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Entry: 4FQX
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HEADER    IMMUNE SYSTEM                           25-JUN-12   4FQX              
TITLE     CRYSTAL STRUCTURE OF HLA-DM BOUND TO HLA-DR1                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DM ALPHA CHAIN;   
COMPND   3 CHAIN: C;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 27-225;                                       
COMPND   5 SYNONYM: MHC CLASS II ANTIGEN DMA, REALLY INTERESTING NEW GENE 6     
COMPND   6 PROTEIN;                                                             
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DM BETA CHAIN;    
COMPND  10 CHAIN: D;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 19-211;                                       
COMPND  12 SYNONYM: MHC CLASS II ANTIGEN DMB, REALLY INTERESTING NEW GENE 7     
COMPND  13 PROTEIN;                                                             
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: SYNTHETIC PEPTIDE;                                         
COMPND  17 CHAIN: E;                                                            
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 MOL_ID: 4;                                                           
COMPND  20 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DR ALPHA CHAIN;   
COMPND  21 CHAIN: A;                                                            
COMPND  22 FRAGMENT: UNP RESIDUES 26-216;                                       
COMPND  23 SYNONYM: MHC CLASS II ANTIGEN DRA;                                   
COMPND  24 ENGINEERED: YES;                                                     
COMPND  25 MOL_ID: 5;                                                           
COMPND  26 MOLECULE: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DRB1-1 BETA CHAIN;
COMPND  27 CHAIN: B;                                                            
COMPND  28 FRAGMENT: UNP RESIDUES 30-221;                                       
COMPND  29 SYNONYM: MHC CLASS II ANTIGEN DRB1*1, DR-1, DR1;                     
COMPND  30 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: DM ALPHA CHAIN, DMA, HLA CLASS II HISTOCOMPATIBILITY ANTIGEN,  
SOURCE   6 HLA-DMA, RING6;                                                      
SOURCE   7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: LEC3.2.8.1;                                
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PEE14.1;                                  
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 GENE: DM BETA CHAIN, DMB, HLA CLASS II HISTOCOMPATIBILITY ANTIGEN,   
SOURCE  17 HLA-DMB, RING7;                                                      
SOURCE  18 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  20 EXPRESSION_SYSTEM_STRAIN: LEC3.2.8.1;                                
SOURCE  21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  22 EXPRESSION_SYSTEM_PLASMID: PEE14.1;                                  
SOURCE  23 MOL_ID: 3;                                                           
SOURCE  24 SYNTHETIC: YES;                                                      
SOURCE  25 MOL_ID: 4;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  27 ORGANISM_COMMON: HUMAN;                                              
SOURCE  28 ORGANISM_TAXID: 9606;                                                
SOURCE  29 GENE: HLA-DR1 ALPHA CHAIN, HLA-DRA, HLA-DRA1, MHC CLASS II MOLECULE; 
SOURCE  30 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  31 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  32 MOL_ID: 5;                                                           
SOURCE  33 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  34 ORGANISM_COMMON: HUMAN;                                              
SOURCE  35 ORGANISM_TAXID: 9606;                                                
SOURCE  36 GENE: BETA CHAIN, HLA-DR1, HLA-DRB1, MHC CLASS II MOLECULE;          
SOURCE  37 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  38 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    IMMUNE COMPLEX, PEPTIDE LOADING, PEPTIDE EDITING, ANTIGEN             
KEYWDS   2 PRESENTATION, IMMUNE SYSTEM                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.K.SETHI,W.POS,K.W.WUCHERPFENNIG                                     
REVDAT   3   29-JUL-20 4FQX    1       COMPND REMARK SEQADV HETNAM              
REVDAT   3 2                   1       LINK   SITE   ATOM                       
REVDAT   2   15-NOV-17 4FQX    1       REMARK                                   
REVDAT   1   09-JAN-13 4FQX    0                                                
JRNL        AUTH   W.POS,D.K.SETHI,M.J.CALL,M.S.SCHULZE,A.K.ANDERS,J.PYRDOL,    
JRNL        AUTH 2 K.W.WUCHERPFENNIG                                            
JRNL        TITL   CRYSTAL STRUCTURE OF THE HLA-DM-HLA-DR1 COMPLEX DEFINES      
JRNL        TITL 2 MECHANISMS FOR RAPID PEPTIDE SELECTION.                      
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 151  1557 2012              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   23260142                                                     
JRNL        DOI    10.1016/J.CELL.2012.11.025                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8_1069                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.14                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 34135                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.194                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1742                            
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 36.1448 -  5.9424    0.94     2805   143  0.1855 0.2139        
REMARK   3     2  5.9424 -  4.7200    0.96     2717   166  0.1541 0.1946        
REMARK   3     3  4.7200 -  4.1243    0.97     2707   150  0.1455 0.1797        
REMARK   3     4  4.1243 -  3.7477    0.98     2720   142  0.1789 0.2447        
REMARK   3     5  3.7477 -  3.4793    0.98     2696   140  0.1911 0.2427        
REMARK   3     6  3.4793 -  3.2743    0.98     2748   139  0.2098 0.2544        
REMARK   3     7  3.2743 -  3.1104    0.98     2714   144  0.2335 0.2816        
REMARK   3     8  3.1104 -  2.9751    0.98     2700   144  0.2549 0.3030        
REMARK   3     9  2.9751 -  2.8606    0.98     2712   142  0.2611 0.3329        
REMARK   3    10  2.8606 -  2.7619    0.99     2674   154  0.2619 0.3394        
REMARK   3    11  2.7619 -  2.6756    0.98     2691   154  0.2630 0.3312        
REMARK   3    12  2.6756 -  2.5991    0.92     2509   124  0.2639 0.3240        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.330            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.930           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 63.91                          
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      :  0.009           6263                                  
REMARK   3   ANGLE     :  1.188           8530                                  
REMARK   3   CHIRALITY :  0.079            928                                  
REMARK   3   PLANARITY :  0.006           1109                                  
REMARK   3   DIHEDRAL  : 15.957           2252                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 18                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ( CHAIN C AND RESID 15:137 )                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.6200   8.4382 -12.9916              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7234 T22:   0.3916                                     
REMARK   3      T33:   0.5557 T12:  -0.6064                                     
REMARK   3      T13:  -0.2811 T23:   0.1957                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3078 L22:   0.2424                                     
REMARK   3      L33:   0.4352 L12:   0.2333                                     
REMARK   3      L13:  -0.0588 L23:  -0.1637                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3899 S12:   0.1404 S13:   0.2782                       
REMARK   3      S21:   0.0321 S22:  -0.2790 S23:  -0.2093                       
REMARK   3      S31:  -0.9460 S32:   0.5463 S33:  -0.3460                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: ( CHAIN C AND RESID 138:147 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.2837  -7.8231 -27.2399              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4759 T22:   0.9878                                     
REMARK   3      T33:   0.9446 T12:  -0.2702                                     
REMARK   3      T13:   0.0715 T23:   0.0277                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0175 L22:   0.0052                                     
REMARK   3      L33:  -0.0019 L12:  -0.0025                                     
REMARK   3      L13:  -0.0124 L23:   0.0055                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0551 S12:   0.1532 S13:  -0.0389                       
REMARK   3      S21:  -0.0194 S22:   0.0152 S23:   0.0212                       
REMARK   3      S31:   0.0291 S32:   0.1059 S33:   0.0026                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: ( CHAIN C AND RESID 148:200 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.6157  -4.9859 -23.9651              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4184 T22:   0.5326                                     
REMARK   3      T33:   0.4144 T12:  -0.1360                                     
REMARK   3      T13:  -0.0055 T23:   0.1140                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1097 L22:   0.0735                                     
REMARK   3      L33:   0.3766 L12:  -0.0718                                     
REMARK   3      L13:   0.0804 L23:   0.0224                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1694 S12:   0.2642 S13:   0.1687                       
REMARK   3      S21:   0.0270 S22:  -0.1123 S23:  -0.2596                       
REMARK   3      S31:  -0.4956 S32:   0.2481 S33:  -0.2086                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: ( CHAIN D AND RESID 3:133 )                            
REMARK   3    ORIGIN FOR THE GROUP (A): -20.1527  14.2929 -13.2402              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1966 T22:   0.1094                                     
REMARK   3      T33:   0.5380 T12:   0.0147                                     
REMARK   3      T13:  -0.3621 T23:   0.1129                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3137 L22:   0.4312                                     
REMARK   3      L33:   0.2542 L12:   0.1030                                     
REMARK   3      L13:  -0.2064 L23:  -0.2320                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3348 S12:   0.1020 S13:   0.2563                       
REMARK   3      S21:   0.1428 S22:  -0.0685 S23:   0.0595                       
REMARK   3      S31:  -0.8394 S32:  -0.2896 S33:  -0.1659                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: ( CHAIN D AND RESID 134:157 )                          
REMARK   3    ORIGIN FOR THE GROUP (A): -27.4693   3.6563 -30.9583              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6531 T22:   0.4677                                     
REMARK   3      T33:   0.5298 T12:  -0.0558                                     
REMARK   3      T13:  -0.1470 T23:   0.1089                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0320 L22:   0.0453                                     
REMARK   3      L33:   0.0209 L12:  -0.0496                                     
REMARK   3      L13:  -0.0337 L23:   0.0403                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1294 S12:  -0.0058 S13:  -0.0485                       
REMARK   3      S21:  -0.1113 S22:  -0.2038 S23:   0.2393                       
REMARK   3      S31:  -0.2445 S32:   0.0920 S33:   0.0002                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: ( CHAIN D AND RESID 158:193 )                          
REMARK   3    ORIGIN FOR THE GROUP (A): -30.6600   2.0788 -43.6638              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9649 T22:   0.4445                                     
REMARK   3      T33:   0.4366 T12:  -0.1889                                     
REMARK   3      T13:  -0.2859 T23:   0.1994                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5788 L22:   0.0837                                     
REMARK   3      L33:   0.3230 L12:  -0.1952                                     
REMARK   3      L13:  -0.4418 L23:   0.1519                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3924 S12:   0.3025 S13:  -0.0355                       
REMARK   3      S21:  -0.0293 S22:  -0.3865 S23:  -0.0619                       
REMARK   3      S31:  -0.2515 S32:  -0.5354 S33:  -0.1850                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: ( CHAIN E AND RESID 87:93 )                            
REMARK   3    ORIGIN FOR THE GROUP (A): -26.6457 -11.6481  23.1359              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5087 T22:   0.5078                                     
REMARK   3      T33:   0.6470 T12:  -0.0387                                     
REMARK   3      T13:  -0.0301 T23:  -0.1008                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0043 L22:   0.0149                                     
REMARK   3      L33:   0.0075 L12:   0.0001                                     
REMARK   3      L13:   0.0062 L23:  -0.0036                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1870 S12:  -0.0532 S13:   0.1357                       
REMARK   3      S21:  -0.0193 S22:  -0.0328 S23:  -0.0876                       
REMARK   3      S31:  -0.0283 S32:  -0.0911 S33:   0.0006                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 2:45 )                             
REMARK   3    ORIGIN FOR THE GROUP (A): -23.3604 -12.2209   2.4233              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2640 T22:   0.3435                                     
REMARK   3      T33:   0.3424 T12:   0.0074                                     
REMARK   3      T13:  -0.0269 T23:   0.0041                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0019 L22:   0.0434                                     
REMARK   3      L33:   0.0886 L12:  -0.0124                                     
REMARK   3      L13:   0.0086 L23:  -0.0140                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1127 S12:  -0.1049 S13:   0.0480                       
REMARK   3      S21:   0.1202 S22:  -0.0153 S23:  -0.0043                       
REMARK   3      S31:  -0.2684 S32:   0.0467 S33:   0.0000                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 46:76 )                            
REMARK   3    ORIGIN FOR THE GROUP (A): -21.8755  -9.4083  10.2287              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4703 T22:   0.4307                                     
REMARK   3      T33:   0.3632 T12:   0.0051                                     
REMARK   3      T13:  -0.0550 T23:  -0.0149                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0691 L22:   0.0267                                     
REMARK   3      L33:   0.0231 L12:   0.0026                                     
REMARK   3      L13:  -0.0228 L23:   0.0180                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0491 S12:  -0.1471 S13:   0.1605                       
REMARK   3      S21:   0.0017 S22:  -0.0232 S23:   0.1635                       
REMARK   3      S31:  -0.4029 S32:  -0.0065 S33:  -0.0000                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: ( CHAIN A AND RESID 77:101 )                           
REMARK   3    ORIGIN FOR THE GROUP (A): -21.0661 -26.9340  -6.9073              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3118 T22:   0.3416                                     
REMARK   3      T33:   0.3466 T12:   0.0024                                     
REMARK   3      T13:  -0.0058 T23:   0.0154                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1797 L22:   0.0299                                     
REMARK   3      L33:   0.0451 L12:   0.0538                                     
REMARK   3      L13:  -0.0153 L23:   0.0365                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0770 S12:   0.1986 S13:  -0.0386                       
REMARK   3      S21:  -0.0425 S22:  -0.0376 S23:  -0.0087                       
REMARK   3      S31:   0.0664 S32:   0.0286 S33:   0.0001                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: ( CHAIN A AND RESID 102:154 )                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.3665 -22.5874  -8.1483              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2496 T22:   0.3337                                     
REMARK   3      T33:   0.3221 T12:  -0.0086                                     
REMARK   3      T13:  -0.0091 T23:   0.0132                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0606 L22:   0.0625                                     
REMARK   3      L33:   0.0671 L12:  -0.0613                                     
REMARK   3      L13:   0.0432 L23:  -0.0116                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1008 S12:   0.2278 S13:  -0.0013                       
REMARK   3      S21:  -0.0189 S22:  -0.0555 S23:   0.0935                       
REMARK   3      S31:  -0.1125 S32:  -0.1026 S33:   0.0000                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: ( CHAIN A AND RESID 155:181 )                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.8362 -31.3782 -13.7832              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4112 T22:   0.4241                                     
REMARK   3      T33:   0.4473 T12:   0.0650                                     
REMARK   3      T13:   0.0069 T23:   0.0245                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0722 L22:   0.1059                                     
REMARK   3      L33:   0.0129 L12:   0.0057                                     
REMARK   3      L13:   0.0265 L23:   0.0053                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0753 S12:   0.0891 S13:  -0.1977                       
REMARK   3      S21:   0.0752 S22:  -0.1009 S23:  -0.0054                       
REMARK   3      S31:   0.3019 S32:   0.1355 S33:  -0.0003                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: ( CHAIN B AND RESID -5:17 )                            
REMARK   3    ORIGIN FOR THE GROUP (A): -21.0410 -25.0367  10.7711              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2198 T22:   0.3927                                     
REMARK   3      T33:   0.2835 T12:   0.0607                                     
REMARK   3      T13:  -0.0277 T23:   0.0452                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0169 L22:   0.0040                                     
REMARK   3      L33:   0.0438 L12:  -0.0218                                     
REMARK   3      L13:  -0.0118 L23:  -0.0511                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1264 S12:  -0.0054 S13:   0.1471                       
REMARK   3      S21:  -0.1808 S22:  -0.0320 S23:   0.0634                       
REMARK   3      S31:   0.0864 S32:  -0.1138 S33:   0.0003                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: ( CHAIN B AND RESID 18:84 )                            
REMARK   3    ORIGIN FOR THE GROUP (A): -37.7612 -12.4817  14.4692              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2653 T22:   0.4028                                     
REMARK   3      T33:   0.3886 T12:   0.1386                                     
REMARK   3      T13:   0.0188 T23:  -0.0015                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1372 L22:   0.1989                                     
REMARK   3      L33:   0.1419 L12:   0.1184                                     
REMARK   3      L13:   0.0647 L23:   0.0384                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1022 S12:  -0.0536 S13:   0.1929                       
REMARK   3      S21:   0.1788 S22:  -0.0567 S23:  -0.0772                       
REMARK   3      S31:  -0.1003 S32:  -0.3849 S33:   0.0041                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: ( CHAIN B AND RESID 85:97 )                            
REMARK   3    ORIGIN FOR THE GROUP (A): -34.0170  -4.6354 -12.0245              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2624 T22:   0.2274                                     
REMARK   3      T33:   0.5071 T12:   0.0616                                     
REMARK   3      T13:  -0.0035 T23:   0.1127                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2695 L22:   0.1374                                     
REMARK   3      L33:   0.1088 L12:   0.1834                                     
REMARK   3      L13:  -0.1693 L23:  -0.1181                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1417 S12:   0.2438 S13:  -0.0714                       
REMARK   3      S21:  -0.2025 S22:  -0.0448 S23:  -0.0276                       
REMARK   3      S31:   0.0042 S32:  -0.0974 S33:  -0.0118                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: ( CHAIN B AND RESID 98:144 )                           
REMARK   3    ORIGIN FOR THE GROUP (A): -38.4544 -23.5370 -26.0701              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2540 T22:   0.3079                                     
REMARK   3      T33:   0.2637 T12:  -0.0666                                     
REMARK   3      T13:  -0.0257 T23:   0.0085                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0679 L22:   0.0820                                     
REMARK   3      L33:   0.0611 L12:   0.0089                                     
REMARK   3      L13:   0.0174 L23:  -0.0736                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2140 S12:   0.1602 S13:   0.1141                       
REMARK   3      S21:   0.0103 S22:   0.1641 S23:   0.0296                       
REMARK   3      S31:  -0.1654 S32:  -0.0466 S33:   0.0000                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: ( CHAIN B AND RESID 145:170 )                          
REMARK   3    ORIGIN FOR THE GROUP (A): -33.9992 -24.8818 -23.4770              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4172 T22:   0.3090                                     
REMARK   3      T33:   0.3803 T12:  -0.0449                                     
REMARK   3      T13:  -0.0052 T23:   0.0170                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1290 L22:   0.1088                                     
REMARK   3      L33:   0.0781 L12:  -0.0556                                     
REMARK   3      L13:  -0.0854 L23:  -0.0454                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0297 S12:  -0.0419 S13:   0.0473                       
REMARK   3      S21:  -0.2784 S22:   0.0948 S23:  -0.1856                       
REMARK   3      S31:   0.0853 S32:   0.0644 S33:   0.0000                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: ( CHAIN B AND RESID 171:190 )                          
REMARK   3    ORIGIN FOR THE GROUP (A): -39.5034 -17.5744 -30.1457              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4012 T22:   0.4736                                     
REMARK   3      T33:   0.4154 T12:  -0.0083                                     
REMARK   3      T13:  -0.0498 T23:   0.0656                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0103 L22:   0.0415                                     
REMARK   3      L33:   0.0386 L12:  -0.0004                                     
REMARK   3      L13:   0.0325 L23:  -0.0251                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1842 S12:   0.4443 S13:   0.1161                       
REMARK   3      S21:  -0.2934 S22:  -0.0445 S23:   0.1303                       
REMARK   3      S31:   0.0918 S32:  -0.0992 S33:   0.0000                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4FQX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUL-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000073243.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-APR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34280                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.53300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.26                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.02                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 5.5, VAPOR DIFFUSION, HANGING DROP,   
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       33.09500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       69.20800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       60.82450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       69.20800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.09500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       60.82450            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14950 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 34790 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -68.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E, A, B, F                      
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5290 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18940 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, A, B, F                            
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     VAL C     1                                                      
REMARK 465     PRO C     2                                                      
REMARK 465     GLU C     3                                                      
REMARK 465     ALA C     4                                                      
REMARK 465     PRO C     5                                                      
REMARK 465     THR C     6                                                      
REMARK 465     PRO C     7                                                      
REMARK 465     MET C     8                                                      
REMARK 465     TRP C     9                                                      
REMARK 465     PRO C    10                                                      
REMARK 465     ASP C    11                                                      
REMARK 465     ASP C    12                                                      
REMARK 465     LEU C    13                                                      
REMARK 465     GLN C    14                                                      
REMARK 465     VAL C   201                                                      
REMARK 465     PRO C   202                                                      
REMARK 465     ARG C   203                                                      
REMARK 465     GLY D     1                                                      
REMARK 465     GLY D     2                                                      
REMARK 465     GLY D   194                                                      
REMARK 465     CYS D   195                                                      
REMARK 465     LEU D   196                                                      
REMARK 465     VAL D   197                                                      
REMARK 465     PRO D   198                                                      
REMARK 465     ARG D   199                                                      
REMARK 465     GLY E    84                                                      
REMARK 465     LYS E    85                                                      
REMARK 465     GLN E    86                                                      
REMARK 465     LYS E    94                                                      
REMARK 465     ILE A     1                                                      
REMARK 465     ALA A   182                                                      
REMARK 465     PRO A   183                                                      
REMARK 465     SER A   184                                                      
REMARK 465     PRO A   185                                                      
REMARK 465     LEU A   186                                                      
REMARK 465     PRO A   187                                                      
REMARK 465     GLU A   188                                                      
REMARK 465     THR A   189                                                      
REMARK 465     THR A   190                                                      
REMARK 465     GLU A   191                                                      
REMARK 465     LYS B   105                                                      
REMARK 465     THR B   106                                                      
REMARK 465     GLN B   107                                                      
REMARK 465     PRO B   108                                                      
REMARK 465     LEU B   109                                                      
REMARK 465     GLN B   110                                                      
REMARK 465     HIS B   111                                                      
REMARK 465     HIS B   112                                                      
REMARK 465     ASN B   113                                                      
REMARK 465     ARG B   191                                                      
REMARK 465     SER B   192                                                      
REMARK 465     SER B   193                                                      
REMARK 465     GLY B   194                                                      
REMARK 465     GLY B   195                                                      
REMARK 465     GLY B   196                                                      
REMARK 465     SER B   197                                                      
REMARK 465     LEU B   198                                                      
REMARK 465     PRO B   199                                                      
REMARK 465     ALA B   200                                                      
REMARK 465     THR B   201                                                      
REMARK 465     GLY B   202                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     PHE C 145    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU A 141    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  65    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH1  ARG D   110     OE2  GLU B   187              2.10            
REMARK 500   ND2  ASN A   118     O5   NAG F     1              2.17            
REMARK 500   O    GLN D    70     ND2  ASN D    74              2.18            
REMARK 500   OE2  GLU C   181     NH1  ARG C   184              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN C  50       36.32     38.27                                   
REMARK 500    PHE C 127      117.43   -175.36                                   
REMARK 500    GLU C 143      -64.48    -25.62                                   
REMARK 500    ASP C 183       19.55   -153.13                                   
REMARK 500    LEU D  13     -159.76    -86.51                                   
REMARK 500    ASP D  21      173.19    177.79                                   
REMARK 500    LYS D  30       -0.91     68.70                                   
REMARK 500    GLN D  84      -46.28   -140.25                                   
REMARK 500    PRO D 124     -170.55    -69.49                                   
REMARK 500    HIS D 145       74.08     44.25                                   
REMARK 500    ASP B   2       75.64     64.96                                   
REMARK 500    ASN B  19       76.09     48.29                                   
REMARK 500    ASN B  33     -101.47     51.00                                   
REMARK 500    TYR B  78      -63.50   -105.68                                   
REMARK 500    THR B  90     -151.03    -71.22                                   
REMARK 500    PRO B 165      150.35    -48.11                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  4FQX C    1   199  UNP    P28067   DMA_HUMAN       27    225             
DBREF  4FQX D    1   193  UNP    P28068   DMB_HUMAN       19    211             
DBREF  4FQX A    1   191  UNP    P01903   DRA_HUMAN       26    216             
DBREF  4FQX B    1   192  UNP    P04229   2B11_HUMAN      30    221             
DBREF  4FQX E   84    94  PDB    4FQX     4FQX            84     94             
SEQADV 4FQX GLN C  136  UNP  P28067    HIS   162 VARIANT                        
SEQADV 4FQX HIS C  137  UNP  P28067    ASP   163 VARIANT                        
SEQADV 4FQX ASP C  165  UNP  P28067    ASN   191 ENGINEERED MUTATION            
SEQADV 4FQX LEU C  200  UNP  P28067              EXPRESSION TAG                 
SEQADV 4FQX VAL C  201  UNP  P28067              EXPRESSION TAG                 
SEQADV 4FQX PRO C  202  UNP  P28067              EXPRESSION TAG                 
SEQADV 4FQX ARG C  203  UNP  P28067              EXPRESSION TAG                 
SEQADV 4FQX SER D   46  UNP  P28068    CYS    64 ENGINEERED MUTATION            
SEQADV 4FQX ASP D   92  UNP  P28068    ASN   110 ENGINEERED MUTATION            
SEQADV 4FQX GLY D  194  UNP  P28068              EXPRESSION TAG                 
SEQADV 4FQX CYS D  195  UNP  P28068              EXPRESSION TAG                 
SEQADV 4FQX LEU D  196  UNP  P28068              EXPRESSION TAG                 
SEQADV 4FQX VAL D  197  UNP  P28068              EXPRESSION TAG                 
SEQADV 4FQX PRO D  198  UNP  P28068              EXPRESSION TAG                 
SEQADV 4FQX ARG D  199  UNP  P28068              EXPRESSION TAG                 
SEQADV 4FQX CYS A   65  UNP  P01903    VAL    90 ENGINEERED MUTATION            
SEQADV 4FQX VAL B   -5  UNP  P04229              EXPRESSION TAG                 
SEQADV 4FQX LEU B   -4  UNP  P04229              EXPRESSION TAG                 
SEQADV 4FQX PHE B   -3  UNP  P04229              EXPRESSION TAG                 
SEQADV 4FQX GLN B   -2  UNP  P04229              EXPRESSION TAG                 
SEQADV 4FQX GLY B   -1  UNP  P04229              EXPRESSION TAG                 
SEQADV 4FQX PRO B    0  UNP  P04229              EXPRESSION TAG                 
SEQADV 4FQX SER B   30  UNP  P04229    CYS    59 ENGINEERED MUTATION            
SEQADV 4FQX SER B  193  UNP  P04229              EXPRESSION TAG                 
SEQADV 4FQX GLY B  194  UNP  P04229              EXPRESSION TAG                 
SEQADV 4FQX GLY B  195  UNP  P04229              EXPRESSION TAG                 
SEQADV 4FQX GLY B  196  UNP  P04229              EXPRESSION TAG                 
SEQADV 4FQX SER B  197  UNP  P04229              EXPRESSION TAG                 
SEQADV 4FQX LEU B  198  UNP  P04229              EXPRESSION TAG                 
SEQADV 4FQX PRO B  199  UNP  P04229              EXPRESSION TAG                 
SEQADV 4FQX ALA B  200  UNP  P04229              EXPRESSION TAG                 
SEQADV 4FQX THR B  201  UNP  P04229              EXPRESSION TAG                 
SEQADV 4FQX GLY B  202  UNP  P04229              EXPRESSION TAG                 
SEQRES   1 C  203  VAL PRO GLU ALA PRO THR PRO MET TRP PRO ASP ASP LEU          
SEQRES   2 C  203  GLN ASN HIS THR PHE LEU HIS THR VAL TYR CYS GLN ASP          
SEQRES   3 C  203  GLY SER PRO SER VAL GLY LEU SER GLU ALA TYR ASP GLU          
SEQRES   4 C  203  ASP GLN LEU PHE PHE PHE ASP PHE SER GLN ASN THR ARG          
SEQRES   5 C  203  VAL PRO ARG LEU PRO GLU PHE ALA ASP TRP ALA GLN GLU          
SEQRES   6 C  203  GLN GLY ASP ALA PRO ALA ILE LEU PHE ASP LYS GLU PHE          
SEQRES   7 C  203  CYS GLU TRP MET ILE GLN GLN ILE GLY PRO LYS LEU ASP          
SEQRES   8 C  203  GLY LYS ILE PRO VAL SER ARG GLY PHE PRO ILE ALA GLU          
SEQRES   9 C  203  VAL PHE THR LEU LYS PRO LEU GLU PHE GLY LYS PRO ASN          
SEQRES  10 C  203  THR LEU VAL CYS PHE VAL SER ASN LEU PHE PRO PRO MET          
SEQRES  11 C  203  LEU THR VAL ASN TRP GLN HIS HIS SER VAL PRO VAL GLU          
SEQRES  12 C  203  GLY PHE GLY PRO THR PHE VAL SER ALA VAL ASP GLY LEU          
SEQRES  13 C  203  SER PHE GLN ALA PHE SER TYR LEU ASP PHE THR PRO GLU          
SEQRES  14 C  203  PRO SER ASP ILE PHE SER CYS ILE VAL THR HIS GLU ILE          
SEQRES  15 C  203  ASP ARG TYR THR ALA ILE ALA TYR TRP VAL PRO ARG ASN          
SEQRES  16 C  203  ALA LEU PRO SER LEU VAL PRO ARG                              
SEQRES   1 D  199  GLY GLY PHE VAL ALA HIS VAL GLU SER THR CYS LEU LEU          
SEQRES   2 D  199  ASP ASP ALA GLY THR PRO LYS ASP PHE THR TYR CYS ILE          
SEQRES   3 D  199  SER PHE ASN LYS ASP LEU LEU THR CYS TRP ASP PRO GLU          
SEQRES   4 D  199  GLU ASN LYS MET ALA PRO SER GLU PHE GLY VAL LEU ASN          
SEQRES   5 D  199  SER LEU ALA ASN VAL LEU SER GLN HIS LEU ASN GLN LYS          
SEQRES   6 D  199  ASP THR LEU MET GLN ARG LEU ARG ASN GLY LEU GLN ASN          
SEQRES   7 D  199  CYS ALA THR HIS THR GLN PRO PHE TRP GLY SER LEU THR          
SEQRES   8 D  199  ASP ARG THR ARG PRO PRO SER VAL GLN VAL ALA LYS THR          
SEQRES   9 D  199  THR PRO PHE ASN THR ARG GLU PRO VAL MET LEU ALA CYS          
SEQRES  10 D  199  TYR VAL TRP GLY PHE TYR PRO ALA GLU VAL THR ILE THR          
SEQRES  11 D  199  TRP ARG LYS ASN GLY LYS LEU VAL MET PRO HIS SER SER          
SEQRES  12 D  199  ALA HIS LYS THR ALA GLN PRO ASN GLY ASP TRP THR TYR          
SEQRES  13 D  199  GLN THR LEU SER HIS LEU ALA LEU THR PRO SER TYR GLY          
SEQRES  14 D  199  ASP THR TYR THR CYS VAL VAL GLU HIS ILE GLY ALA PRO          
SEQRES  15 D  199  GLU PRO ILE LEU ARG ASP TRP THR PRO GLY LEU GLY CYS          
SEQRES  16 D  199  LEU VAL PRO ARG                                              
SEQRES   1 E   11  GLY LYS GLN ASN CYS LEU LYS LEU ALA THR LYS                  
SEQRES   1 A  191  ILE LYS GLU GLU HIS VAL ILE ILE GLN ALA GLU PHE TYR          
SEQRES   2 A  191  LEU ASN PRO ASP GLN SER GLY GLU PHE MET PHE ASP PHE          
SEQRES   3 A  191  ASP GLY ASP GLU ILE PHE HIS VAL ASP MET ALA LYS LYS          
SEQRES   4 A  191  GLU THR VAL TRP ARG LEU GLU GLU PHE GLY ARG PHE ALA          
SEQRES   5 A  191  SER PHE GLU ALA GLN GLY ALA LEU ALA ASN ILE ALA CYS          
SEQRES   6 A  191  ASP LYS ALA ASN LEU GLU ILE MET THR LYS ARG SER ASN          
SEQRES   7 A  191  TYR THR PRO ILE THR ASN VAL PRO PRO GLU VAL THR VAL          
SEQRES   8 A  191  LEU THR ASN SER PRO VAL GLU LEU ARG GLU PRO ASN VAL          
SEQRES   9 A  191  LEU ILE CYS PHE ILE ASP LYS PHE THR PRO PRO VAL VAL          
SEQRES  10 A  191  ASN VAL THR TRP LEU ARG ASN GLY LYS PRO VAL THR THR          
SEQRES  11 A  191  GLY VAL SER GLU THR VAL PHE LEU PRO ARG GLU ASP HIS          
SEQRES  12 A  191  LEU PHE ARG LYS PHE HIS TYR LEU PRO PHE LEU PRO SER          
SEQRES  13 A  191  THR GLU ASP VAL TYR ASP CYS ARG VAL GLU HIS TRP GLY          
SEQRES  14 A  191  LEU ASP GLU PRO LEU LEU LYS HIS TRP GLU PHE ASP ALA          
SEQRES  15 A  191  PRO SER PRO LEU PRO GLU THR THR GLU                          
SEQRES   1 B  208  VAL LEU PHE GLN GLY PRO GLY ASP THR ARG PRO ARG PHE          
SEQRES   2 B  208  LEU TRP GLN LEU LYS PHE GLU CYS HIS PHE PHE ASN GLY          
SEQRES   3 B  208  THR GLU ARG VAL ARG LEU LEU GLU ARG SER ILE TYR ASN          
SEQRES   4 B  208  GLN GLU GLU SER VAL ARG PHE ASP SER ASP VAL GLY GLU          
SEQRES   5 B  208  TYR ARG ALA VAL THR GLU LEU GLY ARG PRO ASP ALA GLU          
SEQRES   6 B  208  TYR TRP ASN SER GLN LYS ASP LEU LEU GLU GLN ARG ARG          
SEQRES   7 B  208  ALA ALA VAL ASP THR TYR CYS ARG HIS ASN TYR GLY VAL          
SEQRES   8 B  208  GLY GLU SER PHE THR VAL GLN ARG ARG VAL GLU PRO LYS          
SEQRES   9 B  208  VAL THR VAL TYR PRO SER LYS THR GLN PRO LEU GLN HIS          
SEQRES  10 B  208  HIS ASN LEU LEU VAL CYS SER VAL SER GLY PHE TYR PRO          
SEQRES  11 B  208  GLY SER ILE GLU VAL ARG TRP PHE ARG ASN GLY GLN GLU          
SEQRES  12 B  208  GLU LYS ALA GLY VAL VAL SER THR GLY LEU ILE GLN ASN          
SEQRES  13 B  208  GLY ASP TRP THR PHE GLN THR LEU VAL MET LEU GLU THR          
SEQRES  14 B  208  VAL PRO ARG SER GLY GLU VAL TYR THR CYS GLN VAL GLU          
SEQRES  15 B  208  HIS PRO SER VAL THR SER PRO LEU THR VAL GLU TRP ARG          
SEQRES  16 B  208  ALA ARG SER SER GLY GLY GLY SER LEU PRO ALA THR GLY          
MODRES 4FQX ASN A  118  ASN  GLYCOSYLATION SITE                                 
HET    NAG  F   1      14                                                       
HET    NAG  F   2      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
FORMUL   6  NAG    2(C8 H15 N O6)                                               
FORMUL   7  HOH   *124(H2 O)                                                    
HELIX    1   1 LEU C   56  GLU C   65  5                                  10    
HELIX    2   2 ASP C   68  ASP C   91  1                                  24    
HELIX    3   3 LEU D   51  ASN D   63  1                                  13    
HELIX    4   4 LYS D   65  GLN D   70  1                                   6    
HELIX    5   5 ASN D   74  THR D   83  1                                  10    
HELIX    6   6 SER D   89  ARG D   93  5                                   5    
HELIX    7   7 LEU A   45  GLU A   47  5                                   3    
HELIX    8   8 PHE A   48  ALA A   56  1                                   9    
HELIX    9   9 GLY A   58  SER A   77  1                                  20    
HELIX   10  10 THR B   51  LEU B   53  5                                   3    
HELIX   11  11 GLY B   54  SER B   63  1                                  10    
HELIX   12  12 GLN B   64  ALA B   73  1                                  10    
HELIX   13  13 ALA B   73  TYR B   78  1                                   6    
HELIX   14  14 TYR B   78  VAL B   85  1                                   8    
SHEET    1   A 8 THR C  51  PRO C  54  0                                        
SHEET    2   A 8 ASP C  40  ASP C  46 -1  N  ASP C  46   O  THR C  51           
SHEET    3   A 8 VAL C  31  TYR C  37 -1  N  GLU C  35   O  LEU C  42           
SHEET    4   A 8 PHE C  18  GLN C  25 -1  N  TYR C  23   O  GLY C  32           
SHEET    5   A 8 VAL D   4  CYS D  11 -1  O  VAL D   7   N  VAL C  22           
SHEET    6   A 8 PHE D  22  PHE D  28 -1  O  CYS D  25   N  GLU D   8           
SHEET    7   A 8 ASP D  31  ASP D  37 -1  O  TRP D  36   N  TYR D  24           
SHEET    8   A 8 LYS D  42  PRO D  45 -1  O  ALA D  44   N  CYS D  35           
SHEET    1   B 9 VAL C  96  ARG C  98  0                                        
SHEET    2   B 9 GLU A  40  TRP A  43  1  O  THR A  41   N  ARG C  98           
SHEET    3   B 9 ASP A  29  ASP A  35 -1  N  HIS A  33   O  VAL A  42           
SHEET    4   B 9 SER A  19  PHE A  26 -1  N  PHE A  26   O  ASP A  29           
SHEET    5   B 9 HIS A   5  ASN A  15 -1  N  LEU A  14   O  SER A  19           
SHEET    6   B 9 PHE B   7  PHE B  18 -1  O  CYS B  15   N  ILE A   7           
SHEET    7   B 9 ARG B  23  TYR B  32 -1  O  ARG B  23   N  PHE B  18           
SHEET    8   B 9 GLU B  35  ASP B  41 -1  O  GLU B  35   N  TYR B  32           
SHEET    9   B 9 TYR B  47  ALA B  49 -1  O  ARG B  48   N  ARG B  39           
SHEET    1   C 4 ILE C 102  THR C 107  0                                        
SHEET    2   C 4 ASN C 117  LEU C 126 -1  O  SER C 124   N  ILE C 102           
SHEET    3   C 4 SER C 157  PHE C 166 -1  O  ALA C 160   N  VAL C 123           
SHEET    4   C 4 THR C 148  VAL C 153 -1  N  SER C 151   O  GLN C 159           
SHEET    1   D 4 VAL C 140  PRO C 141  0                                        
SHEET    2   D 4 LEU C 131  HIS C 137 -1  N  HIS C 137   O  VAL C 140           
SHEET    3   D 4 PHE C 174  HIS C 180 -1  O  THR C 179   N  THR C 132           
SHEET    4   D 4 THR C 186  TRP C 191 -1  O  ALA C 187   N  VAL C 178           
SHEET    1   E 4 SER D  98  THR D 104  0                                        
SHEET    2   E 4 VAL D 113  PHE D 122 -1  O  ALA D 116   N  ALA D 102           
SHEET    3   E 4 TYR D 156  LEU D 164 -1  O  SER D 160   N  CYS D 117           
SHEET    4   E 4 GLN D 149  PRO D 150 -1  N  GLN D 149   O  GLN D 157           
SHEET    1   F 4 LYS D 136  VAL D 138  0                                        
SHEET    2   F 4 THR D 128  LYS D 133 -1  N  LYS D 133   O  LYS D 136           
SHEET    3   F 4 TYR D 172  GLU D 177 -1  O  GLU D 177   N  THR D 128           
SHEET    4   F 4 ILE D 185  TRP D 189 -1  O  ARG D 187   N  CYS D 174           
SHEET    1   G 4 GLU A  88  THR A  93  0                                        
SHEET    2   G 4 ASN A 103  PHE A 112 -1  O  ASP A 110   N  GLU A  88           
SHEET    3   G 4 PHE A 145  PHE A 153 -1  O  PHE A 153   N  ASN A 103           
SHEET    4   G 4 SER A 133  GLU A 134 -1  N  SER A 133   O  TYR A 150           
SHEET    1   H 4 GLU A  88  THR A  93  0                                        
SHEET    2   H 4 ASN A 103  PHE A 112 -1  O  ASP A 110   N  GLU A  88           
SHEET    3   H 4 PHE A 145  PHE A 153 -1  O  PHE A 153   N  ASN A 103           
SHEET    4   H 4 LEU A 138  PRO A 139 -1  N  LEU A 138   O  ARG A 146           
SHEET    1   I 4 LYS A 126  PRO A 127  0                                        
SHEET    2   I 4 ASN A 118  ARG A 123 -1  N  ARG A 123   O  LYS A 126           
SHEET    3   I 4 VAL A 160  GLU A 166 -1  O  ASP A 162   N  LEU A 122           
SHEET    4   I 4 LEU A 174  GLU A 179 -1  O  TRP A 178   N  TYR A 161           
SHEET    1   J 4 LYS B  98  TYR B 102  0                                        
SHEET    2   J 4 LEU B 115  PHE B 122 -1  O  VAL B 116   N  TYR B 102           
SHEET    3   J 4 PHE B 155  LEU B 161 -1  O  LEU B 161   N  LEU B 115           
SHEET    4   J 4 VAL B 142  SER B 144 -1  N  VAL B 143   O  MET B 160           
SHEET    1   K 4 LYS B  98  TYR B 102  0                                        
SHEET    2   K 4 LEU B 115  PHE B 122 -1  O  VAL B 116   N  TYR B 102           
SHEET    3   K 4 PHE B 155  LEU B 161 -1  O  LEU B 161   N  LEU B 115           
SHEET    4   K 4 ILE B 148  GLN B 149 -1  N  ILE B 148   O  GLN B 156           
SHEET    1   L 4 GLN B 136  GLU B 137  0                                        
SHEET    2   L 4 GLU B 128  ARG B 133 -1  N  ARG B 133   O  GLN B 136           
SHEET    3   L 4 TYR B 171  GLU B 176 -1  O  GLN B 174   N  ARG B 130           
SHEET    4   L 4 LEU B 184  TRP B 188 -1  O  LEU B 184   N  VAL B 175           
SSBOND   1 CYS C   24    CYS C   79                          1555   1555  2.04  
SSBOND   2 CYS C  121    CYS C  176                          1555   1555  2.03  
SSBOND   3 CYS D   11    CYS D   79                          1555   1555  2.03  
SSBOND   4 CYS D   25    CYS D   35                          1555   1555  2.04  
SSBOND   5 CYS D  117    CYS D  174                          1555   1555  2.02  
SSBOND   6 CYS E   88    CYS A   65                          1555   1555  2.04  
SSBOND   7 CYS A  107    CYS A  163                          1555   1555  2.04  
SSBOND   8 CYS B   15    CYS B   79                          1555   1555  2.09  
SSBOND   9 CYS B  117    CYS B  173                          1555   1555  2.03  
LINK         ND2 ASN A 118                 C1  NAG F   1     1555   1555  1.45  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.46  
CISPEP   1 SER C   28    PRO C   29          0         0.48                     
CISPEP   2 PHE C  127    PRO C  128          0         0.16                     
CISPEP   3 TYR D  123    PRO D  124          0        -0.53                     
CISPEP   4 ASN A   15    PRO A   16          0         3.46                     
CISPEP   5 THR A  113    PRO A  114          0        -4.02                     
CISPEP   6 TYR B  123    PRO B  124          0         3.04                     
CRYST1   66.190  121.649  138.416  90.00  90.00  90.00 P 21 21 21    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      0.015108  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008220  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007225        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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