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Database: PDB
Entry: 5XAN
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Original site: 5XAN 
HEADER    MEMBRANE PROTEIN                        14-MAR-17   5XAN              
TITLE     CRYSTAL STRUCTURE OF SECDF IN I FORM (P212121 SPACE GROUP)            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN TRANSLOCASE SUBUNIT SECD;                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 28-768;                                       
COMPND   5 SYNONYM: PROTEIN-EXPORT MEMBRANE PROTEIN SECF;                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DEINOCOCCUS RADIODURANS STR. R1;                
SOURCE   3 ORGANISM_TAXID: 243230;                                              
SOURCE   4 STRAIN: R1;                                                          
SOURCE   5 GENE: SECD, SECF, DR_1822;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: C41(DE3);                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28                                     
KEYWDS    MEMBRANE PROTEIN, ALFA HELICAL, SEC TRANSLOCON                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.TSUKAZAKI,Y.TANAKA,A.FURUKWA                                        
REVDAT   5   11-NOV-20 5XAN    1       REMARK                                   
REVDAT   4   14-OCT-20 5XAN    1       SOURCE                                   
REVDAT   3   22-MAY-19 5XAN    1       TITLE                                    
REVDAT   2   04-OCT-17 5XAN    1       REMARK                                   
REVDAT   1   17-MAY-17 5XAN    0                                                
JRNL        AUTH   A.FURUKAWA,K.YOSHIKAIE,T.MORI,H.MORI,Y.V.MORIMOTO,Y.SUGANO,  
JRNL        AUTH 2 S.IWAKI,T.MINAMINO,Y.SUGITA,Y.TANAKA,T.TSUKAZAKI             
JRNL        TITL   TUNNEL FORMATION INFERRED FROM THE I-FORM STRUCTURES OF THE  
JRNL        TITL 2 PROTON-DRIVEN PROTEIN SECRETION MOTOR SECDF                  
JRNL        REF    CELL REP                      V.  19   895 2017              
JRNL        REFN                   ESSN 2211-1247                               
JRNL        PMID   28467902                                                     
JRNL        DOI    10.1016/J.CELREP.2017.04.030                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.10.1_2155                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.20                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 45733                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.215                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.210                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1927                            
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 48.2028 -  6.6226    0.99     3412   149  0.1758 0.2085        
REMARK   3     2  6.6226 -  5.2586    1.00     3254   144  0.2209 0.2842        
REMARK   3     3  5.2586 -  4.5945    0.99     3158   139  0.1950 0.2473        
REMARK   3     4  4.5945 -  4.1747    0.88     2849   125  0.1888 0.2262        
REMARK   3     5  4.1747 -  3.8756    1.00     3151   139  0.2071 0.3201        
REMARK   3     6  3.8756 -  3.6472    1.00     3172   139  0.2150 0.2828        
REMARK   3     7  3.6472 -  3.4646    1.00     3154   139  0.2216 0.2448        
REMARK   3     8  3.4646 -  3.3138    1.00     3126   137  0.2287 0.3023        
REMARK   3     9  3.3138 -  3.1863    1.00     3109   137  0.2313 0.2460        
REMARK   3    10  3.1863 -  3.0763    1.00     3139   138  0.2391 0.3101        
REMARK   3    11  3.0763 -  2.9802    0.99     3132   138  0.2421 0.3086        
REMARK   3    12  2.9802 -  2.8950    0.99     3093   136  0.2500 0.3121        
REMARK   3    13  2.8950 -  2.8188    0.98     3072   136  0.2440 0.2932        
REMARK   3    14  2.8188 -  2.7500    0.96     2985   131  0.2428 0.3166        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.340           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 41.67                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.70                          
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      :  0.010          11380                                  
REMARK   3   ANGLE     :  1.057          15424                                  
REMARK   3   CHIRALITY :  0.054           1846                                  
REMARK   3   PLANARITY :  0.007           1938                                  
REMARK   3   DIHEDRAL  : 19.603           6767                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 14                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 30 THROUGH 78 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -42.1628 -12.3513 -41.4305              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2647 T22:   1.0713                                     
REMARK   3      T33:   0.4762 T12:  -0.7079                                     
REMARK   3      T13:   0.0040 T23:  -0.1023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7507 L22:   1.9609                                     
REMARK   3      L33:   1.3218 L12:   0.9989                                     
REMARK   3      L13:  -0.8502 L23:  -1.6783                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3926 S12:   0.3843 S13:  -0.5604                       
REMARK   3      S21:  -0.6886 S22:  -0.0047 S23:   0.0436                       
REMARK   3      S31:   2.1383 S32:  -1.3565 S33:   0.4953                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 79 THROUGH 145 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -37.2618   5.6970 -68.0303              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2616 T22:   0.5007                                     
REMARK   3      T33:   0.3441 T12:  -0.0712                                     
REMARK   3      T13:   0.0018 T23:  -0.0405                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1024 L22:   9.0565                                     
REMARK   3      L33:   7.0045 L12:  -5.9252                                     
REMARK   3      L13:   2.5471 L23:  -0.7379                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0902 S12:   0.1039 S13:  -0.3549                       
REMARK   3      S21:   0.1107 S22:  -0.2475 S23:   0.9223                       
REMARK   3      S31:   0.1384 S32:  -0.9143 S33:   0.1285                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 146 THROUGH 236 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -37.3970   0.7803 -94.7273              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2230 T22:   0.3120                                     
REMARK   3      T33:   0.3661 T12:   0.0359                                     
REMARK   3      T13:  -0.0462 T23:  -0.0418                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5828 L22:   4.6474                                     
REMARK   3      L33:   4.6735 L12:   0.8825                                     
REMARK   3      L13:  -0.3575 L23:   0.0045                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1689 S12:   0.1465 S13:  -0.2300                       
REMARK   3      S21:   0.1347 S22:  -0.0724 S23:  -0.7009                       
REMARK   3      S31:   0.2382 S32:   0.8104 S33:  -0.0151                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 237 THROUGH 288 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -35.7813  -0.4960 -84.1603              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3456 T22:   0.4388                                     
REMARK   3      T33:   0.3080 T12:   0.0029                                     
REMARK   3      T13:  -0.0051 T23:  -0.0241                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2195 L22:   1.8474                                     
REMARK   3      L33:   3.9035 L12:   2.4895                                     
REMARK   3      L13:   3.5667 L23:   2.3963                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2842 S12:  -0.0720 S13:  -0.2027                       
REMARK   3      S21:   0.1325 S22:   0.1162 S23:  -0.2609                       
REMARK   3      S31:   0.2552 S32:   0.3888 S33:  -0.2916                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 289 THROUGH 453 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -32.7364  -2.7909 -27.7075              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3681 T22:   0.3529                                     
REMARK   3      T33:   0.2484 T12:  -0.1507                                     
REMARK   3      T13:  -0.0040 T23:   0.0090                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6349 L22:   1.8640                                     
REMARK   3      L33:   5.7216 L12:   0.1522                                     
REMARK   3      L13:   0.1801 L23:  -0.2622                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0167 S12:  -0.3259 S13:  -0.0675                       
REMARK   3      S21:   0.2287 S22:  -0.0658 S23:   0.0746                       
REMARK   3      S31:   0.8524 S32:  -0.6979 S33:   0.0324                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 454 THROUGH 518 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -13.6430   7.3775 -32.5073              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3874 T22:   0.4448                                     
REMARK   3      T33:   0.3795 T12:   0.1037                                     
REMARK   3      T13:   0.0002 T23:   0.0238                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4241 L22:   0.7531                                     
REMARK   3      L33:   1.2601 L12:   0.9714                                     
REMARK   3      L13:   0.2497 L23:   0.2978                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0807 S12:  -0.2539 S13:  -0.2688                       
REMARK   3      S21:   0.2864 S22:  -0.0852 S23:  -0.0753                       
REMARK   3      S31:   0.5336 S32:   0.5740 S33:   0.0231                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 519 THROUGH 680 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -19.3174  10.7869 -45.2852              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1756 T22:   0.1852                                     
REMARK   3      T33:   0.2731 T12:  -0.0572                                     
REMARK   3      T13:  -0.0013 T23:  -0.0056                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4984 L22:   1.2690                                     
REMARK   3      L33:   6.0506 L12:  -0.2586                                     
REMARK   3      L13:  -0.4896 L23:   0.7313                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1035 S12:  -0.0792 S13:  -0.0362                       
REMARK   3      S21:  -0.0410 S22:   0.1030 S23:  -0.0928                       
REMARK   3      S31:   0.3179 S32:   0.5014 S33:  -0.0181                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 681 THROUGH 757 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -18.4035  10.3221 -22.1257              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2515 T22:   0.3808                                     
REMARK   3      T33:   0.2656 T12:  -0.0813                                     
REMARK   3      T13:   0.0328 T23:  -0.0080                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1115 L22:   3.7320                                     
REMARK   3      L33:   7.1961 L12:  -0.5655                                     
REMARK   3      L13:  -0.7071 L23:   1.4646                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1461 S12:  -0.3094 S13:   0.2804                       
REMARK   3      S21:  -0.1148 S22:   0.2572 S23:  -0.2040                       
REMARK   3      S31:  -0.7718 S32:   0.5769 S33:  -0.3634                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 28 THROUGH 92 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -57.3430  15.8099 -47.1215              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2775 T22:   0.2787                                     
REMARK   3      T33:   0.3355 T12:  -0.0314                                     
REMARK   3      T13:  -0.0207 T23:  -0.0661                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8257 L22:   3.9456                                     
REMARK   3      L33:   5.3126 L12:  -1.7285                                     
REMARK   3      L13:   2.1620 L23:  -4.2595                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2309 S12:   0.2120 S13:  -0.2436                       
REMARK   3      S21:  -0.2596 S22:  -0.4646 S23:  -0.1757                       
REMARK   3      S31:   0.3374 S32:   0.4939 S33:   0.2673                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 93 THROUGH 145 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -65.9341  26.1194 -69.8900              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2523 T22:   0.1318                                     
REMARK   3      T33:   0.2041 T12:  -0.0050                                     
REMARK   3      T13:   0.0434 T23:  -0.0064                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7747 L22:   3.9535                                     
REMARK   3      L33:   8.8177 L12:   2.0256                                     
REMARK   3      L13:   1.0588 L23:  -0.7481                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2127 S12:  -0.2445 S13:  -0.4204                       
REMARK   3      S21:  -0.0943 S22:  -0.1537 S23:  -0.1975                       
REMARK   3      S31:   0.3776 S32:  -0.2859 S33:  -0.0354                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 146 THROUGH 344 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -58.8934  23.0060 -76.5529              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1821 T22:   0.1691                                     
REMARK   3      T33:   0.2609 T12:   0.0010                                     
REMARK   3      T13:   0.0328 T23:  -0.0036                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5127 L22:   0.2259                                     
REMARK   3      L33:   4.5372 L12:   0.1181                                     
REMARK   3      L13:   0.6441 L23:   0.2978                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0016 S12:   0.0501 S13:  -0.0715                       
REMARK   3      S21:  -0.0817 S22:   0.0673 S23:  -0.0649                       
REMARK   3      S31:  -0.0483 S32:   0.2948 S33:  -0.0513                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 345 THROUGH 472 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -58.3345  27.4705 -24.3244              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1807 T22:   0.4124                                     
REMARK   3      T33:   0.2615 T12:  -0.0276                                     
REMARK   3      T13:   0.0104 T23:  -0.0064                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9316 L22:   2.3464                                     
REMARK   3      L33:   4.0762 L12:   0.1584                                     
REMARK   3      L13:  -0.6942 L23:  -0.1949                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0034 S12:  -0.4782 S13:   0.1354                       
REMARK   3      S21:   0.3622 S22:  -0.0720 S23:   0.0078                       
REMARK   3      S31:  -0.0696 S32:  -0.0172 S33:   0.0892                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 473 THROUGH 649 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -57.5505  47.0125 -50.8915              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4515 T22:   0.3010                                     
REMARK   3      T33:   0.3156 T12:  -0.0643                                     
REMARK   3      T13:  -0.0934 T23:   0.0213                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2485 L22:   0.9075                                     
REMARK   3      L33:   6.3029 L12:   0.1742                                     
REMARK   3      L13:  -2.0664 L23:  -0.2515                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0452 S12:  -0.2555 S13:   0.0671                       
REMARK   3      S21:   0.0478 S22:  -0.0554 S23:  -0.0966                       
REMARK   3      S31:  -1.0052 S32:   0.5523 S33:  -0.0650                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 650 THROUGH 760 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -61.2275  43.7127 -23.5604              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4090 T22:   0.3448                                     
REMARK   3      T33:   0.2658 T12:  -0.0494                                     
REMARK   3      T13:   0.0070 T23:   0.0158                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7257 L22:   1.4841                                     
REMARK   3      L33:   6.2623 L12:  -0.2715                                     
REMARK   3      L13:   0.1330 L23:  -0.0769                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0120 S12:  -0.2162 S13:   0.2669                       
REMARK   3      S21:   0.2136 S22:   0.0319 S23:   0.1021                       
REMARK   3      S31:  -0.8576 S32:  -0.6052 S33:  -0.0772                       
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 5XAN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-MAR-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300003194.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-MAY-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL32XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 9M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 47548                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : 0.14100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.75                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 3AQP                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.25                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 40% PEG 200, 100MM NA-CITRATE, 100MM     
REMARK 280  LISO4, PH 6.6, LIPIDIC CUBIC PHASE, TEMPERATURE 298K                
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       31.77250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      184.87300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.90700            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      184.87300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.77250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.90700            
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: MONOMERIC                         
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 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 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     MET A    27                                                      
REMARK 465     SER A    28                                                      
REMARK 465     ARG A    29                                                      
REMARK 465     LYS A   758                                                      
REMARK 465     ASN A   759                                                      
REMARK 465     ARG A   760                                                      
REMARK 465     ALA A   761                                                      
REMARK 465     ALA A   762                                                      
REMARK 465     LYS A   763                                                      
REMARK 465     PRO A   764                                                      
REMARK 465     VAL A   765                                                      
REMARK 465     THR A   766                                                      
REMARK 465     ASN A   767                                                      
REMARK 465     SER A   768                                                      
REMARK 465     HIS A   769                                                      
REMARK 465     HIS A   770                                                      
REMARK 465     HIS A   771                                                      
REMARK 465     HIS A   772                                                      
REMARK 465     HIS A   773                                                      
REMARK 465     HIS A   774                                                      
REMARK 465     HIS A   775                                                      
REMARK 465     HIS A   776                                                      
REMARK 465     MET B    27                                                      
REMARK 465     ALA B   761                                                      
REMARK 465     ALA B   762                                                      
REMARK 465     LYS B   763                                                      
REMARK 465     PRO B   764                                                      
REMARK 465     VAL B   765                                                      
REMARK 465     THR B   766                                                      
REMARK 465     ASN B   767                                                      
REMARK 465     SER B   768                                                      
REMARK 465     HIS B   769                                                      
REMARK 465     HIS B   770                                                      
REMARK 465     HIS B   771                                                      
REMARK 465     HIS B   772                                                      
REMARK 465     HIS B   773                                                      
REMARK 465     HIS B   774                                                      
REMARK 465     HIS B   775                                                      
REMARK 465     HIS B   776                                                      
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    LYS A   464     CD2  HIS A   465              1.68            
REMARK 500   O    MET B   471     NZ   LYS B   475              2.02            
REMARK 500   NH1  ARG A   285     OE1  GLU A   585              2.05            
REMARK 500   OD1  ASP A   365     O    HOH A   901              2.06            
REMARK 500   OD2  ASP A   401     NH1  ARG A   617              2.06            
REMARK 500   NH2  ARG B   617     OD2  ASP B   672              2.10            
REMARK 500   OE2  GLU A   520     NH1  ARG A   523              2.18            
REMARK 500   OD1  ASP B   365     O    HOH B   901              2.19            
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    TYR A  67   CG    TYR A  67   CD2    -0.136                       
REMARK 500    TYR A  67   CG    TYR A  67   CD1    -0.084                       
REMARK 500    TYR A  67   CE1   TYR A  67   CZ     -0.106                       
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  51   NE  -  CZ  -  NH1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    ARG A  51   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    LEU A 450   CB  -  CG  -  CD2 ANGL. DEV. = -13.6 DEGREES          
REMARK 500    LEU A 659   CA  -  CB  -  CG  ANGL. DEV. =  14.1 DEGREES          
REMARK 500    ASP B 235   CB  -  CG  -  OD1 ANGL. DEV. =   6.8 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    ARG A  51       81.67     39.52                                   
REMARK 500    ASN A  64     -177.34    174.99                                   
REMARK 500    LYS A 123       -2.54   -141.28                                   
REMARK 500    ALA A 148       45.11     77.64                                   
REMARK 500    ALA A 185      142.44   -171.87                                   
REMARK 500    PHE A 249      -67.39   -124.35                                   
REMARK 500    ASN A 257       90.52    -64.16                                   
REMARK 500    ALA A 283      135.54    179.22                                   
REMARK 500    LEU A 440      -66.18    -92.05                                   
REMARK 500    HIS A 465       41.54     79.07                                   
REMARK 500    SER B 173       10.35     59.21                                   
REMARK 500    PHE B 249      -90.42   -114.26                                   
REMARK 500    SER B 272       20.78   -150.26                                   
REMARK 500    HIS B 467       63.21   -109.72                                   
REMARK 500    ILE B 744      -55.72   -120.38                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLN A   66     TYR A   67                 -143.97                    
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 954        DISTANCE =  5.94 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     OLC A  801                                                       
REMARK 610     OLC A  802                                                       
REMARK 610     OLC A  803                                                       
REMARK 610     OLC A  804                                                       
REMARK 610     OLC B  801                                                       
REMARK 610     OLC B  803                                                       
REMARK 610     OLC B  804                                                       
REMARK 610     OLC B  805                                                       
REMARK 610     15P B  806                                                       
REMARK 610     15P B  807                                                       
REMARK 610     15P B  808                                                       
REMARK 610     15P B  809                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC B 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC B 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC B 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC B 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC B 805                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 15P B 806                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 15P B 807                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 15P B 808                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 15P B 809                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5XAM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5XAP   RELATED DB: PDB                                   
DBREF  5XAN A   28   768  UNP    Q9RTE3   Q9RTE3_DEIRA    28    768             
DBREF  5XAN B   28   768  UNP    Q9RTE3   Q9RTE3_DEIRA    28    768             
SEQADV 5XAN MET A   27  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAN CYS A  143  UNP  Q9RTE3    ILE   143 ENGINEERED MUTATION            
SEQADV 5XAN CYS A  268  UNP  Q9RTE3    LEU   268 ENGINEERED MUTATION            
SEQADV 5XAN HIS A  769  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAN HIS A  770  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAN HIS A  771  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAN HIS A  772  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAN HIS A  773  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAN HIS A  774  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAN HIS A  775  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAN HIS A  776  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAN MET B   27  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAN CYS B  143  UNP  Q9RTE3    ILE   143 ENGINEERED MUTATION            
SEQADV 5XAN CYS B  268  UNP  Q9RTE3    LEU   268 ENGINEERED MUTATION            
SEQADV 5XAN HIS B  769  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAN HIS B  770  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAN HIS B  771  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAN HIS B  772  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAN HIS B  773  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAN HIS B  774  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAN HIS B  775  UNP  Q9RTE3              EXPRESSION TAG                 
SEQADV 5XAN HIS B  776  UNP  Q9RTE3              EXPRESSION TAG                 
SEQRES   1 A  750  MET SER ARG PRO ASN PRO TRP THR ALA LEU LEU LEU LEU          
SEQRES   2 A  750  LEU THR LEU LEU GLY SER LEU LEU TYR ILE TRP ARG PRO          
SEQRES   3 A  750  TRP GLU HIS LYS ASN ASP PRO TRP SER LEU TRP ASN ASP          
SEQRES   4 A  750  GLN TYR GLN PHE MET THR LEU GLY LEU ASP LEU LYS GLY          
SEQRES   5 A  750  GLY LEU ARG ILE GLU LEU ALA PRO GLU SER GLY THR ALA          
SEQRES   6 A  750  THR ARG ASP GLU LEU ASP ARG VAL LYS THR VAL ILE GLU          
SEQRES   7 A  750  ASN ARG ILE ASN ALA LEU GLY VAL ALA GLU PRO THR VAL          
SEQRES   8 A  750  THR VAL SER GLY GLY LYS ARG VAL VAL VAL GLU ILE PRO          
SEQRES   9 A  750  GLY ALA THR PRO ALA VAL GLN ASP ARG ALA ARG SER CYS          
SEQRES  10 A  750  ILE GLN GLN THR ALA ARG LEU GLU PHE ARG ILE VAL ASN          
SEQRES  11 A  750  SER ASP ALA LYS PRO ASP PRO ALA VAL ARG GLU LYS ASN          
SEQRES  12 A  750  PRO ARG SER SER GLY TYR THR LEU ALA GLN LEU GLY PRO          
SEQRES  13 A  750  VAL VAL ALA THR GLY GLU THR ILE ALA ASP ALA THR SER          
SEQRES  14 A  750  GLY THR ASP GLN ARG SER GLY GLN TRP VAL VAL ASN PHE          
SEQRES  15 A  750  LYS THR THR ASP ALA GLY ALA LYS THR PHE GLY ASP PHE          
SEQRES  16 A  750  THR GLY LYS ASN VAL ASN ARG LEU MET ALA VAL VAL LEU          
SEQRES  17 A  750  ASP ASP GLN ILE GLN SER VAL ALA THR ILE ASN GLN ARG          
SEQRES  18 A  750  LEU PHE ARG ASP ILE GLN ILE SER GLY ASN PHE THR PRO          
SEQRES  19 A  750  GLU GLU ALA SER GLN LEU ALA CYS VAL LEU LYS SER GLY          
SEQRES  20 A  750  ALA LEU PRO ILE LYS ILE VAL THR ALA ALA GLU ARG SER          
SEQRES  21 A  750  ILE GLY PRO SER LEU GLY ALA ASP ALA ILE ARG SER GLY          
SEQRES  22 A  750  ALA ILE ALA ALA LEU VAL GLY ILE GLY LEU VAL PHE VAL          
SEQRES  23 A  750  MET LEU PHE ALA TYR TYR GLY LEU TRP PHE GLY LEU VAL          
SEQRES  24 A  750  GLY ALA LEU GLY LEU LEU PHE SER SER ILE ILE ILE LEU          
SEQRES  25 A  750  GLY ILE LEU GLY GLY PHE GLY ALA THR LEU THR LEU PRO          
SEQRES  26 A  750  GLY ILE ALA GLY LEU VAL LEU THR ILE GLY ALA ALA VAL          
SEQRES  27 A  750  ASP GLY ASN VAL ILE SER PHE GLU ARG ILE LYS GLU GLU          
SEQRES  28 A  750  LEU ALA ARG GLY LYS GLY ILE LYS ASN ALA ILE GLY ALA          
SEQRES  29 A  750  GLY TYR GLU HIS SER THR ALA ALA ILE LEU ASP VAL ASN          
SEQRES  30 A  750  ALA SER HIS LEU LEU SER ALA LEU ALA LEU TYR ASN TYR          
SEQRES  31 A  750  SER THR GLY ALA VAL LYS GLY PHE ALA VAL THR LEU ILE          
SEQRES  32 A  750  ILE GLY VAL ILE ALA SER THR PHE SER ASN LEU VAL PHE          
SEQRES  33 A  750  ALA LYS TRP PHE MET GLN TRP LEU ALA GLN ARG ARG PRO          
SEQRES  34 A  750  ASN MET SER ALA PRO GLN TRP ILE LYS HIS THR HIS PHE          
SEQRES  35 A  750  ASP PHE MET LYS PRO ALA LYS VAL ILE THR THR LEU SER          
SEQRES  36 A  750  VAL LEU LEU ALA LEU ALA GLY ALA ALA LEU VAL ALA THR          
SEQRES  37 A  750  ARG GLY LEU ASN TYR GLY VAL ASP PHE ALA PRO GLY THR          
SEQRES  38 A  750  THR LEU THR ALA ARG VAL ASP ARG GLN VAL THR THR GLU          
SEQRES  39 A  750  GLN LEU ARG ASN SER VAL ILE GLY ALA GLY VAL SER LYS          
SEQRES  40 A  750  VAL THR GLY GLN SER ALA THR ILE GLN ARG ASP THR THR          
SEQRES  41 A  750  PRO GLY GLN GLN GLY GLN ASN PHE THR VAL LYS VAL PRO          
SEQRES  42 A  750  GLU LEU ASN ASP ALA GLU VAL LYS GLN ILE GLY ALA ALA          
SEQRES  43 A  750  ILE GLY LYS LEU PRO GLN GLY GLN VAL LEU ALA SER GLU          
SEQRES  44 A  750  THR VAL GLY PRO ALA VAL GLY LYS GLU LEU THR GLN LYS          
SEQRES  45 A  750  THR ILE TYR ALA VAL LEU LEU GLY LEU GLY LEU ILE LEU          
SEQRES  46 A  750  VAL TYR VAL GLY PHE ARG PHE ASP PHE ILE MET GLY LEU          
SEQRES  47 A  750  GLY SER ILE ILE ALA ALA ILE HIS ASP VAL ALA ILE ALA          
SEQRES  48 A  750  MET GLY LEU PHE SER LEU LEU GLY LEU GLU PHE THR VAL          
SEQRES  49 A  750  ALA SER VAL ALA ALA LEU LEU THR LEU ILE GLY TYR SER          
SEQRES  50 A  750  LEU ASN ASP SER ILE ILE VAL SER ASP ARG ILE ARG GLU          
SEQRES  51 A  750  ASN MET LYS THR MET ARG GLY HIS SER TYR ARG GLU ILE          
SEQRES  52 A  750  VAL ASN ALA ALA ILE ASN GLN THR LEU SER ARG THR VAL          
SEQRES  53 A  750  MET THR SER VAL SER THR MET LEU PRO LEU ILE SER LEU          
SEQRES  54 A  750  LEU ILE PHE GLY GLY PRO VAL LEU ARG ASP PHE SER LEU          
SEQRES  55 A  750  ILE LEU LEU VAL GLY ILE LEU VAL GLY THR TYR SER SER          
SEQRES  56 A  750  ILE TYR ILE VAL ALA PRO LEU VAL VAL TYR PHE GLU GLU          
SEQRES  57 A  750  TRP ARG ASP LYS ASN ARG ALA ALA LYS PRO VAL THR ASN          
SEQRES  58 A  750  SER HIS HIS HIS HIS HIS HIS HIS HIS                          
SEQRES   1 B  750  MET SER ARG PRO ASN PRO TRP THR ALA LEU LEU LEU LEU          
SEQRES   2 B  750  LEU THR LEU LEU GLY SER LEU LEU TYR ILE TRP ARG PRO          
SEQRES   3 B  750  TRP GLU HIS LYS ASN ASP PRO TRP SER LEU TRP ASN ASP          
SEQRES   4 B  750  GLN TYR GLN PHE MET THR LEU GLY LEU ASP LEU LYS GLY          
SEQRES   5 B  750  GLY LEU ARG ILE GLU LEU ALA PRO GLU SER GLY THR ALA          
SEQRES   6 B  750  THR ARG ASP GLU LEU ASP ARG VAL LYS THR VAL ILE GLU          
SEQRES   7 B  750  ASN ARG ILE ASN ALA LEU GLY VAL ALA GLU PRO THR VAL          
SEQRES   8 B  750  THR VAL SER GLY GLY LYS ARG VAL VAL VAL GLU ILE PRO          
SEQRES   9 B  750  GLY ALA THR PRO ALA VAL GLN ASP ARG ALA ARG SER CYS          
SEQRES  10 B  750  ILE GLN GLN THR ALA ARG LEU GLU PHE ARG ILE VAL ASN          
SEQRES  11 B  750  SER ASP ALA LYS PRO ASP PRO ALA VAL ARG GLU LYS ASN          
SEQRES  12 B  750  PRO ARG SER SER GLY TYR THR LEU ALA GLN LEU GLY PRO          
SEQRES  13 B  750  VAL VAL ALA THR GLY GLU THR ILE ALA ASP ALA THR SER          
SEQRES  14 B  750  GLY THR ASP GLN ARG SER GLY GLN TRP VAL VAL ASN PHE          
SEQRES  15 B  750  LYS THR THR ASP ALA GLY ALA LYS THR PHE GLY ASP PHE          
SEQRES  16 B  750  THR GLY LYS ASN VAL ASN ARG LEU MET ALA VAL VAL LEU          
SEQRES  17 B  750  ASP ASP GLN ILE GLN SER VAL ALA THR ILE ASN GLN ARG          
SEQRES  18 B  750  LEU PHE ARG ASP ILE GLN ILE SER GLY ASN PHE THR PRO          
SEQRES  19 B  750  GLU GLU ALA SER GLN LEU ALA CYS VAL LEU LYS SER GLY          
SEQRES  20 B  750  ALA LEU PRO ILE LYS ILE VAL THR ALA ALA GLU ARG SER          
SEQRES  21 B  750  ILE GLY PRO SER LEU GLY ALA ASP ALA ILE ARG SER GLY          
SEQRES  22 B  750  ALA ILE ALA ALA LEU VAL GLY ILE GLY LEU VAL PHE VAL          
SEQRES  23 B  750  MET LEU PHE ALA TYR TYR GLY LEU TRP PHE GLY LEU VAL          
SEQRES  24 B  750  GLY ALA LEU GLY LEU LEU PHE SER SER ILE ILE ILE LEU          
SEQRES  25 B  750  GLY ILE LEU GLY GLY PHE GLY ALA THR LEU THR LEU PRO          
SEQRES  26 B  750  GLY ILE ALA GLY LEU VAL LEU THR ILE GLY ALA ALA VAL          
SEQRES  27 B  750  ASP GLY ASN VAL ILE SER PHE GLU ARG ILE LYS GLU GLU          
SEQRES  28 B  750  LEU ALA ARG GLY LYS GLY ILE LYS ASN ALA ILE GLY ALA          
SEQRES  29 B  750  GLY TYR GLU HIS SER THR ALA ALA ILE LEU ASP VAL ASN          
SEQRES  30 B  750  ALA SER HIS LEU LEU SER ALA LEU ALA LEU TYR ASN TYR          
SEQRES  31 B  750  SER THR GLY ALA VAL LYS GLY PHE ALA VAL THR LEU ILE          
SEQRES  32 B  750  ILE GLY VAL ILE ALA SER THR PHE SER ASN LEU VAL PHE          
SEQRES  33 B  750  ALA LYS TRP PHE MET GLN TRP LEU ALA GLN ARG ARG PRO          
SEQRES  34 B  750  ASN MET SER ALA PRO GLN TRP ILE LYS HIS THR HIS PHE          
SEQRES  35 B  750  ASP PHE MET LYS PRO ALA LYS VAL ILE THR THR LEU SER          
SEQRES  36 B  750  VAL LEU LEU ALA LEU ALA GLY ALA ALA LEU VAL ALA THR          
SEQRES  37 B  750  ARG GLY LEU ASN TYR GLY VAL ASP PHE ALA PRO GLY THR          
SEQRES  38 B  750  THR LEU THR ALA ARG VAL ASP ARG GLN VAL THR THR GLU          
SEQRES  39 B  750  GLN LEU ARG ASN SER VAL ILE GLY ALA GLY VAL SER LYS          
SEQRES  40 B  750  VAL THR GLY GLN SER ALA THR ILE GLN ARG ASP THR THR          
SEQRES  41 B  750  PRO GLY GLN GLN GLY GLN ASN PHE THR VAL LYS VAL PRO          
SEQRES  42 B  750  GLU LEU ASN ASP ALA GLU VAL LYS GLN ILE GLY ALA ALA          
SEQRES  43 B  750  ILE GLY LYS LEU PRO GLN GLY GLN VAL LEU ALA SER GLU          
SEQRES  44 B  750  THR VAL GLY PRO ALA VAL GLY LYS GLU LEU THR GLN LYS          
SEQRES  45 B  750  THR ILE TYR ALA VAL LEU LEU GLY LEU GLY LEU ILE LEU          
SEQRES  46 B  750  VAL TYR VAL GLY PHE ARG PHE ASP PHE ILE MET GLY LEU          
SEQRES  47 B  750  GLY SER ILE ILE ALA ALA ILE HIS ASP VAL ALA ILE ALA          
SEQRES  48 B  750  MET GLY LEU PHE SER LEU LEU GLY LEU GLU PHE THR VAL          
SEQRES  49 B  750  ALA SER VAL ALA ALA LEU LEU THR LEU ILE GLY TYR SER          
SEQRES  50 B  750  LEU ASN ASP SER ILE ILE VAL SER ASP ARG ILE ARG GLU          
SEQRES  51 B  750  ASN MET LYS THR MET ARG GLY HIS SER TYR ARG GLU ILE          
SEQRES  52 B  750  VAL ASN ALA ALA ILE ASN GLN THR LEU SER ARG THR VAL          
SEQRES  53 B  750  MET THR SER VAL SER THR MET LEU PRO LEU ILE SER LEU          
SEQRES  54 B  750  LEU ILE PHE GLY GLY PRO VAL LEU ARG ASP PHE SER LEU          
SEQRES  55 B  750  ILE LEU LEU VAL GLY ILE LEU VAL GLY THR TYR SER SER          
SEQRES  56 B  750  ILE TYR ILE VAL ALA PRO LEU VAL VAL TYR PHE GLU GLU          
SEQRES  57 B  750  TRP ARG ASP LYS ASN ARG ALA ALA LYS PRO VAL THR ASN          
SEQRES  58 B  750  SER HIS HIS HIS HIS HIS HIS HIS HIS                          
HET    OLC  A 801      10                                                       
HET    OLC  A 802       8                                                       
HET    OLC  A 803      10                                                       
HET    OLC  A 804      13                                                       
HET    OLC  B 801      21                                                       
HET    OLC  B 802      25                                                       
HET    OLC  B 803      14                                                       
HET    OLC  B 804       6                                                       
HET    OLC  B 805       5                                                       
HET    15P  B 806      13                                                       
HET    15P  B 807      12                                                       
HET    15P  B 808      10                                                       
HET    15P  B 809       9                                                       
HETNAM     OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE                   
HETNAM     15P POLYETHYLENE GLYCOL (N=34)                                       
HETSYN     OLC 1-OLEOYL-R-GLYCEROL                                              
HETSYN     15P PEG 1500                                                         
FORMUL   3  OLC    9(C21 H40 O4)                                                
FORMUL  12  15P    4(C69 H140 O35)                                              
FORMUL  16  HOH   *122(H2 O)                                                    
HELIX    1 AA1 ASN A   31  ARG A   51  1                                  21    
HELIX    2 AA2 GLY A   73  GLY A   78  1                                   6    
HELIX    3 AA3 THR A   92  ASN A  108  1                                  17    
HELIX    4 AA4 ALA A  109  GLY A  111  5                                   3    
HELIX    5 AA5 GLY A  121  LYS A  123  5                                   3    
HELIX    6 AA6 THR A  133  GLN A  146  1                                  14    
HELIX    7 AA7 ASP A  162  ASN A  169  1                                   8    
HELIX    8 AA8 PRO A  170  SER A  173  5                                   4    
HELIX    9 AA9 THR A  176  ALA A  178  5                                   3    
HELIX   10 AB1 THR A  211  LYS A  224  1                                  14    
HELIX   11 AB2 THR A  259  GLY A  273  1                                  15    
HELIX   12 AB3 GLY A  288  PHE A  344  1                                  57    
HELIX   13 AB4 THR A  349  ALA A  363  1                                  15    
HELIX   14 AB5 VAL A  364  GLY A  381  1                                  18    
HELIX   15 AB6 GLY A  383  HIS A  394  1                                  12    
HELIX   16 AB7 SER A  395  HIS A  406  1                                  12    
HELIX   17 AB8 LEU A  407  TYR A  414  1                                   8    
HELIX   18 AB9 THR A  418  ARG A  454  1                                  37    
HELIX   19 AC1 LYS A  475  ARG A  495  1                                  21    
HELIX   20 AC2 THR A  518  GLY A  528  1                                  11    
HELIX   21 AC3 ASN A  562  LYS A  575  1                                  14    
HELIX   22 AC4 GLY A  588  PHE A  618  1                                  31    
HELIX   23 AC5 ASP A  619  GLY A  645  1                                  27    
HELIX   24 AC6 THR A  649  SER A  663  1                                  15    
HELIX   25 AC7 SER A  663  MET A  681  1                                  19    
HELIX   26 AC8 SER A  685  THR A  697  1                                  13    
HELIX   27 AC9 THR A  697  GLY A  719  1                                  23    
HELIX   28 AD1 GLY A  720  ILE A  744  1                                  25    
HELIX   29 AD2 ILE A  744  ASP A  757  1                                  14    
HELIX   30 AD3 ASN B   31  ARG B   51  1                                  21    
HELIX   31 AD4 PRO B   52  HIS B   55  5                                   4    
HELIX   32 AD5 GLY B   73  GLY B   78  1                                   6    
HELIX   33 AD6 THR B   92  ASN B  108  1                                  17    
HELIX   34 AD7 ALA B  109  GLY B  111  5                                   3    
HELIX   35 AD8 THR B  133  GLN B  146  1                                  14    
HELIX   36 AD9 ASP B  162  ASN B  169  1                                   8    
HELIX   37 AE1 PRO B  170  SER B  173  5                                   4    
HELIX   38 AE2 THR B  176  ALA B  178  5                                   3    
HELIX   39 AE3 THR B  211  LYS B  224  1                                  14    
HELIX   40 AE4 THR B  259  LYS B  271  1                                  13    
HELIX   41 AE5 GLY B  288  GLY B  345  1                                  58    
HELIX   42 AE6 THR B  349  ALA B  363  1                                  15    
HELIX   43 AE7 VAL B  364  GLY B  381  1                                  18    
HELIX   44 AE8 GLY B  383  ASN B  415  1                                  33    
HELIX   45 AE9 THR B  418  VAL B  441  1                                  24    
HELIX   46 AF1 VAL B  441  ARG B  454  1                                  14    
HELIX   47 AF2 LYS B  475  GLY B  496  1                                  22    
HELIX   48 AF3 THR B  518  GLY B  528  1                                  11    
HELIX   49 AF4 ASN B  562  LYS B  575  1                                  14    
HELIX   50 AF5 GLY B  588  PHE B  618  1                                  31    
HELIX   51 AF6 ASP B  619  GLY B  645  1                                  27    
HELIX   52 AF7 THR B  649  MET B  681  1                                  33    
HELIX   53 AF8 SER B  685  THR B  697  1                                  13    
HELIX   54 AF9 THR B  697  GLY B  719  1                                  23    
HELIX   55 AG1 GLY B  720  ILE B  744  1                                  25    
HELIX   56 AG2 ILE B  744  ARG B  760  1                                  17    
SHEET    1 AA1 2 THR A  71  LEU A  72  0                                        
SHEET    2 AA1 2 THR A 347  LEU A 348  1  O  LEU A 348   N  THR A  71           
SHEET    1 AA2 8 THR A 116  SER A 120  0                                        
SHEET    2 AA2 8 ARG A 124  PRO A 130 -1  O  VAL A 126   N  THR A 118           
SHEET    3 AA2 8 GLY A  79  PRO A  86 -1  N  LEU A  80   O  ILE A 129           
SHEET    4 AA2 8 ILE A 279  ILE A 287 -1  O  VAL A 280   N  ALA A  85           
SHEET    5 AA2 8 GLN A 580  VAL A 587 -1  O  THR A 586   N  GLU A 284           
SHEET    6 AA2 8 GLY A 506  VAL A 513 -1  N  THR A 510   O  ALA A 583           
SHEET    7 AA2 8 GLN A 552  VAL A 558 -1  O  VAL A 558   N  THR A 507           
SHEET    8 AA2 8 THR A 540  ARG A 543 -1  N  GLN A 542   O  THR A 555           
SHEET    1 AA3 4 LEU A 180  THR A 186  0                                        
SHEET    2 AA3 4 LEU A 150  VAL A 155 -1  N  PHE A 152   O  VAL A 184           
SHEET    3 AA3 4 LEU A 229  LEU A 234 -1  O  ALA A 231   N  ARG A 153           
SHEET    4 AA3 4 GLN A 237  THR A 243 -1  O  GLN A 239   N  VAL A 232           
SHEET    1 AA4 3 ILE A 190  ASP A 198  0                                        
SHEET    2 AA4 3 GLN A 203  THR A 210 -1  O  VAL A 205   N  GLY A 196           
SHEET    3 AA4 3 ASP A 251  SER A 255 -1  O  ILE A 252   N  PHE A 208           
SHEET    1 AA5 2 ASN A 498  TYR A 499  0                                        
SHEET    2 AA5 2 GLU A 647  PHE A 648  1  O  PHE A 648   N  ASN A 498           
SHEET    1 AA6 2 THR B  71  LEU B  72  0                                        
SHEET    2 AA6 2 THR B 347  LEU B 348  1  O  LEU B 348   N  THR B  71           
SHEET    1 AA7 8 THR B 116  SER B 120  0                                        
SHEET    2 AA7 8 ARG B 124  PRO B 130 -1  O  ARG B 124   N  SER B 120           
SHEET    3 AA7 8 GLY B  79  PRO B  86 -1  N  ILE B  82   O  VAL B 127           
SHEET    4 AA7 8 ILE B 279  ILE B 287 -1  O  ILE B 287   N  GLY B  79           
SHEET    5 AA7 8 GLN B 580  VAL B 587 -1  O  SER B 584   N  SER B 286           
SHEET    6 AA7 8 GLY B 506  VAL B 513 -1  N  ARG B 512   O  GLN B 580           
SHEET    7 AA7 8 GLN B 552  VAL B 558 -1  O  PHE B 554   N  ALA B 511           
SHEET    8 AA7 8 THR B 540  ARG B 543 -1  N  GLN B 542   O  THR B 555           
SHEET    1 AA8 4 LEU B 180  THR B 186  0                                        
SHEET    2 AA8 4 LEU B 150  VAL B 155 -1  N  ILE B 154   O  GLY B 181           
SHEET    3 AA8 4 LEU B 229  LEU B 234 -1  O  ALA B 231   N  ARG B 153           
SHEET    4 AA8 4 GLN B 237  THR B 243 -1  O  GLN B 239   N  VAL B 232           
SHEET    1 AA9 3 ILE B 190  THR B 197  0                                        
SHEET    2 AA9 3 TRP B 204  THR B 210 -1  O  LYS B 209   N  ASP B 192           
SHEET    3 AA9 3 ASP B 251  ILE B 254 -1  O  ILE B 252   N  PHE B 208           
SHEET    1 AB1 2 ASN B 498  TYR B 499  0                                        
SHEET    2 AB1 2 GLU B 647  PHE B 648  1  O  PHE B 648   N  ASN B 498           
SSBOND   1 CYS A  143    CYS A  268                          1555   1555  2.04  
SSBOND   2 CYS B  143    CYS B  268                          1555   1555  2.04  
SITE     1 AC1  3 SER A 334  ILE A 353  ILE A 360                               
SITE     1 AC2  2 TYR A 499  PHE A 503                                          
SITE     1 AC3  1 HIS A 632                                                     
SITE     1 AC4  1 PHE A 616                                                     
SITE     1 AC5  8 ALA A 487  THR A 494  ARG A 495  LEU A 643                    
SITE     2 AC5  8 PHE B 344  ILE B 430  ILE B 433  OLC B 802                    
SITE     1 AC6  7 ARG A 495  SER B  45  TYR B  48  GLY B 343                    
SITE     2 AC6  7 PHE B 344  PHE B 437  OLC B 801                               
SITE     1 AC7  5 TRP B  63  ILE B 296  SER B 334  LEU B 356                    
SITE     2 AC7  5 ILE B 360                                                     
SITE     1 AC8  1 LEU B  62                                                     
SITE     1 AC9  2 TRP B  50  TRP B  60                                          
SITE     1 AD1  5 ARG B 200  MET B 230  THR B 243  LEU B 248                    
SITE     2 AD1  5 ASP B 251                                                     
SITE     1 AD2  7 ALA B 362  HIS B 406  SER B 409  SER B 435                    
SITE     2 AD2  7 THR B 658  TYR B 662  15P B 808                               
SITE     1 AD3  3 LEU B 413  LEU B 657  15P B 807                               
SITE     1 AD4  4 SER B 405  HIS B 406  SER B 409  TYR B 613                    
CRYST1   63.545   73.814  369.746  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      0.015737  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013548  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002705        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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