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Database: PDB
Entry: 5B83
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HEADER    SIGNALING PROTEIN                       12-JUN-16   5B83              
TITLE     CRYSTAL STRUCTURE OF OPTINEURIN UBAN IN COMPLEX WITH LINEAR UBIQUITIN 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TETRA UBIQUITIN;                                           
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: OPTINEURIN;                                                
COMPND   7 CHAIN: B, C, E, F;                                                   
COMPND   8 FRAGMENT: UNP RESIDUES 416-510;                                      
COMPND   9 SYNONYM: E3-14.7K-INTERACTING PROTEIN,FIP-2,HUNTINGTIN YEAST PARTNER 
COMPND  10 L,HUNTINGTIN-INTERACTING PROTEIN 7,HIP-7,HUNTINGTIN-INTERACTING      
COMPND  11 PROTEIN L,NEMO-RELATED PROTEIN,OPTIC NEUROPATHY-INDUCING PROTEIN,    
COMPND  12 TRANSCRIPTION FACTOR IIIA-INTERACTING PROTEIN,TFIIIA-INTP;           
COMPND  13 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: UBC;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: OPTN, FIP2, GLC1E, HIP7, HYPL, NRP;                            
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    UBIQUITIN, COILED-COIL, CELLULAR, SIGNALING, NFKB PATHWAY, SIGNALING  
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.ISHII,O.NUREKI                                                      
REVDAT   1   07-SEP-16 5B83    0                                                
JRNL        AUTH   S.NAKAZAWA,D.OIKAWA,R.ISHII,T.AYAKI,H.TAKAHASHI,H.TAKEDA,    
JRNL        AUTH 2 R.ISHITANI,K.KAMEI,I.TAKEYOSHI,H.KAWAKAMI,K.IWAI,I.HATADA,   
JRNL        AUTH 3 T.SAWASAKI,H.ITO,O.NUREKI,F.TOKUNAGA                         
JRNL        TITL   LINEAR UBIQUITINATION IS INVOLVED IN THE PATHOGENESIS OF     
JRNL        TITL 2 OPTINEURIN-ASSOCIATED AMYOTROPHIC LATERAL SCLEROSIS          
JRNL        REF    NAT COMMUN                    V.   7 12547 2016              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   27552911                                                     
JRNL        DOI    10.1038/NCOMMS12547                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.69 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.69                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.06                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 40445                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2026                            
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 49.0691 -  6.4885    1.00     2966   157  0.1876 0.2208        
REMARK   3     2  6.4885 -  5.1519    1.00     2809   148  0.2065 0.2498        
REMARK   3     3  5.1519 -  4.5012    1.00     2810   147  0.1681 0.2304        
REMARK   3     4  4.5012 -  4.0899    1.00     2760   145  0.1640 0.2179        
REMARK   3     5  4.0899 -  3.7969    1.00     2772   146  0.1788 0.2182        
REMARK   3     6  3.7969 -  3.5731    1.00     2718   143  0.2000 0.2628        
REMARK   3     7  3.5731 -  3.3942    1.00     2740   145  0.2054 0.2817        
REMARK   3     8  3.3942 -  3.2465    1.00     2745   145  0.2188 0.2365        
REMARK   3     9  3.2465 -  3.1215    1.00     2732   143  0.2314 0.2901        
REMARK   3    10  3.1215 -  3.0138    1.00     2720   143  0.2323 0.3132        
REMARK   3    11  3.0138 -  2.9196    1.00     2727   143  0.2384 0.3052        
REMARK   3    12  2.9196 -  2.8361    1.00     2689   142  0.2499 0.3512        
REMARK   3    13  2.8361 -  2.7615    1.00     2736   144  0.2690 0.3107        
REMARK   3    14  2.7615 -  2.6941    0.92     2495   135  0.3041 0.3827        
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)     : 0.420            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.710           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.010           6709                                  
REMARK   3   ANGLE     :  1.131           9014                                  
REMARK   3   CHIRALITY :  0.056           1060                                  
REMARK   3   PLANARITY :  0.006           1167                                  
REMARK   3   DIHEDRAL  : 15.179           4236                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 55 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):   4.3083  36.8260  15.9629              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0908 T22:   1.3785                                     
REMARK   3      T33:   0.7800 T12:   0.0832                                     
REMARK   3      T13:   0.2224 T23:   0.1723                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.7697 L22:   5.7921                                     
REMARK   3      L33:   7.4025 L12:   0.6867                                     
REMARK   3      L13:  -3.2992 L23:  -1.9998                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4520 S12:   0.2544 S13:  -0.2490                       
REMARK   3      S21:  -1.2493 S22:  -0.6557 S23:  -0.6832                       
REMARK   3      S31:  -0.2489 S32:   1.7223 S33:   0.2179                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 56 THROUGH 186 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  22.0081  42.5212  36.1425              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2743 T22:   0.5008                                     
REMARK   3      T33:   0.4696 T12:   0.0042                                     
REMARK   3      T13:   0.0346 T23:  -0.0465                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6789 L22:   1.0258                                     
REMARK   3      L33:   1.0459 L12:   0.6984                                     
REMARK   3      L13:   0.4540 L23:   0.0508                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0958 S12:   0.4441 S13:  -0.2881                       
REMARK   3      S21:  -0.1502 S22:   0.0591 S23:  -0.0078                       
REMARK   3      S31:   0.1548 S32:  -0.0992 S33:   0.0257                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 187 THROUGH 302 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  54.6480  36.1854  50.8371              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1619 T22:   0.3828                                     
REMARK   3      T33:   0.4173 T12:  -0.0044                                     
REMARK   3      T13:   0.0557 T23:  -0.0113                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7894 L22:   6.0911                                     
REMARK   3      L33:   3.3206 L12:  -2.8018                                     
REMARK   3      L13:   2.0667 L23:  -3.3413                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0069 S12:   0.1608 S13:  -0.0209                       
REMARK   3      S21:   0.1896 S22:  -0.0009 S23:   0.2797                       
REMARK   3      S31:  -0.0532 S32:  -0.2389 S33:   0.0147                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 443 THROUGH 501 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  63.1660  41.5313  35.1132              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3879 T22:   0.6357                                     
REMARK   3      T33:   0.4187 T12:   0.0374                                     
REMARK   3      T13:  -0.0245 T23:   0.0676                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5407 L22:   0.7715                                     
REMARK   3      L33:   4.9155 L12:  -1.8274                                     
REMARK   3      L13:   4.3671 L23:  -1.3094                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2643 S12:   0.2892 S13:   0.3976                       
REMARK   3      S21:  -0.1894 S22:  -0.0435 S23:  -0.0940                       
REMARK   3      S31:  -0.6077 S32:  -0.2940 S33:   0.2957                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 445 THROUGH 505 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  66.8103  35.7857  36.8975              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2465 T22:   0.5702                                     
REMARK   3      T33:   0.4482 T12:   0.0235                                     
REMARK   3      T13:   0.0705 T23:  -0.0349                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8324 L22:   1.4611                                     
REMARK   3      L33:   7.8768 L12:  -1.9219                                     
REMARK   3      L13:   6.2357 L23:  -1.6000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3645 S12:   1.3139 S13:  -0.2011                       
REMARK   3      S21:  -0.3267 S22:  -0.3810 S23:   0.0352                       
REMARK   3      S31:   0.3540 S32:   0.7205 S33:  -0.0268                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 1 THROUGH 77 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  74.8738   8.0938  21.5101              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7418 T22:   1.2083                                     
REMARK   3      T33:   0.5022 T12:   0.1380                                     
REMARK   3      T13:  -0.0556 T23:  -0.0128                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6131 L22:   4.1983                                     
REMARK   3      L33:   4.2239 L12:   0.7041                                     
REMARK   3      L13:   1.6132 L23:   2.3140                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2688 S12:   1.9701 S13:   0.0403                       
REMARK   3      S21:  -1.2282 S22:   0.0068 S23:  -0.1986                       
REMARK   3      S31:  -0.0400 S32:  -0.6221 S33:  -0.2256                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 78 THROUGH 153 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  59.6967   4.3918  46.6434              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2867 T22:   0.2716                                     
REMARK   3      T33:   0.2617 T12:   0.0169                                     
REMARK   3      T13:  -0.1007 T23:  -0.0176                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8052 L22:   4.8386                                     
REMARK   3      L33:   2.2081 L12:   2.2757                                     
REMARK   3      L13:  -2.9374 L23:  -2.3992                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0157 S12:   0.1446 S13:   0.1017                       
REMARK   3      S21:  -0.2068 S22:   0.0856 S23:   0.1271                       
REMARK   3      S31:   0.0312 S32:  -0.1782 S33:  -0.1221                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 154 THROUGH 300 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  27.9709   6.6642  51.7702              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2171 T22:   0.3130                                     
REMARK   3      T33:   0.3921 T12:   0.0021                                     
REMARK   3      T13:  -0.0180 T23:  -0.0035                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9646 L22:   7.4910                                     
REMARK   3      L33:   2.6733 L12:  -3.2687                                     
REMARK   3      L13:  -1.6546 L23:   3.5997                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0703 S12:  -0.1221 S13:   0.2024                       
REMARK   3      S21:  -0.2122 S22:   0.1531 S23:  -0.4499                       
REMARK   3      S31:  -0.1986 S32:   0.2232 S33:  -0.2082                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 453 THROUGH 460 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  22.5679  -4.5647  17.8343              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5339 T22:   1.8480                                     
REMARK   3      T33:   0.6563 T12:   0.2137                                     
REMARK   3      T13:  -0.2019 T23:   0.0182                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2086 L22:   7.6986                                     
REMARK   3      L33:   0.6399 L12:   0.3292                                     
REMARK   3      L13:   0.0162 L23:   2.1706                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1884 S12:   2.1257 S13:  -0.1193                       
REMARK   3      S21:  -2.3153 S22:   1.1221 S23:   1.1181                       
REMARK   3      S31:   0.8004 S32:  -1.2896 S33:  -0.8091                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 461 THROUGH 502 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   8.9488  13.6549  49.7996              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2387 T22:   0.3679                                     
REMARK   3      T33:   0.4128 T12:   0.0114                                     
REMARK   3      T13:  -0.0748 T23:   0.0382                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.1526 L22:   6.5135                                     
REMARK   3      L33:   8.3267 L12:  -5.6949                                     
REMARK   3      L13:  -7.8103 L23:   7.0215                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4734 S12:  -0.1405 S13:   0.3102                       
REMARK   3      S21:  -0.5423 S22:   0.1390 S23:  -0.0719                       
REMARK   3      S31:  -1.0474 S32:   0.6708 S33:  -0.3579                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 447 THROUGH 499 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  14.5416   3.4657  42.1840              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4102 T22:   0.5724                                     
REMARK   3      T33:   0.5969 T12:   0.0942                                     
REMARK   3      T13:  -0.1362 T23:  -0.0883                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7678 L22:   2.6707                                     
REMARK   3      L33:   5.5985 L12:  -4.0550                                     
REMARK   3      L13:  -6.2181 L23:   2.8474                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1902 S12:  -0.1557 S13:  -0.6779                       
REMARK   3      S21:  -0.2615 S22:  -0.0508 S23:   0.2795                       
REMARK   3      S31:   0.5932 S32:   0.5393 S33:   0.1862                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 500 THROUGH 505 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -17.5836  18.8571  71.4747              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3865 T22:   0.5487                                     
REMARK   3      T33:   0.7829 T12:   0.1368                                     
REMARK   3      T13:   0.1751 T23:   0.1654                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6255 L22:   0.5001                                     
REMARK   3      L33:   8.2610 L12:   0.5192                                     
REMARK   3      L13:  -5.8149 L23:  -1.1877                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.2269 S12:   0.7202 S13:   2.4661                       
REMARK   3      S21:  -0.1149 S22:  -0.0357 S23:   0.6838                       
REMARK   3      S31:  -0.2741 S32:  -1.1365 S33:  -1.1665                       
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 5B83 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-JUN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1300000697.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-NOV-13                          
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               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40450                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.690                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.14100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.69                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.92000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER, MOLREP                                        
REMARK 200 STARTING MODEL: 2ZVN                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG 3350, 250MM POTASSIUM FORMATE,   
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                     
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       35.66350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      122.42650            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.01900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      122.42650            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.66350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.01900            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, 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     GLY A   303                                                      
REMARK 465     GLY A   304                                                      
REMARK 465     GLY B   409                                                      
REMARK 465     PRO B   410                                                      
REMARK 465     LEU B   411                                                      
REMARK 465     GLY B   412                                                      
REMARK 465     SER B   413                                                      
REMARK 465     HIS B   414                                                      
REMARK 465     MET B   415                                                      
REMARK 465     GLU B   416                                                      
REMARK 465     LYS B   417                                                      
REMARK 465     VAL B   418                                                      
REMARK 465     ASP B   419                                                      
REMARK 465     ARG B   420                                                      
REMARK 465     ALA B   421                                                      
REMARK 465     VAL B   422                                                      
REMARK 465     LEU B   423                                                      
REMARK 465     LYS B   424                                                      
REMARK 465     GLU B   425                                                      
REMARK 465     LEU B   426                                                      
REMARK 465     SER B   427                                                      
REMARK 465     GLU B   428                                                      
REMARK 465     LYS B   429                                                      
REMARK 465     LEU B   430                                                      
REMARK 465     GLU B   431                                                      
REMARK 465     LEU B   432                                                      
REMARK 465     ALA B   433                                                      
REMARK 465     GLU B   434                                                      
REMARK 465     LYS B   435                                                      
REMARK 465     ALA B   436                                                      
REMARK 465     LEU B   437                                                      
REMARK 465     ALA B   438                                                      
REMARK 465     SER B   439                                                      
REMARK 465     LYS B   440                                                      
REMARK 465     GLN B   441                                                      
REMARK 465     LEU B   442                                                      
REMARK 465     GLU B   502                                                      
REMARK 465     ASN B   503                                                      
REMARK 465     ASP B   504                                                      
REMARK 465     ALA B   505                                                      
REMARK 465     PHE B   506                                                      
REMARK 465     GLU B   507                                                      
REMARK 465     ASP B   508                                                      
REMARK 465     GLY B   509                                                      
REMARK 465     GLY B   510                                                      
REMARK 465     GLY C   409                                                      
REMARK 465     PRO C   410                                                      
REMARK 465     LEU C   411                                                      
REMARK 465     GLY C   412                                                      
REMARK 465     SER C   413                                                      
REMARK 465     HIS C   414                                                      
REMARK 465     MET C   415                                                      
REMARK 465     GLU C   416                                                      
REMARK 465     LYS C   417                                                      
REMARK 465     VAL C   418                                                      
REMARK 465     ASP C   419                                                      
REMARK 465     ARG C   420                                                      
REMARK 465     ALA C   421                                                      
REMARK 465     VAL C   422                                                      
REMARK 465     LEU C   423                                                      
REMARK 465     LYS C   424                                                      
REMARK 465     GLU C   425                                                      
REMARK 465     LEU C   426                                                      
REMARK 465     SER C   427                                                      
REMARK 465     GLU C   428                                                      
REMARK 465     LYS C   429                                                      
REMARK 465     LEU C   430                                                      
REMARK 465     GLU C   431                                                      
REMARK 465     LEU C   432                                                      
REMARK 465     ALA C   433                                                      
REMARK 465     GLU C   434                                                      
REMARK 465     LYS C   435                                                      
REMARK 465     ALA C   436                                                      
REMARK 465     LEU C   437                                                      
REMARK 465     ALA C   438                                                      
REMARK 465     SER C   439                                                      
REMARK 465     LYS C   440                                                      
REMARK 465     GLN C   441                                                      
REMARK 465     LEU C   442                                                      
REMARK 465     GLN C   443                                                      
REMARK 465     MET C   444                                                      
REMARK 465     PHE C   506                                                      
REMARK 465     GLU C   507                                                      
REMARK 465     ASP C   508                                                      
REMARK 465     GLY C   509                                                      
REMARK 465     GLY C   510                                                      
REMARK 465     LEU D   301                                                      
REMARK 465     ARG D   302                                                      
REMARK 465     GLY D   303                                                      
REMARK 465     GLY D   304                                                      
REMARK 465     GLY E   409                                                      
REMARK 465     PRO E   410                                                      
REMARK 465     LEU E   411                                                      
REMARK 465     GLY E   412                                                      
REMARK 465     SER E   413                                                      
REMARK 465     HIS E   414                                                      
REMARK 465     MET E   415                                                      
REMARK 465     GLU E   416                                                      
REMARK 465     LYS E   417                                                      
REMARK 465     VAL E   418                                                      
REMARK 465     ASP E   419                                                      
REMARK 465     ARG E   420                                                      
REMARK 465     ALA E   421                                                      
REMARK 465     VAL E   422                                                      
REMARK 465     LEU E   423                                                      
REMARK 465     LYS E   424                                                      
REMARK 465     GLU E   425                                                      
REMARK 465     LEU E   426                                                      
REMARK 465     SER E   427                                                      
REMARK 465     GLU E   428                                                      
REMARK 465     LYS E   429                                                      
REMARK 465     LEU E   430                                                      
REMARK 465     GLU E   431                                                      
REMARK 465     LEU E   432                                                      
REMARK 465     ALA E   433                                                      
REMARK 465     GLU E   434                                                      
REMARK 465     LYS E   435                                                      
REMARK 465     ALA E   436                                                      
REMARK 465     LEU E   437                                                      
REMARK 465     ALA E   438                                                      
REMARK 465     SER E   439                                                      
REMARK 465     LYS E   440                                                      
REMARK 465     GLN E   441                                                      
REMARK 465     LEU E   442                                                      
REMARK 465     GLN E   443                                                      
REMARK 465     MET E   444                                                      
REMARK 465     ASP E   445                                                      
REMARK 465     GLU E   446                                                      
REMARK 465     MET E   447                                                      
REMARK 465     LYS E   448                                                      
REMARK 465     GLN E   449                                                      
REMARK 465     THR E   450                                                      
REMARK 465     ILE E   451                                                      
REMARK 465     ALA E   452                                                      
REMARK 465     ASN E   503                                                      
REMARK 465     ASP E   504                                                      
REMARK 465     ALA E   505                                                      
REMARK 465     PHE E   506                                                      
REMARK 465     GLU E   507                                                      
REMARK 465     ASP E   508                                                      
REMARK 465     GLY E   509                                                      
REMARK 465     GLY E   510                                                      
REMARK 465     GLY F   409                                                      
REMARK 465     PRO F   410                                                      
REMARK 465     LEU F   411                                                      
REMARK 465     GLY F   412                                                      
REMARK 465     SER F   413                                                      
REMARK 465     HIS F   414                                                      
REMARK 465     MET F   415                                                      
REMARK 465     GLU F   416                                                      
REMARK 465     LYS F   417                                                      
REMARK 465     VAL F   418                                                      
REMARK 465     ASP F   419                                                      
REMARK 465     ARG F   420                                                      
REMARK 465     ALA F   421                                                      
REMARK 465     VAL F   422                                                      
REMARK 465     LEU F   423                                                      
REMARK 465     LYS F   424                                                      
REMARK 465     GLU F   425                                                      
REMARK 465     LEU F   426                                                      
REMARK 465     SER F   427                                                      
REMARK 465     GLU F   428                                                      
REMARK 465     LYS F   429                                                      
REMARK 465     LEU F   430                                                      
REMARK 465     GLU F   431                                                      
REMARK 465     LEU F   432                                                      
REMARK 465     ALA F   433                                                      
REMARK 465     GLU F   434                                                      
REMARK 465     LYS F   435                                                      
REMARK 465     ALA F   436                                                      
REMARK 465     LEU F   437                                                      
REMARK 465     ALA F   438                                                      
REMARK 465     SER F   439                                                      
REMARK 465     LYS F   440                                                      
REMARK 465     GLN F   441                                                      
REMARK 465     LEU F   442                                                      
REMARK 465     GLN F   443                                                      
REMARK 465     MET F   444                                                      
REMARK 465     ASP F   445                                                      
REMARK 465     GLU F   446                                                      
REMARK 465     PHE F   506                                                      
REMARK 465     GLU F   507                                                      
REMARK 465     ASP F   508                                                      
REMARK 465     GLY F   509                                                      
REMARK 465     GLY F   510                                                      
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   NH2  ARG E   479     OE2  GLU F   478              2.12            
REMARK 500   N    MET A     1     O    VAL A    17              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NH2  ARG A   282     OD2  ASP D   204     3655     2.06            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 191   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG C 482   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A   2      109.89   -168.88                                   
REMARK 500    GLN A  49      109.05    -51.14                                   
REMARK 500    ASP A  52       34.66     21.56                                   
REMARK 500    SER A  57        0.76    -65.49                                   
REMARK 500    ASN A  60       74.88     61.25                                   
REMARK 500    GLU A  64      -17.78     77.98                                   
REMARK 500    ALA A 198     -112.77     47.53                                   
REMARK 500    GLU A 216       19.36     56.22                                   
REMARK 500    ASP A 267        1.37    -63.97                                   
REMARK 500    ASN A 288       61.04     60.80                                   
REMARK 500    ASN D  60       94.04    -68.27                                   
REMARK 500    LYS D 215      132.49    -39.96                                   
REMARK 500    LYS D 239     -169.59    -72.47                                   
REMARK 500    LEU D 299       46.05    -80.75                                   
REMARK 500    LEU F 500       39.93    -80.79                                   
REMARK 500    GLU F 502       -2.75     93.73                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5B83 A    1   304  UNP    P0CG48   UBC_HUMAN        1    304             
DBREF  5B83 B  416   510  UNP    Q96CV9   OPTN_HUMAN     416    510             
DBREF  5B83 C  416   510  UNP    Q96CV9   OPTN_HUMAN     416    510             
DBREF  5B83 D    1   304  UNP    P0CG48   UBC_HUMAN        1    304             
DBREF  5B83 E  416   510  UNP    Q96CV9   OPTN_HUMAN     416    510             
DBREF  5B83 F  416   510  UNP    Q96CV9   OPTN_HUMAN     416    510             
SEQADV 5B83 GLY B  409  UNP  Q96CV9              EXPRESSION TAG                 
SEQADV 5B83 PRO B  410  UNP  Q96CV9              EXPRESSION TAG                 
SEQADV 5B83 LEU B  411  UNP  Q96CV9              EXPRESSION TAG                 
SEQADV 5B83 GLY B  412  UNP  Q96CV9              EXPRESSION TAG                 
SEQADV 5B83 SER B  413  UNP  Q96CV9              EXPRESSION TAG                 
SEQADV 5B83 HIS B  414  UNP  Q96CV9              EXPRESSION TAG                 
SEQADV 5B83 MET B  415  UNP  Q96CV9              EXPRESSION TAG                 
SEQADV 5B83 GLY C  409  UNP  Q96CV9              EXPRESSION TAG                 
SEQADV 5B83 PRO C  410  UNP  Q96CV9              EXPRESSION TAG                 
SEQADV 5B83 LEU C  411  UNP  Q96CV9              EXPRESSION TAG                 
SEQADV 5B83 GLY C  412  UNP  Q96CV9              EXPRESSION TAG                 
SEQADV 5B83 SER C  413  UNP  Q96CV9              EXPRESSION TAG                 
SEQADV 5B83 HIS C  414  UNP  Q96CV9              EXPRESSION TAG                 
SEQADV 5B83 MET C  415  UNP  Q96CV9              EXPRESSION TAG                 
SEQADV 5B83 GLY E  409  UNP  Q96CV9              EXPRESSION TAG                 
SEQADV 5B83 PRO E  410  UNP  Q96CV9              EXPRESSION TAG                 
SEQADV 5B83 LEU E  411  UNP  Q96CV9              EXPRESSION TAG                 
SEQADV 5B83 GLY E  412  UNP  Q96CV9              EXPRESSION TAG                 
SEQADV 5B83 SER E  413  UNP  Q96CV9              EXPRESSION TAG                 
SEQADV 5B83 HIS E  414  UNP  Q96CV9              EXPRESSION TAG                 
SEQADV 5B83 MET E  415  UNP  Q96CV9              EXPRESSION TAG                 
SEQADV 5B83 GLY F  409  UNP  Q96CV9              EXPRESSION TAG                 
SEQADV 5B83 PRO F  410  UNP  Q96CV9              EXPRESSION TAG                 
SEQADV 5B83 LEU F  411  UNP  Q96CV9              EXPRESSION TAG                 
SEQADV 5B83 GLY F  412  UNP  Q96CV9              EXPRESSION TAG                 
SEQADV 5B83 SER F  413  UNP  Q96CV9              EXPRESSION TAG                 
SEQADV 5B83 HIS F  414  UNP  Q96CV9              EXPRESSION TAG                 
SEQADV 5B83 MET F  415  UNP  Q96CV9              EXPRESSION TAG                 
SEQRES   1 A  304  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 A  304  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 A  304  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 A  304  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 A  304  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 A  304  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY MET GLN          
SEQRES   7 A  304  ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE THR LEU          
SEQRES   8 A  304  GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL LYS ALA          
SEQRES   9 A  304  LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP GLN GLN          
SEQRES  10 A  304  ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP GLY ARG          
SEQRES  11 A  304  THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER THR LEU          
SEQRES  12 A  304  HIS LEU VAL LEU ARG LEU ARG GLY GLY MET GLN ILE PHE          
SEQRES  13 A  304  VAL LYS THR LEU THR GLY LYS THR ILE THR LEU GLU VAL          
SEQRES  14 A  304  GLU PRO SER ASP THR ILE GLU ASN VAL LYS ALA LYS ILE          
SEQRES  15 A  304  GLN ASP LYS GLU GLY ILE PRO PRO ASP GLN GLN ARG LEU          
SEQRES  16 A  304  ILE PHE ALA GLY LYS GLN LEU GLU ASP GLY ARG THR LEU          
SEQRES  17 A  304  SER ASP TYR ASN ILE GLN LYS GLU SER THR LEU HIS LEU          
SEQRES  18 A  304  VAL LEU ARG LEU ARG GLY GLY MET GLN ILE PHE VAL LYS          
SEQRES  19 A  304  THR LEU THR GLY LYS THR ILE THR LEU GLU VAL GLU PRO          
SEQRES  20 A  304  SER ASP THR ILE GLU ASN VAL LYS ALA LYS ILE GLN ASP          
SEQRES  21 A  304  LYS GLU GLY ILE PRO PRO ASP GLN GLN ARG LEU ILE PHE          
SEQRES  22 A  304  ALA GLY LYS GLN LEU GLU ASP GLY ARG THR LEU SER ASP          
SEQRES  23 A  304  TYR ASN ILE GLN LYS GLU SER THR LEU HIS LEU VAL LEU          
SEQRES  24 A  304  ARG LEU ARG GLY GLY                                          
SEQRES   1 B  102  GLY PRO LEU GLY SER HIS MET GLU LYS VAL ASP ARG ALA          
SEQRES   2 B  102  VAL LEU LYS GLU LEU SER GLU LYS LEU GLU LEU ALA GLU          
SEQRES   3 B  102  LYS ALA LEU ALA SER LYS GLN LEU GLN MET ASP GLU MET          
SEQRES   4 B  102  LYS GLN THR ILE ALA LYS GLN GLU GLU ASP LEU GLU THR          
SEQRES   5 B  102  MET THR ILE LEU ARG ALA GLN MET GLU VAL TYR CYS SER          
SEQRES   6 B  102  ASP PHE HIS ALA GLU ARG ALA ALA ARG GLU LYS ILE HIS          
SEQRES   7 B  102  GLU GLU LYS GLU GLN LEU ALA LEU GLN LEU ALA VAL LEU          
SEQRES   8 B  102  LEU LYS GLU ASN ASP ALA PHE GLU ASP GLY GLY                  
SEQRES   1 C  102  GLY PRO LEU GLY SER HIS MET GLU LYS VAL ASP ARG ALA          
SEQRES   2 C  102  VAL LEU LYS GLU LEU SER GLU LYS LEU GLU LEU ALA GLU          
SEQRES   3 C  102  LYS ALA LEU ALA SER LYS GLN LEU GLN MET ASP GLU MET          
SEQRES   4 C  102  LYS GLN THR ILE ALA LYS GLN GLU GLU ASP LEU GLU THR          
SEQRES   5 C  102  MET THR ILE LEU ARG ALA GLN MET GLU VAL TYR CYS SER          
SEQRES   6 C  102  ASP PHE HIS ALA GLU ARG ALA ALA ARG GLU LYS ILE HIS          
SEQRES   7 C  102  GLU GLU LYS GLU GLN LEU ALA LEU GLN LEU ALA VAL LEU          
SEQRES   8 C  102  LEU LYS GLU ASN ASP ALA PHE GLU ASP GLY GLY                  
SEQRES   1 D  304  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 D  304  THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL          
SEQRES   3 D  304  LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 D  304  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 D  304  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 D  304  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY MET GLN          
SEQRES   7 D  304  ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE THR LEU          
SEQRES   8 D  304  GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL LYS ALA          
SEQRES   9 D  304  LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP GLN GLN          
SEQRES  10 D  304  ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP GLY ARG          
SEQRES  11 D  304  THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER THR LEU          
SEQRES  12 D  304  HIS LEU VAL LEU ARG LEU ARG GLY GLY MET GLN ILE PHE          
SEQRES  13 D  304  VAL LYS THR LEU THR GLY LYS THR ILE THR LEU GLU VAL          
SEQRES  14 D  304  GLU PRO SER ASP THR ILE GLU ASN VAL LYS ALA LYS ILE          
SEQRES  15 D  304  GLN ASP LYS GLU GLY ILE PRO PRO ASP GLN GLN ARG LEU          
SEQRES  16 D  304  ILE PHE ALA GLY LYS GLN LEU GLU ASP GLY ARG THR LEU          
SEQRES  17 D  304  SER ASP TYR ASN ILE GLN LYS GLU SER THR LEU HIS LEU          
SEQRES  18 D  304  VAL LEU ARG LEU ARG GLY GLY MET GLN ILE PHE VAL LYS          
SEQRES  19 D  304  THR LEU THR GLY LYS THR ILE THR LEU GLU VAL GLU PRO          
SEQRES  20 D  304  SER ASP THR ILE GLU ASN VAL LYS ALA LYS ILE GLN ASP          
SEQRES  21 D  304  LYS GLU GLY ILE PRO PRO ASP GLN GLN ARG LEU ILE PHE          
SEQRES  22 D  304  ALA GLY LYS GLN LEU GLU ASP GLY ARG THR LEU SER ASP          
SEQRES  23 D  304  TYR ASN ILE GLN LYS GLU SER THR LEU HIS LEU VAL LEU          
SEQRES  24 D  304  ARG LEU ARG GLY GLY                                          
SEQRES   1 E  102  GLY PRO LEU GLY SER HIS MET GLU LYS VAL ASP ARG ALA          
SEQRES   2 E  102  VAL LEU LYS GLU LEU SER GLU LYS LEU GLU LEU ALA GLU          
SEQRES   3 E  102  LYS ALA LEU ALA SER LYS GLN LEU GLN MET ASP GLU MET          
SEQRES   4 E  102  LYS GLN THR ILE ALA LYS GLN GLU GLU ASP LEU GLU THR          
SEQRES   5 E  102  MET THR ILE LEU ARG ALA GLN MET GLU VAL TYR CYS SER          
SEQRES   6 E  102  ASP PHE HIS ALA GLU ARG ALA ALA ARG GLU LYS ILE HIS          
SEQRES   7 E  102  GLU GLU LYS GLU GLN LEU ALA LEU GLN LEU ALA VAL LEU          
SEQRES   8 E  102  LEU LYS GLU ASN ASP ALA PHE GLU ASP GLY GLY                  
SEQRES   1 F  102  GLY PRO LEU GLY SER HIS MET GLU LYS VAL ASP ARG ALA          
SEQRES   2 F  102  VAL LEU LYS GLU LEU SER GLU LYS LEU GLU LEU ALA GLU          
SEQRES   3 F  102  LYS ALA LEU ALA SER LYS GLN LEU GLN MET ASP GLU MET          
SEQRES   4 F  102  LYS GLN THR ILE ALA LYS GLN GLU GLU ASP LEU GLU THR          
SEQRES   5 F  102  MET THR ILE LEU ARG ALA GLN MET GLU VAL TYR CYS SER          
SEQRES   6 F  102  ASP PHE HIS ALA GLU ARG ALA ALA ARG GLU LYS ILE HIS          
SEQRES   7 F  102  GLU GLU LYS GLU GLN LEU ALA LEU GLN LEU ALA VAL LEU          
SEQRES   8 F  102  LEU LYS GLU ASN ASP ALA PHE GLU ASP GLY GLY                  
FORMUL   7  HOH   *59(H2 O)                                                     
HELIX    1 AA1 THR A   22  ASP A   32  1                                  11    
HELIX    2 AA2 PRO A   37  ASP A   39  5                                   3    
HELIX    3 AA3 THR A   55  TYR A   59  5                                   5    
HELIX    4 AA4 THR A   98  GLY A  111  1                                  14    
HELIX    5 AA5 PRO A  113  ASP A  115  5                                   3    
HELIX    6 AA6 THR A  174  GLY A  187  1                                  14    
HELIX    7 AA7 PRO A  189  ASP A  191  5                                   3    
HELIX    8 AA8 THR A  250  GLY A  263  1                                  14    
HELIX    9 AA9 PRO A  265  ASP A  267  5                                   3    
HELIX   10 AB1 LEU A  284  ASN A  288  5                                   5    
HELIX   11 AB2 GLU B  446  VAL B  498  1                                  53    
HELIX   12 AB3 MET C  447  LEU C  458  1                                  12    
HELIX   13 AB4 GLU C  459  ASN C  503  1                                  45    
HELIX   14 AB5 THR D   22  GLY D   35  1                                  14    
HELIX   15 AB6 PRO D   37  ASP D   39  5                                   3    
HELIX   16 AB7 THR D   98  GLY D  111  1                                  14    
HELIX   17 AB8 PRO D  113  ASP D  115  5                                   3    
HELIX   18 AB9 THR D  174  GLY D  187  1                                  14    
HELIX   19 AC1 PRO D  189  ASP D  191  5                                   3    
HELIX   20 AC2 LEU D  208  ASN D  212  5                                   5    
HELIX   21 AC3 THR D  250  GLY D  263  1                                  14    
HELIX   22 AC4 PRO D  265  GLN D  269  5                                   5    
HELIX   23 AC5 ASP E  457  LEU E  500  1                                  44    
HELIX   24 AC6 LYS F  448  LEU F  500  1                                  53    
SHEET    1 AA1 5 THR A  12  LEU A  15  0                                        
SHEET    2 AA1 5 ILE A   3  LYS A   6 -1  N  VAL A   5   O  ILE A  13           
SHEET    3 AA1 5 THR A  66  LEU A  71  1  O  LEU A  67   N  PHE A   4           
SHEET    4 AA1 5 GLN A  41  PHE A  45 -1  N  ILE A  44   O  HIS A  68           
SHEET    5 AA1 5 LYS A  48  LEU A  50 -1  O  LYS A  48   N  PHE A  45           
SHEET    1 AA2 5 THR A  88  VAL A  93  0                                        
SHEET    2 AA2 5 MET A  77  LYS A  82 -1  N  VAL A  81   O  ILE A  89           
SHEET    3 AA2 5 THR A 142  LEU A 147  1  O  LEU A 143   N  LYS A  82           
SHEET    4 AA2 5 GLN A 117  PHE A 121 -1  N  ARG A 118   O  VAL A 146           
SHEET    5 AA2 5 LYS A 124  GLN A 125 -1  O  LYS A 124   N  PHE A 121           
SHEET    1 AA3 5 THR A 164  VAL A 169  0                                        
SHEET    2 AA3 5 MET A 153  LYS A 158 -1  N  VAL A 157   O  ILE A 165           
SHEET    3 AA3 5 THR A 218  LEU A 223  1  O  LEU A 221   N  LYS A 158           
SHEET    4 AA3 5 GLN A 193  PHE A 197 -1  N  ILE A 196   O  HIS A 220           
SHEET    5 AA3 5 LYS A 200  GLN A 201 -1  O  LYS A 200   N  PHE A 197           
SHEET    1 AA4 5 THR A 240  GLU A 244  0                                        
SHEET    2 AA4 5 GLN A 230  LYS A 234 -1  N  ILE A 231   O  LEU A 243           
SHEET    3 AA4 5 THR A 294  LEU A 299  1  O  LEU A 295   N  LYS A 234           
SHEET    4 AA4 5 GLN A 269  PHE A 273 -1  N  ILE A 272   O  HIS A 296           
SHEET    5 AA4 5 LYS A 276  GLN A 277 -1  O  LYS A 276   N  PHE A 273           
SHEET    1 AA5 4 THR D  12  GLU D  16  0                                        
SHEET    2 AA5 4 GLN D   2  LYS D   6 -1  N  VAL D   5   O  ILE D  13           
SHEET    3 AA5 4 THR D  66  LEU D  71  1  O  LEU D  67   N  PHE D   4           
SHEET    4 AA5 4 GLN D  41  ILE D  44 -1  N  ARG D  42   O  VAL D  70           
SHEET    1 AA6 5 THR D  88  VAL D  93  0                                        
SHEET    2 AA6 5 MET D  77  THR D  83 -1  N  MET D  77   O  VAL D  93           
SHEET    3 AA6 5 THR D 142  LEU D 147  1  O  LEU D 143   N  PHE D  80           
SHEET    4 AA6 5 GLN D 117  PHE D 121 -1  N  ILE D 120   O  HIS D 144           
SHEET    5 AA6 5 LYS D 124  GLN D 125 -1  O  LYS D 124   N  PHE D 121           
SHEET    1 AA7 5 THR D 164  VAL D 169  0                                        
SHEET    2 AA7 5 MET D 153  THR D 159 -1  N  ILE D 155   O  LEU D 167           
SHEET    3 AA7 5 THR D 218  LEU D 223  1  O  LEU D 219   N  PHE D 156           
SHEET    4 AA7 5 GLN D 193  PHE D 197 -1  N  ILE D 196   O  HIS D 220           
SHEET    5 AA7 5 LYS D 200  GLN D 201 -1  O  LYS D 200   N  PHE D 197           
SHEET    1 AA8 5 THR D 240  VAL D 245  0                                        
SHEET    2 AA8 5 MET D 229  THR D 235 -1  N  ILE D 231   O  LEU D 243           
SHEET    3 AA8 5 THR D 294  VAL D 298  1  O  LEU D 295   N  PHE D 232           
SHEET    4 AA8 5 ARG D 270  PHE D 273 -1  N  ARG D 270   O  VAL D 298           
SHEET    5 AA8 5 LYS D 276  GLN D 277 -1  O  LYS D 276   N  PHE D 273           
CISPEP   1 LYS F  501    GLU F  502          0       -21.55                     
CRYST1   71.327   82.038  244.853  90.00  90.00  90.00 P 21 21 21   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      0.014020  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012189  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004084        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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