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Database: PDB
Entry: 2QMC
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Original site: 2QMC 
HEADER    TRANSFERASE                             15-JUL-07   2QMC              
TITLE     CRYSTAL STRUCTURE OF HELICOBACTER PYLORI GAMMA-GLUTAMYLTRANSPEPTIDASE 
TITLE    2 T380A MUTANT                                                         
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;                                                     
COMPND  15 MUTATION: 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: PDUET;                                    
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: PDUET                                     
KEYWDS    NTN-HYDROLASE, GLUTAMYLTRANSPEPTIDASE, TRANSFERASE                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.J.BARYCKI,G.BOANCA,A.SAND                                           
REVDAT   4   25-OCT-17 2QMC    1       REMARK                                   
REVDAT   3   13-JUL-11 2QMC    1       VERSN                                    
REVDAT   2   24-FEB-09 2QMC    1       VERSN                                    
REVDAT   1   12-FEB-08 2QMC    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.    1.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
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) : 1.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.35                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 134438                         
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) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 13319                           
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) : 1.55                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.59                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8423                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.26                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2200                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 918                          
REMARK   3   BIN FREE R VALUE                    : 0.2650                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8029                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 588                                     
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) : 21.13                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.29000                                              
REMARK   3    B22 (A**2) : -1.25000                                             
REMARK   3    B33 (A**2) : -0.03000                                             
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): 0.098         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.096         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.062         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.356         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.954                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8248 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11153 ; 1.354 ; 1.972       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1067 ; 6.132 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   328 ;37.836 ;25.274       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1434 ;12.449 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;14.798 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1248 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6172 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4112 ; 0.196 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5777 ; 0.304 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   561 ; 0.101 ; 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):    81 ; 0.188 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    31 ; 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):  5413 ; 0.685 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8466 ; 0.993 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3190 ; 1.860 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2687 ; 2.864 ; 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  : 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   122                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.2613  14.5949  28.2256              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1175 T22:  -0.0765                                     
REMARK   3      T33:  -0.0872 T12:   0.0134                                     
REMARK   3      T13:  -0.0234 T23:  -0.0134                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0527 L22:   1.0189                                     
REMARK   3      L33:   1.6227 L12:   0.1664                                     
REMARK   3      L13:  -0.3904 L23:  -0.1839                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0413 S12:   0.0067 S13:   0.0191                       
REMARK   3      S21:  -0.0624 S22:   0.0179 S23:  -0.0202                       
REMARK   3      S31:  -0.1181 S32:   0.0464 S33:   0.0234                       
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   123        A   196                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.9632  19.4276  31.5255              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0491 T22:  -0.0325                                     
REMARK   3      T33:  -0.0837 T12:   0.0467                                     
REMARK   3      T13:  -0.0208 T23:  -0.0255                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6468 L22:   0.8813                                     
REMARK   3      L33:   1.7277 L12:  -0.1220                                     
REMARK   3      L13:  -0.0423 L23:  -0.3939                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0438 S12:   0.0103 S13:   0.0619                       
REMARK   3      S21:  -0.0481 S22:   0.0634 S23:   0.0834                       
REMARK   3      S31:  -0.1544 S32:  -0.2004 S33:  -0.0197                       
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   197        A   353                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.6727   6.2671  32.1227              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1182 T22:  -0.0326                                     
REMARK   3      T33:  -0.1156 T12:   0.0054                                     
REMARK   3      T13:   0.0002 T23:   0.0212                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4863 L22:   1.2730                                     
REMARK   3      L33:   0.8461 L12:  -0.1975                                     
REMARK   3      L13:  -0.0015 L23:   0.4165                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0385 S12:  -0.0628 S13:   0.0270                       
REMARK   3      S21:   0.0563 S22:   0.0828 S23:  -0.0623                       
REMARK   3      S31:  -0.0058 S32:  -0.0014 S33:  -0.0443                       
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   354        A   372                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.9733 -21.6063  30.3581              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0448 T22:  -0.0217                                     
REMARK   3      T33:   0.0340 T12:   0.0163                                     
REMARK   3      T13:  -0.0069 T23:   0.0405                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4716 L22:   3.3791                                     
REMARK   3      L33:   2.1573 L12:   0.6407                                     
REMARK   3      L13:  -0.9713 L23:   1.2263                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0463 S12:  -0.0179 S13:  -0.3407                       
REMARK   3      S21:   0.1313 S22:  -0.0159 S23:  -0.4288                       
REMARK   3      S31:   0.3367 S32:   0.3268 S33:  -0.0304                       
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   459                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.8467   8.2838  33.9731              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1231 T22:  -0.0418                                     
REMARK   3      T33:  -0.1062 T12:   0.0202                                     
REMARK   3      T13:  -0.0124 T23:   0.0041                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6396 L22:   0.8623                                     
REMARK   3      L33:   1.1620 L12:  -0.1038                                     
REMARK   3      L13:  -0.0974 L23:   0.1718                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0633 S12:  -0.1069 S13:  -0.0358                       
REMARK   3      S21:   0.0674 S22:   0.0458 S23:   0.0297                       
REMARK   3      S31:   0.0415 S32:  -0.0461 S33:   0.0176                       
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   460        B   555                          
REMARK   3    ORIGIN FOR THE GROUP (A):  23.8427  -4.3162  17.2440              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0884 T22:  -0.0340                                     
REMARK   3      T33:  -0.1128 T12:  -0.0027                                     
REMARK   3      T13:  -0.0193 T23:   0.0032                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6488 L22:   2.3531                                     
REMARK   3      L33:   1.0524 L12:   0.2227                                     
REMARK   3      L13:   0.0848 L23:   0.0622                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0660 S12:   0.0752 S13:   0.0078                       
REMARK   3      S21:  -0.1718 S22:   0.1084 S23:   0.0283                       
REMARK   3      S31:   0.0781 S32:  -0.0276 S33:  -0.0425                       
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):  24.2525   8.1877  11.5234              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0008 T22:  -0.0252                                     
REMARK   3      T33:   0.0006 T12:  -0.0003                                     
REMARK   3      T13:  -0.0070 T23:   0.0590                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  19.7244 L22:   8.9714                                     
REMARK   3      L33:   5.4998 L12:  13.2923                                     
REMARK   3      L13:  -7.3964 L23:  -5.1775                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0327 S12:   0.5877 S13:   0.7339                       
REMARK   3      S21:  -0.4048 S22:   0.4555 S23:   0.3970                       
REMARK   3      S31:  -0.1144 S32:  -0.4376 S33:  -0.4227                       
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   141                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.4834   9.0099 -18.4786              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0145 T22:  -0.0510                                     
REMARK   3      T33:   0.1191 T12:   0.0556                                     
REMARK   3      T13:   0.1054 T23:   0.1048                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5468 L22:   1.3295                                     
REMARK   3      L33:   1.6235 L12:   0.0197                                     
REMARK   3      L13:  -0.3189 L23:  -0.0462                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1963 S12:   0.1410 S13:   0.4036                       
REMARK   3      S21:   0.1429 S22:  -0.0095 S23:   0.1427                       
REMARK   3      S31:  -0.2310 S32:  -0.0969 S33:  -0.1868                       
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   142        C   211                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.2316  16.8523 -17.2354              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1517 T22:  -0.0269                                     
REMARK   3      T33:   0.1580 T12:   0.0309                                     
REMARK   3      T13:   0.1051 T23:   0.0988                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5621 L22:   1.8650                                     
REMARK   3      L33:   1.1372 L12:   1.0813                                     
REMARK   3      L13:  -0.3994 L23:  -0.2441                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1550 S12:   0.1094 S13:   0.5055                       
REMARK   3      S21:   0.3712 S22:   0.0114 S23:   0.1245                       
REMARK   3      S31:  -0.2222 S32:   0.1515 S33:  -0.1664                       
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   212        C   349                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.4681  -0.2452 -18.8789              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0691 T22:  -0.0052                                     
REMARK   3      T33:   0.0114 T12:   0.0561                                     
REMARK   3      T13:   0.0373 T23:   0.0569                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1646 L22:   0.9169                                     
REMARK   3      L33:   1.0541 L12:   0.3129                                     
REMARK   3      L13:  -0.1435 L23:  -0.5280                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1362 S12:   0.2157 S13:   0.2684                       
REMARK   3      S21:  -0.0065 S22:   0.0844 S23:   0.2182                       
REMARK   3      S31:  -0.0591 S32:  -0.1972 S33:  -0.2206                       
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   350        C   379                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.5119 -24.3420 -14.3971              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0509 T22:   0.0112                                     
REMARK   3      T33:   0.0605 T12:  -0.0536                                     
REMARK   3      T13:  -0.0456 T23:  -0.0173                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3710 L22:   1.8111                                     
REMARK   3      L33:   0.3639 L12:  -0.5853                                     
REMARK   3      L13:  -0.8336 L23:   0.6641                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1166 S12:  -0.0029 S13:  -0.1608                       
REMARK   3      S21:  -0.0092 S22:  -0.0677 S23:   0.3257                       
REMARK   3      S31:   0.5092 S32:  -0.2253 S33:  -0.0489                       
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   459                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.8535   2.5319 -20.4930              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0579 T22:  -0.0320                                     
REMARK   3      T33:   0.0160 T12:   0.0590                                     
REMARK   3      T13:   0.0608 T23:   0.0802                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3242 L22:   0.7446                                     
REMARK   3      L33:   1.0636 L12:   0.2101                                     
REMARK   3      L13:  -0.2179 L23:  -0.5008                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1541 S12:   0.2057 S13:   0.2507                       
REMARK   3      S21:   0.0476 S22:   0.0165 S23:   0.1258                       
REMARK   3      S31:  -0.0817 S32:  -0.0198 S33:  -0.1706                       
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   460        D   553                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.9258  -6.6758  -1.8836              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0447 T22:  -0.0567                                     
REMARK   3      T33:  -0.0433 T12:  -0.0262                                     
REMARK   3      T13:   0.0242 T23:  -0.0098                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3824 L22:   1.3346                                     
REMARK   3      L33:   1.6424 L12:  -0.0456                                     
REMARK   3      L13:  -0.2192 L23:  -0.3216                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1941 S12:  -0.1390 S13:   0.1779                       
REMARK   3      S21:   0.1306 S22:   0.0115 S23:   0.0488                       
REMARK   3      S31:  -0.0703 S32:  -0.0512 S33:  -0.2055                       
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   554        D   565                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.1436   7.8058   1.8664              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1477 T22:   0.1208                                     
REMARK   3      T33:   0.0884 T12:   0.0241                                     
REMARK   3      T13:   0.1057 T23:  -0.0766                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.8701 L22:  16.0034                                     
REMARK   3      L33:   0.2538 L12: -12.9556                                     
REMARK   3      L13:  -0.8061 L23:   1.2910                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4905 S12:  -0.8450 S13:   0.0490                       
REMARK   3      S21:   0.4074 S22:   0.4731 S23:  -0.0712                       
REMARK   3      S31:  -0.2432 S32:  -0.0708 S33:   0.0174                       
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 2QMC 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 DEPOSITION ID IS D_1000043778.                                   
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 : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 135161                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550                              
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     (%) : 93.2                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : 0.08400                            
REMARK 200  R SYM                      (I) : 0.06800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.61                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.53800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.41300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.590                              
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   (%): 41.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11                     
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       53.33700            
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: 11620 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: 11420 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     GLN A   373                                                      
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 C 154    CG   CD   CE   NZ                                   
REMARK 470     LYS D 551    CG   CD   CE   NZ                                   
REMARK 470     LYS D 553    CG   CD   CE   NZ                                   
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    ALA A  79      -47.79   -142.47                                   
REMARK 500    MET A 371        1.89     55.80                                   
REMARK 500    ASN B 400     -108.25     83.71                                   
REMARK 500    ALA B 406       -1.50     71.92                                   
REMARK 500    ASN B 446       -6.48     71.81                                   
REMARK 500    PHE B 465      -50.71   -121.49                                   
REMARK 500    TRP B 507      -62.96     79.35                                   
REMARK 500    ASP B 542       79.89   -160.20                                   
REMARK 500    LYS C  36      -54.66   -121.23                                   
REMARK 500    ALA C  79      -46.72   -144.94                                   
REMARK 500    LYS C 125       -0.78     68.57                                   
REMARK 500    ASN D 400     -106.46     81.85                                   
REMARK 500    ALA D 406       -0.13     69.50                                   
REMARK 500    ASN D 418       47.66   -109.61                                   
REMARK 500    ASN D 446      -11.05     73.83                                   
REMARK 500    TRP D 507      -64.01     76.93                                   
REMARK 500    ASP D 542       80.91   -162.14                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     GTB B    1                                                       
REMARK 610     GTB D    1                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTB B 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTB D 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2NQO   RELATED DB: PDB                                   
REMARK 900 APOENZYME                                                            
REMARK 900 RELATED ID: 2QM6   RELATED DB: PDB                                   
DBREF  2QMC A   25   379  UNP    O25743   O25743_HELPY    25    379             
DBREF  2QMC B  380   567  UNP    O25743   O25743_HELPY   380    567             
DBREF  2QMC C   25   379  UNP    O25743   O25743_HELPY    25    379             
DBREF  2QMC D  380   567  UNP    O25743   O25743_HELPY   380    567             
SEQADV 2QMC MET A    3  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC GLY A    4  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC SER A    5  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC SER A    6  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC HIS A    7  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC HIS A    8  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC HIS A    9  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC HIS A   10  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC HIS A   11  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC HIS A   12  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC SER A   13  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC SER A   14  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC GLY A   15  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC LEU A   16  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC VAL A   17  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC PRO A   18  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC ARG A   19  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC GLY A   20  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC SER A   21  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC HIS A   22  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC MET A   23  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC ALA A   24  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC ALA B  380  UNP  O25743    THR   380 ENGINEERED                     
SEQADV 2QMC MET C    3  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC GLY C    4  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC SER C    5  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC SER C    6  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC HIS C    7  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC HIS C    8  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC HIS C    9  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC HIS C   10  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC HIS C   11  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC HIS C   12  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC SER C   13  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC SER C   14  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC GLY C   15  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC LEU C   16  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC VAL C   17  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC PRO C   18  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC ARG C   19  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC GLY C   20  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC SER C   21  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC HIS C   22  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC MET C   23  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC ALA C   24  UNP  O25743              EXPRESSION TAG                 
SEQADV 2QMC ALA D  380  UNP  O25743    THR   380 ENGINEERED                     
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  ALA 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  ALA 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    GTB  B   1      15                                                       
HET    GTB  D   1      15                                                       
HETNAM     GTB S-(P-NITROBENZYL)GLUTATHIONE                                     
FORMUL   5  GTB    2(C17 H22 N4 O8 S)                                           
FORMUL   7  HOH   *588(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  SER A  258  1                                   7    
HELIX   13  13 SER A  284  GLU A  297  1                                  14    
HELIX   14  14 ASP A  300  GLY A  305  1                                   6    
HELIX   15  15 ALA A  308  MET A  330  1                                  23    
HELIX   16  16 PRO A  339  ILE A  344  1                                   6    
HELIX   17  17 ASN A  345  THR A  355  1                                  11    
HELIX   18  18 PRO A  363  ILE A  367  5                                   5    
HELIX   19  19 LYS A  368  GLY A  372  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  ASN B  491  1                                  17    
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  GLY C  169  1                                  16    
HELIX   30  30 SER C  173  ALA C  183  1                                  11    
HELIX   31  31 ALA C  183  LEU C  188  1                                   6    
HELIX   32  32 TYR C  190  PHE C  197  1                                   8    
HELIX   33  33 GLN C  213  GLY C  227  1                                  15    
HELIX   34  34 ALA C  228  GLN C  233  1                                   6    
HELIX   35  35 GLN C  233  ASN C  247  1                                  15    
HELIX   36  36 THR C  252  TYR C  259  1                                   8    
HELIX   37  37 SER C  284  GLU C  297  1                                  14    
HELIX   38  38 ASN C  298  ALA C  299  5                                   2    
HELIX   39  39 ASP C  300  LEU C  304  5                                   5    
HELIX   40  40 ALA C  308  MET C  330  1                                  23    
HELIX   41  41 PRO C  339  ILE C  344  1                                   6    
HELIX   42  42 ASN C  345  ILE C  356  1                                  12    
HELIX   43  43 PRO C  363  ILE C  367  5                                   5    
HELIX   44  44 ASN D  418  PHE D  423  5                                   6    
HELIX   45  45 GLY D  472  SER D  474  5                                   3    
HELIX   46  46 ARG D  475  ASN D  491  1                                  17    
HELIX   47  47 ASN D  493  ALA D  500  1                                   8    
HELIX   48  48 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  ILE A 277   O  ILE B 457           
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  GLY A  85   O  THR B 398           
SHEET    5   B 6 ASN A  97  PHE A 102 -1  O  VAL A  98   N  ILE A  90           
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  PHE D 465   O  VAL D 548           
SHEET    5   F 7 THR D 456  LYS D 460 -1  N  THR D 456   O  VAL D 468           
SHEET    6   F 7 TYR C 274  SER C 278 -1  N  LYS C 275   O  LEU D 459           
SHEET    7   F 7 VAL C 267  TYR C 271 -1  N  GLY C 269   O  ILE C 276           
SHEET    1   G 6 LEU C  39  LEU C  41  0                                        
SHEET    2   G 6 THR D 381  ALA D 386 -1  O  SER D 384   N  LEU C  41           
SHEET    3   G 6 ALA D 392  THR D 398 -1  O  VAL D 393   N  VAL D 385           
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 PHE C 198  LYS C 199  0                                        
SHEET    2   I 2 LEU C 203  ASP C 204 -1  O  LEU C 203   N  LYS C 199           
SHEET    1   J 2 LEU D 512  ILE D 514  0                                        
SHEET    2   J 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        15.34                     
CISPEP   2 LEU B  508    PRO B  509          0        -1.91                     
CISPEP   3 PRO C  281    PRO C  282          0        11.75                     
CISPEP   4 LEU D  508    PRO D  509          0        -2.02                     
SITE     1 AC1 15 ARG A 103  ALA B 380  ASN B 400  ALA B 401                    
SITE     2 AC1 15 SER B 402  GLU B 419  ASP B 422  TYR B 433                    
SITE     3 AC1 15 SER B 451  SER B 452  MET B 453  PRO B 471                    
SITE     4 AC1 15 GLY B 472  GLY B 473  HOH B 601                               
SITE     1 AC2 15 ARG C 103  ALA D 380  ASN D 400  ALA D 401                    
SITE     2 AC2 15 SER D 402  GLU D 419  ASP D 422  TYR D 433                    
SITE     3 AC2 15 SER D 451  SER D 452  MET D 453  PRO D 471                    
SITE     4 AC2 15 GLY D 472  GLY D 473  HOH D 600                               
CRYST1   57.140  106.674   87.194  90.00 104.96  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      0.017501  0.000000  0.004677        0.00000                         
SCALE2      0.000000  0.009374  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011871        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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