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Database: PDB
Entry: 3W8J
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HEADER    OXIDOREDUCTASE/ISOMERASE                13-MAR-13   3W8J              
TITLE     CRYSTAL STRUCTURE OF P5 A0 IN A COMPLEX WITH PRX4 C-TERM              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN DISULFIDE-ISOMERASE A6;                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: P5 A0, UNP RESIDUES 20-140;                                
COMPND   5 SYNONYM: ENDOPLASMIC RETICULUM PROTEIN 5, ER PROTEIN 5, ERP5, PROTEIN
COMPND   6 DISULFIDE ISOMERASE P5, THIOREDOXIN DOMAIN-CONTAINING PROTEIN 7;     
COMPND   7 EC: 5.3.4.1;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: C-TERMINAL PEPTIDE FROM PEROXIREDOXIN-4;                   
COMPND  12 CHAIN: C, D;                                                         
COMPND  13 FRAGMENT: UNP RESIDUES 244-263;                                      
COMPND  14 SYNONYM: ANTIOXIDANT ENZYME AOE372, PEROXIREDOXIN IV, PRX-IV,        
COMPND  15 THIOREDOXIN PEROXIDASE AO372, THIOREDOXIN-DEPENDENT PEROXIDE         
COMPND  16 REDUCTASE A0372;                                                     
COMPND  17 EC: 1.11.1.15;                                                       
COMPND  18 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: PDIA6, ERP5, P5, TXNDC7;                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PET15B;                               
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  13 ORGANISM_COMMON: MOUSE;                                              
SOURCE  14 ORGANISM_TAXID: 10090                                                
KEYWDS    PDI FAMILY MEMBER, THIOREDOXIN FOLD, PROTEIN DISULFIDE ISOMERASE,     
KEYWDS   2 OXIDOREDUCTASE-ISOMERASE COMPLEX                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.INABA,M.SUZUKI,R.KOJIMA                                             
REVDAT   1   04-SEP-13 3W8J    0                                                
JRNL        AUTH   Y.SATO,R.KOJIMA,M.OKUMURA,M.HAGIWARA,S.MASUI,K.MAEGAWA,      
JRNL        AUTH 2 M.SAIKI,T.HORIBE,M.SUZUKI,K.INABA                            
JRNL        TITL   SYNERGISTIC COOPERATION OF PDI FAMILY MEMBERS IN             
JRNL        TITL 2 PEROXIREDOXIN 4-DRIVEN OXIDATIVE PROTEIN FOLDING             
JRNL        REF    SCI REP                       V.   3  2456 2013              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   23949117                                                     
JRNL        DOI    10.1038/SREP02456                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.1_1168)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.67                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 82.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 14047                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.185                           
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.050                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 709                             
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 41.6767 -  3.5907    0.99     3384   157  0.1609 0.2110        
REMARK   3     2  3.5907 -  2.8502    1.00     3204   189  0.1866 0.2597        
REMARK   3     3  2.8502 -  2.4900    0.93     2948   160  0.2133 0.2687        
REMARK   3     4  2.4900 -  2.2623    0.71     2236   125  0.2242 0.3060        
REMARK   3     5  2.2623 -  2.1002    0.49     1566    78  0.2085 0.2643        
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)     : 0.220            
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) : 42.58                          
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      :  0.007           2028                                  
REMARK   3   ANGLE     :  1.036           2739                                  
REMARK   3   CHIRALITY :  0.067            296                                  
REMARK   3   PLANARITY :  0.004            355                                  
REMARK   3   DIHEDRAL  : 14.108            731                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 17                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 22:36)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   19.820   43.730    9.836              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6611 T22:   0.3773                                     
REMARK   3      T33:   0.3703 T12:  -0.0720                                     
REMARK   3      T13:  -0.1702 T23:   0.0709                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0464 L22:   0.3137                                     
REMARK   3      L33:   0.0660 L12:   0.1156                                     
REMARK   3      L13:   0.0519 L23:   0.1472                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1729 S12:   0.2175 S13:  -0.4203                       
REMARK   3      S21:  -0.4784 S22:   0.2707 S23:   0.0815                       
REMARK   3      S31:   0.8466 S32:  -0.5342 S33:   0.0100                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 37:47)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   16.827   49.813   18.272              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1088 T22:   1.3879                                     
REMARK   3      T33:   0.3916 T12:  -0.0132                                     
REMARK   3      T13:  -0.0178 T23:   0.2335                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1721 L22:   0.1607                                     
REMARK   3      L33:   0.2876 L12:   0.1619                                     
REMARK   3      L13:   0.2242 L23:   0.2140                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1037 S12:   0.1195 S13:  -0.1014                       
REMARK   3      S21:   0.0218 S22:  -0.0732 S23:   0.2194                       
REMARK   3      S31:   0.0372 S32:  -0.4249 S33:  -0.4708                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 48:57)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   22.578   52.224   -0.866              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3385 T22:   0.3335                                     
REMARK   3      T33:   0.2609 T12:   0.0102                                     
REMARK   3      T13:  -0.0567 T23:   0.0068                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0211 L22:   0.7743                                     
REMARK   3      L33:   0.1924 L12:   0.0640                                     
REMARK   3      L13:  -0.0148 L23:  -0.2150                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1998 S12:  -0.0259 S13:  -0.1849                       
REMARK   3      S21:  -0.6590 S22:   0.3336 S23:   0.4411                       
REMARK   3      S31:   0.0576 S32:  -0.4303 S33:   0.0178                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 58:73)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   31.367   50.418    7.250              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3524 T22:   0.2416                                     
REMARK   3      T33:   0.2421 T12:   0.0971                                     
REMARK   3      T13:  -0.0067 T23:  -0.0074                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1291 L22:   0.0778                                     
REMARK   3      L33:   0.0339 L12:   0.0354                                     
REMARK   3      L13:   0.0702 L23:   0.0010                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0737 S12:   0.0519 S13:   0.1030                       
REMARK   3      S21:  -0.1889 S22:   0.1482 S23:  -0.1648                       
REMARK   3      S31:  -0.3569 S32:   0.0463 S33:  -0.0001                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 74:94)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  18.6575  49.3837   8.0666              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1942 T22:   0.6356                                     
REMARK   3      T33:   0.1421 T12:  -0.1237                                     
REMARK   3      T13:  -0.1277 T23:   0.0779                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7349 L22:   0.5085                                     
REMARK   3      L33:   0.4495 L12:   0.4392                                     
REMARK   3      L13:   0.4082 L23:   0.0235                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1122 S12:   0.2489 S13:  -0.2772                       
REMARK   3      S21:  -0.1313 S22:   0.1099 S23:  -0.2078                       
REMARK   3      S31:   0.2567 S32:  -0.4971 S33:   0.2789                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 95:106)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.0014  57.8492   5.4482              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3383 T22:   0.5663                                     
REMARK   3      T33:   0.2877 T12:   0.1991                                     
REMARK   3      T13:  -0.0055 T23:  -0.0068                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0852 L22:   0.9581                                     
REMARK   3      L33:   0.0958 L12:   0.2848                                     
REMARK   3      L13:   0.0737 L23:   0.2614                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0107 S12:  -0.4452 S13:   0.0305                       
REMARK   3      S21:  -0.0203 S22:   0.3014 S23:   0.3786                       
REMARK   3      S31:  -0.3011 S32:  -0.4950 S33:  -0.0334                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 107:121)                         
REMARK   3    ORIGIN FOR THE GROUP (A):   22.652   60.793   11.565              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2617 T22:   0.6953                                     
REMARK   3      T33:   0.3783 T12:   0.2284                                     
REMARK   3      T13:  -0.0890 T23:   0.0556                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1944 L22:   1.9358                                     
REMARK   3      L33:   0.3748 L12:   0.3496                                     
REMARK   3      L13:  -0.0117 L23:   0.6782                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3305 S12:  -0.5675 S13:   0.4556                       
REMARK   3      S21:  -0.2166 S22:   0.1797 S23:   0.0728                       
REMARK   3      S31:  -0.5791 S32:  -0.6134 S33:  -0.0336                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 122:140)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  26.8543  60.1663  22.1400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2967 T22:   0.2975                                     
REMARK   3      T33:   0.3130 T12:   0.0742                                     
REMARK   3      T13:  -0.0526 T23:  -0.0460                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0789 L22:   0.1233                                     
REMARK   3      L33:   0.2550 L12:  -0.0031                                     
REMARK   3      L13:  -0.0417 L23:   0.0773                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0162 S12:  -0.1454 S13:   0.1912                       
REMARK   3      S21:  -0.2349 S22:   0.0360 S23:   0.0471                       
REMARK   3      S31:  -0.4663 S32:   0.0210 S33:   0.0010                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain 'B' and (resseq 21:36)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  27.3317  43.7710  42.5431              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3023 T22:   0.2138                                     
REMARK   3      T33:   0.2772 T12:  -0.1432                                     
REMARK   3      T13:   0.0794 T23:   0.0349                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8497 L22:   0.4003                                     
REMARK   3      L33:   1.4882 L12:  -0.5382                                     
REMARK   3      L13:  -0.9300 L23:   0.7469                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0409 S12:  -0.3852 S13:  -0.1395                       
REMARK   3      S21:   0.1991 S22:   0.1901 S23:   0.3414                       
REMARK   3      S31:   0.4836 S32:  -0.1084 S33:   0.1593                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: chain 'B' and (resseq 37:47)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   35.413   43.017   31.579              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3088 T22:   0.2004                                     
REMARK   3      T33:   0.2286 T12:   0.0198                                     
REMARK   3      T13:   0.0128 T23:  -0.0543                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0831 L22:   0.0103                                     
REMARK   3      L33:   0.0434 L12:   0.0045                                     
REMARK   3      L13:   0.0587 L23:  -0.0106                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0058 S12:   0.1659 S13:   0.0875                       
REMARK   3      S21:  -0.1961 S22:  -0.0811 S23:  -0.1706                       
REMARK   3      S31:   0.2241 S32:  -0.3040 S33:  -0.0001                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: chain 'B' and (resseq 48:78)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  29.4969  52.9283  42.6862              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3022 T22:   0.2478                                     
REMARK   3      T33:   0.2493 T12:   0.0280                                     
REMARK   3      T13:   0.0551 T23:  -0.0643                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3284 L22:   0.3227                                     
REMARK   3      L33:   0.0844 L12:   0.0853                                     
REMARK   3      L13:  -0.0095 L23:  -0.0352                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1396 S12:  -0.0923 S13:   0.0464                       
REMARK   3      S21:   0.1317 S22:  -0.2261 S23:   0.1216                       
REMARK   3      S31:   0.1005 S32:  -0.2008 S33:  -0.0001                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: chain 'B' and (resseq 79:88)                           
REMARK   3    ORIGIN FOR THE GROUP (A):   36.850   42.960   48.577              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4748 T22:   0.2226                                     
REMARK   3      T33:   0.1940 T12:  -0.0266                                     
REMARK   3      T13:   0.0437 T23:  -0.0012                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1486 L22:   0.0274                                     
REMARK   3      L33:   0.0563 L12:  -0.0171                                     
REMARK   3      L13:   0.0981 L23:   0.0085                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0239 S12:  -0.3184 S13:   0.0266                       
REMARK   3      S21:   0.5028 S22:   0.1153 S23:   0.3400                       
REMARK   3      S31:   0.4094 S32:  -0.3174 S33:   0.0102                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: chain 'B' and (resseq 89:113)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.5425  48.1928  40.2881              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2228 T22:   0.2381                                     
REMARK   3      T33:   0.2533 T12:   0.0154                                     
REMARK   3      T13:   0.0263 T23:  -0.0357                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1463 L22:   0.1667                                     
REMARK   3      L33:   0.1257 L12:   0.1597                                     
REMARK   3      L13:   0.0769 L23:   0.1249                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1177 S12:   0.0000 S13:  -0.0584                       
REMARK   3      S21:   0.1264 S22:   0.0692 S23:  -0.3401                       
REMARK   3      S31:   0.0262 S32:   0.2166 S33:   0.0001                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: chain 'B' and (resseq 114:121)                         
REMARK   3    ORIGIN FOR THE GROUP (A):   34.011   61.746   40.285              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3485 T22:   0.0230                                     
REMARK   3      T33:   0.2008 T12:   0.0822                                     
REMARK   3      T13:   0.1324 T23:  -0.1149                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0018 L22:   0.2926                                     
REMARK   3      L33:   0.3538 L12:  -0.0019                                     
REMARK   3      L13:  -0.0313 L23:  -0.0973                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0268 S12:   0.2291 S13:  -0.0230                       
REMARK   3      S21:  -0.2220 S22:  -0.3248 S23:  -0.3802                       
REMARK   3      S31:   0.0863 S32:   0.2440 S33:  -0.0154                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: chain 'B' and (resseq 122:140)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  35.2326  56.7000  26.0782              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2862 T22:   0.1342                                     
REMARK   3      T33:   0.1780 T12:   0.0662                                     
REMARK   3      T13:   0.0021 T23:  -0.0141                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1254 L22:   0.1945                                     
REMARK   3      L33:   0.3162 L12:   0.0295                                     
REMARK   3      L13:   0.1284 L23:   0.2117                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0231 S12:  -0.0814 S13:   0.1671                       
REMARK   3      S21:  -0.2097 S22:   0.1492 S23:   0.0293                       
REMARK   3      S31:  -0.4167 S32:   0.3398 S33:  -0.0018                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: chain 'C' and (resseq 0:5)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  21.1290  59.4222  -4.9052              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4779 T22:   0.4163                                     
REMARK   3      T33:   0.3227 T12:   0.0677                                     
REMARK   3      T13:  -0.0600 T23:  -0.0126                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0642 L22:   0.0042                                     
REMARK   3      L33:   0.0117 L12:  -0.0029                                     
REMARK   3      L13:   0.0233 L23:   0.0051                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1017 S12:  -0.0632 S13:   0.2027                       
REMARK   3      S21:   0.1699 S22:  -0.2826 S23:  -0.1982                       
REMARK   3      S31:  -0.2087 S32:   0.1730 S33:  -0.0001                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: chain 'D' and (resseq 0:5)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  40.5807  55.4364  53.2685              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4270 T22:   0.3698                                     
REMARK   3      T33:   0.3602 T12:   0.0039                                     
REMARK   3      T13:   0.0165 T23:  -0.0568                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0314 L22:   0.0104                                     
REMARK   3      L33:   0.0098 L12:   0.0197                                     
REMARK   3      L13:   0.0000 L23:  -0.0007                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2341 S12:  -0.1330 S13:   0.0270                       
REMARK   3      S21:  -0.0417 S22:  -0.1571 S23:  -0.1696                       
REMARK   3      S31:   0.1033 S32:   0.0168 S33:  -0.0010                       
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 3W8J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-MAR-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB096020.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-JAN-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-5A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16851                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 41.670                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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   (%): 37.23                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.96                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG 2000 MME, 0.1M POTASSIUM         
REMARK 280  THIOCYANATE, 0.1M TRIS-HCL (PH 7.3), VAPOR DIFFUSION, HANGING       
REMARK 280  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       19.52250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       66.67650            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       26.68750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       66.67650            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       19.52250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       26.68750            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1030 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7030 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -4.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1720 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7180 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     SER A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     HIS A     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 465     HIS A     6                                                      
REMARK 465     HIS A     7                                                      
REMARK 465     HIS A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     GLY A    11                                                      
REMARK 465     LEU A    12                                                      
REMARK 465     VAL A    13                                                      
REMARK 465     PRO A    14                                                      
REMARK 465     ARG A    15                                                      
REMARK 465     GLY A    16                                                      
REMARK 465     SER A    17                                                      
REMARK 465     HIS A    18                                                      
REMARK 465     MET A    19                                                      
REMARK 465     MET B    -1                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     SER B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     HIS B     4                                                      
REMARK 465     HIS B     5                                                      
REMARK 465     HIS B     6                                                      
REMARK 465     HIS B     7                                                      
REMARK 465     HIS B     8                                                      
REMARK 465     SER B     9                                                      
REMARK 465     SER B    10                                                      
REMARK 465     GLY B    11                                                      
REMARK 465     LEU B    12                                                      
REMARK 465     VAL B    13                                                      
REMARK 465     PRO B    14                                                      
REMARK 465     ARG B    15                                                      
REMARK 465     GLY B    16                                                      
REMARK 465     SER B    17                                                      
REMARK 465     HIS B    18                                                      
REMARK 465     HIS C    -2                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     TRP C     6                                                      
REMARK 465     LYS C     7                                                      
REMARK 465     PRO C     8                                                      
REMARK 465     GLY C     9                                                      
REMARK 465     SER C    10                                                      
REMARK 465     GLU C    11                                                      
REMARK 465     THR C    12                                                      
REMARK 465     ILE C    13                                                      
REMARK 465     ILE C    14                                                      
REMARK 465     PRO C    15                                                      
REMARK 465     ASP C    16                                                      
REMARK 465     PRO C    17                                                      
REMARK 465     HIS D    -2                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     TRP D     6                                                      
REMARK 465     LYS D     7                                                      
REMARK 465     PRO D     8                                                      
REMARK 465     GLY D     9                                                      
REMARK 465     SER D    10                                                      
REMARK 465     GLU D    11                                                      
REMARK 465     THR D    12                                                      
REMARK 465     ILE D    13                                                      
REMARK 465     ILE D    14                                                      
REMARK 465     PRO D    15                                                      
REMARK 465     ASP D    16                                                      
REMARK 465     PRO D    17                                                      
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     MET B  19    CB   CG   SD   CE                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  34        0.44   -158.43                                   
REMARK 500    GLN A  41       37.62    -86.06                                   
REMARK 500    ASP A  82       92.11    -68.88                                   
REMARK 500    VAL B  39      -64.13   -102.90                                   
REMARK 500    HIS B  86       67.17   -103.31                                   
REMARK 500    ARG B 118       39.69    -91.40                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B 206   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL B  27   O                                                      
REMARK 620 2 SER B  22   O   136.9                                              
REMARK 620 3 ASP B  25   O   104.2  87.0                                        
REMARK 620 4 ASP B  25   OD1  75.7  69.3  69.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 201   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  49   OE2                                                    
REMARK 620 2 ALA A  58   O   101.6                                              
REMARK 620 3 TYR A  21   OH   89.7 148.3                                        
REMARK 620 4 THR A  62   OG1 167.4  67.6  96.6                                  
REMARK 620 5 GLU A  49   OE1  42.6 138.9  47.3 143.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B 205   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA B  58   O                                                      
REMARK 620 2 THR B  62   OG1  75.8                                              
REMARK 620 3 GLU B  49   OE2 102.8 161.8                                        
REMARK 620 4 TYR B  21   OH  141.2  85.1  85.2                                  
REMARK 620 5 GLU B  49   OE1 135.1 130.8  39.6  46.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 202   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A  22   O                                                      
REMARK 620 2 VAL A  27   O   115.5                                              
REMARK 620 3 ASP A  25   O    85.6  99.8                                        
REMARK 620 4 ASP A  25   OD1  60.5  66.9  61.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 201                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 202                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 205                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 206                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3VWW   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF P5 A0                                           
REMARK 900 RELATED ID: 3VWU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3VWV   RELATED DB: PDB                                   
DBREF  3W8J A   20   140  UNP    Q15084   PDIA6_HUMAN     20    140             
DBREF  3W8J B   20   140  UNP    Q15084   PDIA6_HUMAN     20    140             
DBREF  3W8J C   -2    17  UNP    O08807   PRDX4_MOUSE    244    263             
DBREF  3W8J D   -2    17  UNP    O08807   PRDX4_MOUSE    244    263             
SEQADV 3W8J MET A   -1  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J GLY A    0  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J SER A    1  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J SER A    2  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J HIS A    3  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J HIS A    4  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J HIS A    5  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J HIS A    6  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J HIS A    7  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J HIS A    8  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J SER A    9  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J SER A   10  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J GLY A   11  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J LEU A   12  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J VAL A   13  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J PRO A   14  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J ARG A   15  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J GLY A   16  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J SER A   17  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J HIS A   18  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J MET A   19  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J ALA A   58  UNP  Q15084    CYS    58 ENGINEERED MUTATION            
SEQADV 3W8J MET B   -1  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J GLY B    0  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J SER B    1  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J SER B    2  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J HIS B    3  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J HIS B    4  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J HIS B    5  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J HIS B    6  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J HIS B    7  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J HIS B    8  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J SER B    9  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J SER B   10  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J GLY B   11  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J LEU B   12  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J VAL B   13  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J PRO B   14  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J ARG B   15  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J GLY B   16  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J SER B   17  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J HIS B   18  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J MET B   19  UNP  Q15084              EXPRESSION TAG                 
SEQADV 3W8J ALA B   58  UNP  Q15084    CYS    58 ENGINEERED MUTATION            
SEQRES   1 A  142  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  142  LEU VAL PRO ARG GLY SER HIS MET LEU TYR SER SER SER          
SEQRES   3 A  142  ASP ASP VAL ILE GLU LEU THR PRO SER ASN PHE ASN ARG          
SEQRES   4 A  142  GLU VAL ILE GLN SER ASP SER LEU TRP LEU VAL GLU PHE          
SEQRES   5 A  142  TYR ALA PRO TRP CYS GLY HIS ALA GLN ARG LEU THR PRO          
SEQRES   6 A  142  GLU TRP LYS LYS ALA ALA THR ALA LEU LYS ASP VAL VAL          
SEQRES   7 A  142  LYS VAL GLY ALA VAL ASP ALA ASP LYS HIS HIS SER LEU          
SEQRES   8 A  142  GLY GLY GLN TYR GLY VAL GLN GLY PHE PRO THR ILE LYS          
SEQRES   9 A  142  ILE PHE GLY SER ASN LYS ASN ARG PRO GLU ASP TYR GLN          
SEQRES  10 A  142  GLY GLY ARG THR GLY GLU ALA ILE VAL ASP ALA ALA LEU          
SEQRES  11 A  142  SER ALA LEU ARG GLN LEU VAL LYS ASP ARG LEU GLY              
SEQRES   1 B  142  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  142  LEU VAL PRO ARG GLY SER HIS MET LEU TYR SER SER SER          
SEQRES   3 B  142  ASP ASP VAL ILE GLU LEU THR PRO SER ASN PHE ASN ARG          
SEQRES   4 B  142  GLU VAL ILE GLN SER ASP SER LEU TRP LEU VAL GLU PHE          
SEQRES   5 B  142  TYR ALA PRO TRP CYS GLY HIS ALA GLN ARG LEU THR PRO          
SEQRES   6 B  142  GLU TRP LYS LYS ALA ALA THR ALA LEU LYS ASP VAL VAL          
SEQRES   7 B  142  LYS VAL GLY ALA VAL ASP ALA ASP LYS HIS HIS SER LEU          
SEQRES   8 B  142  GLY GLY GLN TYR GLY VAL GLN GLY PHE PRO THR ILE LYS          
SEQRES   9 B  142  ILE PHE GLY SER ASN LYS ASN ARG PRO GLU ASP TYR GLN          
SEQRES  10 B  142  GLY GLY ARG THR GLY GLU ALA ILE VAL ASP ALA ALA LEU          
SEQRES  11 B  142  SER ALA LEU ARG GLN LEU VAL LYS ASP ARG LEU GLY              
SEQRES   1 C   20  HIS GLY GLU VAL CYS PRO ALA GLY TRP LYS PRO GLY SER          
SEQRES   2 C   20  GLU THR ILE ILE PRO ASP PRO                                  
SEQRES   1 D   20  HIS GLY GLU VAL CYS PRO ALA GLY TRP LYS PRO GLY SER          
SEQRES   2 D   20  GLU THR ILE ILE PRO ASP PRO                                  
HET      K  A 201       1                                                       
HET      K  A 202       1                                                       
HET    GOL  B 201       6                                                       
HET    GOL  B 202       6                                                       
HET    GOL  B 203       6                                                       
HET    GOL  B 204       6                                                       
HET      K  B 205       1                                                       
HET      K  B 206       1                                                       
HETNAM       K POTASSIUM ION                                                    
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5    K    4(K 1+)                                                      
FORMUL   7  GOL    4(C3 H8 O3)                                                  
FORMUL  13  HOH   *62(H2 O)                                                     
HELIX    1   1 ASN A   34  VAL A   39  1                                   6    
HELIX    2   2 CYS A   55  LEU A   72  1                                  18    
HELIX    3   3 HIS A   86  TYR A   93  1                                   8    
HELIX    4   4 THR A  119  GLY A  140  1                                  22    
HELIX    5   5 ASN B   34  VAL B   39  1                                   6    
HELIX    6   6 CYS B   55  LEU B   72  1                                  18    
HELIX    7   7 HIS B   86  TYR B   93  1                                   8    
HELIX    8   8 THR B  119  GLY B  140  1                                  22    
SHEET    1   A 5 ILE A  28  GLU A  29  0                                        
SHEET    2   A 5 LYS A  77  ASP A  82  1  O  VAL A  78   N  ILE A  28           
SHEET    3   A 5 TRP A  46  TYR A  51  1  N  LEU A  47   O  GLY A  79           
SHEET    4   A 5 THR A 100  PHE A 104 -1  O  PHE A 104   N  TRP A  46           
SHEET    5   A 5 GLU A 112  ASP A 113 -1  O  GLU A 112   N  ILE A 103           
SHEET    1   B 2 GLY A  97  PHE A  98  0                                        
SHEET    2   B 2 CYS C   2  PRO C   3 -1  O  CYS C   2   N  PHE A  98           
SHEET    1   C 5 ILE B  28  LEU B  30  0                                        
SHEET    2   C 5 LYS B  77  ASP B  82  1  O  ALA B  80   N  LEU B  30           
SHEET    3   C 5 TRP B  46  TYR B  51  1  N  LEU B  47   O  GLY B  79           
SHEET    4   C 5 THR B 100  PHE B 104 -1  O  THR B 100   N  PHE B  50           
SHEET    5   C 5 GLU B 112  TYR B 114 -1  O  GLU B 112   N  ILE B 103           
SHEET    1   D 2 GLY B  97  PHE B  98  0                                        
SHEET    2   D 2 CYS D   2  PRO D   3 -1  O  CYS D   2   N  PHE B  98           
SSBOND   1 CYS A   55    CYS C    2                          1555   1555  2.07  
SSBOND   2 CYS B   55    CYS D    2                          1555   1555  2.06  
LINK         O   VAL B  27                 K     K B 206     1555   1555  2.57  
LINK         O   SER B  22                 K     K B 206     1555   1555  2.58  
LINK         OE2 GLU A  49                 K     K A 201     1555   1555  2.68  
LINK         O   ALA B  58                 K     K B 205     1555   1555  2.70  
LINK         O   ALA A  58                 K     K A 201     1555   1555  2.73  
LINK         O   SER A  22                 K     K A 202     1555   1555  2.74  
LINK         OH  TYR A  21                 K     K A 201     1555   1555  2.74  
LINK         OG1 THR B  62                 K     K B 205     1555   1555  2.76  
LINK         OG1 THR A  62                 K     K A 201     1555   1555  2.79  
LINK         O   VAL A  27                 K     K A 202     1555   1555  2.80  
LINK         OE2 GLU B  49                 K     K B 205     1555   1555  2.82  
LINK         O   ASP A  25                 K     K A 202     1555   1555  2.88  
LINK         O   ASP B  25                 K     K B 206     1555   1555  2.89  
LINK         OD1 ASP B  25                 K     K B 206     1555   1555  3.05  
LINK         OH  TYR B  21                 K     K B 205     1555   1555  3.12  
LINK         OE1 GLU A  49                 K     K A 201     1555   1555  3.23  
LINK         OD1 ASP A  25                 K     K A 202     1555   1555  3.35  
LINK         OE1 GLU B  49                 K     K B 205     1555   1555  3.48  
CISPEP   1 PHE A   98    PRO A   99          0        -2.46                     
CISPEP   2 PHE B   98    PRO B   99          0        -6.30                     
SITE     1 AC1  4 TYR A  21  GLU A  49  ALA A  58  THR A  62                    
SITE     1 AC2  3 SER A  22  ASP A  25  VAL A  27                               
SITE     1 AC3  5 ILE B  40  ASN B 109  GLU B 121  ALA B 122                    
SITE     2 AC3  5 ASP B 125                                                     
SITE     1 AC4  3 GLN A  41  ASP B 137  HOH B 330                               
SITE     1 AC5  5 ALA B  83  VAL B  95  PHE B  98  GLY D   5                    
SITE     2 AC5  5 HOH D 102                                                     
SITE     1 AC6  2 GLN B  96  HOH D 102                                          
SITE     1 AC7  5 LEU B  20  TYR B  21  GLU B  49  ALA B  58                    
SITE     2 AC7  5 THR B  62                                                     
SITE     1 AC8  4 SER B  22  SER B  23  ASP B  25  VAL B  27                    
CRYST1   39.045   53.375  133.353  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.025611  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018735  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007499        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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