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Database: PDB
Entry: 4QRD
LinkDB: 4QRD
Original site: 4QRD 
HEADER    LIGASE/LIGASE INHIBITOR                 30-JUN-14   4QRD              
TITLE     STRUCTURE OF METHIONYL-TRNA SYNTHETASE IN COMPLEX WITH N-(1H-         
TITLE    2 BENZIMIDAZOL-2-YLMETHYL)-N'-(2,4-DICHLOROPHENYL)-6-(MORPHOLIN-4-YL)- 
TITLE    3 1,3,5-TRIAZINE-2,4-DIAMINE                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: METHIONYL-TRNA SYNTHETASE;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 6.1.1.10;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE   3 ORGANISM_TAXID: 1280;                                                
SOURCE   4 GENE: METG, CH52_03385;                                              
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PROTEIN SYNTHESIS, AMINOACYL-TRNA SYNTHETASE, AMINOACYLATION,         
KEYWDS   2 CYTOSOL, LIGASE-LIGASE INHIBITOR COMPLEX                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.LI,M.T.HILGERS,M.STIDHAM,V.BROWN-DRIVER,K.J.SHAW,J.FINN             
REVDAT   1   29-JUL-15 4QRD    0                                                
JRNL        AUTH   X.LI,M.T.HILGERS,M.STIDHAM,V.BROWN-DRIVER,K.J.SHAW,J.FINN    
JRNL        TITL   DISCOVERY AND SAR OF A NOVEL SERIES OF PYRIMIDINE            
JRNL        TITL 2 ANTIBACTERIALS TARGETING METHIONYL-TRNA SYNTHETASE           
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.97 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 1.97                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.25                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 69.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 28282                          
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) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.283                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1426                            
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) : 1.97                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.02                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1758                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 62.21                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2820                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 94                           
REMARK   3   BIN FREE R VALUE                    : 0.3970                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4220                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 263                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.56                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.13000                                              
REMARK   3    B22 (A**2) : -0.21000                                             
REMARK   3    B33 (A**2) : 0.09000                                              
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): 0.326         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.263         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.161         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.127        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.947                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.889                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4373 ; 0.020 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5939 ; 1.881 ; 1.965       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   520 ; 6.874 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   212 ;37.361 ;24.670       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   744 ;18.404 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;16.493 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   633 ; 0.128 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3357 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2152 ; 0.226 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2912 ; 0.312 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   243 ; 0.214 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     1 ; 0.023 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    63 ; 0.318 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    22 ; 0.688 ; 0.200       
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):  2697 ; 0.773 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4214 ; 1.224 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2005 ; 1.822 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1724 ; 2.381 ; 4.500       
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  : 11                                         
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     2        A    97                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.1970 -12.3950 -26.4860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0298 T22:  -0.2072                                     
REMARK   3      T33:   0.0475 T12:   0.0218                                     
REMARK   3      T13:  -0.0165 T23:  -0.0120                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3334 L22:   0.5241                                     
REMARK   3      L33:   0.2662 L12:   0.6339                                     
REMARK   3      L13:  -0.2548 L23:  -0.0720                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0107 S12:   0.0771 S13:  -0.1053                       
REMARK   3      S21:  -0.0811 S22:  -0.0062 S23:   0.0275                       
REMARK   3      S31:  -0.0510 S32:  -0.0248 S33:   0.0169                       
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    98        A   117                          
REMARK   3    ORIGIN FOR THE GROUP (A):   4.6130 -13.2120  -5.3460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0006 T22:  -0.1202                                     
REMARK   3      T33:   0.0109 T12:  -0.0170                                     
REMARK   3      T13:  -0.0191 T23:   0.0435                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1133 L22:   2.3889                                     
REMARK   3      L33:   4.2030 L12:  -1.0034                                     
REMARK   3      L13:  -1.0737 L23:   2.5619                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0438 S12:  -0.2508 S13:  -0.2585                       
REMARK   3      S21:   0.1324 S22:  -0.0609 S23:   0.0672                       
REMARK   3      S31:   0.3101 S32:  -0.1122 S33:   0.1047                       
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   118        A   136                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.7370   1.4610 -14.7460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0194 T22:  -0.2140                                     
REMARK   3      T33:   0.0311 T12:   0.0384                                     
REMARK   3      T13:  -0.0050 T23:   0.0088                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6083 L22:   1.2922                                     
REMARK   3      L33:   2.3009 L12:  -0.3162                                     
REMARK   3      L13:   0.7709 L23:  -1.6929                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1058 S12:   0.0119 S13:   0.0407                       
REMARK   3      S21:   0.0306 S22:  -0.0448 S23:   0.0505                       
REMARK   3      S31:  -0.1654 S32:   0.1477 S33:   0.1506                       
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   137        A   161                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.5150  12.1220 -22.8340              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0037 T22:  -0.1199                                     
REMARK   3      T33:  -0.0411 T12:   0.0151                                     
REMARK   3      T13:  -0.0257 T23:  -0.0020                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1321 L22:  11.3826                                     
REMARK   3      L33:   0.9283 L12:  -4.0840                                     
REMARK   3      L13:  -0.8093 L23:   2.1069                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3194 S12:  -0.0271 S13:  -0.0294                       
REMARK   3      S21:  -0.2391 S22:  -0.3947 S23:   0.0537                       
REMARK   3      S31:  -0.0035 S32:  -0.0946 S33:   0.0753                       
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   174        A   192                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.3630   7.2950  -6.5040              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1092 T22:  -0.2539                                     
REMARK   3      T33:  -0.0358 T12:  -0.0753                                     
REMARK   3      T13:  -0.0162 T23:  -0.0189                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.5707 L22:   2.0576                                     
REMARK   3      L33:   6.0163 L12:   1.3863                                     
REMARK   3      L13:  -4.4084 L23:  -1.9800                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3274 S12:  -0.1845 S13:   0.2800                       
REMARK   3      S21:   0.2313 S22:  -0.1246 S23:  -0.1141                       
REMARK   3      S31:  -0.5345 S32:   0.2331 S33:  -0.2028                       
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 :   A   193        A   234                          
REMARK   3    ORIGIN FOR THE GROUP (A):   1.1960   0.0260 -12.0510              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0575 T22:  -0.2269                                     
REMARK   3      T33:  -0.0010 T12:   0.0100                                     
REMARK   3      T13:  -0.0093 T23:   0.0068                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0151 L22:   0.1101                                     
REMARK   3      L33:   1.4620 L12:  -0.2365                                     
REMARK   3      L13:  -0.6786 L23:   0.3936                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0777 S12:  -0.1503 S13:   0.0665                       
REMARK   3      S21:  -0.0530 S22:   0.0089 S23:   0.0509                       
REMARK   3      S31:  -0.2573 S32:  -0.1575 S33:  -0.0867                       
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 :   A   235        A   302                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.2230  -5.2810 -13.9890              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0066 T22:  -0.1800                                     
REMARK   3      T33:   0.0131 T12:   0.0131                                     
REMARK   3      T13:  -0.0126 T23:   0.0138                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0081 L22:   0.3803                                     
REMARK   3      L33:   1.4512 L12:   0.1766                                     
REMARK   3      L13:  -0.1237 L23:   0.1416                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0983 S12:  -0.1499 S13:  -0.0549                       
REMARK   3      S21:   0.0131 S22:  -0.0119 S23:   0.0172                       
REMARK   3      S31:  -0.1710 S32:   0.0879 S33:  -0.0864                       
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 :   A   303        A   317                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.5420   2.5490 -40.0180              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0155 T22:   0.0146                                     
REMARK   3      T33:   0.0136 T12:  -0.0135                                     
REMARK   3      T13:  -0.0922 T23:  -0.0025                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  58.3033 L22:   4.9497                                     
REMARK   3      L33:   8.4254 L12:  -9.1354                                     
REMARK   3      L13:  19.4193 L23:  -5.6670                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1218 S12:  -0.4314 S13:  -0.5411                       
REMARK   3      S21:  -0.5986 S22:   0.0029 S23:   0.2845                       
REMARK   3      S31:   0.5744 S32:  -0.5348 S33:  -0.1246                       
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 :   A   318        A   475                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.1600  -0.8910 -44.5740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0562 T22:  -0.1878                                     
REMARK   3      T33:  -0.0009 T12:   0.0053                                     
REMARK   3      T13:  -0.0226 T23:  -0.0246                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8067 L22:   0.1661                                     
REMARK   3      L33:   0.7985 L12:   0.0879                                     
REMARK   3      L13:  -0.4388 L23:  -0.3109                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0122 S12:   0.0860 S13:  -0.0119                       
REMARK   3      S21:   0.0109 S22:   0.0188 S23:  -0.0001                       
REMARK   3      S31:   0.0341 S32:   0.0232 S33:  -0.0066                       
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 :   A   476        A   520                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.4550 -12.1340 -41.8750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0550 T22:  -0.2668                                     
REMARK   3      T33:  -0.0018 T12:   0.0667                                     
REMARK   3      T13:   0.0266 T23:  -0.0445                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3163 L22:   1.0898                                     
REMARK   3      L33:   3.3546 L12:   0.3825                                     
REMARK   3      L13:   0.7458 L23:  -1.4944                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0046 S12:   0.0105 S13:  -0.3349                       
REMARK   3      S21:  -0.1234 S22:  -0.0602 S23:  -0.1386                       
REMARK   3      S31:   0.3354 S32:  -0.0376 S33:   0.0555                       
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 :   A   162        A   173                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.6010   0.0760  -9.0750              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0338 T22:  -0.1423                                     
REMARK   3      T33:  -0.0365 T12:   0.0083                                     
REMARK   3      T13:   0.0249 T23:  -0.0048                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3736 L22:   1.2676                                     
REMARK   3      L33:   4.4007 L12:  -1.0018                                     
REMARK   3      L13:   2.5136 L23:  -2.2729                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0499 S12:   0.0307 S13:  -0.1212                       
REMARK   3      S21:  -0.1444 S22:   0.0426 S23:   0.0883                       
REMARK   3      S31:  -0.0332 S32:   0.0676 S33:   0.0072                       
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: NULL                                      
REMARK   4                                                                      
REMARK   4 4QRD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JUL-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB086416.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-JUL-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.970                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 21.250                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 69.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.97                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 69.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, TRIS PH 7.9, VAPOR             
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 295K                           
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       31.21900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       59.11100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.36300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       59.11100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.21900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.36300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -26                                                      
REMARK 465     GLY A   -25                                                      
REMARK 465     HIS A   -24                                                      
REMARK 465     HIS A   -23                                                      
REMARK 465     HIS A   -22                                                      
REMARK 465     HIS A   -21                                                      
REMARK 465     HIS A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     ASP A   -18                                                      
REMARK 465     TYR A   -17                                                      
REMARK 465     ASP A   -16                                                      
REMARK 465     ILE A   -15                                                      
REMARK 465     PRO A   -14                                                      
REMARK 465     THR A   -13                                                      
REMARK 465     THR A   -12                                                      
REMARK 465     GLU A   -11                                                      
REMARK 465     ASN A   -10                                                      
REMARK 465     LEU A    -9                                                      
REMARK 465     TYR A    -8                                                      
REMARK 465     PHE A    -7                                                      
REMARK 465     GLN A    -6                                                      
REMARK 465     GLY A    -5                                                      
REMARK 465     ALA A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     MET A    -2                                                      
REMARK 465     ALA A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
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 A   338     NE   ARG A   355              2.03            
REMARK 500   OH   TYR A    13     O    HIS A    23              2.03            
REMARK 500   NZ   LYS A   480     O    HOH A   802              2.03            
REMARK 500   OH   TYR A   378     O    HOH A   865              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   793     O    HOH A   916     3544     1.34            
REMARK 500   O    HOH A   760     O    HOH A   909     3554     1.44            
REMARK 500   O    HOH A   801     O    HOH A   829     2554     1.52            
REMARK 500   O    HOH A   891     O    HOH A   920     2554     1.55            
REMARK 500   O    HOH A   758     O    HOH A   927     2555     1.64            
REMARK 500   O    HOH A   751     O    HOH A   922     3644     1.84            
REMARK 500   O    HOH A   828     O    HOH A   841     1455     2.01            
REMARK 500   O    HOH A   778     O    HOH A   787     2554     2.09            
REMARK 500   O    HOH A   762     O    HOH A   801     2555     2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 239   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP A 329   CB  -  CG  -  OD1 ANGL. DEV. =   7.9 DEGREES          
REMARK 500    ARG A 332   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG A 332   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  89       31.88    -88.10                                   
REMARK 500    PHE A 205      -36.48   -131.91                                   
REMARK 500    ASN A 229       78.46   -157.06                                   
REMARK 500    MET A 304     -144.01   -117.07                                   
REMARK 500    ASP A 306       11.66   -164.64                                   
REMARK 500    GLU A 392      -34.45    -37.58                                   
REMARK 500    THR A 439       64.30     35.87                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LYS A 207        24.3      L          L   OUTSIDE RANGE           
REMARK 500    ASN A 366        24.5      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 809        DISTANCE =  5.33 ANGSTROMS                       
REMARK 525    HOH A 867        DISTANCE =  6.07 ANGSTROMS                       
REMARK 525    HOH A 868        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH A 880        DISTANCE =  6.38 ANGSTROMS                       
REMARK 525    HOH A 902        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH A 936        DISTANCE =  5.40 ANGSTROMS                       
REMARK 525    HOH A 944        DISTANCE =  5.01 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3BJ A 602                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4QRE   RELATED DB: PDB                                   
DBREF  4QRD A    1   520  UNP    W8U1H8   W8U1H8_STAAU     1    520             
SEQADV 4QRD MET A  -26  UNP  W8U1H8              EXPRESSION TAG                 
SEQADV 4QRD GLY A  -25  UNP  W8U1H8              EXPRESSION TAG                 
SEQADV 4QRD HIS A  -24  UNP  W8U1H8              EXPRESSION TAG                 
SEQADV 4QRD HIS A  -23  UNP  W8U1H8              EXPRESSION TAG                 
SEQADV 4QRD HIS A  -22  UNP  W8U1H8              EXPRESSION TAG                 
SEQADV 4QRD HIS A  -21  UNP  W8U1H8              EXPRESSION TAG                 
SEQADV 4QRD HIS A  -20  UNP  W8U1H8              EXPRESSION TAG                 
SEQADV 4QRD HIS A  -19  UNP  W8U1H8              EXPRESSION TAG                 
SEQADV 4QRD ASP A  -18  UNP  W8U1H8              EXPRESSION TAG                 
SEQADV 4QRD TYR A  -17  UNP  W8U1H8              EXPRESSION TAG                 
SEQADV 4QRD ASP A  -16  UNP  W8U1H8              EXPRESSION TAG                 
SEQADV 4QRD ILE A  -15  UNP  W8U1H8              EXPRESSION TAG                 
SEQADV 4QRD PRO A  -14  UNP  W8U1H8              EXPRESSION TAG                 
SEQADV 4QRD THR A  -13  UNP  W8U1H8              EXPRESSION TAG                 
SEQADV 4QRD THR A  -12  UNP  W8U1H8              EXPRESSION TAG                 
SEQADV 4QRD GLU A  -11  UNP  W8U1H8              EXPRESSION TAG                 
SEQADV 4QRD ASN A  -10  UNP  W8U1H8              EXPRESSION TAG                 
SEQADV 4QRD LEU A   -9  UNP  W8U1H8              EXPRESSION TAG                 
SEQADV 4QRD TYR A   -8  UNP  W8U1H8              EXPRESSION TAG                 
SEQADV 4QRD PHE A   -7  UNP  W8U1H8              EXPRESSION TAG                 
SEQADV 4QRD GLN A   -6  UNP  W8U1H8              EXPRESSION TAG                 
SEQADV 4QRD GLY A   -5  UNP  W8U1H8              EXPRESSION TAG                 
SEQADV 4QRD ALA A   -4  UNP  W8U1H8              EXPRESSION TAG                 
SEQADV 4QRD HIS A   -3  UNP  W8U1H8              EXPRESSION TAG                 
SEQADV 4QRD MET A   -2  UNP  W8U1H8              EXPRESSION TAG                 
SEQADV 4QRD ALA A   -1  UNP  W8U1H8              EXPRESSION TAG                 
SEQADV 4QRD SER A    0  UNP  W8U1H8              EXPRESSION TAG                 
SEQRES   1 A  547  MET GLY HIS HIS HIS HIS HIS HIS ASP TYR ASP ILE PRO          
SEQRES   2 A  547  THR THR GLU ASN LEU TYR PHE GLN GLY ALA HIS MET ALA          
SEQRES   3 A  547  SER MET ALA LYS GLU THR PHE TYR ILE THR THR PRO ILE          
SEQRES   4 A  547  TYR TYR PRO SER GLY ASN LEU HIS ILE GLY HIS ALA TYR          
SEQRES   5 A  547  SER THR VAL ALA GLY ASP VAL ILE ALA ARG TYR LYS ARG          
SEQRES   6 A  547  MET GLN GLY TYR ASP VAL ARG TYR LEU THR GLY THR ASP          
SEQRES   7 A  547  GLU HIS GLY GLN LYS ILE GLN GLU LYS ALA GLN LYS ALA          
SEQRES   8 A  547  GLY LYS THR GLU ILE GLU TYR LEU ASP GLU MET ILE ALA          
SEQRES   9 A  547  GLY ILE LYS GLN LEU TRP ALA LYS LEU GLU ILE SER ASN          
SEQRES  10 A  547  ASP ASP PHE ILE ARG THR THR GLU GLU ARG HIS LYS HIS          
SEQRES  11 A  547  VAL VAL GLU GLN VAL PHE GLU ARG LEU LEU LYS GLN GLY          
SEQRES  12 A  547  ASP ILE TYR LEU GLY GLU TYR GLU GLY TRP TYR SER VAL          
SEQRES  13 A  547  PRO ASP GLU THR TYR TYR THR GLU SER GLN LEU VAL ASP          
SEQRES  14 A  547  PRO GLN TYR GLU ASN GLY LYS ILE ILE GLY GLY LYS SER          
SEQRES  15 A  547  PRO ASP SER GLY HIS GLU VAL GLU LEU VAL LYS GLU GLU          
SEQRES  16 A  547  SER TYR PHE PHE ASN ILE SER LYS TYR THR ASP ARG LEU          
SEQRES  17 A  547  LEU GLU PHE TYR ASP GLN ASN PRO ASP PHE ILE GLN PRO          
SEQRES  18 A  547  PRO SER ARG LYS ASN GLU MET ILE ASN ASN PHE ILE LYS          
SEQRES  19 A  547  PRO GLY LEU ALA ASP LEU ALA VAL SER ARG THR SER PHE          
SEQRES  20 A  547  ASN TRP GLY VAL HIS VAL PRO SER ASN PRO LYS HIS VAL          
SEQRES  21 A  547  VAL TYR VAL TRP ILE ASP ALA LEU VAL ASN TYR ILE SER          
SEQRES  22 A  547  ALA LEU GLY TYR LEU SER ASP ASP GLU SER LEU PHE ASN          
SEQRES  23 A  547  LYS TYR TRP PRO ALA ASP ILE HIS LEU MET ALA LYS GLU          
SEQRES  24 A  547  ILE VAL ARG PHE HIS SER ILE ILE TRP PRO ILE LEU LEU          
SEQRES  25 A  547  MET ALA LEU ASP LEU PRO LEU PRO LYS LYS VAL PHE ALA          
SEQRES  26 A  547  HIS GLY TRP ILE LEU MET LYS ASP GLY LYS MET SER LYS          
SEQRES  27 A  547  SER LYS GLY ASN VAL VAL ASP PRO ASN ILE LEU ILE ASP          
SEQRES  28 A  547  ARG TYR GLY LEU ASP ALA THR ARG TYR TYR LEU MET ARG          
SEQRES  29 A  547  GLU LEU PRO PHE GLY SER ASP GLY VAL PHE THR PRO GLU          
SEQRES  30 A  547  ALA PHE VAL GLU ARG THR ASN PHE ASP LEU ALA ASN ASP          
SEQRES  31 A  547  LEU GLY ASN LEU VAL ASN ARG THR ILE SER MET VAL ASN          
SEQRES  32 A  547  LYS TYR PHE ASP GLY GLU LEU PRO ALA TYR GLN GLY PRO          
SEQRES  33 A  547  LEU HIS GLU LEU ASP GLU GLU MET GLU ALA MET ALA LEU          
SEQRES  34 A  547  GLU THR VAL LYS SER TYR THR GLU SER MET GLU SER LEU          
SEQRES  35 A  547  GLN PHE SER VAL ALA LEU SER THR VAL TRP LYS PHE ILE          
SEQRES  36 A  547  SER ARG THR ASN LYS TYR ILE ASP GLU THR THR PRO TRP          
SEQRES  37 A  547  VAL LEU ALA LYS ASP ASP SER GLN LYS ASP MET LEU GLY          
SEQRES  38 A  547  ASN VAL MET ALA HIS LEU VAL GLU ASN ILE ARG TYR ALA          
SEQRES  39 A  547  ALA VAL LEU LEU ARG PRO PHE LEU THR HIS ALA PRO LYS          
SEQRES  40 A  547  GLU ILE PHE GLU GLN LEU ASN ILE ASN ASN PRO GLN PHE          
SEQRES  41 A  547  MET GLU PHE SER SER LEU GLU GLN TYR GLY VAL LEU THR          
SEQRES  42 A  547  GLU SER ILE MET VAL THR GLY GLN PRO LYS PRO ILE PHE          
SEQRES  43 A  547  PRO                                                          
HET     MG  A 601       1                                                       
HET    3BJ  A 602      32                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     3BJ N-(1H-BENZIMIDAZOL-2-YLMETHYL)-N'-(2,4-DICHLOROPHENYL)-          
HETNAM   2 3BJ  6-(MORPHOLIN-4-YL)-1,3,5-TRIAZINE-2,4-DIAMINE                   
FORMUL   2   MG    MG 2+                                                        
FORMUL   3  3BJ    C21 H20 CL2 N8 O                                             
FORMUL   4  HOH   *263(H2 O)                                                    
HELIX    1   1 HIS A   20  GLN A   40  1                                  21    
HELIX    2   2 GLY A   54  ALA A   64  1                                  11    
HELIX    3   3 THR A   67  LEU A   86  1                                  20    
HELIX    4   4 GLU A   98  GLN A  115  1                                  18    
HELIX    5   5 THR A  136  LEU A  140  5                                   5    
HELIX    6   6 ILE A  174  LYS A  176  5                                   3    
HELIX    7   7 TYR A  177  ASN A  188  1                                  12    
HELIX    8   8 SER A  196  PHE A  205  1                                  10    
HELIX    9   9 TYR A  235  VAL A  242  1                                   8    
HELIX   10  10 VAL A  242  ALA A  247  1                                   6    
HELIX   11  11 GLU A  255  TRP A  262  1                                   8    
HELIX   12  12 ILE A  273  ILE A  279  1                                   7    
HELIX   13  13 ILE A  279  LEU A  288  1                                  10    
HELIX   14  14 ASP A  318  GLY A  327  1                                  10    
HELIX   15  15 GLY A  327  GLU A  338  1                                  12    
HELIX   16  16 THR A  348  ASP A  359  1                                  12    
HELIX   17  17 ASN A  362  PHE A  379  1                                  18    
HELIX   18  18 LEU A  393  SER A  414  1                                  22    
HELIX   19  19 GLN A  416  THR A  439  1                                  24    
HELIX   20  20 THR A  439  ALA A  444  1                                   6    
HELIX   21  21 LYS A  445  SER A  448  5                                   4    
HELIX   22  22 GLN A  449  ARG A  472  1                                  24    
HELIX   23  23 HIS A  477  ASN A  487  1                                  11    
HELIX   24  24 ASN A  490  GLU A  500  5                                  11    
SHEET    1   A 6 ASP A  92  ARG A  95  0                                        
SHEET    2   A 6 ASP A  43  THR A  50  1  N  THR A  50   O  ILE A  94           
SHEET    3   A 6 THR A   5  TYR A  13  1  N  ILE A   8   O  ARG A  45           
SHEET    4   A 6 ILE A 266  ALA A 270  1  O  LEU A 268   N  THR A   9           
SHEET    5   A 6 VAL A 296  HIS A 299  1  O  HIS A 299   N  MET A 269           
SHEET    6   A 6 ILE A 192  GLN A 193  1  N  GLN A 193   O  ALA A 298           
SHEET    1   B 4 THR A 133  TYR A 135  0                                        
SHEET    2   B 4 ILE A 118  SER A 128 -1  N  SER A 128   O  THR A 133           
SHEET    3   B 4 GLU A 163  PHE A 172 -1  O  GLU A 167   N  TYR A 123           
SHEET    4   B 4 LEU A 213  ALA A 214 -1  O  LEU A 213   N  PHE A 172           
SHEET    1   C 2 VAL A 141  GLU A 146  0                                        
SHEET    2   C 2 LYS A 149  LYS A 154 -1  O  ILE A 151   N  GLN A 144           
SHEET    1   D 3 SER A 216  ARG A 217  0                                        
SHEET    2   D 3 ASN A 229  VAL A 234 -1  O  VAL A 233   N  ARG A 217           
SHEET    3   D 3 HIS A 225  VAL A 226 -1  N  VAL A 226   O  HIS A 232           
SHEET    1   E 2 ILE A 302  LEU A 303  0                                        
SHEET    2   E 2 GLY A 345  VAL A 346  1  O  GLY A 345   N  LEU A 303           
SHEET    1   F 2 GLU A 382  LEU A 383  0                                        
SHEET    2   F 2 ILE A 509  MET A 510 -1  O  ILE A 509   N  LEU A 383           
LINK        MG    MG A 601                 O   HOH A 832     1555   1555  1.97  
CISPEP   1 GLN A  193    PRO A  194          0        -1.32                     
CISPEP   2 PRO A  208    GLY A  209          0       -19.52                     
CISPEP   3 TRP A  262    PRO A  263          0         0.68                     
CISPEP   4 ASP A  306    GLY A  307          0         2.72                     
SITE     1 AC1  1 HOH A 832                                                     
SITE     1 AC2 13 ILE A  12  TYR A  14  ASP A  51  HIS A  53                    
SITE     2 AC2 13 GLY A  54  THR A 133  TYR A 235  VAL A 236                    
SITE     3 AC2 13 TRP A 237  ASN A 243  TYR A 244  PHE A 276                    
SITE     4 AC2 13 HIS A 277                                                     
CRYST1   62.438   76.726  118.222  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016016  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013033  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008459        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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