C   83  1                                  12    
HELIX   40 AE4 LEU C   92  VAL C   97  5                                   6    
HELIX   41 AE5 ASP C   98  TRP C  106  5                                   9    
HELIX   42 AE6 ASP C  112  GLU C  121  1                                  10    
HELIX   43 AE7 SER C  122  MSE C  132  1                                  11    
HELIX   44 AE8 GLU C  133  TYR C  135  5                                   3    
HELIX   45 AE9 LYS C  158  LYS C  163  5                                   6    
HELIX   46 AF1 ASN C  172  MSE C  182  1                                  11    
HELIX   47 AF2 PRO C  190  SER C  192  5                                   3    
HELIX   48 AF3 GLU C  193  GLN C  200  1                                   8    
HELIX   49 AF4 TYR C  210  SER C  216  1                                   7    
HELIX   50 AF5 GLY C  217  GLN C  222  5                                   6    
HELIX   51 AF6 LEU C  241  ASN C  245  1                                   5    
HELIX   52 AF7 PRO C  248  HIS C  284  1                                  37    
HELIX   53 AF8 SER C  292  TYR C  314  1                                  23    
HELIX   54 AF9 TRP C  316  LYS C  328  1                                  13    
SHEET    1 AA1 6 TYR A  60  TYR A  65  0                                        
SHEET    2 AA1 6 THR A  26  GLY A  31  1  N  ILE A  28   O  GLU A  61           
SHEET    3 AA1 6 ALA A  87  THR A  90  1  O  ALA A  87   N  LYS A  29           
SHEET    4 AA1 6 PHE A 232  SER A 240 -1  O  LEU A 236   N  THR A  90           
SHEET    5 AA1 6 ILE A 137  SER A 152 -1  N  LEU A 140   O  LEU A 237           
SHEET    6 AA1 6 GLY A 205  PRO A 209 -1  O  ASN A 208   N  VAL A 149           
SHEET    1 AA2 7 TYR A  60  TYR A  65  0                                        
SHEET    2 AA2 7 THR A  26  GLY A  31  1  N  ILE A  28   O  GLU A  61           
SHEET    3 AA2 7 ALA A  87  THR A  90  1  O  ALA A  87   N  LYS A  29           
SHEET    4 AA2 7 PHE A 232  SER A 240 -1  O  LEU A 236   N  THR A  90           
SHEET    5 AA2 7 ILE A 137  SER A 152 -1  N  LEU A 140   O  LEU A 237           
SHEET    6 AA2 7 TYR A 224  ILE A 226 -1  O  ILE A 226   N  ILE A 150           
SHEET    7 AA2 7 GLU A 287  ILE A 289  1  O  ILE A 289   N  ILE A 225           
SHEET    1 AA3 2 ARG A 166  VAL A 169  0                                        
SHEET    2 AA3 2 ASN A 185  SER A 188  1  O  ASN A 185   N  LEU A 167           
SHEET    1 AA4 6 TYR B  60  TYR B  65  0                                        
SHEET    2 AA4 6 THR B  26  GLY B  31  1  N  LEU B  30   O  ARG B  63           
SHEET    3 AA4 6 ALA B  87  THR B  90  1  O  ALA B  87   N  GLY B  31           
SHEET    4 AA4 6 PHE B 232  SER B 240 -1  O  LEU B 236   N  THR B  90           
SHEET    5 AA4 6 ILE B 137  SER B 152 -1  N  LEU B 140   O  LEU B 237           
SHEET    6 AA4 6 GLY B 205  PRO B 209 -1  O  ASN B 208   N  VAL B 149           
SHEET    1 AA5 7 TYR B  60  TYR B  65  0                                        
SHEET    2 AA5 7 THR B  26  GLY B  31  1  N  LEU B  30   O  ARG B  63           
SHEET    3 AA5 7 ALA B  87  THR B  90  1  O  ALA B  87   N  GLY B  31           
SHEET    4 AA5 7 PHE B 232  SER B 240 -1  O  LEU B 236   N  THR B  90           
SHEET    5 AA5 7 ILE B 137  SER B 152 -1  N  LEU B 140   O  LEU B 237           
SHEET    6 AA5 7 TYR B 224  ILE B 226 -1  O  ILE B 226   N  ILE B 150           
SHEET    7 AA5 7 GLU B 287  ILE B 289  1  O  ILE B 289   N  ILE B 225           
SHEET    1 AA6 2 ARG B 166  VAL B 169  0                                        
SHEET    2 AA6 2 ASN B 185  SER B 188  1  O  GLN B 187   N  LEU B 167           
SHEET    1 AA7 6 TYR C  60  TYR C  65  0                                        
SHEET    2 AA7 6 THR C  26  GLY C  31  1  N  LEU C  30   O  ARG C  63           
SHEET    3 AA7 6 ALA C  87  THR C  90  1  O  ALA C  87   N  GLY C  31           
SHEET    4 AA7 6 PHE C 232  SER C 240 -1  O  GLN C 238   N  GLY C  88           
SHEET    5 AA7 6 ILE C 137  SER C 152 -1  N  LYS C 138   O  ILE C 239           
SHEET    6 AA7 6 GLY C 205  PRO C 209 -1  O  ASN C 208   N  VAL C 149           
SHEET    1 AA8 7 TYR C  60  TYR C  65  0                                        
SHEET    2 AA8 7 THR C  26  GLY C  31  1  N  LEU C  30   O  ARG C  63           
SHEET    3 AA8 7 ALA C  87  THR C  90  1  O  ALA C  87   N  GLY C  31           
SHEET    4 AA8 7 PHE C 232  SER C 240 -1  O  GLN C 238   N  GLY C  88           
SHEET    5 AA8 7 ILE C 137  SER C 152 -1  N  LYS C 138   O  ILE C 239           
SHEET    6 AA8 7 TYR C 224  ILE C 226 -1  O  ILE C 226   N  ILE C 150           
SHEET    7 AA8 7 GLU C 287  ILE C 289  1  O  ILE C 289   N  ILE C 225           
SHEET    1 AA9 2 ARG C 166  VAL C 169  0                                        
SHEET    2 AA9 2 ASN C 185  SER C 188  1  O  GLN C 187   N  VAL C 169           
LINK         C   LYS A 131                 N   MSE A 132     1555   1555  1.33  
LINK         C   MSE A 132                 N   GLU A 133     1555   1555  1.33  
LINK         C   GLY A 143                 N   MSE A 144     1555   1555  1.32  
LINK         C   MSE A 144                 N   ASN A 145     1555   1555  1.34  
LINK         C   ALA A 181                 N   MSE A 182     1555   1555  1.33  
LINK         C   MSE A 182                 N   ASN A 183     1555   1555  1.33  
LINK         C   SER A 188                 N   MSE A 189     1555   1555  1.33  
LINK         C   MSE A 189                 N   PRO A 190     1555   1555  1.33  
LINK         C   TYR A 210                 N   MSE A 211     1555   1555  1.34  
LINK         C   MSE A 211                 N   LEU A 212     1555   1555  1.33  
LINK         C   ASP A 298                 N   MSE A 299     1555   1555  1.33  
LINK         C   MSE A 299                 N   VAL A 300     1555   1555  1.33  
LINK         C   LYS B 131                 N   MSE B 132     1555   1555  1.33  
LINK         C   MSE B 132                 N   GLU B 133     1555   1555  1.34  
LINK         C   GLY B 143                 N   MSE B 144     1555   1555  1.33  
LINK         C   MSE B 144                 N   ASN B 145     1555   1555  1.33  
LINK         C   ALA B 181                 N   MSE B 182     1555   1555  1.33  
LINK         C   MSE B 182                 N   ASN B 183     1555   1555  1.33  
LINK         C   SER B 188                 N  AMSE B 189     1555   1555  1.34  
LINK         C   SER B 188                 N  BMSE B 189     1555   1555  1.33  
LINK         C  AMSE B 189                 N   PRO B 190     1555   1555  1.34  
LINK         C  BMSE B 189                 N   PRO B 190     1555   1555  1.34  
LINK         C   TYR B 210                 N   MSE B 211     1555   1555  1.33  
LINK         C   MSE B 211                 N   LEU B 212     1555   1555  1.33  
LINK         C   ASP B 298                 N   MSE B 299     1555   1555  1.33  
LINK         C   MSE B 299                 N   VAL B 300     1555   1555  1.33  
LINK         C   LYS C 131                 N   MSE C 132     1555   1555  1.33  
LINK         C   MSE C 132                 N   GLU C 133     1555   1555  1.33  
LINK         C   GLY C 143                 N   MSE C 144     1555   1555  1.32  
LINK         C   MSE C 144                 N   ASN C 145     1555   1555  1.34  
LINK         C   ALA C 181                 N   MSE C 182     1555   1555  1.34  
LINK         C   MSE C 182                 N   ASN C 183     1555   1555  1.33  
LINK         C  ASER C 188                 N   MSE C 189     1555   1555  1.33  
LINK         C  BSER C 188                 N   MSE C 189     1555   1555  1.33  
LINK         C   MSE C 189                 N   PRO C 190     1555   1555  1.34  
LINK         C   TYR C 210                 N   MSE C 211     1555   1555  1.33  
LINK         C   MSE C 211                 N   LEU C 212     1555   1555  1.33  
LINK         C   ASP C 298                 N   MSE C 299     1555   1555  1.33  
LINK         C   MSE C 299                 N   VAL C 300     1555   1555  1.33  
SITE     1 AC1 16 TYR A  33  GLU A  73  GLY A  91  LEU A  92                    
SITE     2 AC1 16 LEU A  93  GLU A 105  ARG A 148  ARG A 168                    
SITE     3 AC1 16 PRO A 170  ASN A 172  PHE A 175  LEU A 191                    
SITE     4 AC1 16 ASN A 208  HOH A 581  HOH A 584  HOH A 906                    
SITE     1 AC2  2 ARG A  81  HOH C 505                                          
SITE     1 AC3  8 LEU A  70  GLN A  75  GLY A  79  ASN A  82                    
SITE     2 AC3  8 THR A  84  ILE A  85  HOH A 780  SER B 188                    
SITE     1 AC4 17 TYR B  33  GLU B  73  GLY B  91  LEU B  92                    
SITE     2 AC4 17 LEU B  93  GLU B 105  ARG B 148  ARG B 168                    
SITE     3 AC4 17 PRO B 170  ASN B 172  PHE B 175  LEU B 191                    
SITE     4 AC4 17 ASN B 208  HOH B 552  HOH B 555  HOH B 558                    
SITE     5 AC4 17 HOH B 573                                                     
SITE     1 AC5  5 LYS B  29  ARG B  63  TYR B  65  HOH B 899                    
SITE     2 AC5  5 LYS C 134                                                     
SITE     1 AC6 16 TYR C  33  GLU C  73  GLY C  91  LEU C  92                    
SITE     2 AC6 16 GLU C 105  ARG C 148  ARG C 168  PRO C 170                    
SITE     3 AC6 16 ASN C 172  PHE C 175  LEU C 191  ASN C 208                    
SITE     4 AC6 16 HOH C 569  HOH C 573  HOH C 576  HOH C 587                    
SITE     1 AC7  6 LYS B 312  ASP C 112  ASN C 113  GLN C 114                    
SITE     2 AC7  6 HOH C 538  HOH C 727                                          
SITE     1 AC8  6 LYS A 180  ASP C  36  PRO C  66  GLN C  69                    
SITE     2 AC8  6 HOH C 800  HOH C 835                                          
SITE     1 AC9  3 ASN C 126  LEU C 140  HOH C 651                               
SITE     1 AD1  7 GLU B 199  GLU B 220  VAL B 221  VAL C 176                    
SITE     2 AD1  7 GLN C 187  SER C 188  HOH C 839                               
SITE     1 AD2  9 THR B 196  HOH B 751  HOH B 834  LEU C 171                    
SITE     2 AD2  9 ASN C 172  SER C 173  SER C 188  HOH C 806                    
SITE     3 AD2  9 HOH C 927                                                     
CRYST1  133.449   76.537  112.977  90.00 114.01  90.00 C 1 2 1      12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007493  0.000000  0.003337        0.00000                         
SCALE2      0.000000  0.013066  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009690        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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