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Database: PDB
Entry: 6MGG
LinkDB: 6MGG
Original site: 6MGG 
HEADER    LIGASE                                  13-SEP-18   6MGG              
TITLE     SUCCINYL-COA SYNTHASE FROM FRANCISELLA TULARENSIS, PHOSPHORYLATED, IN 
TITLE    2 COMPLEX WITH COA                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUCCINATE--COA LIGASE [ADP-FORMING] SUBUNIT ALPHA;         
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: SUCCINYL-COA SYNTHETASE SUBUNIT ALPHA,SCS-ALPHA;            
COMPND   5 EC: 6.2.1.5;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 OTHER_DETAILS: H247 IS PHOSPHORYLATED;                               
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: SUCCINATE--COA LIGASE [ADP-FORMING] SUBUNIT BETA;          
COMPND  11 CHAIN: B, D;                                                         
COMPND  12 SYNONYM: SUCCINYL-COA SYNTHETASE SUBUNIT BETA,SCS-BETA;              
COMPND  13 EC: 6.2.1.5;                                                         
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: FRANCISELLA TULARENSIS SUBSP. TULARENSIS        
SOURCE   3 (STRAIN SCHU S4 / SCHU 4);                                           
SOURCE   4 ORGANISM_TAXID: 177416;                                              
SOURCE   5 STRAIN: SCHU S4 / SCHU 4;                                            
SOURCE   6 GENE: SUCD, BZ14_337;                                                
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PMCSG92;                                  
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: FRANCISELLA TULARENSIS SUBSP. TULARENSIS        
SOURCE  14 (STRAIN SCHU S4 / SCHU 4);                                           
SOURCE  15 ORGANISM_TAXID: 177416;                                              
SOURCE  16 STRAIN: SCHU S4 / SCHU 4;                                            
SOURCE  17 GENE: SUCC, FTT_0504C;                                               
SOURCE  18 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  20 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  22 EXPRESSION_SYSTEM_PLASMID: PMCSG92                                   
KEYWDS    SUCCINYL-COA SYNTHASE, STRUCTURAL GENOMICS, CPX_02187_02692,          
KEYWDS   2 IDP02187, IDP02692, CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS     
KEYWDS   3 DISEASES, CSGID, LIGASE                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.OSIPIUK,N.MALTSEVA,R.JEDRZEJCZAK,K.J.F.SATCHELL,A.JOACHIMIAK,CENTER 
AUTHOR   2 FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES (CSGID)               
REVDAT   1   26-SEP-18 6MGG    0                                                
JRNL        AUTH   J.OSIPIUK,N.MALTSEVA,R.JEDRZEJCZAK,K.J.F.SATCHELL,           
JRNL        AUTH 2 A.JOACHIMIAK,                                                
JRNL        AUTH 3 CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES        
JRNL        AUTH 4 (CSGID)                                                      
JRNL        TITL   SUCCINYL-COA SYNTHASE FROM FRANCISELLA TULARENSIS            
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.78 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0230                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.78                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.18                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 128013                         
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) : 0.178                           
REMARK   3   R VALUE            (WORKING SET) : 0.177                           
REMARK   3   FREE R VALUE                     : 0.214                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6633                            
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) : 1.78                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.83                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 9069                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.45                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2720                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 444                          
REMARK   3   BIN FREE R VALUE                    : 0.3120                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10037                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 114                                     
REMARK   3   SOLVENT ATOMS            : 1076                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.44000                                              
REMARK   3    B22 (A**2) : -0.68000                                             
REMARK   3    B33 (A**2) : -0.46000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.19000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.119         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.116         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.084         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.323         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.962                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.944                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10446 ; 0.011 ; 0.014       
REMARK   3   BOND LENGTHS OTHERS               (A):  9976 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14168 ; 1.522 ; 1.667       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 23336 ; 0.983 ; 1.652       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1384 ; 6.147 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   439 ;37.922 ;24.647       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1835 ;14.061 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    34 ;17.900 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1401 ; 0.076 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11707 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1765 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     2        A   502                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.7817  53.7023   9.4155              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0276 T22:   0.1155                                     
REMARK   3      T33:   0.0788 T12:  -0.0250                                     
REMARK   3      T13:  -0.0145 T23:   0.0291                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2027 L22:   0.4562                                     
REMARK   3      L33:   0.2339 L12:  -0.2041                                     
REMARK   3      L13:  -0.0609 L23:  -0.0696                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0001 S12:  -0.0464 S13:  -0.0110                       
REMARK   3      S21:   0.0233 S22:  -0.0717 S23:  -0.0463                       
REMARK   3      S31:  -0.0210 S32:   0.0771 S33:   0.0719                       
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 :   B     1        B   502                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.1306  33.1107  -2.4950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0581 T22:   0.0581                                     
REMARK   3      T33:   0.1047 T12:  -0.0093                                     
REMARK   3      T13:  -0.0126 T23:   0.0132                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1210 L22:   0.0440                                     
REMARK   3      L33:   0.5047 L12:   0.0642                                     
REMARK   3      L13:  -0.0463 L23:  -0.0306                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0130 S12:  -0.0290 S13:  -0.0572                       
REMARK   3      S21:  -0.0090 S22:  -0.0291 S23:  -0.0366                       
REMARK   3      S31:   0.0367 S32:  -0.0140 S33:   0.0161                       
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 :   C     2        C   502                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.9745   0.0677  32.4115              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0525 T22:   0.0744                                     
REMARK   3      T33:   0.0700 T12:   0.0060                                     
REMARK   3      T13:   0.0048 T23:  -0.0006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1799 L22:   0.4896                                     
REMARK   3      L33:   0.2092 L12:  -0.0245                                     
REMARK   3      L13:  -0.1095 L23:   0.1330                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0278 S12:  -0.0210 S13:   0.0240                       
REMARK   3      S21:   0.0272 S22:   0.0362 S23:   0.0031                       
REMARK   3      S31:   0.0072 S32:   0.0243 S33:  -0.0084                       
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 :   D     1        D   502                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.0020  -0.1281  21.4464              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0017 T22:   0.1638                                     
REMARK   3      T33:   0.1201 T12:  -0.0087                                     
REMARK   3      T13:  -0.0110 T23:  -0.0093                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0470 L22:   0.2906                                     
REMARK   3      L33:   0.3271 L12:  -0.1080                                     
REMARK   3      L13:  -0.0754 L23:   0.1144                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0036 S12:  -0.0196 S13:   0.0476                       
REMARK   3      S21:   0.0077 S22:   0.0290 S23:  -0.0972                       
REMARK   3      S31:  -0.0117 S32:   0.1577 S33:  -0.0255                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 6MGG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-SEP-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000236894.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-JUL-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 134691                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.780                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.180                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.78                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.71200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.790                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: HKL-3000                                              
REMARK 200 STARTING MODEL: 1JKJ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M MAGNESIUM CHLORIDE, 0.1 M TRIS     
REMARK 280  BUFFER, 16% PEG 4000, PH 8.5, VAPOR DIFFUSION, SITTING DROP,        
REMARK 280  TEMPERATURE 289K                                                    
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       79.16900            
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                                                    
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5770 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5240 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     1                                                      
REMARK 465     PHE A   295                                                      
REMARK 465     GLN A   296                                                      
REMARK 465     MET C     1                                                      
REMARK 465     GLY D   322                                                      
REMARK 465     ILE D   323                                                      
REMARK 465     VAL D   324                                                      
REMARK 465     ARG D   325                                                      
REMARK 465     ASN D   353                                                      
REMARK 465     ASN D   354                                                      
REMARK 465     ALA D   355                                                      
REMARK 465     GLU D   356                                                      
REMARK 465     LYS D   357                                                      
REMARK 465     GLY D   358                                                      
REMARK 465     ALA D   359                                                      
REMARK 465     LYS D   360                                                      
REMARK 465     ILE D   361                                                      
REMARK 465     LEU D   362                                                      
REMARK 465     ALA D   363                                                      
REMARK 465     ASP D   364                                                      
REMARK 465     SER D   365                                                      
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 A   645     O    HOH A   664              2.18            
REMARK 500   O    HOH B   680     O    HOH B   755              2.18            
REMARK 500   OE2  GLU C   132     O    HOH C   601              2.19            
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    LEU A   4      -41.68     69.56                                   
REMARK 500    ASP A 116       46.36   -106.17                                   
REMARK 500    GLU A 132      -56.55   -136.11                                   
REMARK 500    SER A 173      -71.05    -77.83                                   
REMARK 500    ASN A 292      116.74   -176.42                                   
REMARK 500    GLU B 129       57.57    -90.88                                   
REMARK 500    ASN B 354       36.95     75.04                                   
REMARK 500    ASP B 373      -72.75    -86.87                                   
REMARK 500    LEU C   4      -43.54     72.11                                   
REMARK 500    ASP C 116       55.18   -103.15                                   
REMARK 500    GLU C 132      -47.09   -134.94                                   
REMARK 500    SER C 173      -71.56    -84.80                                   
REMARK 500    HIS D  50       82.55    -67.37                                   
REMARK 500    ALA D  51      145.51    179.21                                   
REMARK 500    ALA D  57        3.76    -66.25                                   
REMARK 500    PHE D  84       -4.23    -54.92                                   
REMARK 500    VAL D  93       79.28   -110.29                                   
REMARK 500    ASP D 214     -152.39   -145.27                                   
REMARK 500    ASP D 373      -77.20    -76.29                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A 275         0.08    SIDE CHAIN                              
REMARK 500    ARG B  70         0.08    SIDE CHAIN                              
REMARK 500    ARG B 298         0.08    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH D 840        DISTANCE =  6.40 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 502  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 NEP A 247   O2P                                                    
REMARK 620 2 HOH A 695   O   102.9                                              
REMARK 620 3 HOH A 628   O   168.2  88.8                                        
REMARK 620 4 HOH A 636   O    95.3  87.9  86.2                                  
REMARK 620 5 HOH A 647   O    85.1 171.6  83.2  89.1                            
REMARK 620 6 HOH B 545   O    91.3  90.9  87.3 173.4  91.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 502  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 NEP C 247   O2P                                                    
REMARK 620 2 HOH C 635   O   173.9                                              
REMARK 620 3 HOH C 645   O    95.5  83.5                                        
REMARK 620 4 HOH C 733   O    98.5  87.5  88.8                                  
REMARK 620 5 HOH C 721   O    91.5  82.6  95.5 168.7                            
REMARK 620 6 HOH D 662   O    96.7  84.7 167.5  86.5  87.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue COA A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue COA C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 502                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: CSGID-IDP02692   RELATED DB: TARGETTRACK                 
REMARK 900 RELATED ID: CPX_02187_02692   RELATED DB: TARGETTRACK                
DBREF1 6MGG A    1   290  UNP                  A0A0G2RQ73_FRATT                 
DBREF2 6MGG A     A0A0G2RQ73                          1         290             
DBREF  6MGG B    1   387  UNP    Q5NHF3   SUCC_FRATT       1    387             
DBREF1 6MGG C    1   290  UNP                  A0A0G2RQ73_FRATT                 
DBREF2 6MGG C     A0A0G2RQ73                          1         290             
DBREF  6MGG D    1   387  UNP    Q5NHF3   SUCC_FRATT       1    387             
SEQADV 6MGG VAL A   85  UNP  A0A0G2RQ7 ALA    85 ENGINEERED MUTATION            
SEQADV 6MGG GLU A  291  UNP  A0A0G2RQ7           EXPRESSION TAG                 
SEQADV 6MGG ASN A  292  UNP  A0A0G2RQ7           EXPRESSION TAG                 
SEQADV 6MGG LEU A  293  UNP  A0A0G2RQ7           EXPRESSION TAG                 
SEQADV 6MGG TYR A  294  UNP  A0A0G2RQ7           EXPRESSION TAG                 
SEQADV 6MGG PHE A  295  UNP  A0A0G2RQ7           EXPRESSION TAG                 
SEQADV 6MGG GLN A  296  UNP  A0A0G2RQ7           EXPRESSION TAG                 
SEQADV 6MGG THR B   69  UNP  Q5NHF3    ALA    69 ENGINEERED MUTATION            
SEQADV 6MGG VAL C   85  UNP  A0A0G2RQ7 ALA    85 ENGINEERED MUTATION            
SEQADV 6MGG GLU C  291  UNP  A0A0G2RQ7           EXPRESSION TAG                 
SEQADV 6MGG ASN C  292  UNP  A0A0G2RQ7           EXPRESSION TAG                 
SEQADV 6MGG LEU C  293  UNP  A0A0G2RQ7           EXPRESSION TAG                 
SEQADV 6MGG TYR C  294  UNP  A0A0G2RQ7           EXPRESSION TAG                 
SEQADV 6MGG PHE C  295  UNP  A0A0G2RQ7           EXPRESSION TAG                 
SEQADV 6MGG GLN C  296  UNP  A0A0G2RQ7           EXPRESSION TAG                 
SEQADV 6MGG THR D   69  UNP  Q5NHF3    ALA    69 ENGINEERED MUTATION            
SEQRES   1 A  296  MET SER VAL LEU VAL ASP LYS ASN THR LYS VAL LEU VAL          
SEQRES   2 A  296  GLN GLY PHE THR GLY LYS ASN GLY THR PHE HIS SER GLU          
SEQRES   3 A  296  GLN ALA ILE ALA TYR GLY THR ASN ILE VAL GLY GLY VAL          
SEQRES   4 A  296  THR PRO GLY LYS GLY GLY THR THR HIS LEU ASP ARG PRO          
SEQRES   5 A  296  VAL PHE ASN THR MET ALA GLU ALA VAL ALA ALA THR GLY          
SEQRES   6 A  296  ALA ASP ALA SER VAL ILE TYR VAL PRO ALA PRO PHE VAL          
SEQRES   7 A  296  LYS ASP SER ALA ILE GLU VAL ILE ASP SER GLY VAL LYS          
SEQRES   8 A  296  LEU VAL VAL ILE ILE THR GLU GLY VAL PRO THR LEU ASP          
SEQRES   9 A  296  MET LEU VAL VAL LYS GLU TYR LEU LYS ASP LYS ASP VAL          
SEQRES  10 A  296  ARG VAL ILE GLY PRO ASN CYS PRO GLY ILE ILE THR PRO          
SEQRES  11 A  296  GLY GLU CYS LYS ILE GLY ILE MET PRO GLY HIS ILE HIS          
SEQRES  12 A  296  MET LYS GLY LYS VAL GLY ILE ILE SER ARG SER GLY THR          
SEQRES  13 A  296  LEU THR TYR GLU ALA VAL ALA GLN THR THR LYS LEU GLY          
SEQRES  14 A  296  PHE GLY GLN SER THR CYS ILE GLY ILE GLY GLY ASP PRO          
SEQRES  15 A  296  ILE PRO GLY MET ASN GLN ILE GLU ALA LEU LYS LEU LEU          
SEQRES  16 A  296  GLU ASN ASP PRO GLN THR GLU ALA ILE ILE LEU ILE GLY          
SEQRES  17 A  296  GLU ILE GLY GLY THR ALA GLU GLU GLU ALA ALA GLU TYR          
SEQRES  18 A  296  ILE LYS HIS ASN VAL THR LYS PRO VAL ILE GLY TYR ILE          
SEQRES  19 A  296  ALA GLY VAL THR ALA PRO PRO GLY LYS ARG MET GLY NEP          
SEQRES  20 A  296  ALA GLY ALA ILE ILE SER GLY GLY LYS GLY THR ALA GLU          
SEQRES  21 A  296  GLU LYS PHE ALA ALA PHE GLU ALA ALA GLY ILE ALA TYR          
SEQRES  22 A  296  THR ARG SER PRO ALA GLU ILE GLY LYS LYS LEU LYS GLU          
SEQRES  23 A  296  VAL THR GLY TRP GLU ASN LEU TYR PHE GLN                      
SEQRES   1 B  387  MET ASN LEU HIS GLU TYR GLN ALA LYS ASP LEU LEU GLU          
SEQRES   2 B  387  SER TYR GLY LEU LYS VAL GLN LYS GLY ILE VAL ALA HIS          
SEQRES   3 B  387  ASN PRO ASN GLU ALA ALA GLN ALA PHE ASP GLN LEU GLY          
SEQRES   4 B  387  GLY LYS PHE ALA VAL VAL LYS ALA GLN VAL HIS ALA GLY          
SEQRES   5 B  387  GLY ARG GLY LYS ALA GLY GLY VAL LYS VAL VAL LYS SER          
SEQRES   6 B  387  SER GLN GLU THR ARG GLU VAL ALA GLU SER LEU ILE GLY          
SEQRES   7 B  387  LYS ASN LEU VAL THR PHE GLN THR ASP ALA GLU GLY GLN          
SEQRES   8 B  387  PRO VAL ASN SER VAL GLY VAL PHE GLU ASP VAL TYR PRO          
SEQRES   9 B  387  VAL THR ARG GLU LEU TYR LEU GLY ALA VAL VAL ASP ARG          
SEQRES  10 B  387  SER SER ARG LYS VAL THR PHE MET ALA SER THR GLU GLY          
SEQRES  11 B  387  GLY VAL ASP ILE GLU GLU VAL ALA HIS ASN SER PRO GLU          
SEQRES  12 B  387  LYS ILE LEU LYS VAL GLU VAL ASP PRO LEU VAL GLY LEU          
SEQRES  13 B  387  GLN PRO PHE GLN ALA ARG GLU VAL ALA PHE LYS LEU GLY          
SEQRES  14 B  387  LEU GLU GLY LYS GLN ILE ASN ASP PHE VAL LYS THR MET          
SEQRES  15 B  387  LEU GLY ALA TYR LYS ALA PHE ILE GLU CYS ASP PHE ALA          
SEQRES  16 B  387  LEU PHE GLU ILE ASN PRO LEU ALA VAL ARG GLU ASN GLY          
SEQRES  17 B  387  GLU ILE VAL CYS VAL ASP GLY LYS ILE ASN LEU ASP SER          
SEQRES  18 B  387  ASN ALA LEU TYR ARG HIS PRO LYS LEU LEU ALA LEU ARG          
SEQRES  19 B  387  ASP LYS SER GLN GLU ASN ALA LYS GLU LEU LYS ALA SER          
SEQRES  20 B  387  GLU HIS GLU LEU ASN TYR VAL ALA LEU GLU GLY ASN ILE          
SEQRES  21 B  387  GLY CYS MET VAL ASN GLY ALA GLY LEU ALA MET ALA THR          
SEQRES  22 B  387  MET ASP ILE ILE GLN LEU TYR GLY GLY LYS PRO ALA ASN          
SEQRES  23 B  387  PHE LEU ASP VAL GLY GLY GLY ALA THR LYS GLU ARG VAL          
SEQRES  24 B  387  ILE GLU ALA PHE LYS LEU ILE LEU ASP ASP GLU ASN VAL          
SEQRES  25 B  387  LYS ALA ILE LEU ILE ASN ILE PHE GLY GLY ILE VAL ARG          
SEQRES  26 B  387  CYS ASP MET ILE ALA GLU ALA ILE ILE GLU ALA VAL LYS          
SEQRES  27 B  387  GLU VAL ASN VAL THR VAL PRO VAL VAL VAL ARG LEU GLU          
SEQRES  28 B  387  GLY ASN ASN ALA GLU LYS GLY ALA LYS ILE LEU ALA ASP          
SEQRES  29 B  387  SER GLY LEU LYS LEU ILE PRO ALA ASP GLY LEU ALA ASP          
SEQRES  30 B  387  ALA ALA ASP LYS VAL VAL LYS SER LEU GLY                      
SEQRES   1 C  296  MET SER VAL LEU VAL ASP LYS ASN THR LYS VAL LEU VAL          
SEQRES   2 C  296  GLN GLY PHE THR GLY LYS ASN GLY THR PHE HIS SER GLU          
SEQRES   3 C  296  GLN ALA ILE ALA TYR GLY THR ASN ILE VAL GLY GLY VAL          
SEQRES   4 C  296  THR PRO GLY LYS GLY GLY THR THR HIS LEU ASP ARG PRO          
SEQRES   5 C  296  VAL PHE ASN THR MET ALA GLU ALA VAL ALA ALA THR GLY          
SEQRES   6 C  296  ALA ASP ALA SER VAL ILE TYR VAL PRO ALA PRO PHE VAL          
SEQRES   7 C  296  LYS ASP SER ALA ILE GLU VAL ILE ASP SER GLY VAL LYS          
SEQRES   8 C  296  LEU VAL VAL ILE ILE THR GLU GLY VAL PRO THR LEU ASP          
SEQRES   9 C  296  MET LEU VAL VAL LYS GLU TYR LEU LYS ASP LYS ASP VAL          
SEQRES  10 C  296  ARG VAL ILE GLY PRO ASN CYS PRO GLY ILE ILE THR PRO          
SEQRES  11 C  296  GLY GLU CYS LYS ILE GLY ILE MET PRO GLY HIS ILE HIS          
SEQRES  12 C  296  MET LYS GLY LYS VAL GLY ILE ILE SER ARG SER GLY THR          
SEQRES  13 C  296  LEU THR TYR GLU ALA VAL ALA GLN THR THR LYS LEU GLY          
SEQRES  14 C  296  PHE GLY GLN SER THR CYS ILE GLY ILE GLY GLY ASP PRO          
SEQRES  15 C  296  ILE PRO GLY MET ASN GLN ILE GLU ALA LEU LYS LEU LEU          
SEQRES  16 C  296  GLU ASN ASP PRO GLN THR GLU ALA ILE ILE LEU ILE GLY          
SEQRES  17 C  296  GLU ILE GLY GLY THR ALA GLU GLU GLU ALA ALA GLU TYR          
SEQRES  18 C  296  ILE LYS HIS ASN VAL THR LYS PRO VAL ILE GLY TYR ILE          
SEQRES  19 C  296  ALA GLY VAL THR ALA PRO PRO GLY LYS ARG MET GLY NEP          
SEQRES  20 C  296  ALA GLY ALA ILE ILE SER GLY GLY LYS GLY THR ALA GLU          
SEQRES  21 C  296  GLU LYS PHE ALA ALA PHE GLU ALA ALA GLY ILE ALA TYR          
SEQRES  22 C  296  THR ARG SER PRO ALA GLU ILE GLY LYS LYS LEU LYS GLU          
SEQRES  23 C  296  VAL THR GLY TRP GLU ASN LEU TYR PHE GLN                      
SEQRES   1 D  387  MET ASN LEU HIS GLU TYR GLN ALA LYS ASP LEU LEU GLU          
SEQRES   2 D  387  SER TYR GLY LEU LYS VAL GLN LYS GLY ILE VAL ALA HIS          
SEQRES   3 D  387  ASN PRO ASN GLU ALA ALA GLN ALA PHE ASP GLN LEU GLY          
SEQRES   4 D  387  GLY LYS PHE ALA VAL VAL LYS ALA GLN VAL HIS ALA GLY          
SEQRES   5 D  387  GLY ARG GLY LYS ALA GLY GLY VAL LYS VAL VAL LYS SER          
SEQRES   6 D  387  SER GLN GLU THR ARG GLU VAL ALA GLU SER LEU ILE GLY          
SEQRES   7 D  387  LYS ASN LEU VAL THR PHE GLN THR ASP ALA GLU GLY GLN          
SEQRES   8 D  387  PRO VAL ASN SER VAL GLY VAL PHE GLU ASP VAL TYR PRO          
SEQRES   9 D  387  VAL THR ARG GLU LEU TYR LEU GLY ALA VAL VAL ASP ARG          
SEQRES  10 D  387  SER SER ARG LYS VAL THR PHE MET ALA SER THR GLU GLY          
SEQRES  11 D  387  GLY VAL ASP ILE GLU GLU VAL ALA HIS ASN SER PRO GLU          
SEQRES  12 D  387  LYS ILE LEU LYS VAL GLU VAL ASP PRO LEU VAL GLY LEU          
SEQRES  13 D  387  GLN PRO PHE GLN ALA ARG GLU VAL ALA PHE LYS LEU GLY          
SEQRES  14 D  387  LEU GLU GLY LYS GLN ILE ASN ASP PHE VAL LYS THR MET          
SEQRES  15 D  387  LEU GLY ALA TYR LYS ALA PHE ILE GLU CYS ASP PHE ALA          
SEQRES  16 D  387  LEU PHE GLU ILE ASN PRO LEU ALA VAL ARG GLU ASN GLY          
SEQRES  17 D  387  GLU ILE VAL CYS VAL ASP GLY LYS ILE ASN LEU ASP SER          
SEQRES  18 D  387  ASN ALA LEU TYR ARG HIS PRO LYS LEU LEU ALA LEU ARG          
SEQRES  19 D  387  ASP LYS SER GLN GLU ASN ALA LYS GLU LEU LYS ALA SER          
SEQRES  20 D  387  GLU HIS GLU LEU ASN TYR VAL ALA LEU GLU GLY ASN ILE          
SEQRES  21 D  387  GLY CYS MET VAL ASN GLY ALA GLY LEU ALA MET ALA THR          
SEQRES  22 D  387  MET ASP ILE ILE GLN LEU TYR GLY GLY LYS PRO ALA ASN          
SEQRES  23 D  387  PHE LEU ASP VAL GLY GLY GLY ALA THR LYS GLU ARG VAL          
SEQRES  24 D  387  ILE GLU ALA PHE LYS LEU ILE LEU ASP ASP GLU ASN VAL          
SEQRES  25 D  387  LYS ALA ILE LEU ILE ASN ILE PHE GLY GLY ILE VAL ARG          
SEQRES  26 D  387  CYS ASP MET ILE ALA GLU ALA ILE ILE GLU ALA VAL LYS          
SEQRES  27 D  387  GLU VAL ASN VAL THR VAL PRO VAL VAL VAL ARG LEU GLU          
SEQRES  28 D  387  GLY ASN ASN ALA GLU LYS GLY ALA LYS ILE LEU ALA ASP          
SEQRES  29 D  387  SER GLY LEU LYS LEU ILE PRO ALA ASP GLY LEU ALA ASP          
SEQRES  30 D  387  ALA ALA ASP LYS VAL VAL LYS SER LEU GLY                      
MODRES 6MGG NEP A  247  HIS  MODIFIED RESIDUE                                   
MODRES 6MGG NEP C  247  HIS  MODIFIED RESIDUE                                   
HET    NEP  A 247      14                                                       
HET    NEP  C 247      14                                                       
HET    COA  A 501      48                                                       
HET     MG  A 502       1                                                       
HET    EDO  B 401       4                                                       
HET    EDO  B 402       4                                                       
HET    COA  C 501      48                                                       
HET     MG  C 502       1                                                       
HET    EDO  D 501       4                                                       
HET    EDO  D 502       4                                                       
HETNAM     NEP N1-PHOSPHONOHISTIDINE                                            
HETNAM     COA COENZYME A                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  NEP    2(C6 H10 N3 O5 P)                                            
FORMUL   5  COA    2(C21 H36 N7 O16 P3 S)                                       
FORMUL   6   MG    2(MG 2+)                                                     
FORMUL   7  EDO    4(C2 H6 O2)                                                  
FORMUL  13  HOH   *1076(H2 O)                                                   
HELIX    1 AA1 GLY A   18  GLY A   32  1                                  15    
HELIX    2 AA2 THR A   56  GLY A   65  1                                  10    
HELIX    3 AA3 PRO A   74  PRO A   76  5                                   3    
HELIX    4 AA4 PHE A   77  ASP A   87  1                                  11    
HELIX    5 AA5 PRO A  101  LEU A  112  1                                  12    
HELIX    6 AA6 LYS A  113  LYS A  115  5                                   3    
HELIX    7 AA7 PRO A  139  HIS A  143  5                                   5    
HELIX    8 AA8 GLY A  155  LEU A  168  1                                  14    
HELIX    9 AA9 ASN A  187  ASN A  197  1                                  11    
HELIX   10 AB1 THR A  213  VAL A  226  1                                  14    
HELIX   11 AB2 THR A  258  ALA A  269  1                                  12    
HELIX   12 AB3 SER A  276  ALA A  278  5                                   3    
HELIX   13 AB4 GLU A  279  GLY A  289  1                                  11    
HELIX   14 AB5 HIS B    4  TYR B   15  1                                  12    
HELIX   15 AB6 ASN B   27  GLY B   39  1                                  13    
HELIX   16 AB7 SER B   65  ILE B   77  1                                  13    
HELIX   17 AB8 ASP B  133  SER B  141  1                                   9    
HELIX   18 AB9 PRO B  142  ILE B  145  5                                   4    
HELIX   19 AC1 GLN B  157  LEU B  168  1                                  12    
HELIX   20 AC2 GLY B  172  CYS B  192  1                                  21    
HELIX   21 AC3 SER B  221  ARG B  226  5                                   6    
HELIX   22 AC4 HIS B  227  ALA B  232  1                                   6    
HELIX   23 AC5 LEU B  233  ARG B  234  5                                   2    
HELIX   24 AC6 ASP B  235  GLU B  239  5                                   5    
HELIX   25 AC7 ASN B  240  GLU B  248  1                                   9    
HELIX   26 AC8 GLY B  266  TYR B  280  1                                  15    
HELIX   27 AC9 THR B  295  ASP B  308  1                                  14    
HELIX   28 AD1 ARG B  325  LYS B  338  1                                  14    
HELIX   29 AD2 ASN B  354  ASP B  364  1                                  11    
HELIX   30 AD3 GLY B  374  SER B  385  1                                  12    
HELIX   31 AD4 GLY C   18  GLY C   32  1                                  15    
HELIX   32 AD5 THR C   56  GLY C   65  1                                  10    
HELIX   33 AD6 PRO C   74  PRO C   76  5                                   3    
HELIX   34 AD7 PHE C   77  SER C   88  1                                  12    
HELIX   35 AD8 PRO C  101  LEU C  112  1                                  12    
HELIX   36 AD9 LYS C  113  LYS C  115  5                                   3    
HELIX   37 AE1 PRO C  139  HIS C  143  5                                   5    
HELIX   38 AE2 GLY C  155  LEU C  168  1                                  14    
HELIX   39 AE3 ASN C  187  ASN C  197  1                                  11    
HELIX   40 AE4 THR C  213  VAL C  226  1                                  14    
HELIX   41 AE5 THR C  258  ALA C  269  1                                  12    
HELIX   42 AE6 SER C  276  ALA C  278  5                                   3    
HELIX   43 AE7 GLU C  279  GLY C  289  1                                  11    
HELIX   44 AE8 HIS D    4  TYR D   15  1                                  12    
HELIX   45 AE9 ASN D   27  GLY D   39  1                                  13    
HELIX   46 AF1 SER D   65  ILE D   77  1                                  13    
HELIX   47 AF2 ASP D  133  SER D  141  1                                   9    
HELIX   48 AF3 PRO D  142  ILE D  145  5                                   4    
HELIX   49 AF4 GLN D  157  LEU D  168  1                                  12    
HELIX   50 AF5 GLY D  172  CYS D  192  1                                  21    
HELIX   51 AF6 SER D  221  ARG D  226  5                                   6    
HELIX   52 AF7 HIS D  227  ALA D  232  1                                   6    
HELIX   53 AF8 LEU D  233  ARG D  234  5                                   2    
HELIX   54 AF9 ASP D  235  GLU D  239  5                                   5    
HELIX   55 AG1 ASN D  240  GLU D  248  1                                   9    
HELIX   56 AG2 GLY D  266  TYR D  280  1                                  15    
HELIX   57 AG3 THR D  295  ASP D  308  1                                  14    
HELIX   58 AG4 ASP D  327  ASN D  341  1                                  15    
HELIX   59 AG5 GLY D  374  SER D  385  1                                  12    
SHEET    1 AA1 7 THR A  47  HIS A  48  0                                        
SHEET    2 AA1 7 ARG A  51  PHE A  54 -1  O  ARG A  51   N  HIS A  48           
SHEET    3 AA1 7 ASN A  34  VAL A  39  1  N  GLY A  38   O  PHE A  54           
SHEET    4 AA1 7 LYS A  10  GLN A  14  1  N  VAL A  11   O  ASN A  34           
SHEET    5 AA1 7 ALA A  68  ILE A  71  1  O  VAL A  70   N  GLN A  14           
SHEET    6 AA1 7 LEU A  92  ILE A  95  1  O  VAL A  94   N  ILE A  71           
SHEET    7 AA1 7 ARG A 118  ILE A 120  1  O  ILE A 120   N  ILE A  95           
SHEET    1 AA2 7 CYS A 133  GLY A 136  0                                        
SHEET    2 AA2 7 GLY A 126  THR A 129 -1  N  ILE A 127   O  ILE A 135           
SHEET    3 AA2 7 GLN A 172  GLY A 177 -1  O  CYS A 175   N  ILE A 128           
SHEET    4 AA2 7 VAL A 148  SER A 152  1  N  ILE A 150   O  ILE A 176           
SHEET    5 AA2 7 ALA A 203  GLU A 209  1  O  ILE A 207   N  ILE A 151           
SHEET    6 AA2 7 VAL A 230  ALA A 235  1  O  TYR A 233   N  GLY A 208           
SHEET    7 AA2 7 ALA A 272  TYR A 273  1  O  ALA A 272   N  GLY A 232           
SHEET    1 AA3 6 LYS B  18  VAL B  19  0                                        
SHEET    2 AA3 6 ILE B 210  CYS B 212  1  O  CYS B 212   N  LYS B  18           
SHEET    3 AA3 6 PHE B 194  ARG B 205 -1  N  ALA B 203   O  VAL B 211           
SHEET    4 AA3 6 VAL B 105  ASP B 116 -1  N  LEU B 111   O  ILE B 199           
SHEET    5 AA3 6 LYS B 121  SER B 127 -1  O  THR B 123   N  VAL B 114           
SHEET    6 AA3 6 LEU B 146  GLU B 149 -1  O  LEU B 146   N  ALA B 126           
SHEET    1 AA4 4 LYS B  18  VAL B  19  0                                        
SHEET    2 AA4 4 ILE B 210  CYS B 212  1  O  CYS B 212   N  LYS B  18           
SHEET    3 AA4 4 PHE B 194  ARG B 205 -1  N  ALA B 203   O  VAL B 211           
SHEET    4 AA4 4 GLY B 215  LEU B 219 -1  O  ASN B 218   N  ALA B 195           
SHEET    1 AA5 4 GLY B  22  ALA B  25  0                                        
SHEET    2 AA5 4 VAL B  96  GLU B 100 -1  O  VAL B  96   N  ALA B  25           
SHEET    3 AA5 4 ALA B  43  ALA B  47 -1  N  VAL B  44   O  PHE B  99           
SHEET    4 AA5 4 VAL B  60  VAL B  63 -1  O  LYS B  61   N  VAL B  45           
SHEET    1 AA6 2 ASN B  80  LEU B  81  0                                        
SHEET    2 AA6 2 GLN B  91  PRO B  92 -1  O  GLN B  91   N  LEU B  81           
SHEET    1 AA7 2 ASN B 252  ALA B 255  0                                        
SHEET    2 AA7 2 ASN B 286  ASP B 289 -1  O  PHE B 287   N  VAL B 254           
SHEET    1 AA8 4 ILE B 260  VAL B 264  0                                        
SHEET    2 AA8 4 ALA B 314  GLY B 321  1  O  ALA B 314   N  GLY B 261           
SHEET    3 AA8 4 VAL B 346  GLY B 352  1  O  ARG B 349   N  ILE B 317           
SHEET    4 AA8 4 ILE B 370  ALA B 372  1  O  ILE B 370   N  VAL B 346           
SHEET    1 AA9 7 THR C  47  HIS C  48  0                                        
SHEET    2 AA9 7 ARG C  51  PHE C  54 -1  O  ARG C  51   N  HIS C  48           
SHEET    3 AA9 7 ASN C  34  VAL C  39  1  N  GLY C  38   O  PHE C  54           
SHEET    4 AA9 7 LYS C  10  GLN C  14  1  N  VAL C  11   O  ASN C  34           
SHEET    5 AA9 7 ALA C  68  ILE C  71  1  O  VAL C  70   N  GLN C  14           
SHEET    6 AA9 7 LEU C  92  ILE C  95  1  O  VAL C  94   N  ILE C  71           
SHEET    7 AA9 7 ARG C 118  ILE C 120  1  O  ILE C 120   N  ILE C  95           
SHEET    1 AB1 7 CYS C 133  GLY C 136  0                                        
SHEET    2 AB1 7 GLY C 126  THR C 129 -1  N  ILE C 127   O  ILE C 135           
SHEET    3 AB1 7 GLN C 172  GLY C 177 -1  O  CYS C 175   N  ILE C 128           
SHEET    4 AB1 7 VAL C 148  SER C 152  1  N  ILE C 150   O  ILE C 176           
SHEET    5 AB1 7 ALA C 203  GLU C 209  1  O  ALA C 203   N  GLY C 149           
SHEET    6 AB1 7 VAL C 230  ALA C 235  1  O  ILE C 231   N  LEU C 206           
SHEET    7 AB1 7 ALA C 272  TYR C 273  1  O  ALA C 272   N  GLY C 232           
SHEET    1 AB2 4 GLY D  22  ALA D  25  0                                        
SHEET    2 AB2 4 VAL D  96  GLU D 100 -1  O  VAL D  96   N  ALA D  25           
SHEET    3 AB2 4 ALA D  43  ALA D  47 -1  N  VAL D  44   O  PHE D  99           
SHEET    4 AB2 4 VAL D  60  VAL D  63 -1  O  LYS D  61   N  VAL D  45           
SHEET    1 AB3 5 LEU D 146  GLU D 149  0                                        
SHEET    2 AB3 5 LYS D 121  SER D 127 -1  N  ALA D 126   O  LEU D 146           
SHEET    3 AB3 5 VAL D 105  ASP D 116 -1  N  VAL D 114   O  THR D 123           
SHEET    4 AB3 5 PHE D 194  ARG D 205 -1  O  ILE D 199   N  LEU D 111           
SHEET    5 AB3 5 ILE D 210  CYS D 212 -1  O  VAL D 211   N  ALA D 203           
SHEET    1 AB4 5 LEU D 146  GLU D 149  0                                        
SHEET    2 AB4 5 LYS D 121  SER D 127 -1  N  ALA D 126   O  LEU D 146           
SHEET    3 AB4 5 VAL D 105  ASP D 116 -1  N  VAL D 114   O  THR D 123           
SHEET    4 AB4 5 PHE D 194  ARG D 205 -1  O  ILE D 199   N  LEU D 111           
SHEET    5 AB4 5 GLY D 215  LEU D 219 -1  O  ASN D 218   N  ALA D 195           
SHEET    1 AB5 2 ASN D 252  ALA D 255  0                                        
SHEET    2 AB5 2 ASN D 286  ASP D 289 -1  O  PHE D 287   N  VAL D 254           
SHEET    1 AB6 4 ILE D 260  VAL D 264  0                                        
SHEET    2 AB6 4 ALA D 314  PHE D 320  1  O  ALA D 314   N  GLY D 261           
SHEET    3 AB6 4 VAL D 346  GLU D 351  1  O  VAL D 347   N  ILE D 315           
SHEET    4 AB6 4 ILE D 370  ALA D 372  1  O  ILE D 370   N  VAL D 346           
LINK         C   GLY A 246                 N   NEP A 247     1555   1555  1.33  
LINK         C   NEP A 247                 N   ALA A 248     1555   1555  1.33  
LINK         O2P NEP A 247                MG    MG A 502     1555   1555  1.97  
LINK         C   GLY C 246                 N   NEP C 247     1555   1555  1.33  
LINK         C   NEP C 247                 N   ALA C 248     1555   1555  1.33  
LINK         O2P NEP C 247                MG    MG C 502     1555   1555  1.85  
LINK        MG    MG A 502                 O   HOH A 695     1555   1555  2.24  
LINK        MG    MG A 502                 O   HOH A 628     1555   1555  2.16  
LINK        MG    MG A 502                 O   HOH A 636     1555   1555  2.13  
LINK        MG    MG A 502                 O   HOH A 647     1555   1555  2.00  
LINK        MG    MG A 502                 O   HOH B 545     1555   1555  2.07  
LINK        MG    MG C 502                 O   HOH C 635     1555   1555  2.01  
LINK        MG    MG C 502                 O   HOH C 645     1555   1555  2.08  
LINK        MG    MG C 502                 O   HOH C 733     1555   1555  2.26  
LINK        MG    MG C 502                 O   HOH C 721     1555   1555  2.02  
LINK        MG    MG C 502                 O   HOH D 662     1555   1555  2.15  
CISPEP   1 GLY A  121    PRO A  122          0         6.78                     
CISPEP   2 TYR B  103    PRO B  104          0         1.31                     
CISPEP   3 ASN B  200    PRO B  201          0         1.25                     
CISPEP   4 GLY C  121    PRO C  122          0         6.06                     
CISPEP   5 TYR D  103    PRO D  104          0        25.49                     
CISPEP   6 ASN D  200    PRO D  201          0         0.41                     
SITE     1 AC1 35 GLY A  15  THR A  17  GLY A  18  LYS A  19                    
SITE     2 AC1 35 ASN A  20  VAL A  39  PRO A  41  LYS A  43                    
SITE     3 AC1 35 TYR A  72  VAL A  73  SER A  81  ILE A  96                    
SITE     4 AC1 35 THR A  97  GLU A  98  ASN A 123  CYS A 124                    
SITE     5 AC1 35 PRO A 125  ILE A 137  NEP A 247  HOH A 606                    
SITE     6 AC1 35 HOH A 618  HOH A 626  HOH A 628  HOH A 632                    
SITE     7 AC1 35 HOH A 642  HOH A 662  HOH A 665  HOH A 666                    
SITE     8 AC1 35 HOH A 668  HOH A 675  HOH A 689  HOH A 707                    
SITE     9 AC1 35 HOH A 722  HOH A 751  HOH A 753                               
SITE     1 AC2  6 NEP A 247  HOH A 628  HOH A 636  HOH A 647                    
SITE     2 AC2  6 HOH A 695  HOH B 545                                          
SITE     1 AC3  7 MET B   1  ASN B   2  HIS B  50  GLN B 238                    
SITE     2 AC3  7 GLU B 239  HOH B 557  HOH B 663                               
SITE     1 AC4  4 LYS B 147  GLU B 163  LYS B 167  HOH B 660                    
SITE     1 AC5 31 GLY C  15  THR C  17  GLY C  18  LYS C  19                    
SITE     2 AC5 31 ASN C  20  VAL C  39  PRO C  41  LYS C  43                    
SITE     3 AC5 31 TYR C  72  VAL C  73  PRO C  74  SER C  81                    
SITE     4 AC5 31 ILE C  96  THR C  97  GLU C  98  ASN C 123                    
SITE     5 AC5 31 CYS C 124  PRO C 125  ILE C 137  NEP C 247                    
SITE     6 AC5 31 HOH C 607  HOH C 635  HOH C 657  HOH C 668                    
SITE     7 AC5 31 HOH C 683  HOH C 700  HOH C 706  HOH C 716                    
SITE     8 AC5 31 HOH C 725  HOH C 750  HOH C 764                               
SITE     1 AC6  6 NEP C 247  HOH C 635  HOH C 645  HOH C 721                    
SITE     2 AC6  6 HOH C 733  HOH D 662                                          
SITE     1 AC7  4 LYS D 147  GLU D 163  LYS D 167  HOH D 701                    
SITE     1 AC8  6 SER B 365  GLY B 366  ASN D 259  GLY D 282                    
SITE     2 AC8  6 LYS D 283  LEU D 386                                          
CRYST1   66.911  158.338   73.585  90.00 111.73  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      0.014945  0.000000  0.005958        0.00000                         
SCALE2      0.000000  0.006316  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014630        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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