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Database: PDB
Entry: 6O5E
LinkDB: 6O5E
Original site: 6O5E 
HEADER    CELL ADHESION                           01-MAR-19   6O5E              
TITLE     CRYSTAL STRUCTURE OF THE VITRONECTIN HEMOPEXIN-LIKE DOMAIN            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: VITRONECTIN;                                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: HEMOPEXIN-LIKE DOMAIN (UNP RESIDUES 154-285, 324-354, 435- 
COMPND   5 474);                                                                
COMPND   6 SYNONYM: VN, S-PROTEIN, SERUM-SPREADING FACTOR, V75;                 
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: VTN;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    INTEGRIN LIGAND, HEMOPEXIN-LIKE DOMAIN, BETA-PROPELLER, SERUM         
KEYWDS   2 PROTEIN, CELL ADHESION                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.C.LECHTENBERG,K.SHIN,F.M.MARASSI                                    
REVDAT   3   04-DEC-19 6O5E    1       REMARK                                   
REVDAT   2   02-OCT-19 6O5E    1       JRNL                                     
REVDAT   1   18-SEP-19 6O5E    0                                                
JRNL        AUTH   K.SHIN,B.C.LECHTENBERG,L.M.FUJIMOTO,Y.YAO,S.S.BARTRA,        
JRNL        AUTH 2 G.V.PLANO,F.M.MARASSI                                        
JRNL        TITL   STRUCTURE OF HUMAN VITRONECTIN C-TERMINAL DOMAIN AND         
JRNL        TITL 2 INTERACTION WITHYERSINIA PESTISOUTER MEMBRANE PROTEIN AIL.   
JRNL        REF    SCI ADV                       V.   5 X5068 2019              
JRNL        REFN                   ESSN 2375-2548                               
JRNL        PMID   31535027                                                     
JRNL        DOI    10.1126/SCIADV.AAX5068                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.14RC2-3191                                  
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.21                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 28986                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.210                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.080                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1472                            
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 24.2200 -  4.2200    0.98     2540   147  0.1592 0.1860        
REMARK   3     2  4.2200 -  3.3500    0.99     2551   148  0.1520 0.1827        
REMARK   3     3  3.3500 -  2.9300    0.99     2503   147  0.1806 0.2155        
REMARK   3     4  2.9300 -  2.6600    0.99     2526   140  0.1968 0.2433        
REMARK   3     5  2.6600 -  2.4700    0.99     2530   116  0.2013 0.2308        
REMARK   3     6  2.4700 -  2.3300    0.98     2509   128  0.1952 0.2313        
REMARK   3     7  2.3300 -  2.2100    0.98     2479   140  0.2018 0.2530        
REMARK   3     8  2.2100 -  2.1100    0.97     2492   127  0.1909 0.2136        
REMARK   3     9  2.1100 -  2.0300    0.97     2447   132  0.2017 0.2244        
REMARK   3    10  2.0300 -  1.9600    0.96     2484   119  0.2113 0.2459        
REMARK   3    11  1.9600 -  1.9000    0.96     2453   128  0.2481 0.2940        
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)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.104           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.97                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           3131                                  
REMARK   3   ANGLE     :  0.832           4242                                  
REMARK   3   CHIRALITY :  0.048            405                                  
REMARK   3   PLANARITY :  0.005            558                                  
REMARK   3   DIHEDRAL  :  9.193           1803                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 13                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 153 THROUGH 195 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   6.7833  46.3170  34.8927              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2814 T22:   0.2999                                     
REMARK   3      T33:   0.3047 T12:  -0.0034                                     
REMARK   3      T13:  -0.0570 T23:   0.0296                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0750 L22:   0.8136                                     
REMARK   3      L33:   2.4184 L12:  -0.2936                                     
REMARK   3      L13:  -0.5499 L23:   0.7707                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0074 S12:   0.3237 S13:   0.0379                       
REMARK   3      S21:  -0.3872 S22:  -0.1905 S23:   0.1406                       
REMARK   3      S31:   0.0466 S32:  -0.3130 S33:  -0.0010                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 196 THROUGH 207 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   1.0708  52.9295  43.3513              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2818 T22:   0.3696                                     
REMARK   3      T33:   0.3422 T12:   0.0787                                     
REMARK   3      T13:  -0.0605 T23:   0.0425                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0804 L22:   0.2003                                     
REMARK   3      L33:   1.1568 L12:   0.2971                                     
REMARK   3      L13:   0.7246 L23:   0.0722                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4379 S12:  -0.5678 S13:   0.6548                       
REMARK   3      S21:   0.0666 S22:   0.3373 S23:   0.2307                       
REMARK   3      S31:  -0.7108 S32:  -0.5126 S33:  -0.0135                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 208 THROUGH 338 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  13.2130  47.8128  53.6331              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2562 T22:   0.3033                                     
REMARK   3      T33:   0.2085 T12:   0.0385                                     
REMARK   3      T13:  -0.0544 T23:   0.0116                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7165 L22:   2.0970                                     
REMARK   3      L33:   2.5854 L12:   0.5390                                     
REMARK   3      L13:  -0.8654 L23:   0.2653                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0650 S12:  -0.5747 S13:   0.0321                       
REMARK   3      S21:   0.3015 S22:   0.0203 S23:  -0.0895                       
REMARK   3      S31:   0.1483 S32:   0.1495 S33:  -0.0125                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 339 THROUGH 440 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  22.8065  46.6526  41.8632              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2346 T22:   0.2298                                     
REMARK   3      T33:   0.2900 T12:  -0.0076                                     
REMARK   3      T13:  -0.0250 T23:   0.0412                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9493 L22:   0.3313                                     
REMARK   3      L33:   2.7352 L12:  -0.7300                                     
REMARK   3      L13:  -0.5588 L23:  -0.1773                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0482 S12:   0.1126 S13:  -0.0819                       
REMARK   3      S21:   0.2268 S22:   0.0711 S23:  -0.1530                       
REMARK   3      S31:  -0.2303 S32:   0.3111 S33:   0.0004                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 441 THROUGH 474 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  24.5189  44.8025  33.3055              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2416 T22:   0.3238                                     
REMARK   3      T33:   0.2848 T12:  -0.0352                                     
REMARK   3      T13:   0.0036 T23:   0.0323                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7524 L22:   2.9369                                     
REMARK   3      L33:   2.8713 L12:   1.1966                                     
REMARK   3      L13:  -0.4127 L23:   1.0241                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0239 S12:   0.3907 S13:  -0.2869                       
REMARK   3      S21:  -0.3305 S22:  -0.0270 S23:  -0.4498                       
REMARK   3      S31:   0.1680 S32:   0.7021 S33:   0.0225                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 154 THROUGH 171 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   4.3013  22.8523  29.3254              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4687 T22:   0.2957                                     
REMARK   3      T33:   0.4973 T12:   0.0210                                     
REMARK   3      T13:   0.0414 T23:  -0.0109                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6284 L22:   0.6974                                     
REMARK   3      L33:   0.6932 L12:   0.5238                                     
REMARK   3      L13:  -0.1717 L23:   0.0392                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0588 S12:  -0.3020 S13:  -0.4783                       
REMARK   3      S21:   0.6527 S22:  -0.1007 S23:   0.8329                       
REMARK   3      S31:  -0.1319 S32:  -0.3101 S33:  -0.0003                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 172 THROUGH 207 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.8304  16.2960  28.9057              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5175 T22:   0.3999                                     
REMARK   3      T33:   0.5842 T12:  -0.0355                                     
REMARK   3      T13:   0.1514 T23:   0.0128                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0298 L22:   0.4079                                     
REMARK   3      L33:   0.7678 L12:   0.1517                                     
REMARK   3      L13:   0.7660 L23:  -0.1477                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0764 S12:  -0.4096 S13:  -0.6215                       
REMARK   3      S21:   0.7506 S22:  -0.0070 S23:   0.8079                       
REMARK   3      S31:   0.3194 S32:  -0.3553 S33:   0.0160                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 208 THROUGH 223 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.5406  22.3347  16.7165              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3018 T22:   0.2805                                     
REMARK   3      T33:   0.4684 T12:   0.0433                                     
REMARK   3      T13:  -0.0696 T23:  -0.1001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6565 L22:   0.4922                                     
REMARK   3      L33:   1.4515 L12:   0.4792                                     
REMARK   3      L13:   0.1890 L23:   0.5840                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0802 S12:   0.1985 S13:  -0.3646                       
REMARK   3      S21:  -0.5576 S22:  -0.4986 S23:   1.3398                       
REMARK   3      S31:  -0.0591 S32:  -0.3096 S33:  -0.0604                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 224 THROUGH 242 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.5085  15.7513  14.7348              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3777 T22:   0.3998                                     
REMARK   3      T33:   0.7114 T12:   0.0339                                     
REMARK   3      T13:  -0.0714 T23:  -0.1585                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6225 L22:   1.0016                                     
REMARK   3      L33:   1.1464 L12:   0.3337                                     
REMARK   3      L13:   0.0681 L23:  -0.9090                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1862 S12:   0.1961 S13:  -0.2197                       
REMARK   3      S21:  -0.3109 S22:  -0.0066 S23:   0.9483                       
REMARK   3      S31:  -0.0290 S32:  -0.4609 S33:   0.0220                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 243 THROUGH 338 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   8.4937  23.3756   9.5561              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5543 T22:   0.3620                                     
REMARK   3      T33:   0.2864 T12:   0.0717                                     
REMARK   3      T13:   0.0978 T23:  -0.0276                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1571 L22:   1.8912                                     
REMARK   3      L33:   1.0128 L12:  -0.0179                                     
REMARK   3      L13:  -0.3247 L23:  -0.7775                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2333 S12:   0.5918 S13:  -0.1562                       
REMARK   3      S21:  -0.9487 S22:  -0.0390 S23:  -0.1623                       
REMARK   3      S31:  -0.2605 S32:  -0.0235 S33:   0.1304                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 339 THROUGH 440 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  11.8939  29.0847  20.4067              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2869 T22:   0.2680                                     
REMARK   3      T33:   0.3191 T12:   0.0313                                     
REMARK   3      T13:   0.0496 T23:  -0.0250                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4966 L22:   2.2286                                     
REMARK   3      L33:   1.7732 L12:   1.6573                                     
REMARK   3      L13:   0.8279 L23:   0.1972                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1330 S12:  -0.0150 S13:  -0.0724                       
REMARK   3      S21:  -0.4683 S22:   0.1171 S23:  -0.4563                       
REMARK   3      S31:   0.1536 S32:   0.1238 S33:   0.0003                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 441 THROUGH 458 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  15.4000  35.0689  22.5205              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3369 T22:   0.2538                                     
REMARK   3      T33:   0.2517 T12:  -0.0114                                     
REMARK   3      T13:   0.0077 T23:  -0.0012                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9147 L22:   1.2996                                     
REMARK   3      L33:   0.1593 L12:   1.0059                                     
REMARK   3      L13:  -0.0701 L23:   0.0957                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0806 S12:   0.2009 S13:  -0.2454                       
REMARK   3      S21:  -0.2452 S22:  -0.0908 S23:  -0.2860                       
REMARK   3      S31:   0.2110 S32:   0.3040 S33:  -0.0003                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 459 THROUGH 474 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  13.7042  30.0914  34.3902              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5060 T22:   0.2557                                     
REMARK   3      T33:   0.3411 T12:  -0.0674                                     
REMARK   3      T13:  -0.0146 T23:   0.0318                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4118 L22:   0.4599                                     
REMARK   3      L33:   0.2606 L12:  -0.2117                                     
REMARK   3      L13:  -0.1643 L23:  -0.0282                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0932 S12:  -0.3620 S13:  -0.2253                       
REMARK   3      S21:   0.9981 S22:  -0.1849 S23:  -0.3137                       
REMARK   3      S31:   0.2551 S32:   0.1488 S33:   0.0007                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: (CHAIN 'A' AND (RESID 154 THROUGH 184 OR    
REMARK   3                          RESID 193 THROUGH 213 OR RESID 217          
REMARK   3                          THROUGH 240 OR RESID 242 THROUGH 474 OR     
REMARK   3                          RESID 501 THROUGH 505))                     
REMARK   3     SELECTION          : (CHAIN 'B' AND (RESID 154 THROUGH 240 OR    
REMARK   3                          RESID 242 THROUGH 474 OR RESID 501          
REMARK   3                          THROUGH 504))                               
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6O5E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAR-19.                  
REMARK 100 THE DEPOSITION ID IS D_1000239945.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-JAN-19                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E SUPERBRIGHT            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS HTC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM 7.2.2                       
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.7.3                      
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29017                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 26.960                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 2.300                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.94                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
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: PDB ENTRIES 1QHU, 1RTG, 2MQS, 3C7X, 4RT6             
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 UL PROTEIN SOLUTION + 1 UL             
REMARK 280  PRECIPITATE SOLUTION [0.09 M IMIDAZOLE/MES, PH 6.5, 27 MM SODIUM    
REMARK 280  NITRATE, 27 MM SODIUM PHOSPHATE DIBASIC, 27 MM AMMONIUM SULFATE,    
REMARK 280  11.25% V/V MPD, 11.25% W/V PEG1000, 11.25% W/V PEG3350, 3% W/V D-   
REMARK 280  (+)-TREHALOSE], VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       48.68000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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     ALA A   262                                                      
REMARK 465     HIS A   263                                                      
REMARK 465     SER A   264                                                      
REMARK 465     TYR A   265                                                      
REMARK 465     SER A   266                                                      
REMARK 465     GLY A   267                                                      
REMARK 465     ARG A   268                                                      
REMARK 465     GLN A   323                                                      
REMARK 465     ARG A   324                                                      
REMARK 465     THR A   325                                                      
REMARK 465     SER A   326                                                      
REMARK 465     ALA A   327                                                      
REMARK 465     GLY A   328                                                      
REMARK 465     THR A   329                                                      
REMARK 465     ARG A   330                                                      
REMARK 465     MET B   153                                                      
REMARK 465     GLU B   185                                                      
REMARK 465     LYS B   186                                                      
REMARK 465     ALA B   187                                                      
REMARK 465     VAL B   188                                                      
REMARK 465     ARG B   189                                                      
REMARK 465     PRO B   190                                                      
REMARK 465     GLY B   191                                                      
REMARK 465     TYR B   192                                                      
REMARK 465     ASN B   214                                                      
REMARK 465     SER B   215                                                      
REMARK 465     GLN B   216                                                      
REMARK 465     ALA B   262                                                      
REMARK 465     HIS B   263                                                      
REMARK 465     SER B   264                                                      
REMARK 465     TYR B   265                                                      
REMARK 465     SER B   266                                                      
REMARK 465     GLY B   267                                                      
REMARK 465     ARG B   268                                                      
REMARK 465     GLN B   323                                                      
REMARK 465     ARG B   324                                                      
REMARK 465     THR B   325                                                      
REMARK 465     SER B   326                                                      
REMARK 465     ALA B   327                                                      
REMARK 465     GLY B   328                                                      
REMARK 465     THR B   329                                                      
REMARK 465     ARG B   330                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B   627     O    HOH B   672              2.17            
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 189       76.04   -119.06                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 501  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 162   O                                                      
REMARK 620 2 ASP A 207   O    86.8                                              
REMARK 620 3 ASP A 255   O   134.7  83.2                                        
REMARK 620 4 ASP A 347   O    82.9 147.8  82.7                                  
REMARK 620 5 HOH A 689   O   118.7 112.9 105.8  98.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 503  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE A 164   O                                                      
REMARK 620 2 ALA A 209   O    83.7                                              
REMARK 620 3 ALA A 257   O   165.3  88.3                                        
REMARK 620 4 ALA A 349   O    95.7 172.1  90.6                                  
REMARK 620 5 HOH A 621   O    75.0  85.4  92.1  86.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 501  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 162   O                                                      
REMARK 620 2 ASP B 207   O    80.4                                              
REMARK 620 3 ASP B 255   O   135.0  88.9                                        
REMARK 620 4 ASP B 347   O    85.7 145.8  79.1                                  
REMARK 620 5 HOH B 664   O   108.8 111.0 115.8 103.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 503  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE B 164   O                                                      
REMARK 620 2 ALA B 209   O    89.7                                              
REMARK 620 3 ALA B 257   O   178.3  90.7                                        
REMARK 620 4 ALA B 349   O    87.0 176.3  92.5                                  
REMARK 620 5 SO4 B 504   O2   88.7  83.9  89.7  94.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NO3 B 506                 
DBREF  6O5E A  154   323  UNP    P04004   VTNC_HUMAN     154    285             
DBREF  6O5E A  324   354  UNP    P04004   VTNC_HUMAN     324    354             
DBREF  6O5E A  435   474  UNP    P04004   VTNC_HUMAN     435    474             
DBREF  6O5E B  154   323  UNP    P04004   VTNC_HUMAN     154    285             
DBREF  6O5E B  324   354  UNP    P04004   VTNC_HUMAN     324    354             
DBREF  6O5E B  435   474  UNP    P04004   VTNC_HUMAN     435    474             
SEQADV 6O5E MET A  153  UNP  P04004              INITIATING METHIONINE          
SEQADV 6O5E SER A  180  UNP  P04004    CYS   180 ENGINEERED MUTATION            
SEQADV 6O5E SER A  215  UNP  P04004    CYS   215 ENGINEERED MUTATION            
SEQADV 6O5E MET B  153  UNP  P04004              INITIATING METHIONINE          
SEQADV 6O5E SER B  180  UNP  P04004    CYS   180 ENGINEERED MUTATION            
SEQADV 6O5E SER B  215  UNP  P04004    CYS   215 ENGINEERED MUTATION            
SEQRES   1 A  204  MET GLU LEU CYS SER GLY LYS PRO PHE ASP ALA PHE THR          
SEQRES   2 A  204  ASP LEU LYS ASN GLY SER LEU PHE ALA PHE ARG GLY GLN          
SEQRES   3 A  204  TYR SER TYR GLU LEU ASP GLU LYS ALA VAL ARG PRO GLY          
SEQRES   4 A  204  TYR PRO LYS LEU ILE ARG ASP VAL TRP GLY ILE GLU GLY          
SEQRES   5 A  204  PRO ILE ASP ALA ALA PHE THR ARG ILE ASN SER GLN GLY          
SEQRES   6 A  204  LYS THR TYR LEU PHE LYS GLY SER GLN TYR TRP ARG PHE          
SEQRES   7 A  204  GLU ASP GLY VAL LEU ASP PRO ASP TYR PRO ARG ASN ILE          
SEQRES   8 A  204  SER ASP GLY PHE ASP GLY ILE PRO ASP ASN VAL ASP ALA          
SEQRES   9 A  204  ALA LEU ALA LEU PRO ALA HIS SER TYR SER GLY ARG GLU          
SEQRES  10 A  204  ARG VAL TYR PHE PHE LYS GLY LYS GLN TYR TRP GLU TYR          
SEQRES  11 A  204  GLN PHE GLN ARG THR SER ALA GLY THR ARG GLN PRO GLN          
SEQRES  12 A  204  PHE ILE SER ARG ASP TRP HIS GLY VAL PRO GLY GLN VAL          
SEQRES  13 A  204  ASP ALA ALA MET ALA GLY ARG ILE SER VAL PHE PHE PHE          
SEQRES  14 A  204  SER GLY ASP LYS TYR TYR ARG VAL ASN LEU ARG THR ARG          
SEQRES  15 A  204  ARG VAL ASP THR VAL ASP PRO PRO TYR PRO ARG SER ILE          
SEQRES  16 A  204  ALA GLN TYR TRP LEU GLY CYS PRO ALA                          
SEQRES   1 B  204  MET GLU LEU CYS SER GLY LYS PRO PHE ASP ALA PHE THR          
SEQRES   2 B  204  ASP LEU LYS ASN GLY SER LEU PHE ALA PHE ARG GLY GLN          
SEQRES   3 B  204  TYR SER TYR GLU LEU ASP GLU LYS ALA VAL ARG PRO GLY          
SEQRES   4 B  204  TYR PRO LYS LEU ILE ARG ASP VAL TRP GLY ILE GLU GLY          
SEQRES   5 B  204  PRO ILE ASP ALA ALA PHE THR ARG ILE ASN SER GLN GLY          
SEQRES   6 B  204  LYS THR TYR LEU PHE LYS GLY SER GLN TYR TRP ARG PHE          
SEQRES   7 B  204  GLU ASP GLY VAL LEU ASP PRO ASP TYR PRO ARG ASN ILE          
SEQRES   8 B  204  SER ASP GLY PHE ASP GLY ILE PRO ASP ASN VAL ASP ALA          
SEQRES   9 B  204  ALA LEU ALA LEU PRO ALA HIS SER TYR SER GLY ARG GLU          
SEQRES  10 B  204  ARG VAL TYR PHE PHE LYS GLY LYS GLN TYR TRP GLU TYR          
SEQRES  11 B  204  GLN PHE GLN ARG THR SER ALA GLY THR ARG GLN PRO GLN          
SEQRES  12 B  204  PHE ILE SER ARG ASP TRP HIS GLY VAL PRO GLY GLN VAL          
SEQRES  13 B  204  ASP ALA ALA MET ALA GLY ARG ILE SER VAL PHE PHE PHE          
SEQRES  14 B  204  SER GLY ASP LYS TYR TYR ARG VAL ASN LEU ARG THR ARG          
SEQRES  15 B  204  ARG VAL ASP THR VAL ASP PRO PRO TYR PRO ARG SER ILE          
SEQRES  16 B  204  ALA GLN TYR TRP LEU GLY CYS PRO ALA                          
HET     NA  A 501       1                                                       
HET     CL  A 502       1                                                       
HET     NA  A 503       1                                                       
HET    SO4  A 504       5                                                       
HET    IMD  A 505      10                                                       
HET     NA  B 501       1                                                       
HET     CL  B 502       1                                                       
HET     NA  B 503       1                                                       
HET    SO4  B 504       5                                                       
HET    SO4  B 505       5                                                       
HET    NO3  B 506       4                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     SO4 SULFATE ION                                                      
HETNAM     IMD IMIDAZOLE                                                        
HETNAM     NO3 NITRATE ION                                                      
FORMUL   3   NA    4(NA 1+)                                                     
FORMUL   4   CL    2(CL 1-)                                                     
FORMUL   6  SO4    3(O4 S 2-)                                                   
FORMUL   7  IMD    C3 H5 N2 1+                                                  
FORMUL  13  NO3    N O3 1-                                                      
FORMUL  14  HOH   *168(H2 O)                                                    
HELIX    1 AA1 ILE A  196  GLY A  201  1                                   6    
HELIX    2 AA2 ILE A  243  PHE A  247  1                                   5    
HELIX    3 AA3 ILE A  335  TRP A  339  1                                   5    
HELIX    4 AA4 ILE A  465  TRP A  469  1                                   5    
HELIX    5 AA5 ILE B  196  TRP B  200  1                                   5    
HELIX    6 AA6 ILE B  243  PHE B  247  1                                   5    
HELIX    7 AA7 ILE B  335  TRP B  339  1                                   5    
HELIX    8 AA8 ILE B  465  TRP B  469  1                                   5    
SHEET    1 AA1 4 ALA A 163  PHE A 164  0                                        
SHEET    2 AA1 4 SER A 171  ARG A 176 -1  O  PHE A 175   N  ALA A 163           
SHEET    3 AA1 4 TYR A 179  ASP A 184 -1  O  LEU A 183   N  LEU A 172           
SHEET    4 AA1 4 PRO A 193  LEU A 195 -1  O  LYS A 194   N  SER A 180           
SHEET    1 AA2 4 ALA A 208  THR A 211  0                                        
SHEET    2 AA2 4 THR A 219  LYS A 223 -1  O  TYR A 220   N  PHE A 210           
SHEET    3 AA2 4 GLN A 226  GLU A 231 -1  O  PHE A 230   N  THR A 219           
SHEET    4 AA2 4 VAL A 234  LEU A 235 -1  O  VAL A 234   N  GLU A 231           
SHEET    1 AA3 4 ALA A 208  THR A 211  0                                        
SHEET    2 AA3 4 THR A 219  LYS A 223 -1  O  TYR A 220   N  PHE A 210           
SHEET    3 AA3 4 GLN A 226  GLU A 231 -1  O  PHE A 230   N  THR A 219           
SHEET    4 AA3 4 ARG A 241  ASN A 242 -1  O  ARG A 241   N  TYR A 227           
SHEET    1 AA4 4 ALA A 256  ALA A 259  0                                        
SHEET    2 AA4 4 ARG A 270  LYS A 275 -1  O  TYR A 272   N  LEU A 258           
SHEET    3 AA4 4 GLN A 278  GLN A 283 -1  O  TYR A 282   N  VAL A 271           
SHEET    4 AA4 4 GLN A 333  PHE A 334 -1  O  GLN A 333   N  TYR A 279           
SHEET    1 AA5 4 ALA A 348  ALA A 351  0                                        
SHEET    2 AA5 4 SER A 435  SER A 440 -1  O  PHE A 437   N  MET A 350           
SHEET    3 AA5 4 LYS A 443  ASN A 448 -1  O  VAL A 447   N  VAL A 436           
SHEET    4 AA5 4 ARG A 453  VAL A 454 -1  O  ARG A 453   N  ASN A 448           
SHEET    1 AA6 4 ALA A 348  ALA A 351  0                                        
SHEET    2 AA6 4 SER A 435  SER A 440 -1  O  PHE A 437   N  MET A 350           
SHEET    3 AA6 4 LYS A 443  ASN A 448 -1  O  VAL A 447   N  VAL A 436           
SHEET    4 AA6 4 ARG A 463  SER A 464 -1  O  ARG A 463   N  TYR A 444           
SHEET    1 AA7 4 ALA B 163  ASP B 166  0                                        
SHEET    2 AA7 4 LEU B 172  ARG B 176 -1  O  PHE B 173   N  THR B 165           
SHEET    3 AA7 4 TYR B 179  LEU B 183 -1  O  TYR B 181   N  ALA B 174           
SHEET    4 AA7 4 LYS B 194  LEU B 195 -1  O  LYS B 194   N  SER B 180           
SHEET    1 AA8 4 ALA B 208  THR B 211  0                                        
SHEET    2 AA8 4 LYS B 218  LYS B 223 -1  O  TYR B 220   N  PHE B 210           
SHEET    3 AA8 4 GLN B 226  GLU B 231 -1  O  PHE B 230   N  THR B 219           
SHEET    4 AA8 4 VAL B 234  LEU B 235 -1  O  VAL B 234   N  GLU B 231           
SHEET    1 AA9 4 ALA B 208  THR B 211  0                                        
SHEET    2 AA9 4 LYS B 218  LYS B 223 -1  O  TYR B 220   N  PHE B 210           
SHEET    3 AA9 4 GLN B 226  GLU B 231 -1  O  PHE B 230   N  THR B 219           
SHEET    4 AA9 4 ARG B 241  ASN B 242 -1  O  ARG B 241   N  TYR B 227           
SHEET    1 AB1 4 ALA B 256  LEU B 260  0                                        
SHEET    2 AB1 4 ARG B 270  LYS B 275 -1  O  ARG B 270   N  LEU B 260           
SHEET    3 AB1 4 GLN B 278  GLN B 283 -1  O  TYR B 282   N  VAL B 271           
SHEET    4 AB1 4 GLN B 333  PHE B 334 -1  O  GLN B 333   N  TYR B 279           
SHEET    1 AB2 4 ALA B 348  ALA B 351  0                                        
SHEET    2 AB2 4 SER B 435  SER B 440 -1  O  PHE B 437   N  MET B 350           
SHEET    3 AB2 4 LYS B 443  ASN B 448 -1  O  VAL B 447   N  VAL B 436           
SHEET    4 AB2 4 ARG B 453  VAL B 454 -1  O  ARG B 453   N  ASN B 448           
SHEET    1 AB3 4 ALA B 348  ALA B 351  0                                        
SHEET    2 AB3 4 SER B 435  SER B 440 -1  O  PHE B 437   N  MET B 350           
SHEET    3 AB3 4 LYS B 443  ASN B 448 -1  O  VAL B 447   N  VAL B 436           
SHEET    4 AB3 4 ARG B 463  SER B 464 -1  O  ARG B 463   N  TYR B 444           
SSBOND   1 CYS A  156    CYS A  472                          1555   1555  2.04  
SSBOND   2 CYS B  156    CYS B  472                          1555   1555  2.03  
LINK         O   ASP A 162                NA    NA A 501     1555   1555  2.31  
LINK         O   PHE A 164                NA    NA A 503     1555   1555  2.33  
LINK         O   ASP A 207                NA    NA A 501     1555   1555  2.31  
LINK         O   ALA A 209                NA    NA A 503     1555   1555  2.24  
LINK         O   ASP A 255                NA    NA A 501     1555   1555  2.30  
LINK         O   ALA A 257                NA    NA A 503     1555   1555  2.26  
LINK         O   ASP A 347                NA    NA A 501     1555   1555  2.32  
LINK         O   ALA A 349                NA    NA A 503     1555   1555  2.30  
LINK         O   ASP B 162                NA    NA B 501     1555   1555  2.22  
LINK         O   PHE B 164                NA    NA B 503     1555   1555  2.31  
LINK         O   ASP B 207                NA    NA B 501     1555   1555  2.20  
LINK         O   ALA B 209                NA    NA B 503     1555   1555  2.26  
LINK         O   ASP B 255                NA    NA B 501     1555   1555  2.21  
LINK         O   ALA B 257                NA    NA B 503     1555   1555  2.19  
LINK         O   ASP B 347                NA    NA B 501     1555   1555  2.36  
LINK         O   ALA B 349                NA    NA B 503     1555   1555  2.21  
LINK        NA    NA A 501                 O   HOH A 689     1555   1555  2.09  
LINK        NA    NA A 503                 O   HOH A 621     1555   1555  2.33  
LINK        NA    NA B 501                 O   HOH B 664     1555   1555  2.15  
LINK        NA    NA B 503                 O2  SO4 B 504     1555   1555  2.82  
CISPEP   1 GLY A  204    PRO A  205          0        -3.38                     
CISPEP   2 TYR A  239    PRO A  240          0         5.00                     
CISPEP   3 ASP A  458    PRO A  459          0        -3.16                     
CISPEP   4 TYR A  461    PRO A  462          0        -1.42                     
CISPEP   5 GLY B  204    PRO B  205          0        -5.23                     
CISPEP   6 TYR B  239    PRO B  240          0         3.64                     
CISPEP   7 ASP B  458    PRO B  459          0         1.35                     
CISPEP   8 TYR B  461    PRO B  462          0         2.04                     
SITE     1 AC1  5 ASP A 162  ASP A 207  ASP A 255  ASP A 347                    
SITE     2 AC1  5 HOH A 689                                                     
SITE     1 AC2  7 ALA A 163  PHE A 164  ALA A 208  ALA A 209                    
SITE     2 AC2  7 ALA A 257  ALA A 349   NA A 503                               
SITE     1 AC3  6 PHE A 164  ALA A 209  ALA A 257  ALA A 349                    
SITE     2 AC3  6  CL A 502  HOH A 621                                          
SITE     1 AC4 10 TYR A 220  TYR A 227  ARG A 229  TYR A 239                    
SITE     2 AC4 10 PHE A 247  HOH A 628  HOH A 632  HOH A 637                    
SITE     3 AC4 10 HOH A 652  ARG B 450                                          
SITE     1 AC5  2 HOH A 635  ILE B 354                                          
SITE     1 AC6  5 ASP B 162  ASP B 207  ASP B 255  ASP B 347                    
SITE     2 AC6  5 HOH B 664                                                     
SITE     1 AC7  7 ALA B 163  PHE B 164  ALA B 209  ALA B 257                    
SITE     2 AC7  7 ALA B 348  ALA B 349   NA B 503                               
SITE     1 AC8  6 PHE B 164  ALA B 209  ALA B 257  ALA B 349                    
SITE     2 AC8  6  CL B 502  SO4 B 504                                          
SITE     1 AC9 13 PHE B 164  THR B 165  ASP B 166  LYS B 168                    
SITE     2 AC9 13 ALA B 209  PHE B 210  THR B 211  ALA B 257                    
SITE     3 AC9 13 LEU B 258  ALA B 259  MET B 350  ALA B 351                    
SITE     4 AC9 13  NA B 503                                                     
SITE     1 AD1  6 TYR B 220  TYR B 227  ARG B 229  TYR B 239                    
SITE     2 AD1  6 ARG B 241  HOH B 610                                          
SITE     1 AD2  3 ARG B 446  ARG B 463  HOH B 618                               
CRYST1   40.560   97.360   49.160  90.00  99.90  90.00 P 1 21 1      4          
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      0.024655  0.000000  0.004303        0.00000                         
SCALE2      0.000000  0.010271  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020649        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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