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LongText Report for: 6ru1-pdb

Name Class
6ru1-pdb
HEADER    HYDROLASE                               27-MAY-19   6RU1              
TITLE     CRYSTAL STRUCTURE OF GLUCURONOYL ESTERASE FROM CERRENA UNICOLOR       
TITLE    2 INACTIVE S270A VARIANT IN COMPLEX WITH THE ALDOURONIC ACID UM4X      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 4-O-METHYL-GLUCURONOYL METHYLESTERASE;                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC DOMAIN;                                          
COMPND   5 SYNONYM: GLUCURONOYL ESTERASE,GE;                                    
COMPND   6 EC: 3.1.1.-;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CERRENA UNICOLOR;                               
SOURCE   3 ORGANISM_TAXID: 90312;                                               
SOURCE   4 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;                            
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE   6 EXPRESSION_SYSTEM_VARIANT: X-33;                                     
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PPICZ-ALPHA                               
KEYWDS    CE15, ESTERASE, ALPHA/BETA-HYDROLASE, LIGAND-BOUND, HYDROLASE         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.A.ERNST,C.MOSBECH,A.LANGKILDE,P.WESTH,A.MEYER,J.W.AGGER,S.LARSEN    
REVDAT   1   18-MAR-20 6RU1    0                                                
JRNL        AUTH   H.A.ERNST,C.MOSBECH,A.E.LANGKILDE,P.WESTH,A.S.MEYER,         
JRNL        AUTH 2 J.W.AGGER,S.LARSEN                                           
JRNL        TITL   THE STRUCTURAL BASIS OF FUNGAL GLUCURONOYL ESTERASE ACTIVITY 
JRNL        TITL 2 ON NATURAL SUBSTRATES.                                       
JRNL        REF    NAT COMMUN                    V.  11  1026 2020              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   32094331                                                     
JRNL        DOI    10.1038/S41467-020-14833-9                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.39 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.13_2998                                     
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) : 1.39                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.12                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 188017                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.163                           
REMARK   3   R VALUE            (WORKING SET) : 0.163                           
REMARK   3   FREE R VALUE                     : 0.177                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 9369                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 42.1393 -  4.3160    0.96     6269   336  0.1514 0.1568        
REMARK   3     2  4.3160 -  3.4262    0.98     6065   310  0.1429 0.1511        
REMARK   3     3  3.4262 -  2.9932    0.99     6037   332  0.1590 0.1705        
REMARK   3     4  2.9932 -  2.7196    0.99     6023   311  0.1615 0.1734        
REMARK   3     5  2.7196 -  2.5247    0.99     6059   305  0.1598 0.1630        
REMARK   3     6  2.5247 -  2.3759    0.99     5979   323  0.1586 0.1787        
REMARK   3     7  2.3759 -  2.2569    1.00     5999   313  0.1575 0.1664        
REMARK   3     8  2.2569 -  2.1587    1.00     5965   307  0.1573 0.1697        
REMARK   3     9  2.1587 -  2.0756    1.00     6015   299  0.1528 0.1609        
REMARK   3    10  2.0756 -  2.0039    1.00     5917   331  0.1561 0.1959        
REMARK   3    11  2.0039 -  1.9413    1.00     5988   321  0.1543 0.1763        
REMARK   3    12  1.9413 -  1.8858    1.00     5953   332  0.1559 0.1735        
REMARK   3    13  1.8858 -  1.8361    1.00     5937   281  0.1551 0.1672        
REMARK   3    14  1.8361 -  1.7913    1.00     5959   312  0.1593 0.1577        
REMARK   3    15  1.7913 -  1.7506    1.00     5957   303  0.1633 0.1833        
REMARK   3    16  1.7506 -  1.7134    1.00     5954   296  0.1683 0.2092        
REMARK   3    17  1.7134 -  1.6791    1.00     5924   326  0.1657 0.1845        
REMARK   3    18  1.6791 -  1.6474    1.00     5938   302  0.1728 0.2009        
REMARK   3    19  1.6474 -  1.6180    1.00     5907   324  0.1684 0.1929        
REMARK   3    20  1.6180 -  1.5906    1.00     5908   300  0.1676 0.1875        
REMARK   3    21  1.5906 -  1.5649    1.00     5908   325  0.1706 0.1900        
REMARK   3    22  1.5649 -  1.5408    1.00     5880   330  0.1774 0.2048        
REMARK   3    23  1.5408 -  1.5182    1.00     5899   330  0.1928 0.2132        
REMARK   3    24  1.5182 -  1.4968    1.00     5909   276  0.1952 0.2149        
REMARK   3    25  1.4968 -  1.4765    1.00     5909   305  0.2031 0.2173        
REMARK   3    26  1.4765 -  1.4574    1.00     5881   314  0.2071 0.2257        
REMARK   3    27  1.4574 -  1.4391    1.00     5924   303  0.2176 0.2284        
REMARK   3    28  1.4391 -  1.4218    1.00     5928   295  0.2239 0.2589        
REMARK   3    29  1.4218 -  1.4053    1.00     5827   314  0.2290 0.2441        
REMARK   3    30  1.4053 -  1.3895    0.98     5830   313  0.2362 0.2542        
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)     : 0.120            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.510           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 12.45                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.16                          
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 11                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 73 THROUGH 110 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  44.1927   7.7104  35.8964              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1128 T22:   0.1167                                     
REMARK   3      T33:   0.1343 T12:   0.0041                                     
REMARK   3      T13:  -0.0352 T23:  -0.0163                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6729 L22:   2.2778                                     
REMARK   3      L33:   4.9425 L12:   0.1291                                     
REMARK   3      L13:  -1.4450 L23:   0.8110                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0917 S12:  -0.2199 S13:   0.2505                       
REMARK   3      S21:   0.1756 S22:  -0.0351 S23:   0.0444                       
REMARK   3      S31:  -0.2286 S32:  -0.1040 S33:  -0.0490                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 111 THROUGH 149 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  26.4706  10.3454  27.8826              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1049 T22:   0.0749                                     
REMARK   3      T33:   0.1037 T12:  -0.0007                                     
REMARK   3      T13:   0.0151 T23:  -0.0150                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6945 L22:   0.5526                                     
REMARK   3      L33:   0.6267 L12:  -0.4834                                     
REMARK   3      L13:   0.3699 L23:  -0.0693                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0155 S12:  -0.0538 S13:  -0.0186                       
REMARK   3      S21:   0.0587 S22:  -0.0069 S23:   0.0632                       
REMARK   3      S31:  -0.0006 S32:  -0.0625 S33:  -0.0094                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 150 THROUGH 172 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  11.9469  17.0840  19.2897              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1051 T22:   0.1363                                     
REMARK   3      T33:   0.1672 T12:   0.0380                                     
REMARK   3      T13:   0.0075 T23:  -0.0005                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9943 L22:   6.9876                                     
REMARK   3      L33:   5.4545 L12:   1.5171                                     
REMARK   3      L13:   1.1202 L23:   5.4445                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0125 S12:  -0.0079 S13:   0.0311                       
REMARK   3      S21:  -0.3602 S22:   0.0461 S23:   0.0225                       
REMARK   3      S31:  -0.3190 S32:  -0.1027 S33:  -0.0418                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 173 THROUGH 205 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  12.2043  -1.9259  18.5195              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1157 T22:   0.1359                                     
REMARK   3      T33:   0.1709 T12:  -0.0277                                     
REMARK   3      T13:  -0.0013 T23:  -0.0239                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2087 L22:   0.8757                                     
REMARK   3      L33:   3.3358 L12:  -0.5153                                     
REMARK   3      L13:  -1.1884 L23:  -0.0917                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1210 S12:   0.0793 S13:  -0.1299                       
REMARK   3      S21:   0.0102 S22:   0.0132 S23:   0.1751                       
REMARK   3      S31:   0.2551 S32:  -0.3177 S33:   0.0879                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 206 THROUGH 370 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  30.9477   6.8238  17.1337              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1089 T22:   0.0928                                     
REMARK   3      T33:   0.1018 T12:   0.0037                                     
REMARK   3      T13:  -0.0013 T23:  -0.0019                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5470 L22:   0.5353                                     
REMARK   3      L33:   0.3676 L12:   0.0190                                     
REMARK   3      L13:  -0.0691 L23:  -0.0540                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0060 S12:   0.0378 S13:   0.0336                       
REMARK   3      S21:  -0.0059 S22:  -0.0117 S23:   0.0402                       
REMARK   3      S31:  -0.0123 S32:  -0.0226 S33:   0.0045                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 371 THROUGH 458 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  34.0894 -10.1377  20.9270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1276 T22:   0.0757                                     
REMARK   3      T33:   0.1191 T12:   0.0019                                     
REMARK   3      T13:  -0.0018 T23:   0.0006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0710 L22:   0.6407                                     
REMARK   3      L33:   0.8617 L12:   0.0964                                     
REMARK   3      L13:  -0.1445 L23:   0.1776                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0084 S12:   0.0016 S13:  -0.0912                       
REMARK   3      S21:   0.0174 S22:  -0.0210 S23:   0.0474                       
REMARK   3      S31:   0.0683 S32:  -0.0155 S33:   0.0132                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 73 THROUGH 128 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  65.4556  48.0951  31.2272              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1090 T22:   0.0935                                     
REMARK   3      T33:   0.0900 T12:  -0.0039                                     
REMARK   3      T13:  -0.0223 T23:  -0.0213                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5519 L22:   2.1122                                     
REMARK   3      L33:   2.9697 L12:   0.2756                                     
REMARK   3      L13:  -0.3693 L23:  -0.5563                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0048 S12:  -0.2560 S13:   0.0728                       
REMARK   3      S21:   0.2106 S22:   0.0007 S23:   0.0471                       
REMARK   3      S31:  -0.0580 S32:  -0.0685 S33:  -0.0193                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 129 THROUGH 317 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  45.3612  48.5357  15.3563              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1290 T22:   0.0961                                     
REMARK   3      T33:   0.1114 T12:   0.0045                                     
REMARK   3      T13:  -0.0037 T23:  -0.0009                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3702 L22:   0.3982                                     
REMARK   3      L33:   0.2572 L12:  -0.0670                                     
REMARK   3      L13:  -0.0632 L23:   0.0158                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0084 S12:   0.0135 S13:  -0.0136                       
REMARK   3      S21:   0.0101 S22:   0.0001 S23:   0.0704                       
REMARK   3      S31:   0.0009 S32:  -0.0173 S33:   0.0085                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 318 THROUGH 338 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  63.5623  57.4484  10.8506              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1322 T22:   0.0697                                     
REMARK   3      T33:   0.0957 T12:  -0.0107                                     
REMARK   3      T13:   0.0018 T23:   0.0160                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2658 L22:   0.8912                                     
REMARK   3      L33:   2.8299 L12:  -1.5001                                     
REMARK   3      L13:   1.9188 L23:  -0.3587                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0137 S12:   0.1120 S13:   0.1467                       
REMARK   3      S21:   0.0175 S22:  -0.0848 S23:  -0.0418                       
REMARK   3      S31:  -0.1455 S32:   0.1002 S33:   0.0979                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 339 THROUGH 422 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  58.4517  36.2756  13.5659              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1232 T22:   0.1003                                     
REMARK   3      T33:   0.1130 T12:   0.0108                                     
REMARK   3      T13:  -0.0035 T23:  -0.0051                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3832 L22:   0.5728                                     
REMARK   3      L33:   0.3144 L12:   0.2023                                     
REMARK   3      L13:  -0.0819 L23:  -0.1559                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0001 S12:   0.0345 S13:  -0.0481                       
REMARK   3      S21:  -0.0319 S22:  -0.0169 S23:   0.0027                       
REMARK   3      S31:   0.0502 S32:  -0.0020 S33:   0.0168                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 423 THROUGH 458 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  64.8387  31.9595  15.7687              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1304 T22:   0.0932                                     
REMARK   3      T33:   0.1220 T12:   0.0224                                     
REMARK   3      T13:  -0.0028 T23:   0.0099                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8744 L22:   0.6048                                     
REMARK   3      L33:   0.3792 L12:   0.4736                                     
REMARK   3      L13:   0.0153 L23:   0.0594                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0200 S12:  -0.0273 S13:  -0.1115                       
REMARK   3      S21:   0.0155 S22:  -0.0147 S23:  -0.0321                       
REMARK   3      S31:   0.0372 S32:   0.0661 S33:   0.0060                       
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 6RU1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-MAY-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292102594.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-JUL-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PETRA III, EMBL C/O DESY           
REMARK 200  BEAMLINE                       : P13 (MX1)                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97625                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.7.3                      
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 188224                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.390                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.140                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.09900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 11.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.39                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.41                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.00200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 6RTV                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.05                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES PH 7, 0.1 M KCL, 25% W/V     
REMARK 280  SOKALAN CP7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      130.40750            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       42.12000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       42.12000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       65.20375            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       42.12000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       42.12000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      195.61125            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       42.12000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       42.12000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       65.20375            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       42.12000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       42.12000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      195.61125            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      130.40750            
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 886  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLU A   459                                                      
REMARK 465     ASN A   460                                                      
REMARK 465     LEU A   461                                                      
REMARK 465     TYR A   462                                                      
REMARK 465     PHE A   463                                                      
REMARK 465     GLN A   464                                                      
REMARK 465     GLY A   465                                                      
REMARK 465     VAL A   466                                                      
REMARK 465     ASP A   467                                                      
REMARK 465     HIS A   468                                                      
REMARK 465     HIS A   469                                                      
REMARK 465     HIS A   470                                                      
REMARK 465     HIS A   471                                                      
REMARK 465     HIS A   472                                                      
REMARK 465     HIS A   473                                                      
REMARK 465     GLU B   459                                                      
REMARK 465     ASN B   460                                                      
REMARK 465     LEU B   461                                                      
REMARK 465     TYR B   462                                                      
REMARK 465     PHE B   463                                                      
REMARK 465     GLN B   464                                                      
REMARK 465     GLY B   465                                                      
REMARK 465     VAL B   466                                                      
REMARK 465     ASP B   467                                                      
REMARK 465     HIS B   468                                                      
REMARK 465     HIS B   469                                                      
REMARK 465     HIS B   470                                                      
REMARK 465     HIS B   471                                                      
REMARK 465     HIS B   472                                                      
REMARK 465     HIS B   473                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  92       96.15   -161.33                                   
REMARK 500    ARG A 109      -32.19   -132.03                                   
REMARK 500    ARG A 109      -30.83   -132.74                                   
REMARK 500    SER A 162      -12.64     88.13                                   
REMARK 500    GLN A 213       47.64   -147.33                                   
REMARK 500    GLN A 213       47.64   -150.65                                   
REMARK 500    SER A 215     -171.62   -173.06                                   
REMARK 500    ALA A 270     -129.30     62.15                                   
REMARK 500    ASN A 325     -168.38   -161.49                                   
REMARK 500    PRO A 343       36.55    -83.61                                   
REMARK 500    SER A 370       65.15     64.38                                   
REMARK 500    TRP A 449      -33.25   -134.10                                   
REMARK 500    ASN B  92       93.88   -162.51                                   
REMARK 500    ARG B 109      -32.61   -131.10                                   
REMARK 500    ARG B 109      -30.42   -132.27                                   
REMARK 500    GLN B 213       47.87   -146.37                                   
REMARK 500    ALA B 270     -127.95     62.59                                   
REMARK 500    PRO B 343       34.23    -83.54                                   
REMARK 500    SER B 370       64.90     66.37                                   
REMARK 500    TRP B 449      -33.02   -135.62                                   
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 B 509  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ILE B 259   O                                                      
REMARK 620 2 GOL B 507   O2   99.5                                              
REMARK 620 3 GOL B 507   O3  169.2  70.1                                        
REMARK 620 4 HOH B 806   O    97.4 163.2  93.1                                  
REMARK 620 5 HOH B 812   O    90.5  91.4  92.3  88.2                            
REMARK 620 6 HOH B 804   O    84.3  92.7  93.3  89.3 173.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA B 509                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 501 bound   
REMARK 800  to ASN A 104                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 501 bound   
REMARK 800  to ASN B 104                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues GCV B    
REMARK 800  502 through XYP B 504                                               
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6RTV   RELATED DB: PDB                                   
REMARK 900 APO-FORM OF SAME PROTEIN                                             
DBREF1 6RU1 A   79   458  UNP                  GCE_CERUI                        
DBREF2 6RU1 A     A0A0A7EQR3                         95         474             
DBREF1 6RU1 B   79   458  UNP                  GCE_CERUI                        
DBREF2 6RU1 B     A0A0A7EQR3                         95         474             
SEQADV 6RU1 GLU A   73  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 ALA A   74  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 GLU A   75  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 ALA A   76  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 GLU A   77  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 PHE A   78  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 ALA A  270  UNP  A0A0A7EQR SER   286 ENGINEERED MUTATION            
SEQADV 6RU1 GLU A  459  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 ASN A  460  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 LEU A  461  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 TYR A  462  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 PHE A  463  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 GLN A  464  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 GLY A  465  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 VAL A  466  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 ASP A  467  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 HIS A  468  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 HIS A  469  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 HIS A  470  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 HIS A  471  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 HIS A  472  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 HIS A  473  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 GLU B   73  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 ALA B   74  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 GLU B   75  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 ALA B   76  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 GLU B   77  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 PHE B   78  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 ALA B  270  UNP  A0A0A7EQR SER   286 ENGINEERED MUTATION            
SEQADV 6RU1 GLU B  459  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 ASN B  460  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 LEU B  461  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 TYR B  462  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 PHE B  463  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 GLN B  464  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 GLY B  465  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 VAL B  466  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 ASP B  467  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 HIS B  468  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 HIS B  469  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 HIS B  470  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 HIS B  471  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 HIS B  472  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQADV 6RU1 HIS B  473  UNP  A0A0A7EQR           EXPRESSION TAG                 
SEQRES   1 A  401  GLU ALA GLU ALA GLU PHE GLY ALA CYS GLY ALA ILE ALA          
SEQRES   2 A  401  SER THR VAL PRO ASN TYR ASN ASN ALA LYS LEU PRO ASP          
SEQRES   3 A  401  PRO PHE THR PHE ALA ASN GLY THR ALA LEU ARG THR LYS          
SEQRES   4 A  401  ALA ASP TRP SER CYS ARG ARG ALA GLU ILE SER ALA LEU          
SEQRES   5 A  401  ILE GLN ASN TYR GLU ALA GLY THR LEU PRO PRO LYS PRO          
SEQRES   6 A  401  PRO VAL VAL THR ALA SER PHE SER LYS SER GLY ASN THR          
SEQRES   7 A  401  GLY THR LEU ALA ILE THR ALA GLY LEU SER ASN SER GLN          
SEQRES   8 A  401  THR ILE LYS PHE SER PRO THR ILE SER TYR PRO SER GLY          
SEQRES   9 A  401  THR PRO PRO ALA ASN GLY TRP PRO LEU ILE ILE ALA TYR          
SEQRES  10 A  401  GLU GLY GLY SER ILE PRO ILE PRO ALA GLY VAL ALA THR          
SEQRES  11 A  401  LEU THR TYR SER ASN SER ASP MET ALA GLN GLN ASN SER          
SEQRES  12 A  401  ALA SER SER ARG GLY GLN GLY LEU PHE TYR GLN LEU TYR          
SEQRES  13 A  401  GLY SER THR HIS SER ALA SER ALA MET THR ALA TRP VAL          
SEQRES  14 A  401  TRP GLY VAL SER ARG ILE ILE ASP ALA LEU GLU MET THR          
SEQRES  15 A  401  PRO THR ALA GLN ILE ASN THR GLN ARG ILE GLY VAL THR          
SEQRES  16 A  401  GLY CYS ALA ARG ASP GLY LYS GLY ALA LEU MET ALA GLY          
SEQRES  17 A  401  ALA PHE GLU GLU ARG ILE ALA LEU THR ILE PRO GLN GLU          
SEQRES  18 A  401  SER GLY SER GLY GLY ASP ALA CYS TRP ARG LEU SER LYS          
SEQRES  19 A  401  TYR GLU ILE ASP ASN GLY ASN GLN VAL GLN ASP ALA VAL          
SEQRES  20 A  401  GLU ILE VAL GLY GLU ASN VAL TRP PHE SER THR ASN PHE          
SEQRES  21 A  401  ASN ASN TYR VAL GLN LYS LEU PRO THR VAL PRO GLU ASP          
SEQRES  22 A  401  HIS HIS LEU LEU ALA ALA MET VAL ALA PRO ARG ALA MET          
SEQRES  23 A  401  ILE SER PHE GLU ASN THR ASP TYR LEU TRP LEU SER PRO          
SEQRES  24 A  401  MET SER SER PHE GLY CYS MET THR ALA ALA HIS THR VAL          
SEQRES  25 A  401  TRP GLN GLY LEU GLY ILE ALA ASP SER HIS GLY PHE ALA          
SEQRES  26 A  401  GLN VAL GLY GLY HIS ALA HIS CYS ALA TRP PRO SER SER          
SEQRES  27 A  401  LEU THR PRO GLN LEU ASN ALA PHE ILE ASN ARG PHE LEU          
SEQRES  28 A  401  LEU ASP GLN SER ALA THR THR ASN VAL PHE THR THR ASN          
SEQRES  29 A  401  ASN GLN PHE GLY LYS VAL GLN TRP ASN ALA ALA ASN TRP          
SEQRES  30 A  401  ILE THR TRP THR THR PRO THR LEU THR GLU ASN LEU TYR          
SEQRES  31 A  401  PHE GLN GLY VAL ASP HIS HIS HIS HIS HIS HIS                  
SEQRES   1 B  401  GLU ALA GLU ALA GLU PHE GLY ALA CYS GLY ALA ILE ALA          
SEQRES   2 B  401  SER THR VAL PRO ASN TYR ASN ASN ALA LYS LEU PRO ASP          
SEQRES   3 B  401  PRO PHE THR PHE ALA ASN GLY THR ALA LEU ARG THR LYS          
SEQRES   4 B  401  ALA ASP TRP SER CYS ARG ARG ALA GLU ILE SER ALA LEU          
SEQRES   5 B  401  ILE GLN ASN TYR GLU ALA GLY THR LEU PRO PRO LYS PRO          
SEQRES   6 B  401  PRO VAL VAL THR ALA SER PHE SER LYS SER GLY ASN THR          
SEQRES   7 B  401  GLY THR LEU ALA ILE THR ALA GLY LEU SER ASN SER GLN          
SEQRES   8 B  401  THR ILE LYS PHE SER PRO THR ILE SER TYR PRO SER GLY          
SEQRES   9 B  401  THR PRO PRO ALA ASN GLY TRP PRO LEU ILE ILE ALA TYR          
SEQRES  10 B  401  GLU GLY GLY SER ILE PRO ILE PRO ALA GLY VAL ALA THR          
SEQRES  11 B  401  LEU THR TYR SER ASN SER ASP MET ALA GLN GLN ASN SER          
SEQRES  12 B  401  ALA SER SER ARG GLY GLN GLY LEU PHE TYR GLN LEU TYR          
SEQRES  13 B  401  GLY SER THR HIS SER ALA SER ALA MET THR ALA TRP VAL          
SEQRES  14 B  401  TRP GLY VAL SER ARG ILE ILE ASP ALA LEU GLU MET THR          
SEQRES  15 B  401  PRO THR ALA GLN ILE ASN THR GLN ARG ILE GLY VAL THR          
SEQRES  16 B  401  GLY CYS ALA ARG ASP GLY LYS GLY ALA LEU MET ALA GLY          
SEQRES  17 B  401  ALA PHE GLU GLU ARG ILE ALA LEU THR ILE PRO GLN GLU          
SEQRES  18 B  401  SER GLY SER GLY GLY ASP ALA CYS TRP ARG LEU SER LYS          
SEQRES  19 B  401  TYR GLU ILE ASP ASN GLY ASN GLN VAL GLN ASP ALA VAL          
SEQRES  20 B  401  GLU ILE VAL GLY GLU ASN VAL TRP PHE SER THR ASN PHE          
SEQRES  21 B  401  ASN ASN TYR VAL GLN LYS LEU PRO THR VAL PRO GLU ASP          
SEQRES  22 B  401  HIS HIS LEU LEU ALA ALA MET VAL ALA PRO ARG ALA MET          
SEQRES  23 B  401  ILE SER PHE GLU ASN THR ASP TYR LEU TRP LEU SER PRO          
SEQRES  24 B  401  MET SER SER PHE GLY CYS MET THR ALA ALA HIS THR VAL          
SEQRES  25 B  401  TRP GLN GLY LEU GLY ILE ALA ASP SER HIS GLY PHE ALA          
SEQRES  26 B  401  GLN VAL GLY GLY HIS ALA HIS CYS ALA TRP PRO SER SER          
SEQRES  27 B  401  LEU THR PRO GLN LEU ASN ALA PHE ILE ASN ARG PHE LEU          
SEQRES  28 B  401  LEU ASP GLN SER ALA THR THR ASN VAL PHE THR THR ASN          
SEQRES  29 B  401  ASN GLN PHE GLY LYS VAL GLN TRP ASN ALA ALA ASN TRP          
SEQRES  30 B  401  ILE THR TRP THR THR PRO THR LEU THR GLU ASN LEU TYR          
SEQRES  31 B  401  PHE GLN GLY VAL ASP HIS HIS HIS HIS HIS HIS                  
HET    NAG  A 501      14                                                       
HET    EDO  A 502      10                                                       
HET    GOL  A 503      14                                                       
HET    GOL  A 504      14                                                       
HET    GOL  A 505      14                                                       
HET    NAG  B 501      14                                                       
HET    GCV  B 502      23                                                       
HET    XYP  B 503      17                                                       
HET    XYP  B 504      18                                                       
HET    GOL  B 505      14                                                       
HET    GOL  B 506      14                                                       
HET    GOL  B 507      14                                                       
HET    GOL  B 508      14                                                       
HET     NA  B 509       1                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     GOL GLYCEROL                                                         
HETNAM     GCV 4-O-METHYL-ALPHA-D-GLUCURONIC ACID                               
HETNAM     XYP BETA-D-XYLOPYRANOSE                                              
HETNAM      NA SODIUM ION                                                       
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  NAG    2(C8 H15 N O6)                                               
FORMUL   4  EDO    C2 H6 O2                                                     
FORMUL   5  GOL    7(C3 H8 O3)                                                  
FORMUL   9  GCV    C7 H12 O7                                                    
FORMUL   9  XYP    2(C5 H10 O5)                                                 
FORMUL  14   NA    NA 1+                                                        
FORMUL  15  HOH   *734(H2 O)                                                    
HELIX    1 AA1 ALA A   74  GLY A   79  1                                   6    
HELIX    2 AA2 THR A  110  GLU A  129  1                                  20    
HELIX    3 AA3 SER A  206  ALA A  211  1                                   6    
HELIX    4 AA4 SER A  215  ARG A  219  5                                   5    
HELIX    5 AA5 GLY A  222  GLY A  229  1                                   8    
HELIX    6 AA6 SER A  235  MET A  253  1                                  19    
HELIX    7 AA7 THR A  254  ALA A  257  5                                   4    
HELIX    8 AA8 ALA A  270  GLU A  283  1                                  14    
HELIX    9 AA9 CYS A  301  ASN A  311  1                                  11    
HELIX   10 AB1 ASP A  317  ASN A  325  1                                   9    
HELIX   11 AB2 SER A  329  TYR A  335  5                                   7    
HELIX   12 AB3 LYS A  338  VAL A  342  5                                   5    
HELIX   13 AB4 ASP A  345  MET A  352  1                                   8    
HELIX   14 AB5 TYR A  366  LEU A  369  5                                   4    
HELIX   15 AB6 SER A  370  LEU A  388  1                                  19    
HELIX   16 AB7 ILE A  390  ASP A  392  5                                   3    
HELIX   17 AB8 PRO A  408  SER A  410  5                                   3    
HELIX   18 AB9 LEU A  411  LEU A  423  1                                  13    
HELIX   19 AC1 ASN A  445  TRP A  449  5                                   5    
HELIX   20 AC2 ALA B   74  GLY B   79  1                                   6    
HELIX   21 AC3 THR B  110  GLU B  129  1                                  20    
HELIX   22 AC4 SER B  206  ALA B  211  1                                   6    
HELIX   23 AC5 SER B  215  ARG B  219  5                                   5    
HELIX   24 AC6 GLY B  222  GLY B  229  1                                   8    
HELIX   25 AC7 SER B  235  MET B  253  1                                  19    
HELIX   26 AC8 THR B  254  ALA B  257  5                                   4    
HELIX   27 AC9 ALA B  270  GLU B  283  1                                  14    
HELIX   28 AD1 CYS B  301  ASN B  311  1                                  11    
HELIX   29 AD2 ASP B  317  ASN B  325  1                                   9    
HELIX   30 AD3 SER B  329  TYR B  335  5                                   7    
HELIX   31 AD4 LYS B  338  VAL B  342  5                                   5    
HELIX   32 AD5 ASP B  345  MET B  352  1                                   8    
HELIX   33 AD6 TYR B  366  LEU B  369  5                                   4    
HELIX   34 AD7 SER B  370  LEU B  388  1                                  19    
HELIX   35 AD8 ILE B  390  ASP B  392  5                                   3    
HELIX   36 AD9 PRO B  408  SER B  410  5                                   3    
HELIX   37 AE1 LEU B  411  LEU B  423  1                                  13    
HELIX   38 AE2 ASN B  445  TRP B  449  5                                   5    
SHEET    1 AA1 3 VAL A 139  SER A 147  0                                        
SHEET    2 AA1 3 THR A 150  GLY A 158 -1  O  THR A 152   N  SER A 145           
SHEET    3 AA1 3 THR A 164  PHE A 167 -1  O  PHE A 167   N  ILE A 155           
SHEET    1 AA210 VAL A 139  SER A 147  0                                        
SHEET    2 AA210 THR A 150  GLY A 158 -1  O  THR A 152   N  SER A 145           
SHEET    3 AA210 THR A 170  SER A 172 -1  O  ILE A 171   N  GLY A 151           
SHEET    4 AA210 ALA A 201  TYR A 205 -1  O  THR A 202   N  SER A 172           
SHEET    5 AA210 TRP A 183  TYR A 189  1  N  ALA A 188   O  LEU A 203           
SHEET    6 AA210 ILE A 259  CYS A 269  1  O  GLY A 265   N  ILE A 187           
SHEET    7 AA210 LEU A 288  GLN A 292  1  O  ILE A 290   N  VAL A 266           
SHEET    8 AA210 ALA A 357  ASN A 363  1  O  PHE A 361   N  PRO A 291           
SHEET    9 AA210 HIS A 394  VAL A 399  1  O  GLY A 395   N  MET A 358           
SHEET   10 AA210 PHE A 433  THR A 434  1  O  THR A 434   N  PHE A 396           
SHEET    1 AA3 3 VAL B 139  SER B 147  0                                        
SHEET    2 AA3 3 THR B 150  SER B 160 -1  O  THR B 152   N  SER B 145           
SHEET    3 AA3 3 GLN B 163  PHE B 167 -1  O  PHE B 167   N  ILE B 155           
SHEET    1 AA410 VAL B 139  SER B 147  0                                        
SHEET    2 AA410 THR B 150  SER B 160 -1  O  THR B 152   N  SER B 145           
SHEET    3 AA410 THR B 170  SER B 172 -1  O  ILE B 171   N  GLY B 151           
SHEET    4 AA410 ALA B 201  TYR B 205 -1  O  THR B 202   N  SER B 172           
SHEET    5 AA410 TRP B 183  TYR B 189  1  N  ALA B 188   O  LEU B 203           
SHEET    6 AA410 ILE B 259  CYS B 269  1  O  GLY B 265   N  ILE B 187           
SHEET    7 AA410 LEU B 288  GLN B 292  1  O  ILE B 290   N  VAL B 266           
SHEET    8 AA410 ALA B 357  ASN B 363  1  O  ILE B 359   N  THR B 289           
SHEET    9 AA410 HIS B 394  VAL B 399  1  O  GLY B 395   N  MET B 358           
SHEET   10 AA410 PHE B 433  THR B 434  1  O  THR B 434   N  PHE B 396           
SSBOND   1 CYS A   81    CYS A  116                          1555   1555  2.04  
SSBOND   2 CYS A  269    CYS A  405                          1555   1555  2.06  
SSBOND   3 CYS A  301    CYS A  377                          1555   1555  2.14  
SSBOND   4 CYS B   81    CYS B  116                          1555   1555  2.05  
SSBOND   5 CYS B  269    CYS B  405                          1555   1555  2.05  
SSBOND   6 CYS B  301    CYS B  377                          1555   1555  2.13  
LINK         ND2 ASN A 104                 C1  NAG A 501     1555   1555  1.45  
LINK         ND2 ASN B 104                 C1  NAG B 501     1555   1555  1.44  
LINK         O   ILE B 259                NA    NA B 509     1555   1555  2.35  
LINK         C1  GCV B 502                 O2B XYP B 503     1555   1555  1.44  
LINK         C1B XYP B 503                 O4B XYP B 504     1555   1555  1.40  
LINK         O2  GOL B 507                NA    NA B 509     1555   1555  2.49  
LINK         O3  GOL B 507                NA    NA B 509     1555   1555  2.35  
LINK        NA    NA B 509                 O   HOH B 806     1555   1555  2.35  
LINK        NA    NA B 509                 O   HOH B 812     1555   1555  2.47  
LINK        NA    NA B 509                 O   HOH B 804     1555   1555  2.44  
CISPEP   1 ALA A  354    PRO A  355          0         6.64                     
CISPEP   2 ALA B  354    PRO B  355          0         7.99                     
SITE     1 AC1  4 LYS A 274  GLN A 316  GLU A 324  TRP A 368                    
SITE     1 AC2  7 PHE A 282  GLU A 283  GLU A 284  ARG A 285                    
SITE     2 AC2  7 HOH A 653  HOH A 773  HOH A 790                               
SITE     1 AC3  8 TYR A  91  THR A 101  PHE A 102  ALA A 103                    
SITE     2 AC3  8 ARG A 117  PRO A 343  HOH A 605  HOH A 880                    
SITE     1 AC4  7 LYS A 136  PRO A 138  VAL A 139  VAL A 140                    
SITE     2 AC4  7 MET A 253  HOH A 837  MET B 253                               
SITE     1 AC5  8 PHE B 282  GLU B 283  GLU B 284  ARG B 285                    
SITE     2 AC5  8 HOH B 658  HOH B 709  HOH B 785  HOH B 792                    
SITE     1 AC6  7 TYR B  91  THR B 101  PHE B 102  ALA B 103                    
SITE     2 AC6  7 ARG B 117  PRO B 343  HOH B 605                               
SITE     1 AC7 10 GLU A 252  GLU B 252  PRO B 255  ILE B 259                    
SITE     2 AC7 10 THR B 261   NA B 509  HOH B 751  HOH B 762                    
SITE     3 AC7 10 HOH B 800  HOH B 844                                          
SITE     1 AC8  6 PRO B 413  THR B 429  THR B 430  ASN B 431                    
SITE     2 AC8  6 HOH B 753  HOH B 769                                          
SITE     1 AC9  5 ILE B 259  GOL B 507  HOH B 804  HOH B 806                    
SITE     2 AC9  5 HOH B 812                                                     
SITE     1 AD1 15 GLU A  73  GLU A  75  CYS A  81  ALA A  83                    
SITE     2 AD1 15 ILE A  84  PHE A 102  ASN A 104  THR A 106                    
SITE     3 AD1 15 HOH A 632  HOH A 635  HOH A 728  HOH A 809                    
SITE     4 AD1 15 HOH A 820  HOH A 839  ASN B  92                               
SITE     1 AD2 14 ASN A  92  GLU B  73  GLU B  75  CYS B  81                    
SITE     2 AD2 14 ALA B  83  ILE B  84  PHE B 102  ASN B 104                    
SITE     3 AD2 14 THR B 106  HOH B 625  HOH B 655  HOH B 739                    
SITE     4 AD2 14 HOH B 799  HOH B 815                                          
SITE     1 AD3 12 ALA B 270  ARG B 271  LYS B 274  GLN B 316                    
SITE     2 AD3 12 GLU B 324  TRP B 368  LEU B 369  HIS B 404                    
SITE     3 AD3 12 HOH B 667  HOH B 735  HOH B 864  HOH B 888                    
CRYST1   84.240   84.240  260.815  90.00  90.00  90.00 P 41 21 2    16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011871  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011871  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003834        0.00000                         
TER    2991      THR A 458                                                      
TER    5956      THR B 458                                                      
MASTER      557    0   14   38   26    0   29    6 6659    2  214   62          
END                                                                             

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