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LongText Report for: 5n4b-pdb

Name Class
5n4b-pdb
HEADER    HYDROLASE                               10-FEB-17   5N4B              
TITLE     PROLYL OLIGOPEPTIDASE B FROM GALERINA MARGINATA BOUND TO 25MER        
TITLE    2 MACROCYCLIZATION SUBSTRATE - S577A MUTANT                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROLYL OLIGOPEPTIDASE;                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES;                                                       
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: ALPHA-AMANITIN PROPROTEIN;                                 
COMPND   8 CHAIN: D, C;                                                         
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GALERINA MARGINATA;                             
SOURCE   3 ORGANISM_TAXID: 109633;                                              
SOURCE   4 GENE: POPB;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PJ411;                                    
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 SYNTHETIC: YES;                                                      
SOURCE  11 ORGANISM_SCIENTIFIC: GALERINA MARGINATA;                             
SOURCE  12 ORGANISM_TAXID: 109633                                               
KEYWDS    AMANITIN BIOSYNTHESIS, PROLYL OLIGOPEPTIDASE, MACROCYCLASE,           
KEYWDS   2 PEPTIDASE, BETA-PROPELLER, CLOSED FORM, HYDROLASE                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.M.CZEKSTER,S.A.MCMAHON,H.LUDEWIG,J.H.NAISMITH                       
REVDAT   1   01-NOV-17 5N4B    0                                                
JRNL        AUTH   C.M.CZEKSTER,H.LUDEWIG,S.A.MCMAHON,J.H.NAISMITH              
JRNL        TITL   CHARACTERIZATION OF A DUAL FUNCTION MACROCYCLASE ENABLES     
JRNL        TITL 2 DESIGN AND USE OF EFFICIENT MACROCYCLIZATION SUBSTRATES      
JRNL        REF    NAT COMMUN                                 2017              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        DOI    10.1038/S41467-017-00862-4                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.44 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.11RC2_2522: ???)                           
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) : 1.44                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.56                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 288430                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.157                           
REMARK   3   R VALUE            (WORKING SET) : 0.155                           
REMARK   3   FREE R VALUE                     : 0.181                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.090                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 14680                           
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 43.5812 -  4.4729    0.99     9585   538  0.1762 0.1872        
REMARK   3     2  4.4729 -  3.5508    1.00     9368   491  0.1390 0.1547        
REMARK   3     3  3.5508 -  3.1021    1.00     9275   500  0.1522 0.1714        
REMARK   3     4  3.1021 -  2.8185    1.00     9211   540  0.1569 0.1940        
REMARK   3     5  2.8185 -  2.6165    1.00     9144   533  0.1544 0.1888        
REMARK   3     6  2.6165 -  2.4623    1.00     9234   477  0.1516 0.1796        
REMARK   3     7  2.4623 -  2.3390    0.98     8993   502  0.1409 0.1672        
REMARK   3     8  2.3390 -  2.2372    1.00     9199   467  0.1395 0.1621        
REMARK   3     9  2.2372 -  2.1510    0.99     9099   464  0.1404 0.1695        
REMARK   3    10  2.1510 -  2.0768    1.00     9096   496  0.1464 0.1787        
REMARK   3    11  2.0768 -  2.0119    0.99     9084   499  0.1430 0.1546        
REMARK   3    12  2.0119 -  1.9544    1.00     9080   488  0.1428 0.1804        
REMARK   3    13  1.9544 -  1.9029    1.00     9119   485  0.1470 0.1686        
REMARK   3    14  1.9029 -  1.8565    1.00     9098   477  0.1536 0.1760        
REMARK   3    15  1.8565 -  1.8143    1.00     9103   509  0.1501 0.1896        
REMARK   3    16  1.8143 -  1.7757    1.00     9144   491  0.1532 0.1667        
REMARK   3    17  1.7757 -  1.7401    1.00     9052   476  0.1541 0.1891        
REMARK   3    18  1.7401 -  1.7073    1.00     9093   491  0.1565 0.1895        
REMARK   3    19  1.7073 -  1.6768    1.00     9176   462  0.1547 0.1834        
REMARK   3    20  1.6768 -  1.6484    1.00     9094   485  0.1541 0.1939        
REMARK   3    21  1.6484 -  1.6218    1.00     9088   473  0.1552 0.1880        
REMARK   3    22  1.6218 -  1.5968    1.00     9093   466  0.1593 0.1884        
REMARK   3    23  1.5968 -  1.5734    1.00     9079   528  0.1616 0.1895        
REMARK   3    24  1.5734 -  1.5512    1.00     9096   463  0.1664 0.2070        
REMARK   3    25  1.5512 -  1.5302    1.00     9128   461  0.1737 0.2195        
REMARK   3    26  1.5302 -  1.5104    1.00     9091   471  0.1822 0.2194        
REMARK   3    27  1.5104 -  1.4915    1.00     9066   496  0.1912 0.2281        
REMARK   3    28  1.4915 -  1.4735    1.00     9078   469  0.2049 0.2368        
REMARK   3    29  1.4735 -  1.4564    1.00     9012   510  0.2197 0.2308        
REMARK   3    30  1.4564 -  1.4400    0.96     8772   472  0.2379 0.2624        
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)     : 0.130            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.570           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.013          12184                                  
REMARK   3   ANGLE     :  1.216          16590                                  
REMARK   3   CHIRALITY :  0.095           1752                                  
REMARK   3   PLANARITY :  0.009           2166                                  
REMARK   3   DIHEDRAL  : 15.165           4409                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 6 THROUGH 112 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  18.8161  75.6285  19.5001              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0565 T22:   0.0384                                     
REMARK   3      T33:   0.0601 T12:   0.0167                                     
REMARK   3      T13:   0.0067 T23:  -0.0028                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2667 L22:  -0.0112                                     
REMARK   3      L33:   0.2096 L12:  -0.1308                                     
REMARK   3      L13:  -0.0252 L23:   0.1500                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0282 S12:   0.0161 S13:  -0.0498                       
REMARK   3      S21:   0.0158 S22:  -0.0519 S23:  -0.0187                       
REMARK   3      S31:   0.0144 S32:   0.0890 S33:  -0.0233                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 113 THROUGH 403 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   3.3717  68.7912  42.0732              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0418 T22:   0.0353                                     
REMARK   3      T33:   0.0437 T12:  -0.0059                                     
REMARK   3      T13:   0.0015 T23:   0.0086                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3840 L22:   0.3382                                     
REMARK   3      L33:   0.2406 L12:   0.0041                                     
REMARK   3      L13:   0.0222 L23:   0.0040                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0199 S12:  -0.0229 S13:  -0.0600                       
REMARK   3      S21:   0.0028 S22:   0.0023 S23:   0.0002                       
REMARK   3      S31:   0.0118 S32:  -0.0015 S33:   0.1082                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 404 THROUGH 727 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   6.0148  81.8270  18.0305              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0541 T22:   0.0408                                     
REMARK   3      T33:   0.0416 T12:   0.0035                                     
REMARK   3      T13:   0.0039 T23:   0.0085                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2885 L22:   0.1078                                     
REMARK   3      L33:   0.1876 L12:  -0.0307                                     
REMARK   3      L13:  -0.0107 L23:   0.1286                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0020 S12:   0.0395 S13:   0.0055                       
REMARK   3      S21:   0.0069 S22:  -0.0210 S23:   0.0167                       
REMARK   3      S31:   0.0146 S32:   0.0043 S33:  -0.0671                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 6 THROUGH 163 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  30.7555  34.8559  27.7264              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0571 T22:   0.0561                                     
REMARK   3      T33:   0.0494 T12:  -0.0024                                     
REMARK   3      T13:  -0.0045 T23:  -0.0019                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2292 L22:  -0.0024                                     
REMARK   3      L33:   0.2324 L12:  -0.0792                                     
REMARK   3      L13:   0.0827 L23:   0.0183                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0100 S12:  -0.0188 S13:   0.0227                       
REMARK   3      S21:   0.0032 S22:  -0.0342 S23:   0.0095                       
REMARK   3      S31:  -0.0279 S32:  -0.0692 S33:  -0.0179                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 164 THROUGH 313 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  41.4212  50.9108  41.9785              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0735 T22:   0.0677                                     
REMARK   3      T33:   0.0749 T12:   0.0061                                     
REMARK   3      T13:  -0.0096 T23:  -0.0056                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2557 L22:   0.3089                                     
REMARK   3      L33:   0.2180 L12:  -0.0344                                     
REMARK   3      L13:  -0.0480 L23:   0.0555                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0151 S12:  -0.0276 S13:   0.0924                       
REMARK   3      S21:  -0.0151 S22:   0.0122 S23:   0.0073                       
REMARK   3      S31:  -0.0411 S32:  -0.0526 S33:  -0.0003                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 314 THROUGH 348 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  63.7361  42.7821  42.4497              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0567 T22:   0.0519                                     
REMARK   3      T33:   0.0901 T12:  -0.0072                                     
REMARK   3      T13:  -0.0134 T23:  -0.0272                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0388 L22:   0.0240                                     
REMARK   3      L33:   0.0260 L12:  -0.0125                                     
REMARK   3      L13:  -0.0007 L23:  -0.0127                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0270 S12:  -0.0105 S13:   0.0923                       
REMARK   3      S21:   0.0010 S22:   0.0071 S23:  -0.0761                       
REMARK   3      S31:  -0.0434 S32:   0.0686 S33:   0.0000                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 349 THROUGH 518 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  51.2812  22.3257  32.9474              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0527 T22:   0.0523                                     
REMARK   3      T33:   0.0631 T12:  -0.0015                                     
REMARK   3      T13:  -0.0098 T23:  -0.0029                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2123 L22:   0.0898                                     
REMARK   3      L33:   0.1899 L12:   0.0236                                     
REMARK   3      L13:   0.0612 L23:   0.1085                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0062 S12:  -0.0236 S13:  -0.0366                       
REMARK   3      S21:   0.0121 S22:  -0.0037 S23:  -0.0287                       
REMARK   3      S31:   0.0217 S32:  -0.0005 S33:  -0.0248                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 519 THROUGH 727 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  41.7227  35.5258  11.6550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0669 T22:   0.0517                                     
REMARK   3      T33:   0.0474 T12:   0.0059                                     
REMARK   3      T13:  -0.0062 T23:  -0.0001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2452 L22:   0.3434                                     
REMARK   3      L33:   0.2404 L12:  -0.0067                                     
REMARK   3      L13:   0.0841 L23:  -0.0740                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0008 S12:   0.0552 S13:   0.0281                       
REMARK   3      S21:   0.0416 S22:  -0.0200 S23:  -0.0381                       
REMARK   3      S31:  -0.0467 S32:  -0.0170 S33:  -0.0467                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 9 THROUGH 13 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  10.1474  80.8116  24.7975              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4009 T22:   0.3359                                     
REMARK   3      T33:   0.4688 T12:   0.0218                                     
REMARK   3      T13:   0.0035 T23:   0.0196                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0095 L22:   0.0036                                     
REMARK   3      L33:   0.0028 L12:  -0.0010                                     
REMARK   3      L13:   0.0001 L23:  -0.0001                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0045 S12:   0.0064 S13:  -0.0074                       
REMARK   3      S21:  -0.0225 S22:   0.0086 S23:   0.0233                       
REMARK   3      S31:  -0.0062 S32:   0.0029 S33:  -0.0000                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 14 THROUGH 25 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   9.8367  80.9158  39.0362              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1231 T22:   0.0890                                     
REMARK   3      T33:   0.1100 T12:  -0.0174                                     
REMARK   3      T13:  -0.0182 T23:   0.0182                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0036 L22:   0.0164                                     
REMARK   3      L33:   0.0051 L12:   0.0011                                     
REMARK   3      L13:   0.0012 L23:   0.0117                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0219 S12:  -0.0714 S13:  -0.0333                       
REMARK   3      S21:  -0.0915 S22:   0.0493 S23:   0.1112                       
REMARK   3      S31:   0.0073 S32:  -0.0342 S33:   0.0000                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 9 THROUGH 13 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  39.3897  30.5526  25.0252              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3801 T22:   0.3340                                     
REMARK   3      T33:   0.4408 T12:   0.0065                                     
REMARK   3      T13:  -0.0159 T23:   0.0128                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0172 L22:   0.0017                                     
REMARK   3      L33:   0.0036 L12:  -0.0008                                     
REMARK   3      L13:  -0.0008 L23:   0.0001                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0076 S12:   0.0129 S13:   0.0106                       
REMARK   3      S21:  -0.0221 S22:   0.0058 S23:  -0.0063                       
REMARK   3      S31:   0.0048 S32:   0.0004 S33:  -0.0000                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 14 THROUGH 25 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  39.7090  30.2869  39.1933              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1208 T22:   0.1087                                     
REMARK   3      T33:   0.1183 T12:  -0.0181                                     
REMARK   3      T13:   0.0140 T23:  -0.0248                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0092 L22:   0.0218                                     
REMARK   3      L33:   0.0051 L12:  -0.0093                                     
REMARK   3      L13:   0.0014 L23:  -0.0116                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0883 S12:  -0.0357 S13:   0.0435                       
REMARK   3      S21:  -0.0751 S22:   0.0425 S23:  -0.1580                       
REMARK   3      S31:   0.0025 S32:  -0.0328 S33:   0.0000                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5N4B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003416.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-SEP-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : MASSIF-3                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.961                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 4M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 288485                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.440                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : 0.11400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 9.2600                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1H2Z                                                 
REMARK 200                                                                      
REMARK 200 REMARK: SMALL TILES                                                  
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG6000, 100 MM BICINE PH 9.0, 60    
REMARK 280  MM MAGNESIUM FORMATE, AND 2.42% DMSO, 12.5MM HEXAMMINE COBALT       
REMARK 280  CHLORIDE, CRYOPROTECTED WITH 12% GLYCEROL, VAPOR DIFFUSION,         
REMARK 280  SITTING DROP, TEMPERATURE 293.15K                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       49.54200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.63250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       57.35800            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       70.63250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       49.54200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       57.35800            
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                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2200 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2210 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29590 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     THR A   728                                                      
REMARK 465     VAL A   729                                                      
REMARK 465     GLU A   730                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     VAL B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     THR B   728                                                      
REMARK 465     VAL B   729                                                      
REMARK 465     GLU B   730                                                      
REMARK 465     ILE D     1                                                      
REMARK 465     TRP D     2                                                      
REMARK 465     GLY D     3                                                      
REMARK 465     ILE D     4                                                      
REMARK 465     GLY D     5                                                      
REMARK 465     CYS D     6                                                      
REMARK 465     ASN D     7                                                      
REMARK 465     PRO D     8                                                      
REMARK 465     ILE C     1                                                      
REMARK 465     TRP C     2                                                      
REMARK 465     GLY C     3                                                      
REMARK 465     ILE C     4                                                      
REMARK 465     GLY C     5                                                      
REMARK 465     CYS C     6                                                      
REMARK 465     ASN C     7                                                      
REMARK 465     PRO C     8                                                      
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 A 727    CG   CD   CE   NZ                                   
REMARK 470     LYS B 727    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   O    HOH A   913     O    HOH A  1526              1.51            
REMARK 500   O    HOH A  1207     O    HOH A  1541              1.55            
REMARK 500   O    ALA A   490     O    HOH A   801              1.65            
REMARK 500   O    HOH B   813     O    HOH B  1576              1.68            
REMARK 500   O    HOH A   816     O    HOH A  1207              1.70            
REMARK 500   O    HOH A   805     O    HOH A  1361              1.74            
REMARK 500   O    HOH B  1514     O    HOH B  1664              1.81            
REMARK 500   O    HOH B   806     O    HOH B  1395              1.81            
REMARK 500   O    HOH B   838     O    HOH B   885              1.84            
REMARK 500   O    HOH B   848     O    HOH B  1046              1.84            
REMARK 500   O    HOH B   806     O    HOH B  1069              1.90            
REMARK 500   O    TRP C     9     O    HOH C   101              1.91            
REMARK 500   O    HOH A   893     O    HOH A   931              1.91            
REMARK 500   O    HOH A  1547     O    HOH A  1586              1.94            
REMARK 500   O    HOH A   965     O    HOH A  1637              1.95            
REMARK 500   O    HOH A  1587     O    HOH A  1670              1.95            
REMARK 500   NE2  GLN A    24     O    HOH A   802              1.96            
REMARK 500   O    HOH A   852     O    HOH A  1669              1.99            
REMARK 500   O    HOH A  1249     O    HOH A  1570              1.99            
REMARK 500   O    HOH B   829     O    HOH B  1464              2.00            
REMARK 500   O    HOH A   837     O    HOH A   880              2.01            
REMARK 500   O    HOH B  1232     O    HOH B  1643              2.01            
REMARK 500   O    HOH A  1268     O    HOH A  1637              2.02            
REMARK 500   O    HOH B  1383     O    HOH B  1542              2.05            
REMARK 500   O    HOH B  1393     O    HOH B  1706              2.05            
REMARK 500   OE2  GLU B   247     O    HOH B   801              2.06            
REMARK 500   O    LYS A   727     O    HOH A   803              2.07            
REMARK 500   O    HOH B  1250     O    HOH B  1280              2.08            
REMARK 500   O    HOH C   104     O    HOH C   117              2.08            
REMARK 500   O    HOH C   112     O    HOH C   122              2.08            
REMARK 500   O    HOH A   956     O    HOH D   121              2.08            
REMARK 500   O    HOH B   826     O    HOH B  1588              2.09            
REMARK 500   O    HOH B   941     O    HOH B  1646              2.10            
REMARK 500   O    HOH B   813     O    HOH B  1667              2.10            
REMARK 500   NE2  GLN A    38     O    HOH A   804              2.11            
REMARK 500   OE1  GLN B   187     O    HOH B   802              2.12            
REMARK 500   NH1  ARG A   224     O    HOH A   805              2.12            
REMARK 500   OE1  GLU B   268     O    HOH B   803              2.12            
REMARK 500   O    HOH A  1527     O    HOH A  1669              2.13            
REMARK 500   N    ILE A   521     O    HOH A   801              2.13            
REMARK 500   O    HOH B  1392     O    HOH B  1460              2.13            
REMARK 500   O    HOH A   810     O    HOH A   981              2.15            
REMARK 500   O    THR A   281     O    HOH A   806              2.15            
REMARK 500   O    HOH A   811     O    HOH A  1152              2.16            
REMARK 500   O    HOH A  1594     O    HOH A  1623              2.16            
REMARK 500   O    HOH A  1537     O    HOH D   117              2.16            
REMARK 500   NE2  GLN A   187     O    HOH A   807              2.18            
REMARK 500   O    HOH B   827     O    HOH B  1497              2.18            
REMARK 500   O    HOH A   837     O    HOH A  1250              2.18            
REMARK 500   O    HOH B  1632     O    HOH B  1643              2.19            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      54 CLOSE CONTACTS                                
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   840     O    HOH B  1643     3555     1.88            
REMARK 500   O    HOH A  1668     O    HOH B  1132     4455     1.95            
REMARK 500   O    HOH A  1523     O    HOH B  1608     3655     2.00            
REMARK 500   O    HOH A  1622     O    HOH B  1308     3555     2.12            
REMARK 500   O    HOH A  1609     O    HOH B  1433     3555     2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 535   CB    GLU A 535   CG      0.119                       
REMARK 500    TRP B   6   CB    TRP B   6   CG      0.120                       
REMARK 500    SER B 282   N     SER B 282   CA     -0.163                       
REMARK 500    LYS B 570   CA    LYS B 570   C       0.160                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 111   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG A 111   NE  -  CZ  -  NH2 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    ARG A 174   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A 350   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    MET B 145   CG  -  SD  -  CE  ANGL. DEV. =  11.2 DEGREES          
REMARK 500    SER B 282   N   -  CA  -  C   ANGL. DEV. = -18.9 DEGREES          
REMARK 500    ARG B 378   C   -  N   -  CA  ANGL. DEV. =  15.4 DEGREES          
REMARK 500    ARG B 378   O   -  C   -  N   ANGL. DEV. =  10.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 280     -166.58   -167.49                                   
REMARK 500    LYS A 283       40.53    -84.04                                   
REMARK 500    ALA A 311      -26.96   -148.98                                   
REMARK 500    ALA A 332       77.70   -162.92                                   
REMARK 500    TYR A 335      162.27     73.51                                   
REMARK 500    GLU A 369      -37.53     68.76                                   
REMARK 500    GLU A 452      -55.66     72.68                                   
REMARK 500    TYR A 496      -70.95   -124.85                                   
REMARK 500    ARG A 543     -120.72     53.87                                   
REMARK 500    ALA A 577     -119.30     64.23                                   
REMARK 500    ALA A 605      -24.99   -149.11                                   
REMARK 500    THR A 614     -116.30     33.36                                   
REMARK 500    ASP B 280     -162.18   -165.73                                   
REMARK 500    ALA B 311      -27.13   -149.48                                   
REMARK 500    ALA B 332       79.48   -161.63                                   
REMARK 500    TYR B 335      162.22     71.82                                   
REMARK 500    GLU B 369      -36.64     69.58                                   
REMARK 500    GLU B 452      -55.56     73.99                                   
REMARK 500    TYR B 496      -70.14   -124.68                                   
REMARK 500    ARG B 543     -120.38     54.05                                   
REMARK 500    ALA B 577     -119.39     63.29                                   
REMARK 500    ALA B 605      -26.02   -148.17                                   
REMARK 500    THR B 614     -115.19     34.58                                   
REMARK 500    ASP D  23       54.26   -149.00                                   
REMARK 500    ASP C  23       53.77   -147.81                                   
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 A1754        DISTANCE =  5.83 ANGSTROMS                       
DBREF  5N4B A    1   730  UNP    H2E7Q8   H2E7Q8_9AGAR     1    730             
DBREF  5N4B B    1   730  UNP    H2E7Q8   H2E7Q8_9AGAR     1    730             
DBREF  5N4B D    1    25  UNP    H2E7Q5   H2E7Q5_9AGAR    11     35             
DBREF  5N4B C    1    25  UNP    H2E7Q5   H2E7Q5_9AGAR    11     35             
SEQADV 5N4B GLY A    0  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4B ALA A  577  UNP  H2E7Q8    SER   577 ENGINEERED MUTATION            
SEQADV 5N4B GLY B    0  UNP  H2E7Q8              EXPRESSION TAG                 
SEQADV 5N4B ALA B  577  UNP  H2E7Q8    SER   577 ENGINEERED MUTATION            
SEQRES   1 A  731  GLY MET SER SER VAL THR TRP ALA PRO GLY ASN TYR PRO          
SEQRES   2 A  731  SER THR ARG ARG SER ASP HIS VAL ASP THR TYR GLN SER          
SEQRES   3 A  731  ALA SER LYS GLY GLU VAL PRO VAL PRO ASP PRO TYR GLN          
SEQRES   4 A  731  TRP LEU GLU GLU SER THR ASP GLU VAL ASP LYS TRP THR          
SEQRES   5 A  731  THR ALA GLN ALA ASP LEU ALA GLN SER TYR LEU ASP GLN          
SEQRES   6 A  731  ASN ALA ASP ILE GLN LYS LEU ALA GLU LYS PHE ARG ALA          
SEQRES   7 A  731  SER ARG ASN TYR ALA LYS PHE SER ALA PRO THR LEU LEU          
SEQRES   8 A  731  ASP ASP GLY HIS TRP TYR TRP PHE TYR ASN ARG GLY LEU          
SEQRES   9 A  731  GLN SER GLN SER VAL LEU TYR ARG SER LYS GLU PRO ALA          
SEQRES  10 A  731  LEU PRO ASP PHE SER LYS GLY ASP ASP ASN VAL GLY ASP          
SEQRES  11 A  731  VAL PHE PHE ASP PRO ASN VAL LEU ALA ALA ASP GLY SER          
SEQRES  12 A  731  ALA GLY MET VAL LEU CYS LYS PHE SER PRO ASP GLY LYS          
SEQRES  13 A  731  PHE PHE ALA TYR ALA VAL SER HIS LEU GLY GLY ASP TYR          
SEQRES  14 A  731  SER THR ILE TYR VAL ARG SER THR SER SER PRO LEU SER          
SEQRES  15 A  731  GLN ALA SER VAL ALA GLN GLY VAL ASP GLY ARG LEU SER          
SEQRES  16 A  731  ASP GLU VAL LYS TRP PHE LYS PHE SER THR ILE ILE TRP          
SEQRES  17 A  731  THR LYS ASP SER LYS GLY PHE LEU TYR GLN ARG TYR PRO          
SEQRES  18 A  731  ALA ARG GLU ARG HIS GLU GLY THR ARG SER ASP ARG ASN          
SEQRES  19 A  731  ALA MET MET CYS TYR HIS LYS VAL GLY THR THR GLN GLU          
SEQRES  20 A  731  GLU ASP ILE ILE VAL TYR GLN ASP ASN GLU HIS PRO GLU          
SEQRES  21 A  731  TRP ILE TYR GLY ALA ASP THR SER GLU ASP GLY LYS TYR          
SEQRES  22 A  731  LEU TYR LEU TYR GLN PHE LYS ASP THR SER LYS LYS ASN          
SEQRES  23 A  731  LEU LEU TRP VAL ALA GLU LEU ASP GLU ASP GLY VAL LYS          
SEQRES  24 A  731  SER GLY ILE HIS TRP ARG LYS VAL VAL ASN GLU TYR ALA          
SEQRES  25 A  731  ALA ASP TYR ASN ILE ILE THR ASN HIS GLY SER LEU VAL          
SEQRES  26 A  731  TYR ILE LYS THR ASN LEU ASN ALA PRO GLN TYR LYS VAL          
SEQRES  27 A  731  ILE THR ILE ASP LEU SER LYS ASP GLU PRO GLU ILE ARG          
SEQRES  28 A  731  ASP PHE ILE PRO GLU GLU LYS ASP ALA LYS LEU ALA GLN          
SEQRES  29 A  731  VAL ASN CYS ALA ASN GLU GLU TYR PHE VAL ALA ILE TYR          
SEQRES  30 A  731  LYS ARG ASN VAL LYS ASP GLU ILE TYR LEU TYR SER LYS          
SEQRES  31 A  731  ALA GLY VAL GLN LEU THR ARG LEU ALA PRO ASP PHE VAL          
SEQRES  32 A  731  GLY ALA ALA SER ILE ALA ASN ARG GLN LYS GLN THR HIS          
SEQRES  33 A  731  PHE PHE LEU THR LEU SER GLY PHE ASN THR PRO GLY THR          
SEQRES  34 A  731  ILE ALA ARG TYR ASP PHE THR ALA PRO GLU THR GLN ARG          
SEQRES  35 A  731  PHE SER ILE LEU ARG THR THR LYS VAL ASN GLU LEU ASP          
SEQRES  36 A  731  PRO ASP ASP PHE GLU SER THR GLN VAL TRP TYR GLU SER          
SEQRES  37 A  731  LYS ASP GLY THR LYS ILE PRO MET PHE ILE VAL ARG HIS          
SEQRES  38 A  731  LYS SER THR LYS PHE ASP GLY THR ALA ALA ALA ILE GLN          
SEQRES  39 A  731  TYR GLY TYR GLY GLY PHE ALA THR SER ALA ASP PRO PHE          
SEQRES  40 A  731  PHE SER PRO ILE ILE LEU THR PHE LEU GLN THR TYR GLY          
SEQRES  41 A  731  ALA ILE PHE ALA VAL PRO SER ILE ARG GLY GLY GLY GLU          
SEQRES  42 A  731  PHE GLY GLU GLU TRP HIS LYS GLY GLY ARG ARG GLU THR          
SEQRES  43 A  731  LYS VAL ASN THR PHE ASP ASP PHE ILE ALA ALA ALA GLN          
SEQRES  44 A  731  PHE LEU VAL LYS ASN LYS TYR ALA ALA PRO GLY LYS VAL          
SEQRES  45 A  731  ALA ILE ASN GLY ALA ALA ASN GLY GLY LEU LEU VAL MET          
SEQRES  46 A  731  GLY SER ILE VAL ARG ALA PRO GLU GLY THR PHE GLY ALA          
SEQRES  47 A  731  ALA VAL PRO GLU GLY GLY VAL ALA ASP LEU LEU LYS PHE          
SEQRES  48 A  731  HIS LYS PHE THR GLY GLY GLN ALA TRP ILE SER GLU TYR          
SEQRES  49 A  731  GLY ASN PRO SER ILE PRO GLU GLU PHE ASP TYR ILE TYR          
SEQRES  50 A  731  PRO LEU SER PRO VAL HIS ASN VAL ARG THR ASP LYS VAL          
SEQRES  51 A  731  MET PRO ALA THR LEU ILE THR VAL ASN ILE GLY ASP GLY          
SEQRES  52 A  731  ARG VAL VAL PRO MET HIS SER PHE LYS PHE ILE ALA THR          
SEQRES  53 A  731  LEU GLN HIS ASN VAL PRO GLN ASN PRO HIS PRO LEU LEU          
SEQRES  54 A  731  ILE LYS ILE ASP LYS SER TRP LEU GLY HIS GLY MET GLY          
SEQRES  55 A  731  LYS PRO THR ASP LYS ASN VAL LYS ASP ALA ALA ASP LYS          
SEQRES  56 A  731  TRP GLY PHE ILE ALA ARG ALA LEU GLY LEU GLU LEU LYS          
SEQRES  57 A  731  THR VAL GLU                                                  
SEQRES   1 B  731  GLY MET SER SER VAL THR TRP ALA PRO GLY ASN TYR PRO          
SEQRES   2 B  731  SER THR ARG ARG SER ASP HIS VAL ASP THR TYR GLN SER          
SEQRES   3 B  731  ALA SER LYS GLY GLU VAL PRO VAL PRO ASP PRO TYR GLN          
SEQRES   4 B  731  TRP LEU GLU GLU SER THR ASP GLU VAL ASP LYS TRP THR          
SEQRES   5 B  731  THR ALA GLN ALA ASP LEU ALA GLN SER TYR LEU ASP GLN          
SEQRES   6 B  731  ASN ALA ASP ILE GLN LYS LEU ALA GLU LYS PHE ARG ALA          
SEQRES   7 B  731  SER ARG ASN TYR ALA LYS PHE SER ALA PRO THR LEU LEU          
SEQRES   8 B  731  ASP ASP GLY HIS TRP TYR TRP PHE TYR ASN ARG GLY LEU          
SEQRES   9 B  731  GLN SER GLN SER VAL LEU TYR ARG SER LYS GLU PRO ALA          
SEQRES  10 B  731  LEU PRO ASP PHE SER LYS GLY ASP ASP ASN VAL GLY ASP          
SEQRES  11 B  731  VAL PHE PHE ASP PRO ASN VAL LEU ALA ALA ASP GLY SER          
SEQRES  12 B  731  ALA GLY MET VAL LEU CYS LYS PHE SER PRO ASP GLY LYS          
SEQRES  13 B  731  PHE PHE ALA TYR ALA VAL SER HIS LEU GLY GLY ASP TYR          
SEQRES  14 B  731  SER THR ILE TYR VAL ARG SER THR SER SER PRO LEU SER          
SEQRES  15 B  731  GLN ALA SER VAL ALA GLN GLY VAL ASP GLY ARG LEU SER          
SEQRES  16 B  731  ASP GLU VAL LYS TRP PHE LYS PHE SER THR ILE ILE TRP          
SEQRES  17 B  731  THR LYS ASP SER LYS GLY PHE LEU TYR GLN ARG TYR PRO          
SEQRES  18 B  731  ALA ARG GLU ARG HIS GLU GLY THR ARG SER ASP ARG ASN          
SEQRES  19 B  731  ALA MET MET CYS TYR HIS LYS VAL GLY THR THR GLN GLU          
SEQRES  20 B  731  GLU ASP ILE ILE VAL TYR GLN ASP ASN GLU HIS PRO GLU          
SEQRES  21 B  731  TRP ILE TYR GLY ALA ASP THR SER GLU ASP GLY LYS TYR          
SEQRES  22 B  731  LEU TYR LEU TYR GLN PHE LYS ASP THR SER LYS LYS ASN          
SEQRES  23 B  731  LEU LEU TRP VAL ALA GLU LEU ASP GLU ASP GLY VAL LYS          
SEQRES  24 B  731  SER GLY ILE HIS TRP ARG LYS VAL VAL ASN GLU TYR ALA          
SEQRES  25 B  731  ALA ASP TYR ASN ILE ILE THR ASN HIS GLY SER LEU VAL          
SEQRES  26 B  731  TYR ILE LYS THR ASN LEU ASN ALA PRO GLN TYR LYS VAL          
SEQRES  27 B  731  ILE THR ILE ASP LEU SER LYS ASP GLU PRO GLU ILE ARG          
SEQRES  28 B  731  ASP PHE ILE PRO GLU GLU LYS ASP ALA LYS LEU ALA GLN          
SEQRES  29 B  731  VAL ASN CYS ALA ASN GLU GLU TYR PHE VAL ALA ILE TYR          
SEQRES  30 B  731  LYS ARG ASN VAL LYS ASP GLU ILE TYR LEU TYR SER LYS          
SEQRES  31 B  731  ALA GLY VAL GLN LEU THR ARG LEU ALA PRO ASP PHE VAL          
SEQRES  32 B  731  GLY ALA ALA SER ILE ALA ASN ARG GLN LYS GLN THR HIS          
SEQRES  33 B  731  PHE PHE LEU THR LEU SER GLY PHE ASN THR PRO GLY THR          
SEQRES  34 B  731  ILE ALA ARG TYR ASP PHE THR ALA PRO GLU THR GLN ARG          
SEQRES  35 B  731  PHE SER ILE LEU ARG THR THR LYS VAL ASN GLU LEU ASP          
SEQRES  36 B  731  PRO ASP ASP PHE GLU SER THR GLN VAL TRP TYR GLU SER          
SEQRES  37 B  731  LYS ASP GLY THR LYS ILE PRO MET PHE ILE VAL ARG HIS          
SEQRES  38 B  731  LYS SER THR LYS PHE ASP GLY THR ALA ALA ALA ILE GLN          
SEQRES  39 B  731  TYR GLY TYR GLY GLY PHE ALA THR SER ALA ASP PRO PHE          
SEQRES  40 B  731  PHE SER PRO ILE ILE LEU THR PHE LEU GLN THR TYR GLY          
SEQRES  41 B  731  ALA ILE PHE ALA VAL PRO SER ILE ARG GLY GLY GLY GLU          
SEQRES  42 B  731  PHE GLY GLU GLU TRP HIS LYS GLY GLY ARG ARG GLU THR          
SEQRES  43 B  731  LYS VAL ASN THR PHE ASP ASP PHE ILE ALA ALA ALA GLN          
SEQRES  44 B  731  PHE LEU VAL LYS ASN LYS TYR ALA ALA PRO GLY LYS VAL          
SEQRES  45 B  731  ALA ILE ASN GLY ALA ALA ASN GLY GLY LEU LEU VAL MET          
SEQRES  46 B  731  GLY SER ILE VAL ARG ALA PRO GLU GLY THR PHE GLY ALA          
SEQRES  47 B  731  ALA VAL PRO GLU GLY GLY VAL ALA ASP LEU LEU LYS PHE          
SEQRES  48 B  731  HIS LYS PHE THR GLY GLY GLN ALA TRP ILE SER GLU TYR          
SEQRES  49 B  731  GLY ASN PRO SER ILE PRO GLU GLU PHE ASP TYR ILE TYR          
SEQRES  50 B  731  PRO LEU SER PRO VAL HIS ASN VAL ARG THR ASP LYS VAL          
SEQRES  51 B  731  MET PRO ALA THR LEU ILE THR VAL ASN ILE GLY ASP GLY          
SEQRES  52 B  731  ARG VAL VAL PRO MET HIS SER PHE LYS PHE ILE ALA THR          
SEQRES  53 B  731  LEU GLN HIS ASN VAL PRO GLN ASN PRO HIS PRO LEU LEU          
SEQRES  54 B  731  ILE LYS ILE ASP LYS SER TRP LEU GLY HIS GLY MET GLY          
SEQRES  55 B  731  LYS PRO THR ASP LYS ASN VAL LYS ASP ALA ALA ASP LYS          
SEQRES  56 B  731  TRP GLY PHE ILE ALA ARG ALA LEU GLY LEU GLU LEU LYS          
SEQRES  57 B  731  THR VAL GLU                                                  
SEQRES   1 D   25  ILE TRP GLY ILE GLY CYS ASN PRO TRP THR ALA GLU HIS          
SEQRES   2 D   25  VAL ASP GLN THR LEU ALA SER GLY ASN ASP ILE CYS              
SEQRES   1 C   25  ILE TRP GLY ILE GLY CYS ASN PRO TRP THR ALA GLU HIS          
SEQRES   2 C   25  VAL ASP GLN THR LEU ALA SER GLY ASN ASP ILE CYS              
FORMUL   5  HOH   *1941(H2 O)                                                   
HELIX    1 AA1 TYR A   37  GLU A   42  5                                   6    
HELIX    2 AA2 THR A   44  GLN A   64  1                                  21    
HELIX    3 AA3 ALA A   66  ASN A   80  1                                  15    
HELIX    4 AA4 ASP A  119  LYS A  122  5                                   4    
HELIX    5 AA5 GLY A  123  VAL A  127  1                                   5    
HELIX    6 AA6 ASP A  133  LEU A  137  5                                   5    
HELIX    7 AA7 SER A  181  GLY A  188  1                                   8    
HELIX    8 AA8 THR A  244  ASP A  248  5                                   5    
HELIX    9 AA9 ASP A  454  ASP A  456  5                                   3    
HELIX   10 AB1 SER A  508  GLY A  519  1                                  12    
HELIX   11 AB2 GLY A  534  GLY A  540  1                                   7    
HELIX   12 AB3 GLY A  541  THR A  545  5                                   5    
HELIX   13 AB4 LYS A  546  ASN A  563  1                                  18    
HELIX   14 AB5 ALA A  577  ALA A  590  1                                  14    
HELIX   15 AB6 LYS A  609  PHE A  613  5                                   5    
HELIX   16 AB7 GLY A  615  ALA A  618  5                                   4    
HELIX   17 AB8 TRP A  619  GLY A  624  1                                   6    
HELIX   18 AB9 ILE A  628  TYR A  636  1                                   9    
HELIX   19 AC1 SER A  639  ASN A  643  5                                   5    
HELIX   20 AC2 PRO A  666  VAL A  680  1                                  15    
HELIX   21 AC3 PRO A  703  LEU A  722  1                                  20    
HELIX   22 AC4 TYR B   37  GLU B   42  5                                   6    
HELIX   23 AC5 THR B   44  GLN B   64  1                                  21    
HELIX   24 AC6 ALA B   66  ASN B   80  1                                  15    
HELIX   25 AC7 ASP B  119  LYS B  122  5                                   4    
HELIX   26 AC8 GLY B  123  VAL B  127  1                                   5    
HELIX   27 AC9 ASP B  133  LEU B  137  5                                   5    
HELIX   28 AD1 SER B  181  GLY B  188  1                                   8    
HELIX   29 AD2 THR B  244  ASP B  248  5                                   5    
HELIX   30 AD3 ASP B  454  ASP B  456  5                                   3    
HELIX   31 AD4 SER B  508  GLY B  519  1                                  12    
HELIX   32 AD5 GLY B  534  GLY B  540  1                                   7    
HELIX   33 AD6 GLY B  541  THR B  545  5                                   5    
HELIX   34 AD7 LYS B  546  ASN B  563  1                                  18    
HELIX   35 AD8 ALA B  577  ALA B  590  1                                  14    
HELIX   36 AD9 LYS B  609  PHE B  613  5                                   5    
HELIX   37 AE1 GLY B  615  ALA B  618  5                                   4    
HELIX   38 AE2 TRP B  619  GLY B  624  1                                   6    
HELIX   39 AE3 ILE B  628  TYR B  636  1                                   9    
HELIX   40 AE4 PRO B  637  ASN B  643  5                                   7    
HELIX   41 AE5 PRO B  666  VAL B  680  1                                  15    
HELIX   42 AE6 PRO B  703  LEU B  722  1                                  20    
SHEET    1 AA1 2 VAL A  20  SER A  25  0                                        
SHEET    2 AA1 2 GLY A  29  PRO A  34 -1  O  VAL A  33   N  ASP A  21           
SHEET    1 AA2 3 LYS A  83  PHE A  84  0                                        
SHEET    2 AA2 3 TRP A  95  ASN A 100 -1  O  ASN A 100   N  LYS A  83           
SHEET    3 AA2 3 THR A  88  LEU A  89 -1  N  THR A  88   O  TYR A  96           
SHEET    1 AA3 4 LYS A  83  PHE A  84  0                                        
SHEET    2 AA3 4 TRP A  95  ASN A 100 -1  O  ASN A 100   N  LYS A  83           
SHEET    3 AA3 4 VAL A 108  SER A 112 -1  O  TYR A 110   N  TRP A  97           
SHEET    4 AA3 4 GLY A 128  PHE A 132 -1  O  PHE A 131   N  LEU A 109           
SHEET    1 AA4 4 ALA A 143  PHE A 150  0                                        
SHEET    2 AA4 4 PHE A 156  HIS A 163 -1  O  ALA A 160   N  LEU A 147           
SHEET    3 AA4 4 SER A 169  SER A 175 -1  O  THR A 170   N  VAL A 161           
SHEET    4 AA4 4 VAL A 197  PHE A 200 -1  O  VAL A 197   N  ILE A 171           
SHEET    1 AA5 4 ILE A 206  TRP A 207  0                                        
SHEET    2 AA5 4 GLY A 213  ARG A 218 -1  O  LEU A 215   N  ILE A 206           
SHEET    3 AA5 4 MET A 235  LYS A 240 -1  O  CYS A 237   N  TYR A 216           
SHEET    4 AA5 4 ILE A 249  GLN A 253 -1  O  TYR A 252   N  MET A 236           
SHEET    1 AA6 4 ILE A 261  THR A 266  0                                        
SHEET    2 AA6 4 TYR A 272  PHE A 278 -1  O  TYR A 274   N  ASP A 265           
SHEET    3 AA6 4 LEU A 286  GLU A 291 -1  O  ALA A 290   N  LEU A 273           
SHEET    4 AA6 4 ARG A 304  VAL A 307 -1  O  VAL A 307   N  LEU A 287           
SHEET    1 AA7 4 TYR A 314  HIS A 320  0                                        
SHEET    2 AA7 4 LEU A 323  THR A 328 -1  O  TYR A 325   N  ILE A 317           
SHEET    3 AA7 4 LYS A 336  ASP A 341 -1  O  ILE A 338   N  ILE A 326           
SHEET    4 AA7 4 GLU A 348  ILE A 353 -1  O  PHE A 352   N  VAL A 337           
SHEET    1 AA8 4 LYS A 360  ALA A 367  0                                        
SHEET    2 AA8 4 TYR A 371  ARG A 378 -1  O  LYS A 377   N  LYS A 360           
SHEET    3 AA8 4 LYS A 381  TYR A 387 -1  O  TYR A 387   N  PHE A 372           
SHEET    4 AA8 4 GLN A 393  LEU A 397 -1  O  LEU A 394   N  LEU A 386           
SHEET    1 AA9 4 ALA A 404  ALA A 408  0                                        
SHEET    2 AA9 4 HIS A 415  GLY A 422 -1  O  PHE A 417   N  ALA A 408           
SHEET    3 AA9 4 THR A 425  ASP A 433 -1  O  THR A 428   N  LEU A 420           
SHEET    4 AA9 4 PHE A 442  THR A 447 -1  O  ARG A 446   N  ILE A 429           
SHEET    1 AB1 8 PHE A 458  GLU A 466  0                                        
SHEET    2 AB1 8 LYS A 472  HIS A 480 -1  O  ILE A 473   N  TYR A 465           
SHEET    3 AB1 8 ILE A 521  PRO A 525 -1  O  PHE A 522   N  VAL A 478           
SHEET    4 AB1 8 ALA A 491  TYR A 494  1  N  ILE A 492   O  ALA A 523           
SHEET    5 AB1 8 VAL A 571  ALA A 576  1  O  ALA A 572   N  GLN A 493           
SHEET    6 AB1 8 ALA A 597  GLU A 601  1  O  GLU A 601   N  GLY A 575           
SHEET    7 AB1 8 ALA A 652  ASN A 658  1  O  LEU A 654   N  ALA A 598           
SHEET    8 AB1 8 LEU A 687  ASP A 692  1  O  LYS A 690   N  ILE A 655           
SHEET    1 AB2 2 VAL B  20  SER B  25  0                                        
SHEET    2 AB2 2 GLY B  29  PRO B  34 -1  O  VAL B  33   N  ASP B  21           
SHEET    1 AB3 3 LYS B  83  PHE B  84  0                                        
SHEET    2 AB3 3 TRP B  95  ASN B 100 -1  O  ASN B 100   N  LYS B  83           
SHEET    3 AB3 3 THR B  88  LEU B  89 -1  N  THR B  88   O  TYR B  96           
SHEET    1 AB4 4 LYS B  83  PHE B  84  0                                        
SHEET    2 AB4 4 TRP B  95  ASN B 100 -1  O  ASN B 100   N  LYS B  83           
SHEET    3 AB4 4 VAL B 108  SER B 112 -1  O  TYR B 110   N  TRP B  97           
SHEET    4 AB4 4 GLY B 128  PHE B 132 -1  O  PHE B 131   N  LEU B 109           
SHEET    1 AB5 4 ALA B 143  PHE B 150  0                                        
SHEET    2 AB5 4 PHE B 156  HIS B 163 -1  O  ALA B 160   N  LEU B 147           
SHEET    3 AB5 4 SER B 169  SER B 175 -1  O  THR B 170   N  VAL B 161           
SHEET    4 AB5 4 VAL B 197  PHE B 200 -1  O  VAL B 197   N  ILE B 171           
SHEET    1 AB6 4 ILE B 206  TRP B 207  0                                        
SHEET    2 AB6 4 GLY B 213  ARG B 218 -1  O  LEU B 215   N  ILE B 206           
SHEET    3 AB6 4 MET B 235  LYS B 240 -1  O  HIS B 239   N  PHE B 214           
SHEET    4 AB6 4 ILE B 249  TYR B 252 -1  O  TYR B 252   N  MET B 236           
SHEET    1 AB7 4 ILE B 261  THR B 266  0                                        
SHEET    2 AB7 4 TYR B 272  PHE B 278 -1  O  TYR B 274   N  ASP B 265           
SHEET    3 AB7 4 LEU B 286  GLU B 291 -1  O  ALA B 290   N  LEU B 273           
SHEET    4 AB7 4 ARG B 304  VAL B 307 -1  O  VAL B 307   N  LEU B 287           
SHEET    1 AB8 4 TYR B 314  HIS B 320  0                                        
SHEET    2 AB8 4 LEU B 323  THR B 328 -1  O  TYR B 325   N  THR B 318           
SHEET    3 AB8 4 LYS B 336  ASP B 341 -1  O  ILE B 340   N  VAL B 324           
SHEET    4 AB8 4 ILE B 349  ILE B 353 -1  O  PHE B 352   N  VAL B 337           
SHEET    1 AB9 4 LYS B 360  ALA B 367  0                                        
SHEET    2 AB9 4 TYR B 371  ARG B 378 -1  O  VAL B 373   N  ASN B 365           
SHEET    3 AB9 4 LYS B 381  TYR B 387 -1  O  TYR B 387   N  PHE B 372           
SHEET    4 AB9 4 GLN B 393  LEU B 397 -1  O  LEU B 394   N  LEU B 386           
SHEET    1 AC1 4 ALA B 404  ALA B 408  0                                        
SHEET    2 AC1 4 HIS B 415  GLY B 422 -1  O  SER B 421   N  ALA B 404           
SHEET    3 AC1 4 THR B 425  ASP B 433 -1  O  THR B 428   N  LEU B 420           
SHEET    4 AC1 4 PHE B 442  THR B 447 -1  O  ARG B 446   N  ILE B 429           
SHEET    1 AC2 8 PHE B 458  GLU B 466  0                                        
SHEET    2 AC2 8 LYS B 472  HIS B 480 -1  O  ILE B 473   N  TYR B 465           
SHEET    3 AC2 8 ILE B 521  PRO B 525 -1  O  PHE B 522   N  VAL B 478           
SHEET    4 AC2 8 ALA B 491  TYR B 494  1  N  ILE B 492   O  ALA B 523           
SHEET    5 AC2 8 VAL B 571  ALA B 576  1  O  ALA B 572   N  GLN B 493           
SHEET    6 AC2 8 ALA B 597  GLU B 601  1  O  GLU B 601   N  GLY B 575           
SHEET    7 AC2 8 ALA B 652  ASN B 658  1  O  LEU B 654   N  ALA B 598           
SHEET    8 AC2 8 LEU B 687  ASP B 692  1  O  LEU B 688   N  THR B 653           
CRYST1   99.084  114.716  141.265  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010092  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008717  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007079        0.00000                         
TER    5797      LYS A 727                                                      
TER   11595      LYS B 727                                                      
TER   11726      CYS D  25                                                      
TER   11857      CYS C  25                                                      
MASTER      651    0    0   42   82    0    0    613657    4    0  118          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
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