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Database: PDB
Entry: 1R9C
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Original site: 1R9C 
HEADER    TRANSFERASE                             28-OCT-03   1R9C              
TITLE     CRYSTAL STRUCTURE OF FOSFOMYCIN RESISTANCE PROTEIN FOSX FROM          
TITLE    2 MESORHIZOBIUM LOTI                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTATHIONE TRANSFERASE;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 2.5.1.1;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MESORHIZOBIUM LOTI;                             
SOURCE   3 ORGANISM_TAXID: 381;                                                 
SOURCE   4 GENE: FOSFOMYCIN RESISTANCE PROTEIN;                                 
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET20-B(+)                                
KEYWDS    FOSFOMYCIN RESISTANCE PROTEIN, MN BINDING, ANTIBIOTIC RESISTANCE,     
KEYWDS   2 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.L.FILLGROVE,S.PAKHOMOVA,M.E.NEWCOMER,R.N.ARMSTRONG                  
REVDAT   3   13-JUL-11 1R9C    1       VERSN                                    
REVDAT   2   24-FEB-09 1R9C    1       VERSN                                    
REVDAT   1   10-FEB-04 1R9C    0                                                
JRNL        AUTH   K.L.FILLGROVE,S.PAKHOMOVA,M.E.NEWCOMER,R.N.ARMSTRONG         
JRNL        TITL   MECHANISTIC DIVERSITY OF FOSFOMYCIN RESISTANCE IN PATHOGENIC 
JRNL        TITL 2 MICROORGANISMS.                                              
JRNL        REF    J.AM.CHEM.SOC.                V. 125 15730 2003              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   14677948                                                     
JRNL        DOI    10.1021/JA039307Z                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.83 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
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) : 1.83                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 87.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 18860                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1391                            
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) : 1.83                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.88                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 702                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3520                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 53                           
REMARK   3   BIN FREE R VALUE                    : 0.3180                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1950                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 121                                     
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) : 26.16                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.94000                                             
REMARK   3    B22 (A**2) : 3.23000                                              
REMARK   3    B33 (A**2) : -1.29000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.175         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.158         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.109         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.676         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1999 ; 0.015 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2682 ; 1.363 ; 1.942       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   238 ; 6.293 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   287 ; 0.101 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1552 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   767 ; 0.197 ; 0.200       
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):   145 ; 0.144 ; 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):    56 ; 0.233 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.108 ; 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):  1203 ; 0.788 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1908 ; 1.426 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   796 ; 2.537 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   774 ; 3.769 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   130                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.2369  14.9884  45.0010              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0406 T22:   0.0030                                     
REMARK   3      T33:   0.0329 T12:  -0.0005                                     
REMARK   3      T13:   0.0241 T23:   0.0050                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6192 L22:   1.5795                                     
REMARK   3      L33:   2.8172 L12:  -0.0229                                     
REMARK   3      L13:   0.7185 L23:   0.0795                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0011 S12:  -0.0182 S13:  -0.1043                       
REMARK   3      S21:  -0.0339 S22:   0.0915 S23:  -0.0991                       
REMARK   3      S31:   0.0400 S32:   0.1373 S33:  -0.0926                       
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   129                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.3419  20.0727  53.8260              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0500 T22:   0.0247                                     
REMARK   3      T33:   0.0511 T12:   0.0350                                     
REMARK   3      T13:  -0.0021 T23:  -0.0052                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5141 L22:   1.4795                                     
REMARK   3      L33:   3.4345 L12:   0.0571                                     
REMARK   3      L13:  -0.3972 L23:  -0.2000                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0470 S12:  -0.2123 S13:   0.1720                       
REMARK   3      S21:   0.0948 S22:  -0.0277 S23:   0.0578                       
REMARK   3      S31:  -0.1243 S32:  -0.1580 S33:  -0.0193                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1R9C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-NOV-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB020598.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-SEP-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21017                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.830                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.1                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.83                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 55.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.41400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1LQP                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, TRIS, LI2SO4, MNCL2, PH 8.5,    
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       22.51700            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       42.01200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.51700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       42.01200            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER.                          
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: 4030 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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 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     ARG A    99                                                      
REMARK 465     VAL A   100                                                      
REMARK 465     GLU A   101                                                      
REMARK 465     GLY A   102                                                      
REMARK 465     GLU A   103                                                      
REMARK 465     LYS A   131                                                      
REMARK 465     ALA A   132                                                      
REMARK 465     LYS A   133                                                      
REMARK 465     GLY A   134                                                      
REMARK 465     LEU A   135                                                      
REMARK 465     GLU A   136                                                      
REMARK 465     ALA A   137                                                      
REMARK 465     ALA A   138                                                      
REMARK 465     GLN A   139                                                      
REMARK 465     SER B    34                                                      
REMARK 465     ASP B    35                                                      
REMARK 465     THR B    36                                                      
REMARK 465     GLU B    37                                                      
REMARK 465     GLN B    38                                                      
REMARK 465     PHE B    39                                                      
REMARK 465     SER B    40                                                      
REMARK 465     LEU B    41                                                      
REMARK 465     VAL B   100                                                      
REMARK 465     GLU B   101                                                      
REMARK 465     GLY B   102                                                      
REMARK 465     ARG B   130                                                      
REMARK 465     LYS B   131                                                      
REMARK 465     ALA B   132                                                      
REMARK 465     LYS B   133                                                      
REMARK 465     GLY B   134                                                      
REMARK 465     LEU B   135                                                      
REMARK 465     GLU B   136                                                      
REMARK 465     ALA B   137                                                      
REMARK 465     ALA B   138                                                      
REMARK 465     GLN B   139                                                      
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     GLN A  38    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  61    CG   CD   CE   NZ                                   
REMARK 470     LYS A  88    CG   CD   CE   NZ                                   
REMARK 470     PRO A  98    CG   CD                                             
REMARK 470     ARG A 130    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B  42    OG                                                  
REMARK 470     ARG B  43    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  61    CG   CD   CE   NZ                                   
REMARK 470     GLU B  64    CG   CD   OE1  OE2                                  
REMARK 470     ARG B  81    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B  84    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  88    CG   CD   CE   NZ                                   
REMARK 470     ARG B  97    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  99    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 103    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A  51   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP A  76   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A  39       55.34     31.10                                   
REMARK 500    ASP A 111     -154.63    -81.89                                   
REMARK 500    ARG B  43     -164.45    171.19                                   
REMARK 500    PRO B  98       96.21    -52.25                                   
REMARK 500    ASP B 111     -153.07    -82.39                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                              MN A2001  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B   7   NE2                                                    
REMARK 620 2 HOH A2054   O    85.4                                              
REMARK 620 3 HOH B1002   O    94.0  96.2                                        
REMARK 620 4 GLU A 118   OE1  91.2  83.4 174.7                                  
REMARK 620 5 HIS A  69   NE2 111.8 161.3  90.3  88.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B1001  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 118   OE1                                                    
REMARK 620 2 HIS A   7   NE2  91.8                                              
REMARK 620 3 HOH A2002   O   171.1  90.5                                        
REMARK 620 4 HOH B1017   O    90.1  91.9  98.4                                  
REMARK 620 5 HOH B1035   O    99.4 162.7  80.5  75.0                            
REMARK 620 6 HIS B  69   NE2  83.1 105.3  88.0 161.7  89.3                      
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 MN B 1001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 2001                 
DBREF  1R9C A    1   139  UNP    Q98GG1   FOSX_RHILO       1    139             
DBREF  1R9C B    1   139  UNP    Q98GG1   FOSX_RHILO       1    139             
SEQRES   1 A  139  MET ILE GLU GLY LEU SER HIS MET THR PHE ILE VAL ARG          
SEQRES   2 A  139  ASP LEU GLU ARG MET THR ARG ILE LEU GLU GLY VAL PHE          
SEQRES   3 A  139  ASP ALA ARG GLU VAL TYR ALA SER ASP THR GLU GLN PHE          
SEQRES   4 A  139  SER LEU SER ARG GLU LYS PHE PHE LEU ILE GLY ASP ILE          
SEQRES   5 A  139  TRP VAL ALA ILE MET GLN GLY GLU LYS LEU ALA GLU ARG          
SEQRES   6 A  139  SER TYR ASN HIS ILE ALA PHE LYS ILE ASP ASP ALA ASP          
SEQRES   7 A  139  PHE ASP ARG TYR ALA GLU ARG VAL GLY LYS LEU GLY LEU          
SEQRES   8 A  139  ASP MET ARG PRO PRO ARG PRO ARG VAL GLU GLY GLU GLY          
SEQRES   9 A  139  ARG SER ILE TYR PHE TYR ASP ASP ASP ASN HIS MET PHE          
SEQRES  10 A  139  GLU LEU HIS THR GLY THR LEU THR GLU ARG LEU ALA ARG          
SEQRES  11 A  139  LYS ALA LYS GLY LEU GLU ALA ALA GLN                          
SEQRES   1 B  139  MET ILE GLU GLY LEU SER HIS MET THR PHE ILE VAL ARG          
SEQRES   2 B  139  ASP LEU GLU ARG MET THR ARG ILE LEU GLU GLY VAL PHE          
SEQRES   3 B  139  ASP ALA ARG GLU VAL TYR ALA SER ASP THR GLU GLN PHE          
SEQRES   4 B  139  SER LEU SER ARG GLU LYS PHE PHE LEU ILE GLY ASP ILE          
SEQRES   5 B  139  TRP VAL ALA ILE MET GLN GLY GLU LYS LEU ALA GLU ARG          
SEQRES   6 B  139  SER TYR ASN HIS ILE ALA PHE LYS ILE ASP ASP ALA ASP          
SEQRES   7 B  139  PHE ASP ARG TYR ALA GLU ARG VAL GLY LYS LEU GLY LEU          
SEQRES   8 B  139  ASP MET ARG PRO PRO ARG PRO ARG VAL GLU GLY GLU GLY          
SEQRES   9 B  139  ARG SER ILE TYR PHE TYR ASP ASP ASP ASN HIS MET PHE          
SEQRES  10 B  139  GLU LEU HIS THR GLY THR LEU THR GLU ARG LEU ALA ARG          
SEQRES  11 B  139  LYS ALA LYS GLY LEU GLU ALA ALA GLN                          
HET     MN  B1001       1                                                       
HET     MN  A2001       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   3   MN    2(MN 2+)                                                     
FORMUL   5  HOH   *121(H2 O)                                                    
HELIX    1   1 ASP A   14  ASP A   27  1                                  14    
HELIX    2   2 ASP A   35  GLU A   37  5                                   3    
HELIX    3   3 ASP A   75  ALA A   77  5                                   3    
HELIX    4   4 ASP A   78  GLY A   90  1                                  13    
HELIX    5   5 THR A  123  ARG A  130  1                                   8    
HELIX    6   6 ASP B   14  ASP B   27  1                                  14    
HELIX    7   7 ASP B   78  LEU B   89  1                                  12    
HELIX    8   8 THR B  123  LEU B  128  1                                   6    
SHEET    1   A 7 ARG A  29  ALA A  33  0                                        
SHEET    2   A 7 GLU A  44  ILE A  49 -1  O  LEU A  48   N  ARG A  29           
SHEET    3   A 7 ILE A  52  GLN A  58 -1  O  VAL A  54   N  PHE A  47           
SHEET    4   A 7 ILE A   2  VAL A  12  1  N  MET A   8   O  ALA A  55           
SHEET    5   A 7 HIS B  69  ILE B  74 -1  O  LYS B  73   N  GLY A   4           
SHEET    6   A 7 MET B 116  HIS B 120  1  O  HIS B 120   N  PHE B  72           
SHEET    7   A 7 SER B 106  TYR B 110 -1  N  PHE B 109   O  PHE B 117           
SHEET    1   B 7 SER A 106  TYR A 110  0                                        
SHEET    2   B 7 MET A 116  HIS A 120 -1  O  PHE A 117   N  PHE A 109           
SHEET    3   B 7 HIS A  69  LYS A  73  1  N  PHE A  72   O  GLU A 118           
SHEET    4   B 7 GLY B   4  VAL B  12 -1  O  GLY B   4   N  LYS A  73           
SHEET    5   B 7 ILE B  52  GLN B  58  1  O  MET B  57   N  VAL B  12           
SHEET    6   B 7 GLU B  44  ILE B  49 -1  N  PHE B  47   O  VAL B  54           
SHEET    7   B 7 ARG B  29  TYR B  32 -1  N  ARG B  29   O  LEU B  48           
LINK        MN    MN A2001                 NE2 HIS B   7     1555   1555  2.05  
LINK        MN    MN A2001                 O   HOH A2054     1555   1555  2.64  
LINK        MN    MN A2001                 O   HOH B1002     1555   1555  2.22  
LINK        MN    MN A2001                 OE1 GLU A 118     1555   1555  1.93  
LINK        MN    MN A2001                 NE2 HIS A  69     1555   1555  2.06  
LINK        MN    MN B1001                 OE1 GLU B 118     1555   1555  1.92  
LINK        MN    MN B1001                 NE2 HIS A   7     1555   1555  2.06  
LINK        MN    MN B1001                 O   HOH A2002     1555   1555  2.32  
LINK        MN    MN B1001                 O   HOH B1017     1555   1555  2.38  
LINK        MN    MN B1001                 O   HOH B1035     1555   1555  2.49  
LINK        MN    MN B1001                 NE2 HIS B  69     1555   1555  2.06  
SITE     1 AC1  6 HIS A   7  HOH A2002  HIS B  69  GLU B 118                    
SITE     2 AC1  6 HOH B1017  HOH B1035                                          
SITE     1 AC2  6 HIS A  69  GLU A 118  HOH A2054  HOH A2058                    
SITE     2 AC2  6 HIS B   7  HOH B1002                                          
CRYST1   45.034   84.024   66.861  90.00  90.00  90.00 P 21 21 2     8          
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      0.022205  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011901  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014956        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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