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Database: PDB
Entry: 2XXZ
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HEADER    OXIDOREDUCTASE                          12-NOV-10   2XXZ              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN JMJD3 JUMONJI DOMAIN                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LYSINE-SPECIFIC DEMETHYLASE 6B;                            
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: JUMONJI DOMAIN, RESIDUES 1173-1502;                        
COMPND   5 SYNONYM: JMJD3, JMJC DOMAIN-CONTAINING PROTEIN 3, JUMONJI DOMAIN-    
COMPND   6 CONTAINING PROTEIN 3, LYSINE DEMETHYLASE 6B;                         
COMPND   7 EC: 1.14.11.-;                                                       
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3-PRARE2;                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    OXIDOREDUCTASE, HISTONE DEMETHYLATION, OXYGENASE, CHROMATIN           
KEYWDS   2 MODIFICATION                                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.H.CHE,W.W.YUE,T.KROJER,J.R.C.MUNIZ,S.S.NG,A.TUMBER,M.DANIEL,        
AUTHOR   2 N.BURGESS-BROWN,P.SAVITSKY,E.UGOCHUKWU,P.FILIPPAKOPOULOS,            
AUTHOR   3 C.ARROWSMITH,J.WEIGELT,A.EDWARDS,C.BOUNTRA,U.OPPERMANN               
REVDAT   4   24-JAN-18 2XXZ    1       JRNL                                     
REVDAT   3   14-JAN-15 2XXZ    1       REMARK VERSN  FORMUL                     
REVDAT   2   01-DEC-10 2XXZ    1       JRNL                                     
REVDAT   1   24-NOV-10 2XXZ    0                                                
JRNL        AUTH   K.H.CHE,W.W.YUE,T.KROJER,J.R.C.MUNIZ,S.S.NG,A.TUMBER,        
JRNL        AUTH 2 M.DANIEL,N.BURGESS-BROWN,P.SAVITSKY,F.VON DELFT,E.UGOCHUKWU, 
JRNL        AUTH 3 P.FILIPPAKOPOULOS,C.ARROWSMITH,J.WEIGELT,A.EDWARDS,          
JRNL        AUTH 4 C.BOUNTRA,U.OPPERMANN                                        
JRNL        TITL   CRYSTAL STRUCTURE OF THE HUMAN JMJD3 JUMONJI DOMAIN          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0110                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.16                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 61100                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.185                           
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.216                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3016                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4968                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.60                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3330                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 265                          
REMARK   3   BIN FREE R VALUE                    : 0.3480                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4612                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 52                                      
REMARK   3   SOLVENT ATOMS            : 319                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.88                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.19000                                              
REMARK   3    B22 (A**2) : 1.26000                                              
REMARK   3    B33 (A**2) : -1.45000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.103         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.102         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.079         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.236         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.953                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4906 ; 0.013 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  3250 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6714 ; 1.351 ; 1.931       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7900 ; 1.053 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   603 ; 5.971 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   232 ;33.913 ;24.095       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   761 ;13.374 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    27 ;20.631 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   723 ; 0.087 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5506 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1006 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2949 ; 1.688 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1178 ; 0.404 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4804 ; 2.871 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1957 ; 4.105 ; 7.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1902 ; 6.069 ;11.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 10                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1175        A  1212                          
REMARK   3    ORIGIN FOR THE GROUP (A):  49.9007  48.2989 -13.8463              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1221 T22:   0.1863                                     
REMARK   3      T33:   0.1533 T12:   0.0021                                     
REMARK   3      T13:   0.0054 T23:  -0.0150                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9421 L22:   0.9109                                     
REMARK   3      L33:   1.5247 L12:   0.4975                                     
REMARK   3      L13:  -0.0145 L23:  -0.5395                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0088 S12:   0.0763 S13:  -0.0191                       
REMARK   3      S21:  -0.0143 S22:  -0.0187 S23:  -0.0221                       
REMARK   3      S31:   0.1225 S32:   0.0794 S33:   0.0275                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1213        A  1246                          
REMARK   3    ORIGIN FOR THE GROUP (A):  51.9917  54.4655  10.4149              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0821 T22:   0.2205                                     
REMARK   3      T33:   0.1761 T12:   0.0026                                     
REMARK   3      T13:  -0.0006 T23:   0.0065                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9288 L22:   0.6320                                     
REMARK   3      L33:   2.1837 L12:   0.2186                                     
REMARK   3      L13:   0.0690 L23:  -0.4078                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0125 S12:  -0.0564 S13:   0.0542                       
REMARK   3      S21:   0.0783 S22:   0.0089 S23:   0.0193                       
REMARK   3      S31:  -0.1193 S32:  -0.0452 S33:   0.0037                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1247        A  1266                          
REMARK   3    ORIGIN FOR THE GROUP (A):  50.3588  26.0087   9.8115              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6595 T22:   0.2147                                     
REMARK   3      T33:   0.1692 T12:   0.1830                                     
REMARK   3      T13:   0.0368 T23:   0.0634                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2658 L22:   3.2935                                     
REMARK   3      L33:   3.9547 L12:  -0.6355                                     
REMARK   3      L13:   1.1018 L23:  -2.7949                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2004 S12:  -0.5539 S13:  -0.5901                       
REMARK   3      S21:   0.1186 S22:   0.1108 S23:  -0.0687                       
REMARK   3      S31:   0.9193 S32:   0.2853 S33:   0.0895                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1267        A  1325                          
REMARK   3    ORIGIN FOR THE GROUP (A):  57.1112  43.7475  18.2481              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1433 T22:   0.2251                                     
REMARK   3      T33:   0.1621 T12:  -0.0005                                     
REMARK   3      T13:   0.0015 T23:   0.0230                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8404 L22:   1.6504                                     
REMARK   3      L33:   0.8267 L12:   0.7802                                     
REMARK   3      L13:   0.2240 L23:  -0.2082                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0158 S12:  -0.1324 S13:  -0.1712                       
REMARK   3      S21:   0.1060 S22:   0.0501 S23:  -0.0792                       
REMARK   3      S31:   0.1585 S32:   0.0094 S33:  -0.0343                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A  1326        A  1493                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.9322  46.4734   0.7549              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0967 T22:   0.1790                                     
REMARK   3      T33:   0.1737 T12:  -0.0196                                     
REMARK   3      T13:   0.0058 T23:   0.0067                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4915 L22:   0.4974                                     
REMARK   3      L33:   1.3970 L12:  -0.2375                                     
REMARK   3      L13:   0.2676 L23:  -0.0337                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0089 S12:  -0.0481 S13:  -0.0337                       
REMARK   3      S21:   0.0388 S22:   0.0002 S23:   0.0571                       
REMARK   3      S31:   0.1048 S32:  -0.1377 S33:  -0.0091                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B  1175        B  1214                          
REMARK   3    ORIGIN FOR THE GROUP (A):  45.1405  48.7691 -24.7710              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1437 T22:   0.2070                                     
REMARK   3      T33:   0.1441 T12:  -0.0160                                     
REMARK   3      T13:   0.0144 T23:  -0.0120                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7773 L22:   1.5465                                     
REMARK   3      L33:   2.0369 L12:  -0.3633                                     
REMARK   3      L13:  -0.0048 L23:   0.4381                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0240 S12:  -0.0274 S13:   0.0344                       
REMARK   3      S21:   0.0251 S22:  -0.0574 S23:   0.0768                       
REMARK   3      S31:   0.1793 S32:  -0.1424 S33:   0.0334                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B  1215        B  1251                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.5983  54.9251 -48.0549              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2845 T22:   0.2245                                     
REMARK   3      T33:   0.1440 T12:  -0.0666                                     
REMARK   3      T13:  -0.0699 T23:   0.0285                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5921 L22:   2.1619                                     
REMARK   3      L33:   1.9935 L12:   1.7165                                     
REMARK   3      L13:   0.8351 L23:   0.4508                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3125 S12:   0.2302 S13:   0.1558                       
REMARK   3      S21:  -0.5474 S22:   0.2617 S23:   0.2052                       
REMARK   3      S31:  -0.0721 S32:  -0.0632 S33:   0.0507                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B  1252        B  1354                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.3729  48.8428 -49.7312              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2733 T22:   0.2152                                     
REMARK   3      T33:   0.0858 T12:  -0.0602                                     
REMARK   3      T13:  -0.0074 T23:  -0.0123                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5628 L22:   2.4398                                     
REMARK   3      L33:   1.5072 L12:   1.3623                                     
REMARK   3      L13:   0.6305 L23:   0.7672                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2874 S12:   0.2774 S13:   0.0317                       
REMARK   3      S21:  -0.6007 S22:   0.2210 S23:   0.0365                       
REMARK   3      S31:  -0.1097 S32:  -0.0194 S33:   0.0664                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B  1355        B  1484                          
REMARK   3    ORIGIN FOR THE GROUP (A):  44.9821  40.8140 -38.8798              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2052 T22:   0.1149                                     
REMARK   3      T33:   0.1349 T12:  -0.0051                                     
REMARK   3      T13:   0.0002 T23:  -0.0142                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4453 L22:   1.3847                                     
REMARK   3      L33:   1.9709 L12:   0.0974                                     
REMARK   3      L13:   0.4831 L23:   0.1002                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0194 S12:   0.0481 S13:  -0.0411                       
REMARK   3      S21:  -0.1735 S22:   0.0302 S23:   0.0014                       
REMARK   3      S31:   0.1962 S32:   0.0161 S33:  -0.0108                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B  1485        B  1499                          
REMARK   3    ORIGIN FOR THE GROUP (A):  63.5671  58.4688 -24.1731              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1075 T22:   0.2649                                     
REMARK   3      T33:   0.2163 T12:  -0.0099                                     
REMARK   3      T13:  -0.0202 T23:   0.0250                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0776 L22:   3.7115                                     
REMARK   3      L33:   5.5379 L12:   0.4430                                     
REMARK   3      L13:   2.1406 L23:   0.4130                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0369 S12:   0.2432 S13:  -0.0511                       
REMARK   3      S21:  -0.0560 S22:  -0.1332 S23:  -0.2793                       
REMARK   3      S31:  -0.3745 S32:   0.5131 S33:   0.1701                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 2XXZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-NOV-10.                  
REMARK 100 THE DEPOSITION ID IS D_1290046225.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JUN-10                          
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               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : SI (111)                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 61104                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.160                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.96000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       28.37850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       79.84900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.71550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       79.84900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.37850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.71550            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A  1171                                                      
REMARK 465     MET A  1172                                                      
REMARK 465     LEU A  1173                                                      
REMARK 465     PRO A  1174                                                      
REMARK 465     LYS A  1293                                                      
REMARK 465     GLU A  1294                                                      
REMARK 465     SER A  1295                                                      
REMARK 465     GLU A  1296                                                      
REMARK 465     ASP A  1297                                                      
REMARK 465     GLU A  1298                                                      
REMARK 465     GLU A  1299                                                      
REMARK 465     SER A  1300                                                      
REMARK 465     GLU A  1301                                                      
REMARK 465     GLU A  1302                                                      
REMARK 465     PRO A  1303                                                      
REMARK 465     ASP A  1304                                                      
REMARK 465     SER A  1305                                                      
REMARK 465     THR A  1306                                                      
REMARK 465     THR A  1307                                                      
REMARK 465     GLY A  1308                                                      
REMARK 465     THR A  1309                                                      
REMARK 465     PRO A  1310                                                      
REMARK 465     PRO A  1311                                                      
REMARK 465     SER A  1312                                                      
REMARK 465     SER A  1313                                                      
REMARK 465     ALA A  1314                                                      
REMARK 465     PRO A  1315                                                      
REMARK 465     ASP A  1316                                                      
REMARK 465     PRO A  1317                                                      
REMARK 465     LYS A  1318                                                      
REMARK 465     ASN A  1319                                                      
REMARK 465     LEU A  1494                                                      
REMARK 465     GLU A  1495                                                      
REMARK 465     ARG A  1496                                                      
REMARK 465     TYR A  1497                                                      
REMARK 465     GLU A  1498                                                      
REMARK 465     TRP A  1499                                                      
REMARK 465     ASN A  1500                                                      
REMARK 465     GLU A  1501                                                      
REMARK 465     VAL A  1502                                                      
REMARK 465     SER B  1171                                                      
REMARK 465     MET B  1172                                                      
REMARK 465     LEU B  1173                                                      
REMARK 465     PRO B  1174                                                      
REMARK 465     GLU B  1291                                                      
REMARK 465     GLU B  1292                                                      
REMARK 465     LYS B  1293                                                      
REMARK 465     GLU B  1294                                                      
REMARK 465     SER B  1295                                                      
REMARK 465     GLU B  1296                                                      
REMARK 465     ASP B  1297                                                      
REMARK 465     GLU B  1298                                                      
REMARK 465     GLU B  1299                                                      
REMARK 465     SER B  1300                                                      
REMARK 465     GLU B  1301                                                      
REMARK 465     GLU B  1302                                                      
REMARK 465     PRO B  1303                                                      
REMARK 465     ASP B  1304                                                      
REMARK 465     SER B  1305                                                      
REMARK 465     THR B  1306                                                      
REMARK 465     THR B  1307                                                      
REMARK 465     GLY B  1308                                                      
REMARK 465     THR B  1309                                                      
REMARK 465     PRO B  1310                                                      
REMARK 465     PRO B  1311                                                      
REMARK 465     SER B  1312                                                      
REMARK 465     SER B  1313                                                      
REMARK 465     ALA B  1314                                                      
REMARK 465     PRO B  1315                                                      
REMARK 465     ASP B  1316                                                      
REMARK 465     PRO B  1317                                                      
REMARK 465     LYS B  1318                                                      
REMARK 465     ASN B  1319                                                      
REMARK 465     GLY B  1357                                                      
REMARK 465     ASN B  1358                                                      
REMARK 465     MET B  1359                                                      
REMARK 465     LEU B  1360                                                      
REMARK 465     SER B  1361                                                      
REMARK 465     HIS B  1362                                                      
REMARK 465     VAL B  1363                                                      
REMARK 465     GLY B  1364                                                      
REMARK 465     HIS B  1365                                                      
REMARK 465     THR B  1366                                                      
REMARK 465     ASN B  1500                                                      
REMARK 465     GLU B  1501                                                      
REMARK 465     VAL B  1502                                                      
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     ARG A1175    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1177    CE   NZ                                             
REMARK 470     ARG A1260    NE   CZ   NH1  NH2                                  
REMARK 470     GLU A1292    CG   CD   OE1  OE2                                  
REMARK 470     ARG B1175    NE   CZ   NH1  NH2                                  
REMARK 470     GLU B1176    CG   CD   OE1  OE2                                  
REMARK 470     ARG B1260    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS B1320    CG   ND1  CD2  CE1  NE2                             
REMARK 470     THR B1356    OG1  CG2                                            
REMARK 470     LEU B1368    CD1  CD2                                            
REMARK 470     GLU B1498    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B  2018     O    HOH B  2019              1.82            
REMARK 500   O    HOH A  2019     O    HOH B  2018              1.87            
REMARK 500   O    HOH B  2023     O    HOH B  2140              2.02            
REMARK 500   N    LEU B  1215     O    HOH B  2030              2.04            
REMARK 500   O    HOH A  2127     O    HOH A  2160              2.09            
REMARK 500   OE1  GLU A  1241     O    HOH A  2034              2.10            
REMARK 500   O    HOH B  2068     O    HOH B  2078              2.14            
REMARK 500   OD2  ASP A  1428     OG1  THR A  1431              2.15            
REMARK 500   O    HOH A  2105     O    HOH A  2107              2.16            
REMARK 500   OE2  GLU A  1412     O    HOH A  2120              2.19            
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   O    HOH B  2058     O    HOH B  2100     3754     2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A1179       60.60   -117.18                                   
REMARK 500    SER A1235       37.26   -155.60                                   
REMARK 500    SER A1355     -133.22     59.01                                   
REMARK 500    ASN B1179       61.37   -119.94                                   
REMARK 500    SER B1235       72.06   -157.33                                   
REMARK 500    THR B1272     -162.55   -162.79                                   
REMARK 500    ASP B1333       96.32    -68.50                                   
REMARK 500    ARG B1352      -51.48   -125.69                                   
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                              NI A2494  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 8XQ A3001   OAC                                                    
REMARK 620 2 8XQ A3001   NAI  83.8                                              
REMARK 620 3 HIS A1387   NE2  94.0  97.5                                        
REMARK 620 4 GLU A1389   OE2  85.6 167.4  90.0                                  
REMARK 620 5 HOH A2098   O   174.2  97.9  91.3  92.0                            
REMARK 620 6 HOH A2103   O    87.6  82.7 178.4  90.1  87.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A2495  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B2012   O                                                      
REMARK 620 2 HOH B2013   O    73.9                                              
REMARK 620 3 HOH B2011   O   101.6 167.9                                        
REMARK 620 4 GLU A1287   OE2 155.3  81.4 102.8                                  
REMARK 620 5 GLU B1188   OE1  83.9  79.5  88.9  92.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI A2500  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2054   O                                                      
REMARK 620 2 HOH A2060   O    87.7                                              
REMARK 620 3 HOH A2015   O    87.5 172.5                                        
REMARK 620 4 HOH B2150   O   179.4  91.7  93.1                                  
REMARK 620 5 HOH A2013   O    87.7  90.6  83.4  92.3                            
REMARK 620 6 HOH A2059   O    94.3  91.7  94.4  85.7 176.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI B2500  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B2155   O                                                      
REMARK 620 2 HOH B2083   O    88.4                                              
REMARK 620 3 GLU B1389   OE2  89.9  94.5                                        
REMARK 620 4 HIS B1387   NE2 178.3  92.0  88.5                                  
REMARK 620 5 8XQ B3001   NAI  83.0  97.4 165.9  98.5                            
REMARK 620 6 8XQ B3001   OAC  85.0 172.5  89.1  94.7  78.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 2494                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 2500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 2500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 2495                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2496                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2497                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2498                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2501                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2499                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 8XQ A 3001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 8XQ B 3001                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2XUE   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF JMJD3                                           
DBREF  2XXZ A 1173  1502  UNP    O15054   KDM6B_HUMAN   1173   1502             
DBREF  2XXZ B 1173  1502  UNP    O15054   KDM6B_HUMAN   1173   1502             
SEQADV 2XXZ SER A 1171  UNP  O15054              EXPRESSION TAG                 
SEQADV 2XXZ MET A 1172  UNP  O15054              EXPRESSION TAG                 
SEQADV 2XXZ SER B 1171  UNP  O15054              EXPRESSION TAG                 
SEQADV 2XXZ MET B 1172  UNP  O15054              EXPRESSION TAG                 
SEQRES   1 A  332  SER MET LEU PRO ARG GLU LYS LEU ASN PRO PRO THR PRO          
SEQRES   2 A  332  SER ILE TYR LEU GLU SER LYS ARG ASP ALA PHE SER PRO          
SEQRES   3 A  332  VAL LEU LEU GLN PHE CYS THR ASP PRO ARG ASN PRO ILE          
SEQRES   4 A  332  THR VAL ILE ARG GLY LEU ALA GLY SER LEU ARG LEU ASN          
SEQRES   5 A  332  LEU GLY LEU PHE SER THR LYS THR LEU VAL GLU ALA SER          
SEQRES   6 A  332  GLY GLU HIS THR VAL GLU VAL ARG THR GLN VAL GLN GLN          
SEQRES   7 A  332  PRO SER ASP GLU ASN TRP ASP LEU THR GLY THR ARG GLN          
SEQRES   8 A  332  ILE TRP PRO CYS GLU SER SER ARG SER HIS THR THR ILE          
SEQRES   9 A  332  ALA LYS TYR ALA GLN TYR GLN ALA SER SER PHE GLN GLU          
SEQRES  10 A  332  SER LEU GLN GLU GLU LYS GLU SER GLU ASP GLU GLU SER          
SEQRES  11 A  332  GLU GLU PRO ASP SER THR THR GLY THR PRO PRO SER SER          
SEQRES  12 A  332  ALA PRO ASP PRO LYS ASN HIS HIS ILE ILE LYS PHE GLY          
SEQRES  13 A  332  THR ASN ILE ASP LEU SER ASP ALA LYS ARG TRP LYS PRO          
SEQRES  14 A  332  GLN LEU GLN GLU LEU LEU LYS LEU PRO ALA PHE MET ARG          
SEQRES  15 A  332  VAL THR SER THR GLY ASN MET LEU SER HIS VAL GLY HIS          
SEQRES  16 A  332  THR ILE LEU GLY MET ASN THR VAL GLN LEU TYR MET LYS          
SEQRES  17 A  332  VAL PRO GLY SER ARG THR PRO GLY HIS GLN GLU ASN ASN          
SEQRES  18 A  332  ASN PHE CYS SER VAL ASN ILE ASN ILE GLY PRO GLY ASP          
SEQRES  19 A  332  CYS GLU TRP PHE ALA VAL HIS GLU HIS TYR TRP GLU THR          
SEQRES  20 A  332  ILE SER ALA PHE CYS ASP ARG HIS GLY VAL ASP TYR LEU          
SEQRES  21 A  332  THR GLY SER TRP TRP PRO ILE LEU ASP ASP LEU TYR ALA          
SEQRES  22 A  332  SER ASN ILE PRO VAL TYR ARG PHE VAL GLN ARG PRO GLY          
SEQRES  23 A  332  ASP LEU VAL TRP ILE ASN ALA GLY THR VAL HIS TRP VAL          
SEQRES  24 A  332  GLN ALA THR GLY TRP CYS ASN ASN ILE ALA TRP ASN VAL          
SEQRES  25 A  332  GLY PRO LEU THR ALA TYR GLN TYR GLN LEU ALA LEU GLU          
SEQRES  26 A  332  ARG TYR GLU TRP ASN GLU VAL                                  
SEQRES   1 B  332  SER MET LEU PRO ARG GLU LYS LEU ASN PRO PRO THR PRO          
SEQRES   2 B  332  SER ILE TYR LEU GLU SER LYS ARG ASP ALA PHE SER PRO          
SEQRES   3 B  332  VAL LEU LEU GLN PHE CYS THR ASP PRO ARG ASN PRO ILE          
SEQRES   4 B  332  THR VAL ILE ARG GLY LEU ALA GLY SER LEU ARG LEU ASN          
SEQRES   5 B  332  LEU GLY LEU PHE SER THR LYS THR LEU VAL GLU ALA SER          
SEQRES   6 B  332  GLY GLU HIS THR VAL GLU VAL ARG THR GLN VAL GLN GLN          
SEQRES   7 B  332  PRO SER ASP GLU ASN TRP ASP LEU THR GLY THR ARG GLN          
SEQRES   8 B  332  ILE TRP PRO CYS GLU SER SER ARG SER HIS THR THR ILE          
SEQRES   9 B  332  ALA LYS TYR ALA GLN TYR GLN ALA SER SER PHE GLN GLU          
SEQRES  10 B  332  SER LEU GLN GLU GLU LYS GLU SER GLU ASP GLU GLU SER          
SEQRES  11 B  332  GLU GLU PRO ASP SER THR THR GLY THR PRO PRO SER SER          
SEQRES  12 B  332  ALA PRO ASP PRO LYS ASN HIS HIS ILE ILE LYS PHE GLY          
SEQRES  13 B  332  THR ASN ILE ASP LEU SER ASP ALA LYS ARG TRP LYS PRO          
SEQRES  14 B  332  GLN LEU GLN GLU LEU LEU LYS LEU PRO ALA PHE MET ARG          
SEQRES  15 B  332  VAL THR SER THR GLY ASN MET LEU SER HIS VAL GLY HIS          
SEQRES  16 B  332  THR ILE LEU GLY MET ASN THR VAL GLN LEU TYR MET LYS          
SEQRES  17 B  332  VAL PRO GLY SER ARG THR PRO GLY HIS GLN GLU ASN ASN          
SEQRES  18 B  332  ASN PHE CYS SER VAL ASN ILE ASN ILE GLY PRO GLY ASP          
SEQRES  19 B  332  CYS GLU TRP PHE ALA VAL HIS GLU HIS TYR TRP GLU THR          
SEQRES  20 B  332  ILE SER ALA PHE CYS ASP ARG HIS GLY VAL ASP TYR LEU          
SEQRES  21 B  332  THR GLY SER TRP TRP PRO ILE LEU ASP ASP LEU TYR ALA          
SEQRES  22 B  332  SER ASN ILE PRO VAL TYR ARG PHE VAL GLN ARG PRO GLY          
SEQRES  23 B  332  ASP LEU VAL TRP ILE ASN ALA GLY THR VAL HIS TRP VAL          
SEQRES  24 B  332  GLN ALA THR GLY TRP CYS ASN ASN ILE ALA TRP ASN VAL          
SEQRES  25 B  332  GLY PRO LEU THR ALA TYR GLN TYR GLN LEU ALA LEU GLU          
SEQRES  26 B  332  ARG TYR GLU TRP ASN GLU VAL                                  
HET     NI  A2494       1                                                       
HET     NA  A2495       1                                                       
HET     NI  A2500       1                                                       
HET    EDO  A2496       4                                                       
HET    EDO  A2497       4                                                       
HET    EDO  A2498       4                                                       
HET    EDO  A2499       4                                                       
HET    8XQ  A3001      14                                                       
HET     NI  B2500       1                                                       
HET    EDO  B2501       4                                                       
HET    8XQ  B3001      14                                                       
HETNAM      NI NICKEL (II) ION                                                  
HETNAM      NA SODIUM ION                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     8XQ 8-HYDROXYQUINOLINE-5-CARBOXYLIC ACID                             
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3   NI    3(NI 2+)                                                     
FORMUL   4   NA    NA 1+                                                        
FORMUL   6  EDO    5(C2 H6 O2)                                                  
FORMUL  10  8XQ    2(C10 H7 N O3)                                               
FORMUL  14  HOH   *319(H2 O)                                                    
HELIX    1   1 SER A 1189  ALA A 1193  5                                   5    
HELIX    2   2 SER A 1195  ASP A 1204  1                                  10    
HELIX    3   3 GLY A 1214  ARG A 1220  1                                   7    
HELIX    4   4 ASN A 1222  PHE A 1226  5                                   5    
HELIX    5   5 SER A 1227  GLY A 1236  1                                  10    
HELIX    6   6 ILE A 1274  GLU A 1287  1                                  14    
HELIX    7   7 ASP A 1333  LEU A 1345  1                                  13    
HELIX    8   8 PRO A 1348  ARG A 1352  5                                   5    
HELIX    9   9 GLU A 1389  PHE A 1393  5                                   5    
HELIX   10  10 HIS A 1411  HIS A 1413  5                                   3    
HELIX   11  11 TYR A 1414  HIS A 1425  1                                  12    
HELIX   12  12 ILE A 1437  SER A 1444  1                                   8    
HELIX   13  13 ALA A 1487  ALA A 1493  5                                   7    
HELIX   14  14 ARG B 1175  ASN B 1179  5                                   5    
HELIX   15  15 SER B 1189  SER B 1195  1                                   7    
HELIX   16  16 SER B 1195  ASP B 1204  1                                  10    
HELIX   17  17 GLY B 1214  ARG B 1220  1                                   7    
HELIX   18  18 ASN B 1222  PHE B 1226  5                                   5    
HELIX   19  19 SER B 1227  GLY B 1236  1                                  10    
HELIX   20  20 ILE B 1274  GLN B 1290  1                                  17    
HELIX   21  21 TRP B 1337  LEU B 1345  1                                   9    
HELIX   22  22 PRO B 1348  ARG B 1352  5                                   5    
HELIX   23  23 GLU B 1389  PHE B 1393  5                                   5    
HELIX   24  24 HIS B 1411  HIS B 1413  5                                   3    
HELIX   25  25 TYR B 1414  HIS B 1425  1                                  12    
HELIX   26  26 ILE B 1437  SER B 1444  1                                   8    
HELIX   27  27 THR B 1486  TRP B 1499  1                                  14    
SHEET    1  AA 9 SER A1184  TYR A1186  0                                        
SHEET    2  AA 9 ILE A1209  ARG A1213  1  O  VAL A1211   N  ILE A1185           
SHEET    3  AA 9 LEU A1458  ILE A1461 -1  O  LEU A1458   N  ILE A1212           
SHEET    4  AA 9 CYS A1394  PRO A1402 -1  O  SER A1395   N  ILE A1461           
SHEET    5  AA 9 CYS A1475  GLY A1483 -1  O  ASN A1476   N  ILE A1400           
SHEET    6  AA 9 VAL A1373  LYS A1378 -1  O  GLN A1374   N  ALA A1479           
SHEET    7  AA 9 ILE A1322  ASP A1330 -1  O  GLY A1326   N  MET A1377           
SHEET    8  AA 9 THR A1239  VAL A1246 -1  O  GLU A1241   N  THR A1327           
SHEET    9  AA 9 SER A1268  THR A1273 -1  O  SER A1268   N  THR A1244           
SHEET    1  AB 2 SER A1361  HIS A1362  0                                        
SHEET    2  AB 2 HIS A1365  THR A1366 -1  O  HIS A1365   N  HIS A1362           
SHEET    1  AC 4 ARG A1383  HIS A1387  0                                        
SHEET    2  AC 4 VAL A1466  ALA A1471 -1  O  HIS A1467   N  HIS A1387           
SHEET    3  AC 4 CYS A1405  VAL A1410 -1  O  GLU A1406   N  GLN A1470           
SHEET    4  AC 4 TYR A1449  GLN A1453 -1  O  TYR A1449   N  ALA A1409           
SHEET    1  BA 9 SER B1184  TYR B1186  0                                        
SHEET    2  BA 9 ILE B1209  ARG B1213  1  O  VAL B1211   N  ILE B1185           
SHEET    3  BA 9 LEU B1458  ILE B1461 -1  O  LEU B1458   N  ILE B1212           
SHEET    4  BA 9 CYS B1394  PRO B1402 -1  O  SER B1395   N  ILE B1461           
SHEET    5  BA 9 CYS B1475  VAL B1482 -1  O  ASN B1476   N  ILE B1400           
SHEET    6  BA 9 GLN B1374  LYS B1378 -1  O  GLN B1374   N  ALA B1479           
SHEET    7  BA 9 ILE B1322  ASP B1330 -1  O  GLY B1326   N  MET B1377           
SHEET    8  BA 9 THR B1239  VAL B1246 -1  O  GLU B1241   N  THR B1327           
SHEET    9  BA 9 SER B1268  THR B1273 -1  O  SER B1268   N  THR B1244           
SHEET    1  BB 4 ARG B1383  HIS B1387  0                                        
SHEET    2  BB 4 VAL B1466  ALA B1471 -1  O  HIS B1467   N  HIS B1387           
SHEET    3  BB 4 CYS B1405  VAL B1410 -1  O  GLU B1406   N  GLN B1470           
SHEET    4  BB 4 TYR B1449  GLN B1453 -1  O  TYR B1449   N  ALA B1409           
LINK        NI    NI A2494                 OAC 8XQ A3001     1555   1555  2.07  
LINK        NI    NI A2494                 NAI 8XQ A3001     1555   1555  2.15  
LINK        NI    NI A2494                 NE2 HIS A1387     1555   1555  2.02  
LINK        NI    NI A2494                 OE2 GLU A1389     1555   1555  2.13  
LINK        NI    NI A2494                 O   HOH A2098     1555   1555  2.08  
LINK        NI    NI A2494                 O   HOH A2103     1555   1555  2.37  
LINK        NA    NA A2495                 O   HOH B2012     1555   4565  2.30  
LINK        NA    NA A2495                 O   HOH B2013     1555   4565  2.08  
LINK        NA    NA A2495                 O   HOH B2011     1555   4565  2.41  
LINK        NA    NA A2495                 OE2 GLU A1287     1555   1555  2.05  
LINK        NA    NA A2495                 OE1 GLU B1188     1555   4565  2.03  
LINK        NI    NI A2500                 O   HOH A2054     1555   1555  2.16  
LINK        NI    NI A2500                 O   HOH A2060     1555   1555  2.16  
LINK        NI    NI A2500                 O   HOH A2015     1555   4465  2.18  
LINK        NI    NI A2500                 O   HOH B2150     1555   4465  2.11  
LINK        NI    NI A2500                 O   HOH A2013     1555   4465  2.19  
LINK        NI    NI A2500                 O   HOH A2059     1555   1555  2.02  
LINK        NI    NI B2500                 O   HOH B2155     1555   1555  2.17  
LINK        NI    NI B2500                 O   HOH B2083     1555   1555  2.17  
LINK        NI    NI B2500                 OE2 GLU B1389     1555   1555  2.03  
LINK        NI    NI B2500                 NE2 HIS B1387     1555   1555  2.07  
LINK        NI    NI B2500                 NAI 8XQ B3001     1555   1555  2.15  
LINK        NI    NI B2500                 OAC 8XQ B3001     1555   1555  2.12  
CISPEP   1 GLY A 1401    PRO A 1402          0         2.40                     
CISPEP   2 GLY B 1401    PRO B 1402          0         4.84                     
SITE     1 AC1  5 HIS A1387  GLU A1389  HOH A2098  HOH A2103                    
SITE     2 AC1  5 8XQ A3001                                                     
SITE     1 AC2  6 HOH A2013  HOH A2015  HOH A2054  HOH A2059                    
SITE     2 AC2  6 HOH A2060  HOH B2150                                          
SITE     1 AC3  5 HIS B1387  GLU B1389  HOH B2083  HOH B2155                    
SITE     2 AC3  5 8XQ B3001                                                     
SITE     1 AC4  5 GLU A1287  GLU B1188  HOH B2011  HOH B2012                    
SITE     2 AC4  5 HOH B2013                                                     
SITE     1 AC5  4 ILE A1185  TYR A1186  GLN B1200  HOH B2020                    
SITE     1 AC6  7 ASP A1204  GLN A1489  HOH A2163  HOH A2164                    
SITE     2 AC6  7 PRO B1183  SER B1184  PHE B1201                               
SITE     1 AC7  3 ASP A1330  MET A1370  HOH A2015                               
SITE     1 AC8  4 ARG A1191  LYS B1190  ARG B1191  TYR B1497                    
SITE     1 AC9  4 SER A1227  THR A1228  GLY A1401  ASN A1476                    
SITE     1 BC1 12 TYR A1376  LYS A1378  THR A1384  HIS A1387                    
SITE     2 BC1 12 GLU A1389  ASN A1397  TRP A1407  ILE A1461                    
SITE     3 BC1 12 HIS A1467  ASN A1477  HOH A2103   NI A2494                    
SITE     1 BC2 11 TYR B1376  LYS B1378  THR B1384  HIS B1387                    
SITE     2 BC2 11 GLU B1389  ASN B1397  TRP B1407  HIS B1467                    
SITE     3 BC2 11 HOH B2091  HOH B2155   NI B2500                               
CRYST1   56.757   71.431  159.698  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      0.017619  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006262        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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