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Database: PDB
Entry: 4NR2
LinkDB: 4NR2
Original site: 4NR2 
HEADER    TRANSFERASE                             26-NOV-13   4NR2              
TITLE     CRYSTAL STRUCTURE OF STK4 (MST1) SARAH DOMAIN                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE 4;                         
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 FRAGMENT: SARAH DOMAIN, UNP RESIDUES 432-480;                        
COMPND   5 SYNONYM: MAMMALIAN STE20-LIKE PROTEIN KINASE 1, MST-1, STE20-LIKE    
COMPND   6 KINASE MST1, SERINE/THREONINE-PROTEIN KINASE KRS-2, SERINE/THREONINE-
COMPND   7 PROTEIN KINASE 4 37KDA SUBUNIT, MST1/N, SERINE/THREONINE-PROTEIN     
COMPND   8 KINASE 4 18KDA SUBUNIT, MST1/C;                                      
COMPND   9 EC: 2.7.11.1;                                                        
COMPND  10 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: KRS2, MST1, STK4;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, SARAH       
KEYWDS   2 DOMAIN, STK3, MST2, HEPTAD REPEAT, STK4, MST1, TRANSFERASE           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.CHAIKUAD,T.KROJER,J.KOPEC,F.VON DELFT,C.H.ARROWSMITH,A.M.EDWARDS,   
AUTHOR   2 C.BOUNTRA,S.KNAPP,STRUCTURAL GENOMICS CONSORTIUM (SGC)               
REVDAT   2   31-JAN-18 4NR2    1       AUTHOR JRNL                              
REVDAT   1   29-JAN-14 4NR2    0                                                
JRNL        AUTH   A.CHAIKUAD,T.KROJER,J.KOPEC,F.VON DELFT,C.H.ARROWSMITH,      
JRNL        AUTH 2 A.M.EDWARDS,C.BOUNTRA,S.KNAPP,                               
JRNL        AUTH 3 STRUCTURAL GENOMICS CONSORTIUM (SGC)                         
JRNL        TITL   CRYSTAL STRUCTURE OF STK4 (MST1) SARAH DOMAIN                
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 55.27                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 32937                          
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) : 0.209                           
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.240                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1736                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2401                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.45                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3150                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 122                          
REMARK   3   BIN FREE R VALUE                    : 0.3620                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3358                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 223                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 34.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.84                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.90000                                              
REMARK   3    B22 (A**2) : 0.77000                                              
REMARK   3    B33 (A**2) : -3.66000                                             
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): 0.192         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.165         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.138         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.132        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.942                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3527 ; 0.016 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  3524 ; 0.010 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4720 ; 1.592 ; 2.002       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8163 ; 1.596 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   414 ; 4.840 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   187 ;38.188 ;25.401       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   759 ;14.092 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;15.799 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   508 ; 0.088 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3830 ; 0.010 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   726 ; 0.009 ; 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):  1608 ; 2.252 ; 2.603       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1607 ; 2.251 ; 2.602       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2002 ; 3.256 ; 3.866       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2003 ; 3.255 ; 3.868       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1919 ; 3.826 ; 3.095       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1919 ; 3.825 ; 3.095       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2707 ; 6.005 ; 4.447       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  4286 ; 8.776 ;21.695       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  4287 ; 8.775 ;21.703       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 28                                
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A   434    479       B   434    479    2244  0.16  0.05     
REMARK   3    2     A    -1    480       C    -1    480    2724  0.12  0.05     
REMARK   3    3     A   432    479       D   432    479    2447  0.15  0.05     
REMARK   3    4     A    -1    480       E    -1    480    2753  0.10  0.05     
REMARK   3    5     A   434    479       F   434    479    2345  0.15  0.05     
REMARK   3    6     A    -1    480       G    -1    480    2534  0.16  0.05     
REMARK   3    7     A    -1    480       H    -1    480    2749  0.11  0.05     
REMARK   3    8     B   434    479       C   434    479    2329  0.13  0.05     
REMARK   3    9     B   434    479       D   434    479    2340  0.11  0.05     
REMARK   3   10     B   434    479       E   434    479    2294  0.13  0.05     
REMARK   3   11     B   434    480       F   434    480    2459  0.10  0.05     
REMARK   3   12     B   434    479       G   434    479    2364  0.12  0.05     
REMARK   3   13     B   434    479       H   434    479    2303  0.13  0.05     
REMARK   3   14     C   432    479       D   432    479    2480  0.13  0.05     
REMARK   3   15     C    -1    480       E    -1    480    2733  0.08  0.05     
REMARK   3   16     C   434    479       F   434    479    2353  0.13  0.05     
REMARK   3   17     C    -1    480       G    -1    480    2536  0.15  0.05     
REMARK   3   18     C    -1    480       H    -1    480    2776  0.10  0.05     
REMARK   3   19     D   432    479       E   432    479    2482  0.12  0.05     
REMARK   3   20     D   434    479       F   434    479    2469  0.10  0.05     
REMARK   3   21     D   432    479       G   432    479    2479  0.14  0.05     
REMARK   3   22     D   432    479       H   432    479    2474  0.14  0.05     
REMARK   3   23     E   434    479       F   434    479    2359  0.12  0.05     
REMARK   3   24     E    -1    480       G    -1    480    2536  0.16  0.05     
REMARK   3   25     E    -1    480       H    -1    480    2754  0.08  0.05     
REMARK   3   26     F   434    479       G   434    479    2446  0.12  0.05     
REMARK   3   27     F   434    479       H   434    479    2335  0.13  0.05     
REMARK   3   28     G    -1    480       H    -1    480    2548  0.16  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 13                                         
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    -1        A   457                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.2380  41.9940  57.5640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0255 T22:   0.1983                                     
REMARK   3      T33:   0.1280 T12:   0.0414                                     
REMARK   3      T13:   0.0185 T23:   0.0230                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7819 L22:   3.5192                                     
REMARK   3      L33:   5.1556 L12:   0.4488                                     
REMARK   3      L13:   1.1317 L23:  -1.8495                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0397 S12:  -0.0358 S13:   0.0602                       
REMARK   3      S21:  -0.0763 S22:   0.2566 S23:   0.1148                       
REMARK   3      S31:   0.0158 S32:  -0.3830 S33:  -0.2169                       
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   458        A   480                          
REMARK   3    ORIGIN FOR THE GROUP (A):  52.6130  27.2950  86.3580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2562 T22:   0.1396                                     
REMARK   3      T33:   0.1218 T12:   0.0462                                     
REMARK   3      T13:  -0.0391 T23:  -0.0120                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8300 L22:   1.4607                                     
REMARK   3      L33:  14.2065 L12:  -1.9469                                     
REMARK   3      L13:   4.5246 L23:  -3.7038                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1116 S12:  -0.1607 S13:  -0.1435                       
REMARK   3      S21:  -0.1076 S22:   0.1723 S23:   0.0200                       
REMARK   3      S31:   0.9330 S32:  -0.3768 S33:  -0.2839                       
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 :   B   434        B   439                          
REMARK   3    ORIGIN FOR THE GROUP (A):  64.5860  25.0480  96.8980              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9724 T22:   1.0356                                     
REMARK   3      T33:   0.4523 T12:   0.2622                                     
REMARK   3      T13:   0.0823 T23:   0.0010                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  13.3444 L22:   1.2627                                     
REMARK   3      L33:  12.1750 L12:   4.0185                                     
REMARK   3      L13:   9.5293 L23:   3.3837                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4940 S12:   0.1455 S13:  -1.0748                       
REMARK   3      S21:  -0.0620 S22:   0.0554 S23:  -0.1996                       
REMARK   3      S31:   0.4451 S32:  -0.3841 S33:   0.4386                       
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 :   B   440        B   480                          
REMARK   3    ORIGIN FOR THE GROUP (A):  51.4670  41.1790  77.1650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1166 T22:   0.1846                                     
REMARK   3      T33:   0.1335 T12:  -0.0267                                     
REMARK   3      T13:   0.0016 T23:  -0.0111                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1557 L22:   2.1593                                     
REMARK   3      L33:  11.8031 L12:  -1.4579                                     
REMARK   3      L13:   2.8685 L23:  -4.7905                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0673 S12:  -0.0323 S13:   0.1424                       
REMARK   3      S21:   0.1628 S22:  -0.0745 S23:  -0.1161                       
REMARK   3      S31:  -0.3949 S32:   0.1209 S33:   0.1418                       
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 :   C    -1        C   480                          
REMARK   3    ORIGIN FOR THE GROUP (A):  67.3720  57.4930  57.3450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1667 T22:   0.1651                                     
REMARK   3      T33:   0.1336 T12:   0.0296                                     
REMARK   3      T13:  -0.0776 T23:  -0.0024                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0076 L22:   0.3985                                     
REMARK   3      L33:   8.7559 L12:  -0.2068                                     
REMARK   3      L13:  -3.7882 L23:  -0.2317                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1251 S12:  -0.1462 S13:  -0.1219                       
REMARK   3      S21:  -0.1323 S22:  -0.0389 S23:   0.0817                       
REMARK   3      S31:   0.1410 S32:   0.2492 S33:  -0.0862                       
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 :   D   432        D   446                          
REMARK   3    ORIGIN FOR THE GROUP (A):  51.3610  53.8460  84.9790              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1220 T22:   0.3600                                     
REMARK   3      T33:   0.6025 T12:  -0.0380                                     
REMARK   3      T13:   0.0054 T23:   0.0902                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  14.7280 L22:   4.5243                                     
REMARK   3      L33:  11.5730 L12:  -0.3238                                     
REMARK   3      L13: -10.6172 L23:   4.4271                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0362 S12:  -0.3009 S13:  -0.0325                       
REMARK   3      S21:  -0.4911 S22:  -0.5357 S23:   0.6424                       
REMARK   3      S31:  -0.5277 S32:  -0.2638 S33:   0.4995                       
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 :   D   447        D   480                          
REMARK   3    ORIGIN FOR THE GROUP (A):  70.4610  49.9770  59.0100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1848 T22:   0.1724                                     
REMARK   3      T33:   0.2340 T12:   0.1010                                     
REMARK   3      T13:  -0.0940 T23:   0.0224                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2042 L22:   0.1565                                     
REMARK   3      L33:  14.9431 L12:   0.3850                                     
REMARK   3      L13:  -6.2308 L23:  -0.7359                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1593 S12:  -0.2651 S13:  -0.4547                       
REMARK   3      S21:  -0.0817 S22:  -0.1548 S23:  -0.0280                       
REMARK   3      S31:   0.8903 S32:   0.5599 S33:   0.3141                       
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 :   E    -1        E   480                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.7530  34.5600  50.3060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1611 T22:   0.1120                                     
REMARK   3      T33:   0.0804 T12:  -0.0012                                     
REMARK   3      T13:  -0.0093 T23:   0.0038                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2281 L22:   2.1421                                     
REMARK   3      L33:  11.0217 L12:  -0.5134                                     
REMARK   3      L13:  -0.0102 L23:  -2.5933                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0122 S12:  -0.0174 S13:   0.0336                       
REMARK   3      S21:  -0.1878 S22:   0.0213 S23:  -0.0180                       
REMARK   3      S31:   0.3555 S32:  -0.0439 S33:  -0.0336                       
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 :   F   434        F   480                          
REMARK   3    ORIGIN FOR THE GROUP (A):  54.4340  36.0120  41.0440              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1732 T22:   0.1669                                     
REMARK   3      T33:   0.1075 T12:  -0.0097                                     
REMARK   3      T13:  -0.0020 T23:  -0.0054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0604 L22:   3.5435                                     
REMARK   3      L33:  17.1565 L12:  -0.1821                                     
REMARK   3      L13:   0.7404 L23:  -5.2158                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0746 S12:   0.0099 S13:   0.0210                       
REMARK   3      S21:  -0.1436 S22:   0.0366 S23:  -0.0897                       
REMARK   3      S31:  -0.2255 S32:   0.6518 S33:   0.0380                       
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 :   G    -1        G   445                          
REMARK   3    ORIGIN FOR THE GROUP (A):  32.7490  14.9080  60.9370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1337 T22:   0.2047                                     
REMARK   3      T33:   0.2265 T12:  -0.2990                                     
REMARK   3      T13:   0.1906 T23:  -0.0003                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  28.1977 L22:   7.7081                                     
REMARK   3      L33:  18.4667 L12:  14.4794                                     
REMARK   3      L13:   5.0718 L23:   4.7754                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0143 S12:  -1.3156 S13:  -0.2679                       
REMARK   3      S21:   0.1027 S22:  -0.7593 S23:  -0.0171                       
REMARK   3      S31:   0.4158 S32:  -0.8622 S33:   0.7736                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   G   446        G   480                          
REMARK   3    ORIGIN FOR THE GROUP (A):  51.3330  22.8450  36.7120              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2386 T22:   0.1514                                     
REMARK   3      T33:   0.1158 T12:   0.0558                                     
REMARK   3      T13:  -0.0622 T23:   0.0223                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4935 L22:   1.9182                                     
REMARK   3      L33:  12.7538 L12:   1.6994                                     
REMARK   3      L13:  -5.2231 L23:  -2.4082                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0131 S12:  -0.1158 S13:  -0.0532                       
REMARK   3      S21:   0.2802 S22:   0.0379 S23:  -0.1694                       
REMARK   3      S31:   0.4096 S32:   0.4672 S33:  -0.0248                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H    -1        H   446                          
REMARK   3    ORIGIN FOR THE GROUP (A):  53.8820  28.4270  16.0030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1035 T22:   0.0975                                     
REMARK   3      T33:   0.1690 T12:  -0.0467                                     
REMARK   3      T13:  -0.0051 T23:  -0.0226                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0423 L22:   7.1636                                     
REMARK   3      L33:   6.8689 L12:  -3.1964                                     
REMARK   3      L13:  -2.4390 L23:   1.7412                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2512 S12:   0.0425 S13:  -0.1827                       
REMARK   3      S21:  -0.5135 S22:  -0.1745 S23:   0.1155                       
REMARK   3      S31:  -0.3813 S32:   0.2464 S33:  -0.0767                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   447        H   480                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.5630  25.6280  43.8910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2440 T22:   0.1539                                     
REMARK   3      T33:   0.0965 T12:  -0.1070                                     
REMARK   3      T13:   0.0187 T23:   0.0061                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6190 L22:   2.0856                                     
REMARK   3      L33:  10.4477 L12:   1.3599                                     
REMARK   3      L13:  -3.4993 L23:  -2.1890                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2003 S12:  -0.0091 S13:   0.1334                       
REMARK   3      S21:   0.3460 S22:  -0.0447 S23:   0.1366                       
REMARK   3      S31:   0.1564 S32:  -0.1741 S33:  -0.1557                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 4NR2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-DEC-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000083549.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-APR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.5                                
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) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : SI (111) DOUBLE CRYSTAL            
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34702                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 63.750                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : 0.06400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.76800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS                        
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.19                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.3M SODIUM FORMATE, 0.1M ACETATE PH     
REMARK 280  4.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277.15K             
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       27.63000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       72.37000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.87500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       72.37000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.63000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       31.87500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 300 REMARK: THE ASYMMETRIC UNIT CONSISTS OF FOUR DIMERS                  
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: 3390 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7300 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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: 3240 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7480 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2850 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7320 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
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: 3040 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7850 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
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 B    -1                                                      
REMARK 465     MET B     0                                                      
REMARK 465     ASP B   432                                                      
REMARK 465     TYR B   433                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     MET D     0                                                      
REMARK 465     SER F    -1                                                      
REMARK 465     MET F     0                                                      
REMARK 465     ASP F   432                                                      
REMARK 465     TYR F   433                                                      
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     GLU B 434    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 437    CG   CD   CE   NZ                                   
REMARK 470     SER C  -1    OG                                                  
REMARK 470     ASP D 432    CG   OD1  OD2                                       
REMARK 470     LYS E 437    CD   CE   NZ                                        
REMARK 470     GLU F 434    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   OE2  GLU D   442     O    HOH D   522              2.16            
REMARK 500   OH   TYR E   466     OE2  GLU F   458              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    SER D   438     NE2  GLN D   467     4466     2.11            
REMARK 500   OE2  GLU C   461     OD2  ASP H   443     3755     2.12            
REMARK 500   OD2  ASP C   443     OE2  GLU H   461     3755     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H 502                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4L0N   RELATED DB: PDB                                   
REMARK 900 SARAH DOMAIN OF MST2                                                 
DBREF  4NR2 A  432   480  UNP    Q13043   STK4_HUMAN     432    480             
DBREF  4NR2 B  432   480  UNP    Q13043   STK4_HUMAN     432    480             
DBREF  4NR2 C  432   480  UNP    Q13043   STK4_HUMAN     432    480             
DBREF  4NR2 D  432   480  UNP    Q13043   STK4_HUMAN     432    480             
DBREF  4NR2 E  432   480  UNP    Q13043   STK4_HUMAN     432    480             
DBREF  4NR2 F  432   480  UNP    Q13043   STK4_HUMAN     432    480             
DBREF  4NR2 G  432   480  UNP    Q13043   STK4_HUMAN     432    480             
DBREF  4NR2 H  432   480  UNP    Q13043   STK4_HUMAN     432    480             
SEQADV 4NR2 SER A   -1  UNP  Q13043              EXPRESSION TAG                 
SEQADV 4NR2 MET A    0  UNP  Q13043              EXPRESSION TAG                 
SEQADV 4NR2 SER B   -1  UNP  Q13043              EXPRESSION TAG                 
SEQADV 4NR2 MET B    0  UNP  Q13043              EXPRESSION TAG                 
SEQADV 4NR2 SER C   -1  UNP  Q13043              EXPRESSION TAG                 
SEQADV 4NR2 MET C    0  UNP  Q13043              EXPRESSION TAG                 
SEQADV 4NR2 SER D   -1  UNP  Q13043              EXPRESSION TAG                 
SEQADV 4NR2 MET D    0  UNP  Q13043              EXPRESSION TAG                 
SEQADV 4NR2 SER E   -1  UNP  Q13043              EXPRESSION TAG                 
SEQADV 4NR2 MET E    0  UNP  Q13043              EXPRESSION TAG                 
SEQADV 4NR2 SER F   -1  UNP  Q13043              EXPRESSION TAG                 
SEQADV 4NR2 MET F    0  UNP  Q13043              EXPRESSION TAG                 
SEQADV 4NR2 SER G   -1  UNP  Q13043              EXPRESSION TAG                 
SEQADV 4NR2 MET G    0  UNP  Q13043              EXPRESSION TAG                 
SEQADV 4NR2 SER H   -1  UNP  Q13043              EXPRESSION TAG                 
SEQADV 4NR2 MET H    0  UNP  Q13043              EXPRESSION TAG                 
SEQRES   1 A   51  SER MET ASP TYR GLU PHE LEU LYS SER TRP THR VAL GLU          
SEQRES   2 A   51  ASP LEU GLN LYS ARG LEU LEU ALA LEU ASP PRO MET MET          
SEQRES   3 A   51  GLU GLN GLU ILE GLU GLU ILE ARG GLN LYS TYR GLN SER          
SEQRES   4 A   51  LYS ARG GLN PRO ILE LEU ASP ALA ILE GLU ALA LYS              
SEQRES   1 B   51  SER MET ASP TYR GLU PHE LEU LYS SER TRP THR VAL GLU          
SEQRES   2 B   51  ASP LEU GLN LYS ARG LEU LEU ALA LEU ASP PRO MET MET          
SEQRES   3 B   51  GLU GLN GLU ILE GLU GLU ILE ARG GLN LYS TYR GLN SER          
SEQRES   4 B   51  LYS ARG GLN PRO ILE LEU ASP ALA ILE GLU ALA LYS              
SEQRES   1 C   51  SER MET ASP TYR GLU PHE LEU LYS SER TRP THR VAL GLU          
SEQRES   2 C   51  ASP LEU GLN LYS ARG LEU LEU ALA LEU ASP PRO MET MET          
SEQRES   3 C   51  GLU GLN GLU ILE GLU GLU ILE ARG GLN LYS TYR GLN SER          
SEQRES   4 C   51  LYS ARG GLN PRO ILE LEU ASP ALA ILE GLU ALA LYS              
SEQRES   1 D   51  SER MET ASP TYR GLU PHE LEU LYS SER TRP THR VAL GLU          
SEQRES   2 D   51  ASP LEU GLN LYS ARG LEU LEU ALA LEU ASP PRO MET MET          
SEQRES   3 D   51  GLU GLN GLU ILE GLU GLU ILE ARG GLN LYS TYR GLN SER          
SEQRES   4 D   51  LYS ARG GLN PRO ILE LEU ASP ALA ILE GLU ALA LYS              
SEQRES   1 E   51  SER MET ASP TYR GLU PHE LEU LYS SER TRP THR VAL GLU          
SEQRES   2 E   51  ASP LEU GLN LYS ARG LEU LEU ALA LEU ASP PRO MET MET          
SEQRES   3 E   51  GLU GLN GLU ILE GLU GLU ILE ARG GLN LYS TYR GLN SER          
SEQRES   4 E   51  LYS ARG GLN PRO ILE LEU ASP ALA ILE GLU ALA LYS              
SEQRES   1 F   51  SER MET ASP TYR GLU PHE LEU LYS SER TRP THR VAL GLU          
SEQRES   2 F   51  ASP LEU GLN LYS ARG LEU LEU ALA LEU ASP PRO MET MET          
SEQRES   3 F   51  GLU GLN GLU ILE GLU GLU ILE ARG GLN LYS TYR GLN SER          
SEQRES   4 F   51  LYS ARG GLN PRO ILE LEU ASP ALA ILE GLU ALA LYS              
SEQRES   1 G   51  SER MET ASP TYR GLU PHE LEU LYS SER TRP THR VAL GLU          
SEQRES   2 G   51  ASP LEU GLN LYS ARG LEU LEU ALA LEU ASP PRO MET MET          
SEQRES   3 G   51  GLU GLN GLU ILE GLU GLU ILE ARG GLN LYS TYR GLN SER          
SEQRES   4 G   51  LYS ARG GLN PRO ILE LEU ASP ALA ILE GLU ALA LYS              
SEQRES   1 H   51  SER MET ASP TYR GLU PHE LEU LYS SER TRP THR VAL GLU          
SEQRES   2 H   51  ASP LEU GLN LYS ARG LEU LEU ALA LEU ASP PRO MET MET          
SEQRES   3 H   51  GLU GLN GLU ILE GLU GLU ILE ARG GLN LYS TYR GLN SER          
SEQRES   4 H   51  LYS ARG GLN PRO ILE LEU ASP ALA ILE GLU ALA LYS              
HET    EDO  A 501       4                                                       
HET    EDO  A 502       4                                                       
HET    EDO  A 503       4                                                       
HET    EDO  A 504       8                                                       
HET    EDO  B 501       4                                                       
HET    EDO  C 501       4                                                       
HET    EDO  E 501       4                                                       
HET    EDO  F 501       4                                                       
HET    EDO  H 501       4                                                       
HET    EDO  H 502       4                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   9  EDO    10(C2 H6 O2)                                                 
FORMUL  19  HOH   *223(H2 O)                                                    
HELIX    1   1 ASP A  432  LYS A  437  1                                   6    
HELIX    2   2 THR A  440  ALA A  479  1                                  40    
HELIX    3   3 THR B  440  ALA B  479  1                                  40    
HELIX    4   4 ASP C  432  LYS C  437  1                                   6    
HELIX    5   5 THR C  440  ALA C  479  1                                  40    
HELIX    6   6 TYR D  433  LYS D  437  1                                   5    
HELIX    7   7 THR D  440  ALA D  479  1                                  40    
HELIX    8   8 ASP E  432  LYS E  437  1                                   6    
HELIX    9   9 THR E  440  ALA E  479  1                                  40    
HELIX   10  10 THR F  440  ALA F  479  1                                  40    
HELIX   11  11 TYR G  433  TRP G  439  5                                   7    
HELIX   12  12 THR G  440  ALA G  479  1                                  40    
HELIX   13  13 ASP H  432  LYS H  437  1                                   6    
HELIX   14  14 THR H  440  ALA H  479  1                                  40    
SITE     1 AC1  6 LEU A 451  ASP A 452  MET A 455  HOH A 642                    
SITE     2 AC1  6 ARG B 470  EDO B 501                                          
SITE     1 AC2  3 LYS A 465  GLU B 458  PHE E 435                               
SITE     1 AC3  5 ARG A 470  HOH A 603  HOH A 638  ASP B 452                    
SITE     2 AC3  5 MET B 455                                                     
SITE     1 AC4  7 LYS A 446  ARG A 447  ALA A 450  HOH A 602                    
SITE     2 AC4  7 PRO E 453  MET E 454  GLN E 457                               
SITE     1 AC5  7 ASP A 452  EDO A 501  HOH A 642  ARG B 470                    
SITE     2 AC5  7 LEU D 449  ASP D 452  PRO D 453                               
SITE     1 AC6  6 HOH A 635  ARG C 470  LEU D 451  ASP D 452                    
SITE     2 AC6  6 MET D 455  HOH D 507                                          
SITE     1 AC7  5 MET A 454  MET E   0  ARG E 447  HOH E 620                    
SITE     2 AC7  5 LYS F 469                                                     
SITE     1 AC8  4 PHE F 435  ARG F 463  GLN F 464  GLN F 467                    
SITE     1 AC9  6 MET C 454  HOH D 513  LYS G 469  HOH G 517                    
SITE     2 AC9  6 MET H   0  ARG H 447                                          
SITE     1 BC1  5 ARG G 470  LEU H 451  ASP H 452  MET H 455                    
SITE     2 BC1  5 HOH H 605                                                     
CRYST1   55.260   63.750  144.740  90.00  90.00  90.00 P 21 21 21   32          
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      0.018096  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015686  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006909        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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