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Database: PDB
Entry: 2QM6
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HEADER    TRANSFERASE                             14-JUL-07   2QM6              
TITLE     CRYSTAL STRUCTURE OF HELICOBACTER PYLORI GAMMA-GLUTAMYLTRANSPEPTIDASE 
TITLE    2 IN COMPLEX WITH GLUTAMATE                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GAMMA-GLUTAMYLTRANSPEPTIDASE;                              
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: RESIDUES 25-379;                                           
COMPND   5 SYNONYM: GGT;                                                        
COMPND   6 EC: 2.3.2.2;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: GAMMA-GLUTAMYLTRANSPEPTIDASE;                              
COMPND  10 CHAIN: B, D;                                                         
COMPND  11 FRAGMENT: RESIDUES 380-567;                                          
COMPND  12 SYNONYM: GGT;                                                        
COMPND  13 EC: 2.3.2.2;                                                         
COMPND  14 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HELICOBACTER PYLORI;                            
SOURCE   3 ORGANISM_TAXID: 210;                                                 
SOURCE   4 GENE: HP_1118;                                                       
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: ROSETTA2;                                  
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28A;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HELICOBACTER PYLORI;                            
SOURCE  12 ORGANISM_TAXID: 210;                                                 
SOURCE  13 GENE: HP_1118;                                                       
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: ROSETTA2;                                  
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    NTN-HYDROLASE, GLUTAMYLTRANSPEPTIDASE, TRANSFERASE                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.J.BARYCKI,A.SAND,G.BOANCA                                           
REVDAT   3   13-JUL-11 2QM6    1       VERSN                                    
REVDAT   2   24-FEB-09 2QM6    1       VERSN                                    
REVDAT   1   12-FEB-08 2QM6    0                                                
JRNL        AUTH   A.L.MORROW,K.WILLIAMS,A.SAND,G.BOANCA,J.J.BARYCKI            
JRNL        TITL   CHARACTERIZATION OF HELICOBACTER PYLORI                      
JRNL        TITL 2 GAMMA-GLUTAMYLTRANSPEPTIDASE REVEALS THE MOLECULAR BASIS FOR 
JRNL        TITL 3 SUBSTRATE SPECIFICITY AND A CRITICAL ROLE FOR THE TYROSINE   
JRNL        TITL 4 433-CONTAINING LOOP IN CATALYSIS.                            
JRNL        REF    BIOCHEMISTRY                  V.  46 13407 2007              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   17960917                                                     
JRNL        DOI    10.1021/BI701599E                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   G.BOANCA,A.SAND,T.OKADA,H.SUZUKI,H.KUMAGAI,K.FUKUYAMA,       
REMARK   1  AUTH 2 J.J.BARYCKI                                                  
REMARK   1  TITL   AUTOPROCESSING OF HELICOBACTER PYLORI                        
REMARK   1  TITL 2 GAMMA-GLUTAMYLTRANSPEPTIDASE LEADS TO THE FORMATION OF A     
REMARK   1  TITL 3 THREONINE-THREONINE CATALYTIC DYAD.                          
REMARK   1  REF    J.BIOL.CHEM.                  V. 282   534 2007              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1  PMID   17107958                                                     
REMARK   1  DOI    10.1074/JBC.M607694200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.93                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 122321                         
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) : 0.169                           
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.190                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 13494                           
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) : 1.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8992                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.05                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1870                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 1010                         
REMARK   3   BIN FREE R VALUE                    : 0.2380                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8050                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 20                                      
REMARK   3   SOLVENT ATOMS            : 737                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.36                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.07000                                             
REMARK   3    B22 (A**2) : 0.42000                                              
REMARK   3    B33 (A**2) : -0.35000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.03000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.088         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.085         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.050         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.697         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.969                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.963                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8305 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11237 ; 1.228 ; 1.970       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1078 ; 6.113 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   334 ;37.347 ;25.359       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1459 ;11.737 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;16.006 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1255 ; 0.083 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6232 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4026 ; 0.194 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5785 ; 0.303 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   660 ; 0.104 ; 0.200       
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):    47 ; 0.148 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    28 ; 0.119 ; 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):  5472 ; 0.633 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8550 ; 0.939 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3197 ; 1.737 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2687 ; 2.741 ; 4.500       
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  : 14                                         
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    32        A    95                          
REMARK   3    ORIGIN FOR THE GROUP (A):  35.8700 -16.2610  29.1370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0016 T22:   0.0352                                     
REMARK   3      T33:   0.0321 T12:  -0.0075                                     
REMARK   3      T13:  -0.0003 T23:  -0.0162                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5171 L22:   0.4878                                     
REMARK   3      L33:   0.4273 L12:  -0.1575                                     
REMARK   3      L13:   0.2841 L23:  -0.0382                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0145 S12:   0.1112 S13:  -0.1871                       
REMARK   3      S21:  -0.0872 S22:  -0.0078 S23:   0.0493                       
REMARK   3      S31:   0.0987 S32:  -0.0747 S33:  -0.0067                       
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    96        A   206                          
REMARK   3    ORIGIN FOR THE GROUP (A):  51.7690 -13.4680  38.7920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0183 T22:   0.0445                                     
REMARK   3      T33:   0.0394 T12:   0.0042                                     
REMARK   3      T13:   0.0016 T23:   0.0057                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8234 L22:   0.6815                                     
REMARK   3      L33:   0.8833 L12:  -0.4139                                     
REMARK   3      L13:  -0.1148 L23:   0.2351                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0191 S12:  -0.0576 S13:  -0.0195                       
REMARK   3      S21:   0.0059 S22:   0.0458 S23:  -0.0496                       
REMARK   3      S31:   0.0344 S32:   0.0845 S33:  -0.0267                       
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   207        A   355                          
REMARK   3    ORIGIN FOR THE GROUP (A):  39.3790  -2.0020  40.5320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0114 T22:   0.0488                                     
REMARK   3      T33:   0.0153 T12:  -0.0017                                     
REMARK   3      T13:   0.0008 T23:   0.0002                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3318 L22:   0.4990                                     
REMARK   3      L33:   0.5462 L12:  -0.1376                                     
REMARK   3      L13:  -0.0262 L23:  -0.0550                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0403 S12:  -0.0470 S13:  -0.0420                       
REMARK   3      S21:   0.0545 S22:   0.0508 S23:   0.0557                       
REMARK   3      S31:  -0.0391 S32:  -0.0257 S33:  -0.0105                       
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   356        A   372                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.0100  24.3290  37.6650              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0620 T22:   0.0874                                     
REMARK   3      T33:   0.0351 T12:  -0.0004                                     
REMARK   3      T13:  -0.0121 T23:   0.0143                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4893 L22:   3.5412                                     
REMARK   3      L33:   1.4393 L12:   0.7109                                     
REMARK   3      L13:  -0.1298 L23:   1.6886                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0522 S12:   0.0960 S13:   0.2262                       
REMARK   3      S21:  -0.0834 S22:   0.0090 S23:   0.2710                       
REMARK   3      S31:  -0.3769 S32:  -0.4120 S33:  -0.0611                       
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 :   B   380        B   458                          
REMARK   3    ORIGIN FOR THE GROUP (A):  45.0000  -5.2570  40.5720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0113 T22:   0.0382                                     
REMARK   3      T33:   0.0173 T12:  -0.0026                                     
REMARK   3      T13:   0.0055 T23:   0.0030                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3706 L22:   0.5883                                     
REMARK   3      L33:   0.6429 L12:  -0.2244                                     
REMARK   3      L13:  -0.1480 L23:   0.1702                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0113 S12:  -0.0359 S13:  -0.0056                       
REMARK   3      S21:   0.0384 S22:   0.0368 S23:  -0.0319                       
REMARK   3      S31:  -0.0277 S32:   0.0444 S33:  -0.0254                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   459        B   555                          
REMARK   3    ORIGIN FOR THE GROUP (A):  37.9780   6.6290  24.6170              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0409 T22:   0.0640                                     
REMARK   3      T33:   0.0041 T12:  -0.0046                                     
REMARK   3      T13:  -0.0027 T23:  -0.0016                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5911 L22:   1.0858                                     
REMARK   3      L33:   0.7874 L12:   0.1062                                     
REMARK   3      L13:  -0.0218 L23:  -0.0936                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0439 S12:   0.0566 S13:  -0.0312                       
REMARK   3      S21:  -0.0791 S22:   0.0621 S23:   0.0373                       
REMARK   3      S31:  -0.0788 S32:  -0.0342 S33:  -0.0182                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   556        B   565                          
REMARK   3    ORIGIN FOR THE GROUP (A):  36.4330  -5.9330  19.8670              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0512 T22:   0.0737                                     
REMARK   3      T33:   0.0663 T12:  -0.0107                                     
REMARK   3      T13:  -0.0218 T23:  -0.0036                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  24.6435 L22:   9.5630                                     
REMARK   3      L33:   1.7644 L12:  14.5281                                     
REMARK   3      L13:   1.9001 L23:   2.3910                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3556 S12:   0.5694 S13:  -0.8474                       
REMARK   3      S21:  -0.5280 S22:   0.4023 S23:  -0.5238                       
REMARK   3      S31:  -0.0591 S32:   0.0713 S33:  -0.0467                       
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 :   C    32        C   162                          
REMARK   3    ORIGIN FOR THE GROUP (A):  40.7370  -8.5990 -14.9240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0345 T22:   0.0297                                     
REMARK   3      T33:   0.0361 T12:   0.0224                                     
REMARK   3      T13:   0.0218 T23:   0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7617 L22:   1.0377                                     
REMARK   3      L33:   1.0082 L12:   0.3095                                     
REMARK   3      L13:  -0.1960 L23:  -0.2260                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0499 S12:  -0.0087 S13:  -0.1259                       
REMARK   3      S21:  -0.1327 S22:  -0.0039 S23:  -0.0322                       
REMARK   3      S31:   0.1174 S32:   0.0776 S33:   0.0539                       
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 :   C   163        C   245                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.9530 -15.8860 -13.0700              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0265 T22:  -0.0038                                     
REMARK   3      T33:   0.0394 T12:  -0.0319                                     
REMARK   3      T13:  -0.0173 T23:  -0.0060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3340 L22:   1.7657                                     
REMARK   3      L33:   1.8133 L12:   0.4077                                     
REMARK   3      L13:  -0.7643 L23:  -0.7268                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0785 S12:   0.0377 S13:  -0.0789                       
REMARK   3      S21:  -0.1345 S22:   0.0975 S23:   0.1643                       
REMARK   3      S31:   0.2250 S32:  -0.1353 S33:  -0.0190                       
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 :   C   246        C   352                          
REMARK   3    ORIGIN FOR THE GROUP (A):  46.6180  10.6520 -13.8400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0177 T22:   0.0449                                     
REMARK   3      T33:   0.0091 T12:  -0.0103                                     
REMARK   3      T13:   0.0145 T23:   0.0030                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3316 L22:   0.7369                                     
REMARK   3      L33:   0.6793 L12:   0.1480                                     
REMARK   3      L13:  -0.0464 L23:  -0.0173                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0165 S12:   0.0025 S13:  -0.0031                       
REMARK   3      S21:  -0.1143 S22:   0.0400 S23:  -0.0949                       
REMARK   3      S31:  -0.0673 S32:   0.1166 S33:  -0.0236                       
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 :   C   353        C   379                          
REMARK   3    ORIGIN FOR THE GROUP (A):  44.6180  27.1670 -12.9580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0629 T22:  -0.0014                                     
REMARK   3      T33:   0.0276 T12:  -0.0256                                     
REMARK   3      T13:   0.0142 T23:   0.0037                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1709 L22:   0.2170                                     
REMARK   3      L33:   2.4015 L12:   0.2973                                     
REMARK   3      L13:  -0.2509 L23:  -0.6401                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0194 S12:   0.0541 S13:   0.1913                       
REMARK   3      S21:  -0.0452 S22:   0.0394 S23:  -0.0417                       
REMARK   3      S31:  -0.1906 S32:   0.0326 S33:  -0.0201                       
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 :   D   380        D   458                          
REMARK   3    ORIGIN FOR THE GROUP (A):  36.7440  -0.1490 -16.0260              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0282 T22:   0.0192                                     
REMARK   3      T33:   0.0102 T12:   0.0130                                     
REMARK   3      T13:   0.0009 T23:  -0.0006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5864 L22:   0.7650                                     
REMARK   3      L33:   0.8613 L12:   0.2313                                     
REMARK   3      L13:  -0.1900 L23:  -0.2595                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0066 S12:  -0.0039 S13:  -0.0158                       
REMARK   3      S21:  -0.1051 S22:   0.0078 S23:   0.0269                       
REMARK   3      S31:   0.0001 S32:  -0.0170 S33:  -0.0013                       
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 :   D   459        D   557                          
REMARK   3    ORIGIN FOR THE GROUP (A):  44.3600   8.2260   1.6300              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0173 T22:   0.0761                                     
REMARK   3      T33:   0.0070 T12:  -0.0033                                     
REMARK   3      T13:  -0.0072 T23:   0.0143                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6409 L22:   1.2045                                     
REMARK   3      L33:   0.7751 L12:  -0.1941                                     
REMARK   3      L13:  -0.2038 L23:   0.1874                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0130 S12:  -0.1031 S13:  -0.0473                       
REMARK   3      S21:   0.1020 S22:   0.0234 S23:  -0.0596                       
REMARK   3      S31:  -0.0179 S32:   0.1141 S33:  -0.0103                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   558        D   565                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.7560  -3.4140   4.5570              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1020 T22:   0.0799                                     
REMARK   3      T33:   0.0802 T12:   0.0257                                     
REMARK   3      T13:  -0.0191 T23:   0.0108                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  36.3794 L22:  25.1644                                     
REMARK   3      L33:   5.9243 L12: -29.8022                                     
REMARK   3      L13:  -3.1767 L23:   0.5441                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.1543 S12:  -1.0423 S13:  -0.2055                       
REMARK   3      S21:   0.8851 S22:   0.8850 S23:   0.4688                       
REMARK   3      S31:   0.3031 S32:   0.2396 S33:   0.2693                       
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: NULL                                      
REMARK   4                                                                      
REMARK   4 2QM6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-AUG-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB043772.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-MAR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 14-BM-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 136302                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : 0.07500                            
REMARK 200  R SYM                      (I) : 0.08800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.47400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
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: PDB ENTRY 2NQO                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 200 MM HEPES, 25% PEG MME2000, 5 MG/ML   
REMARK 280  PROTEIN, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 292K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       52.38100            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, 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: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11030 ANGSTROM**2                         
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: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10850 ANGSTROM**2                         
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 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     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     HIS A     7                                                      
REMARK 465     HIS A     8                                                      
REMARK 465     HIS A     9                                                      
REMARK 465     HIS A    10                                                      
REMARK 465     HIS A    11                                                      
REMARK 465     HIS A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 465     SER A    14                                                      
REMARK 465     GLY A    15                                                      
REMARK 465     LEU A    16                                                      
REMARK 465     VAL A    17                                                      
REMARK 465     PRO A    18                                                      
REMARK 465     ARG A    19                                                      
REMARK 465     GLY A    20                                                      
REMARK 465     SER A    21                                                      
REMARK 465     HIS A    22                                                      
REMARK 465     MET A    23                                                      
REMARK 465     ALA A    24                                                      
REMARK 465     SER A    25                                                      
REMARK 465     ALA A    26                                                      
REMARK 465     ALA A    27                                                      
REMARK 465     SER A    28                                                      
REMARK 465     TYR A    29                                                      
REMARK 465     PRO A    30                                                      
REMARK 465     PRO A    31                                                      
REMARK 465     LEU A   374                                                      
REMARK 465     HIS A   375                                                      
REMARK 465     GLU A   376                                                      
REMARK 465     GLY A   377                                                      
REMARK 465     SER A   378                                                      
REMARK 465     ASN A   379                                                      
REMARK 465     GLU B   566                                                      
REMARK 465     PHE B   567                                                      
REMARK 465     MET C     3                                                      
REMARK 465     GLY C     4                                                      
REMARK 465     SER C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     HIS C     7                                                      
REMARK 465     HIS C     8                                                      
REMARK 465     HIS C     9                                                      
REMARK 465     HIS C    10                                                      
REMARK 465     HIS C    11                                                      
REMARK 465     HIS C    12                                                      
REMARK 465     SER C    13                                                      
REMARK 465     SER C    14                                                      
REMARK 465     GLY C    15                                                      
REMARK 465     LEU C    16                                                      
REMARK 465     VAL C    17                                                      
REMARK 465     PRO C    18                                                      
REMARK 465     ARG C    19                                                      
REMARK 465     GLY C    20                                                      
REMARK 465     SER C    21                                                      
REMARK 465     HIS C    22                                                      
REMARK 465     MET C    23                                                      
REMARK 465     ALA C    24                                                      
REMARK 465     SER C    25                                                      
REMARK 465     ALA C    26                                                      
REMARK 465     ALA C    27                                                      
REMARK 465     SER C    28                                                      
REMARK 465     TYR C    29                                                      
REMARK 465     PRO C    30                                                      
REMARK 465     PRO C    31                                                      
REMARK 465     GLU D   566                                                      
REMARK 465     PHE D   567                                                      
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     LYS B 553    CG   CD   CE   NZ                                   
REMARK 470     LYS D 553    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH D   622     O    HOH D   680              2.09            
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    LYS A  36      -54.25   -123.11                                   
REMARK 500    ALA A  79      -59.05   -142.04                                   
REMARK 500    LYS A 125       -0.32     68.62                                   
REMARK 500    ASP A 359       34.79   -141.65                                   
REMARK 500    MET A 371       -0.75     53.51                                   
REMARK 500    ASN B 400     -106.62     83.46                                   
REMARK 500    ALA B 406       -0.40     71.45                                   
REMARK 500    ASN B 446       -4.94     73.09                                   
REMARK 500    TRP B 507      -61.31     73.84                                   
REMARK 500    ASP B 542       79.47   -158.73                                   
REMARK 500    LYS C  36      -60.37   -128.11                                   
REMARK 500    ALA C  79      -58.36   -143.05                                   
REMARK 500    LYS C 125       -3.08     72.90                                   
REMARK 500    ASN D 400     -105.09     84.20                                   
REMARK 500    ASN D 446       -5.41     76.22                                   
REMARK 500    TRP D 507      -60.76     78.31                                   
REMARK 500    ASP D 542       82.74   -158.78                                   
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 GLU B 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLU D 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2NQO   RELATED DB: PDB                                   
REMARK 900 APOENZYME                                                            
REMARK 900 RELATED ID: 2QMC   RELATED DB: PDB                                   
DBREF  2QM6 A   25   379  UNP    O25743   O25743_HELPY    25    379             
DBREF  2QM6 B  380   567  UNP    O25743   O25743_HELPY   380    567             
DBREF  2QM6 C   25   379  UNP    O25743   O25743_HELPY    25    379             
DBREF  2QM6 D  380   567  UNP    O25743   O25743_HELPY   380    567             
SEQADV 2QM6 MET A    3  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 GLY A    4  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 SER A    5  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 SER A    6  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 HIS A    7  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 HIS A    8  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 HIS A    9  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 HIS A   10  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 HIS A   11  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 HIS A   12  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 SER A   13  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 SER A   14  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 GLY A   15  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 LEU A   16  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 VAL A   17  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 PRO A   18  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 ARG A   19  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 GLY A   20  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 SER A   21  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 HIS A   22  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 MET A   23  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 ALA A   24  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 MET C    3  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 GLY C    4  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 SER C    5  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 SER C    6  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 HIS C    7  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 HIS C    8  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 HIS C    9  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 HIS C   10  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 HIS C   11  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 HIS C   12  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 SER C   13  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 SER C   14  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 GLY C   15  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 LEU C   16  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 VAL C   17  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 PRO C   18  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 ARG C   19  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 GLY C   20  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 SER C   21  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 HIS C   22  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 MET C   23  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QM6 ALA C   24  UNP  O25743              EXPRESSION TAG                 
SEQRES   1 A  377  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  377  LEU VAL PRO ARG GLY SER HIS MET ALA SER ALA ALA SER          
SEQRES   3 A  377  TYR PRO PRO ILE LYS ASN THR LYS VAL GLY LEU ALA LEU          
SEQRES   4 A  377  SER SER HIS PRO LEU ALA SER GLU ILE GLY GLN LYS VAL          
SEQRES   5 A  377  LEU GLU GLU GLY GLY ASN ALA ILE ASP ALA ALA VAL ALA          
SEQRES   6 A  377  ILE GLY PHE ALA LEU ALA VAL VAL HIS PRO ALA ALA GLY          
SEQRES   7 A  377  ASN ILE GLY GLY GLY GLY PHE ALA VAL ILE HIS LEU ALA          
SEQRES   8 A  377  ASN GLY GLU ASN VAL ALA LEU ASP PHE ARG GLU LYS ALA          
SEQRES   9 A  377  PRO LEU LYS ALA THR LYS ASN MET PHE LEU ASP LYS GLN          
SEQRES  10 A  377  GLY ASN VAL VAL PRO LYS LEU SER GLU ASP GLY TYR LEU          
SEQRES  11 A  377  ALA ALA GLY VAL PRO GLY THR VAL ALA GLY MET GLU ALA          
SEQRES  12 A  377  MET LEU LYS LYS TYR GLY THR LYS LYS LEU SER GLN LEU          
SEQRES  13 A  377  ILE ASP PRO ALA ILE LYS LEU ALA GLU ASN GLY TYR ALA          
SEQRES  14 A  377  ILE SER GLN ARG GLN ALA GLU THR LEU LYS GLU ALA ARG          
SEQRES  15 A  377  GLU ARG PHE LEU LYS TYR SER SER SER LYS LYS TYR PHE          
SEQRES  16 A  377  PHE LYS LYS GLY HIS LEU ASP TYR GLN GLU GLY ASP LEU          
SEQRES  17 A  377  PHE VAL GLN LYS ASP LEU ALA LYS THR LEU ASN GLN ILE          
SEQRES  18 A  377  LYS THR LEU GLY ALA LYS GLY PHE TYR GLN GLY GLN VAL          
SEQRES  19 A  377  ALA GLU LEU ILE GLU LYS ASP MET LYS LYS ASN GLY GLY          
SEQRES  20 A  377  ILE ILE THR LYS GLU ASP LEU ALA SER TYR ASN VAL LYS          
SEQRES  21 A  377  TRP ARG LYS PRO VAL VAL GLY SER TYR ARG GLY TYR LYS          
SEQRES  22 A  377  ILE ILE SER MET SER PRO PRO SER SER GLY GLY THR HIS          
SEQRES  23 A  377  LEU ILE GLN ILE LEU ASN VAL MET GLU ASN ALA ASP LEU          
SEQRES  24 A  377  SER ALA LEU GLY TYR GLY ALA SER LYS ASN ILE HIS ILE          
SEQRES  25 A  377  ALA ALA GLU ALA MET ARG GLN ALA TYR ALA ASP ARG SER          
SEQRES  26 A  377  VAL TYR MET GLY ASP ALA ASP PHE VAL SER VAL PRO VAL          
SEQRES  27 A  377  ASP LYS LEU ILE ASN LYS ALA TYR ALA LYS LYS ILE PHE          
SEQRES  28 A  377  ASP THR ILE GLN PRO ASP THR VAL THR PRO SER SER GLN          
SEQRES  29 A  377  ILE LYS PRO GLY MET GLY GLN LEU HIS GLU GLY SER ASN          
SEQRES   1 B  188  THR THR HIS TYR SER VAL ALA ASP ARG TRP GLY ASN ALA          
SEQRES   2 B  188  VAL SER VAL THR TYR THR ILE ASN ALA SER TYR GLY SER          
SEQRES   3 B  188  ALA ALA SER ILE ASP GLY ALA GLY PHE LEU LEU ASN ASN          
SEQRES   4 B  188  GLU MET ASP ASP PHE SER ILE LYS PRO GLY ASN PRO ASN          
SEQRES   5 B  188  LEU TYR GLY LEU VAL GLY GLY ASP ALA ASN ALA ILE GLU          
SEQRES   6 B  188  ALA ASN LYS ARG PRO LEU SER SER MET SER PRO THR ILE          
SEQRES   7 B  188  VAL LEU LYS ASN ASN LYS VAL PHE LEU VAL VAL GLY SER          
SEQRES   8 B  188  PRO GLY GLY SER ARG ILE ILE THR THR VAL LEU GLN VAL          
SEQRES   9 B  188  ILE SER ASN VAL ILE ASP TYR ASN MET ASN ILE SER GLU          
SEQRES  10 B  188  ALA VAL SER ALA PRO ARG PHE HIS MET GLN TRP LEU PRO          
SEQRES  11 B  188  ASP GLU LEU ARG ILE GLU LYS PHE GLY MET PRO ALA ASP          
SEQRES  12 B  188  VAL LYS ASP ASN LEU THR LYS MET GLY TYR GLN ILE VAL          
SEQRES  13 B  188  THR LYS PRO VAL MET GLY ASP VAL ASN ALA ILE GLN VAL          
SEQRES  14 B  188  LEU PRO LYS THR LYS GLY SER VAL PHE TYR GLY SER THR          
SEQRES  15 B  188  ASP PRO ARG LYS GLU PHE                                      
SEQRES   1 C  377  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  377  LEU VAL PRO ARG GLY SER HIS MET ALA SER ALA ALA SER          
SEQRES   3 C  377  TYR PRO PRO ILE LYS ASN THR LYS VAL GLY LEU ALA LEU          
SEQRES   4 C  377  SER SER HIS PRO LEU ALA SER GLU ILE GLY GLN LYS VAL          
SEQRES   5 C  377  LEU GLU GLU GLY GLY ASN ALA ILE ASP ALA ALA VAL ALA          
SEQRES   6 C  377  ILE GLY PHE ALA LEU ALA VAL VAL HIS PRO ALA ALA GLY          
SEQRES   7 C  377  ASN ILE GLY GLY GLY GLY PHE ALA VAL ILE HIS LEU ALA          
SEQRES   8 C  377  ASN GLY GLU ASN VAL ALA LEU ASP PHE ARG GLU LYS ALA          
SEQRES   9 C  377  PRO LEU LYS ALA THR LYS ASN MET PHE LEU ASP LYS GLN          
SEQRES  10 C  377  GLY ASN VAL VAL PRO LYS LEU SER GLU ASP GLY TYR LEU          
SEQRES  11 C  377  ALA ALA GLY VAL PRO GLY THR VAL ALA GLY MET GLU ALA          
SEQRES  12 C  377  MET LEU LYS LYS TYR GLY THR LYS LYS LEU SER GLN LEU          
SEQRES  13 C  377  ILE ASP PRO ALA ILE LYS LEU ALA GLU ASN GLY TYR ALA          
SEQRES  14 C  377  ILE SER GLN ARG GLN ALA GLU THR LEU LYS GLU ALA ARG          
SEQRES  15 C  377  GLU ARG PHE LEU LYS TYR SER SER SER LYS LYS TYR PHE          
SEQRES  16 C  377  PHE LYS LYS GLY HIS LEU ASP TYR GLN GLU GLY ASP LEU          
SEQRES  17 C  377  PHE VAL GLN LYS ASP LEU ALA LYS THR LEU ASN GLN ILE          
SEQRES  18 C  377  LYS THR LEU GLY ALA LYS GLY PHE TYR GLN GLY GLN VAL          
SEQRES  19 C  377  ALA GLU LEU ILE GLU LYS ASP MET LYS LYS ASN GLY GLY          
SEQRES  20 C  377  ILE ILE THR LYS GLU ASP LEU ALA SER TYR ASN VAL LYS          
SEQRES  21 C  377  TRP ARG LYS PRO VAL VAL GLY SER TYR ARG GLY TYR LYS          
SEQRES  22 C  377  ILE ILE SER MET SER PRO PRO SER SER GLY GLY THR HIS          
SEQRES  23 C  377  LEU ILE GLN ILE LEU ASN VAL MET GLU ASN ALA ASP LEU          
SEQRES  24 C  377  SER ALA LEU GLY TYR GLY ALA SER LYS ASN ILE HIS ILE          
SEQRES  25 C  377  ALA ALA GLU ALA MET ARG GLN ALA TYR ALA ASP ARG SER          
SEQRES  26 C  377  VAL TYR MET GLY ASP ALA ASP PHE VAL SER VAL PRO VAL          
SEQRES  27 C  377  ASP LYS LEU ILE ASN LYS ALA TYR ALA LYS LYS ILE PHE          
SEQRES  28 C  377  ASP THR ILE GLN PRO ASP THR VAL THR PRO SER SER GLN          
SEQRES  29 C  377  ILE LYS PRO GLY MET GLY GLN LEU HIS GLU GLY SER ASN          
SEQRES   1 D  188  THR THR HIS TYR SER VAL ALA ASP ARG TRP GLY ASN ALA          
SEQRES   2 D  188  VAL SER VAL THR TYR THR ILE ASN ALA SER TYR GLY SER          
SEQRES   3 D  188  ALA ALA SER ILE ASP GLY ALA GLY PHE LEU LEU ASN ASN          
SEQRES   4 D  188  GLU MET ASP ASP PHE SER ILE LYS PRO GLY ASN PRO ASN          
SEQRES   5 D  188  LEU TYR GLY LEU VAL GLY GLY ASP ALA ASN ALA ILE GLU          
SEQRES   6 D  188  ALA ASN LYS ARG PRO LEU SER SER MET SER PRO THR ILE          
SEQRES   7 D  188  VAL LEU LYS ASN ASN LYS VAL PHE LEU VAL VAL GLY SER          
SEQRES   8 D  188  PRO GLY GLY SER ARG ILE ILE THR THR VAL LEU GLN VAL          
SEQRES   9 D  188  ILE SER ASN VAL ILE ASP TYR ASN MET ASN ILE SER GLU          
SEQRES  10 D  188  ALA VAL SER ALA PRO ARG PHE HIS MET GLN TRP LEU PRO          
SEQRES  11 D  188  ASP GLU LEU ARG ILE GLU LYS PHE GLY MET PRO ALA ASP          
SEQRES  12 D  188  VAL LYS ASP ASN LEU THR LYS MET GLY TYR GLN ILE VAL          
SEQRES  13 D  188  THR LYS PRO VAL MET GLY ASP VAL ASN ALA ILE GLN VAL          
SEQRES  14 D  188  LEU PRO LYS THR LYS GLY SER VAL PHE TYR GLY SER THR          
SEQRES  15 D  188  ASP PRO ARG LYS GLU PHE                                      
HET    GLU  B   1      10                                                       
HET    GLU  D   1      10                                                       
HETNAM     GLU GLUTAMIC ACID                                                    
FORMUL   5  GLU    2(C5 H9 N O4)                                                
FORMUL   7  HOH   *737(H2 O)                                                    
HELIX    1   1 HIS A   44  GLU A   57  1                                  14    
HELIX    2   2 ASN A   60  HIS A   76  1                                  17    
HELIX    3   3 GLY A  130  ALA A  134  5                                   5    
HELIX    4   4 GLY A  138  GLY A  151  1                                  14    
HELIX    5   5 LYS A  154  ILE A  159  1                                   6    
HELIX    6   6 ILE A  159  GLY A  169  1                                  11    
HELIX    7   7 SER A  173  LEU A  188  1                                  16    
HELIX    8   8 TYR A  190  PHE A  197  1                                   8    
HELIX    9   9 GLN A  213  GLY A  227  1                                  15    
HELIX   10  10 ALA A  228  GLN A  233  1                                   6    
HELIX   11  11 GLN A  233  ASN A  247  1                                  15    
HELIX   12  12 THR A  252  TYR A  259  1                                   8    
HELIX   13  13 SER A  284  GLU A  297  1                                  14    
HELIX   14  14 ASN A  298  ALA A  299  5                                   2    
HELIX   15  15 ASP A  300  LEU A  304  5                                   5    
HELIX   16  16 ALA A  308  MET A  330  1                                  23    
HELIX   17  17 PRO A  339  ILE A  344  1                                   6    
HELIX   18  18 ASN A  345  THR A  355  1                                  11    
HELIX   19  19 PRO A  363  ILE A  367  5                                   5    
HELIX   20  20 ASN B  418  PHE B  423  5                                   6    
HELIX   21  21 GLY B  472  SER B  474  5                                   3    
HELIX   22  22 ARG B  475  ASP B  489  1                                  15    
HELIX   23  23 ASN B  493  ALA B  500  1                                   8    
HELIX   24  24 PRO B  520  GLY B  531  1                                  12    
HELIX   25  25 HIS C   44  GLU C   57  1                                  14    
HELIX   26  26 ASN C   60  HIS C   76  1                                  17    
HELIX   27  27 GLY C  130  ALA C  134  5                                   5    
HELIX   28  28 GLY C  138  GLY C  151  1                                  14    
HELIX   29  29 LYS C  154  ILE C  159  1                                   6    
HELIX   30  30 ILE C  159  GLY C  169  1                                  11    
HELIX   31  31 SER C  173  ALA C  183  1                                  11    
HELIX   32  32 ALA C  183  LEU C  188  1                                   6    
HELIX   33  33 TYR C  190  PHE C  198  1                                   9    
HELIX   34  34 LYS C  199  LEU C  203  5                                   5    
HELIX   35  35 GLN C  213  GLY C  227  1                                  15    
HELIX   36  36 ALA C  228  GLN C  233  1                                   6    
HELIX   37  37 GLN C  233  ASN C  247  1                                  15    
HELIX   38  38 THR C  252  TYR C  259  1                                   8    
HELIX   39  39 SER C  284  ASN C  298  1                                  15    
HELIX   40  40 ALA C  299  LEU C  304  5                                   6    
HELIX   41  41 ALA C  308  MET C  330  1                                  23    
HELIX   42  42 PRO C  339  ASN C  345  1                                   7    
HELIX   43  43 ASN C  345  ILE C  356  1                                  12    
HELIX   44  44 PRO C  363  ILE C  367  5                                   5    
HELIX   45  45 ASN D  418  PHE D  423  5                                   6    
HELIX   46  46 GLY D  472  SER D  474  5                                   3    
HELIX   47  47 ARG D  475  ASP D  489  1                                  15    
HELIX   48  48 ASN D  493  ALA D  500  1                                   8    
HELIX   49  49 PRO D  520  GLY D  531  1                                  12    
SHEET    1   A 7 LYS A  33  ASN A  34  0                                        
SHEET    2   A 7 SER B 555  SER B 560 -1  O  PHE B 557   N  ASN A  34           
SHEET    3   A 7 ALA B 545  PRO B 550 -1  N  GLN B 547   O  TYR B 558           
SHEET    4   A 7 LYS B 463  VAL B 468 -1  N  VAL B 467   O  ILE B 546           
SHEET    5   A 7 THR B 456  LYS B 460 -1  N  THR B 456   O  VAL B 468           
SHEET    6   A 7 TYR A 274  SER A 278 -1  N  LYS A 275   O  LEU B 459           
SHEET    7   A 7 VAL A 267  TYR A 271 -1  N  VAL A 267   O  SER A 278           
SHEET    1   B 6 GLY A  38  LEU A  41  0                                        
SHEET    2   B 6 THR B 381  ASP B 387 -1  O  SER B 384   N  LEU A  41           
SHEET    3   B 6 ALA B 392  THR B 398 -1  O  VAL B 395   N  TYR B 383           
SHEET    4   B 6 GLY A  85  HIS A  91 -1  N  VAL A  89   O  SER B 394           
SHEET    5   B 6 ASN A  97  PHE A 102 -1  O  LEU A 100   N  ALA A  88           
SHEET    6   B 6 LYS A 262  ARG A 264 -1  O  LYS A 262   N  ASP A 101           
SHEET    1   C 2 TYR A 170  ALA A 171  0                                        
SHEET    2   C 2 LEU A 210  PHE A 211 -1  O  PHE A 211   N  TYR A 170           
SHEET    1   D 2 PHE A 198  LYS A 199  0                                        
SHEET    2   D 2 LEU A 203  ASP A 204 -1  O  LEU A 203   N  LYS A 199           
SHEET    1   E 2 LEU B 512  ILE B 514  0                                        
SHEET    2   E 2 ILE B 534  THR B 536  1  O  VAL B 535   N  ILE B 514           
SHEET    1   F 7 LYS C  33  ASN C  34  0                                        
SHEET    2   F 7 SER D 555  SER D 560 -1  O  PHE D 557   N  ASN C  34           
SHEET    3   F 7 ALA D 545  PRO D 550 -1  N  GLN D 547   O  TYR D 558           
SHEET    4   F 7 LYS D 463  VAL D 468 -1  N  VAL D 467   O  ILE D 546           
SHEET    5   F 7 THR D 456  LYS D 460 -1  N  VAL D 458   O  PHE D 465           
SHEET    6   F 7 TYR C 274  SER C 278 -1  N  ILE C 277   O  ILE D 457           
SHEET    7   F 7 VAL C 267  TYR C 271 -1  N  VAL C 267   O  SER C 278           
SHEET    1   G 6 GLY C  38  LEU C  41  0                                        
SHEET    2   G 6 THR D 381  ASP D 387 -1  O  SER D 384   N  LEU C  41           
SHEET    3   G 6 ALA D 392  THR D 398 -1  O  VAL D 395   N  TYR D 383           
SHEET    4   G 6 GLY C  85  HIS C  91 -1  N  VAL C  89   O  SER D 394           
SHEET    5   G 6 ASN C  97  PHE C 102 -1  O  LEU C 100   N  ALA C  88           
SHEET    6   G 6 LYS C 262  ARG C 264 -1  O  LYS C 262   N  ASP C 101           
SHEET    1   H 2 TYR C 170  ALA C 171  0                                        
SHEET    2   H 2 LEU C 210  PHE C 211 -1  O  PHE C 211   N  TYR C 170           
SHEET    1   I 2 LEU D 512  ILE D 514  0                                        
SHEET    2   I 2 ILE D 534  THR D 536  1  O  VAL D 535   N  ILE D 514           
CISPEP   1 PRO A  281    PRO A  282          0        14.23                     
CISPEP   2 LEU B  508    PRO B  509          0        -0.96                     
CISPEP   3 PRO C  281    PRO C  282          0        14.84                     
CISPEP   4 LEU D  508    PRO D  509          0        -1.05                     
SITE     1 AC1 14 ARG A 103  THR B 380  ASN B 400  GLU B 419                    
SITE     2 AC1 14 ASP B 422  TYR B 433  SER B 451  SER B 452                    
SITE     3 AC1 14 MET B 453  GLY B 472  GLY B 473  ILE B 476                    
SITE     4 AC1 14 HOH B 608  HOH B 692                                          
SITE     1 AC2 13 ARG C 103  THR D 380  ASN D 400  GLU D 419                    
SITE     2 AC2 13 ASP D 422  TYR D 433  SER D 451  SER D 452                    
SITE     3 AC2 13 MET D 453  GLY D 472  GLY D 473  ILE D 476                    
SITE     4 AC2 13 HOH D 580                                                     
CRYST1   54.983  104.762   91.910  90.00  91.85  90.00 P 1 21 1      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      0.018187  0.000000  0.000588        0.00000                         
SCALE2      0.000000  0.009545  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010886        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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