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Database: PDB
Entry: 3OT7
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Original site: 3OT7 
HEADER    OXIDOREDUCTASE                          10-SEP-10   3OT7              
TITLE     ESCHERICHIA COLI APO-MANGANESE SUPEROXIDE DISMUTASE                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [MN];                                 
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: MNSOD;                                                      
COMPND   5 EC: 1.15.1.1;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 GENE: SODA, B3908, JW3879;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BW25113 DELTA SODA;                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PBAS2SODA                                 
KEYWDS    OXIDOREDUCTASE, SUPEROXIDE DISMUTASE, MANGANESE ENZYME,               
KEYWDS   2 METALLOPROTEIN, DNA BINDING                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.M.WHITTAKER,T.F.LERCH,O.KIRILLOVA,M.S.CHAPMAN,J.W.WHITTAKER         
REVDAT   2   09-FEB-11 3OT7    1       JRNL                                     
REVDAT   1   22-DEC-10 3OT7    0                                                
JRNL        AUTH   M.M.WHITTAKER,T.F.LERCH,O.KIRILLOVA,M.S.CHAPMAN,             
JRNL        AUTH 2 J.W.WHITTAKER                                                
JRNL        TITL   SUBUNIT DISSOCIATION AND METAL BINDING BY ESCHERICHIA COLI   
JRNL        TITL 2 APO-MANGANESE SUPEROXIDE DISMUTASE.                          
JRNL        REF    ARCH.BIOCHEM.BIOPHYS.         V. 505   213 2011              
JRNL        REFN                   ISSN 0003-9861                               
JRNL        PMID   21044611                                                     
JRNL        DOI    10.1016/J.ABB.2010.10.021                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6_289)                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.64                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 70694                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.050                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3569                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 39.6520 -  5.5534    1.00     2863   156  0.1437 0.1467        
REMARK   3     2  5.5534 -  4.4097    1.00     2765   149  0.1289 0.1788        
REMARK   3     3  4.4097 -  3.8528    1.00     2748   142  0.1314 0.1624        
REMARK   3     4  3.8528 -  3.5008    0.99     2716   134  0.1519 0.2016        
REMARK   3     5  3.5008 -  3.2500    1.00     2671   154  0.1848 0.2350        
REMARK   3     6  3.2500 -  3.0585    1.00     2704   160  0.1958 0.2348        
REMARK   3     7  3.0585 -  2.9054    0.99     2688   147  0.2049 0.2749        
REMARK   3     8  2.9054 -  2.7789    0.99     2647   165  0.2216 0.2469        
REMARK   3     9  2.7789 -  2.6720    0.99     2700   142  0.2212 0.2791        
REMARK   3    10  2.6720 -  2.5798    0.99     2663   153  0.2373 0.3297        
REMARK   3    11  2.5798 -  2.4991    1.00     2682   134  0.2300 0.2448        
REMARK   3    12  2.4991 -  2.4277    1.00     2701   121  0.2276 0.2944        
REMARK   3    13  2.4277 -  2.3638    1.00     2650   141  0.2333 0.2911        
REMARK   3    14  2.3638 -  2.3061    1.00     2690   135  0.2286 0.2975        
REMARK   3    15  2.3061 -  2.2537    1.00     2678   154  0.2380 0.3210        
REMARK   3    16  2.2537 -  2.2058    0.99     2659   149  0.2441 0.3325        
REMARK   3    17  2.2058 -  2.1616    1.00     2629   150  0.2392 0.3030        
REMARK   3    18  2.1616 -  2.1208    1.00     2714   140  0.2458 0.3301        
REMARK   3    19  2.1208 -  2.0830    1.00     2671   125  0.2461 0.2893        
REMARK   3    20  2.0830 -  2.0477    1.00     2672   136  0.2518 0.2855        
REMARK   3    21  2.0477 -  2.0146    1.00     2687   129  0.2500 0.3210        
REMARK   3    22  2.0146 -  1.9836    1.00     2649   131  0.2436 0.3046        
REMARK   3    23  1.9836 -  1.9545    0.99     2699   152  0.2425 0.3094        
REMARK   3    24  1.9545 -  1.9269    0.99     2608   136  0.2460 0.2868        
REMARK   3    25  1.9269 -  1.9009    0.96     2571   134  0.2896 0.3165        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.33                                          
REMARK   3   B_SOL              : 44.55                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.48                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 11.13680                                             
REMARK   3    B22 (A**2) : 1.37960                                              
REMARK   3    B33 (A**2) : -12.51630                                            
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           6741                                  
REMARK   3   ANGLE     :  1.033           9152                                  
REMARK   3   CHIRALITY :  0.075            956                                  
REMARK   3   PLANARITY :  0.004           1191                                  
REMARK   3   DIHEDRAL  : 16.190           2386                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  41.3668  14.5512  10.9744              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2306 T22:   0.1922                                     
REMARK   3      T33:   0.1918 T12:   0.1808                                     
REMARK   3      T13:   0.0459 T23:  -0.0570                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1927 L22:   3.3701                                     
REMARK   3      L33:   4.1539 L12:  -0.9899                                     
REMARK   3      L13:  -0.4876 L23:   2.6682                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1852 S12:  -0.1531 S13:   0.1743                       
REMARK   3      S21:  -0.2022 S22:   0.4559 S23:  -0.3599                       
REMARK   3      S31:   0.6599 S32:   0.5629 S33:  -0.1896                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  17.3956  28.3294  20.6641              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0877 T22:   0.3081                                     
REMARK   3      T33:   0.1679 T12:   0.1204                                     
REMARK   3      T13:  -0.0546 T23:  -0.1218                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2718 L22:   2.1690                                     
REMARK   3      L33:   3.1979 L12:  -0.3694                                     
REMARK   3      L13:  -0.5946 L23:   1.9243                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0477 S12:  -0.0912 S13:   0.0451                       
REMARK   3      S21:  -0.3119 S22:  -0.4725 S23:   0.1736                       
REMARK   3      S31:  -0.2590 S32:  -0.8239 S33:   0.3807                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN C                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  80.2466   9.8844  33.0826              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1337 T22:   0.3056                                     
REMARK   3      T33:   0.1907 T12:   0.0301                                     
REMARK   3      T13:  -0.0068 T23:  -0.0067                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6556 L22:   1.0316                                     
REMARK   3      L33:   3.4508 L12:  -0.0097                                     
REMARK   3      L13:  -0.4236 L23:   1.3035                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1029 S12:  -0.1835 S13:  -0.0409                       
REMARK   3      S21:   0.0348 S22:   0.2534 S23:  -0.0264                       
REMARK   3      S31:   0.2219 S32:   0.6285 S33:  -0.1556                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN D                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  70.2329  36.0800  24.0414              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9162 T22:   0.1573                                     
REMARK   3      T33:   0.2218 T12:   0.0037                                     
REMARK   3      T13:   0.0656 T23:   0.0303                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4965 L22:   0.6860                                     
REMARK   3      L33:   3.3160 L12:  -0.3256                                     
REMARK   3      L13:  -1.3618 L23:   1.0282                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3925 S12:   0.0064 S13:   0.1442                       
REMARK   3      S21:  -0.6949 S22:  -0.0413 S23:   0.0322                       
REMARK   3      S31:  -1.6805 S32:  -0.1106 S33:  -0.3235                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3OT7 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-SEP-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB061542.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-APR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 4.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NOIR-1                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 70968                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.200                              
REMARK 200  R MERGE                    (I) : 0.06900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.93                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1VEW                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 6000, 0.1M BICINE, 1MM EDTA,     
REMARK 280  PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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       89.01650            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       89.01650            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       47.43750            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       53.27400            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       47.43750            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       53.27400            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       89.01650            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       47.43750            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       53.27400            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       89.01650            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       47.43750            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       53.27400            
REMARK 290   SMTRY3   8  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 300 REMARK: THE BIOLOGICAL UNIT IS A DIMER. THERE ARE 2 BIOLOGICAL       
REMARK 300 UNITS IN THE ASYMMETRIC UNIT (CHAINS A & B AND CHAINS C & D)         
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: 1710 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17130 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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: 1720 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17290 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 441  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 634  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH C 265  LIES ON A SPECIAL POSITION.                          
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    HIS A  17      -63.30    -92.16                                   
REMARK 500    LYS A  29      -63.10   -108.62                                   
REMARK 500    LEU A  45       75.57   -113.52                                   
REMARK 500    LYS A  59       34.44   -144.51                                   
REMARK 500    PRO A  64      152.95    -45.74                                   
REMARK 500    LYS A  89      139.56   -178.95                                   
REMARK 500    GLN A  95     -178.11   -170.91                                   
REMARK 500    ASP A 136      -11.36     71.05                                   
REMARK 500    ASN A 145     -130.31     53.33                                   
REMARK 500    TYR A 173       -3.27   -144.27                                   
REMARK 500    GLN A 178     -124.22     46.37                                   
REMARK 500    LYS B  89      127.38    179.88                                   
REMARK 500    ARG B 123      106.64    -59.98                                   
REMARK 500    ASN B 145     -128.53     56.32                                   
REMARK 500    TYR B 173       -2.50   -142.08                                   
REMARK 500    GLN B 178     -132.74     45.98                                   
REMARK 500    LYS B 204       -9.17     67.79                                   
REMARK 500    PRO C  16       30.05    -97.90                                   
REMARK 500    LYS C  29      -60.67   -107.66                                   
REMARK 500    LYS C  89      130.29    177.80                                   
REMARK 500    ASN C 145     -124.09     54.41                                   
REMARK 500    TYR C 173       -4.87   -146.82                                   
REMARK 500    GLN C 178     -122.93     42.28                                   
REMARK 500    LYS C 204        2.91     59.47                                   
REMARK 500    PRO D  16       30.08    -95.51                                   
REMARK 500    LYS D  29      -62.39   -103.96                                   
REMARK 500    ASN D 145     -127.42     54.86                                   
REMARK 500    TYR D 173       -6.10   -142.26                                   
REMARK 500    GLN D 178     -132.57     44.95                                   
REMARK 500    LYS D 204      -13.76     73.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3OT7 A    1   205  UNP    P00448   SODM_ECOLI       2    206             
DBREF  3OT7 B    1   205  UNP    P00448   SODM_ECOLI       2    206             
DBREF  3OT7 C    1   205  UNP    P00448   SODM_ECOLI       2    206             
DBREF  3OT7 D    1   205  UNP    P00448   SODM_ECOLI       2    206             
SEQRES   1 A  205  SER TYR THR LEU PRO SER LEU PRO TYR ALA TYR ASP ALA          
SEQRES   2 A  205  LEU GLU PRO HIS PHE ASP LYS GLN THR MET GLU ILE HIS          
SEQRES   3 A  205  HIS THR LYS HIS HIS GLN THR TYR VAL ASN ASN ALA ASN          
SEQRES   4 A  205  ALA ALA LEU GLU SER LEU PRO GLU PHE ALA ASN LEU PRO          
SEQRES   5 A  205  VAL GLU GLU LEU ILE THR LYS LEU ASP GLN LEU PRO ALA          
SEQRES   6 A  205  ASP LYS LYS THR VAL LEU ARG ASN ASN ALA GLY GLY HIS          
SEQRES   7 A  205  ALA ASN HIS SER LEU PHE TRP LYS GLY LEU LYS LYS GLY          
SEQRES   8 A  205  THR THR LEU GLN GLY ASP LEU LYS ALA ALA ILE GLU ARG          
SEQRES   9 A  205  ASP PHE GLY SER VAL ASP ASN PHE LYS ALA GLU PHE GLU          
SEQRES  10 A  205  LYS ALA ALA ALA SER ARG PHE GLY SER GLY TRP ALA TRP          
SEQRES  11 A  205  LEU VAL LEU LYS GLY ASP LYS LEU ALA VAL VAL SER THR          
SEQRES  12 A  205  ALA ASN GLN ASP SER PRO LEU MET GLY GLU ALA ILE SER          
SEQRES  13 A  205  GLY ALA SER GLY PHE PRO ILE MET GLY LEU ASP VAL TRP          
SEQRES  14 A  205  GLU HIS ALA TYR TYR LEU LYS PHE GLN ASN ARG ARG PRO          
SEQRES  15 A  205  ASP TYR ILE LYS GLU PHE TRP ASN VAL VAL ASN TRP ASP          
SEQRES  16 A  205  GLU ALA ALA ALA ARG PHE ALA ALA LYS LYS                      
SEQRES   1 B  205  SER TYR THR LEU PRO SER LEU PRO TYR ALA TYR ASP ALA          
SEQRES   2 B  205  LEU GLU PRO HIS PHE ASP LYS GLN THR MET GLU ILE HIS          
SEQRES   3 B  205  HIS THR LYS HIS HIS GLN THR TYR VAL ASN ASN ALA ASN          
SEQRES   4 B  205  ALA ALA LEU GLU SER LEU PRO GLU PHE ALA ASN LEU PRO          
SEQRES   5 B  205  VAL GLU GLU LEU ILE THR LYS LEU ASP GLN LEU PRO ALA          
SEQRES   6 B  205  ASP LYS LYS THR VAL LEU ARG ASN ASN ALA GLY GLY HIS          
SEQRES   7 B  205  ALA ASN HIS SER LEU PHE TRP LYS GLY LEU LYS LYS GLY          
SEQRES   8 B  205  THR THR LEU GLN GLY ASP LEU LYS ALA ALA ILE GLU ARG          
SEQRES   9 B  205  ASP PHE GLY SER VAL ASP ASN PHE LYS ALA GLU PHE GLU          
SEQRES  10 B  205  LYS ALA ALA ALA SER ARG PHE GLY SER GLY TRP ALA TRP          
SEQRES  11 B  205  LEU VAL LEU LYS GLY ASP LYS LEU ALA VAL VAL SER THR          
SEQRES  12 B  205  ALA ASN GLN ASP SER PRO LEU MET GLY GLU ALA ILE SER          
SEQRES  13 B  205  GLY ALA SER GLY PHE PRO ILE MET GLY LEU ASP VAL TRP          
SEQRES  14 B  205  GLU HIS ALA TYR TYR LEU LYS PHE GLN ASN ARG ARG PRO          
SEQRES  15 B  205  ASP TYR ILE LYS GLU PHE TRP ASN VAL VAL ASN TRP ASP          
SEQRES  16 B  205  GLU ALA ALA ALA ARG PHE ALA ALA LYS LYS                      
SEQRES   1 C  205  SER TYR THR LEU PRO SER LEU PRO TYR ALA TYR ASP ALA          
SEQRES   2 C  205  LEU GLU PRO HIS PHE ASP LYS GLN THR MET GLU ILE HIS          
SEQRES   3 C  205  HIS THR LYS HIS HIS GLN THR TYR VAL ASN ASN ALA ASN          
SEQRES   4 C  205  ALA ALA LEU GLU SER LEU PRO GLU PHE ALA ASN LEU PRO          
SEQRES   5 C  205  VAL GLU GLU LEU ILE THR LYS LEU ASP GLN LEU PRO ALA          
SEQRES   6 C  205  ASP LYS LYS THR VAL LEU ARG ASN ASN ALA GLY GLY HIS          
SEQRES   7 C  205  ALA ASN HIS SER LEU PHE TRP LYS GLY LEU LYS LYS GLY          
SEQRES   8 C  205  THR THR LEU GLN GLY ASP LEU LYS ALA ALA ILE GLU ARG          
SEQRES   9 C  205  ASP PHE GLY SER VAL ASP ASN PHE LYS ALA GLU PHE GLU          
SEQRES  10 C  205  LYS ALA ALA ALA SER ARG PHE GLY SER GLY TRP ALA TRP          
SEQRES  11 C  205  LEU VAL LEU LYS GLY ASP LYS LEU ALA VAL VAL SER THR          
SEQRES  12 C  205  ALA ASN GLN ASP SER PRO LEU MET GLY GLU ALA ILE SER          
SEQRES  13 C  205  GLY ALA SER GLY PHE PRO ILE MET GLY LEU ASP VAL TRP          
SEQRES  14 C  205  GLU HIS ALA TYR TYR LEU LYS PHE GLN ASN ARG ARG PRO          
SEQRES  15 C  205  ASP TYR ILE LYS GLU PHE TRP ASN VAL VAL ASN TRP ASP          
SEQRES  16 C  205  GLU ALA ALA ALA ARG PHE ALA ALA LYS LYS                      
SEQRES   1 D  205  SER TYR THR LEU PRO SER LEU PRO TYR ALA TYR ASP ALA          
SEQRES   2 D  205  LEU GLU PRO HIS PHE ASP LYS GLN THR MET GLU ILE HIS          
SEQRES   3 D  205  HIS THR LYS HIS HIS GLN THR TYR VAL ASN ASN ALA ASN          
SEQRES   4 D  205  ALA ALA LEU GLU SER LEU PRO GLU PHE ALA ASN LEU PRO          
SEQRES   5 D  205  VAL GLU GLU LEU ILE THR LYS LEU ASP GLN LEU PRO ALA          
SEQRES   6 D  205  ASP LYS LYS THR VAL LEU ARG ASN ASN ALA GLY GLY HIS          
SEQRES   7 D  205  ALA ASN HIS SER LEU PHE TRP LYS GLY LEU LYS LYS GLY          
SEQRES   8 D  205  THR THR LEU GLN GLY ASP LEU LYS ALA ALA ILE GLU ARG          
SEQRES   9 D  205  ASP PHE GLY SER VAL ASP ASN PHE LYS ALA GLU PHE GLU          
SEQRES  10 D  205  LYS ALA ALA ALA SER ARG PHE GLY SER GLY TRP ALA TRP          
SEQRES  11 D  205  LEU VAL LEU LYS GLY ASP LYS LEU ALA VAL VAL SER THR          
SEQRES  12 D  205  ALA ASN GLN ASP SER PRO LEU MET GLY GLU ALA ILE SER          
SEQRES  13 D  205  GLY ALA SER GLY PHE PRO ILE MET GLY LEU ASP VAL TRP          
SEQRES  14 D  205  GLU HIS ALA TYR TYR LEU LYS PHE GLN ASN ARG ARG PRO          
SEQRES  15 D  205  ASP TYR ILE LYS GLU PHE TRP ASN VAL VAL ASN TRP ASP          
SEQRES  16 D  205  GLU ALA ALA ALA ARG PHE ALA ALA LYS LYS                      
FORMUL   5  HOH   *640(H2 O)                                                    
HELIX    1   1 ASP A   19  LYS A   29  1                                  11    
HELIX    2   2 LYS A   29  GLU A   43  1                                  15    
HELIX    3   3 LEU A   45  ASN A   50  1                                   6    
HELIX    4   4 PRO A   52  ILE A   57  1                                   6    
HELIX    5   5 THR A   58  LEU A   63  5                                   6    
HELIX    6   6 LYS A   67  GLY A   87  1                                  21    
HELIX    7   7 GLN A   95  GLY A  107  1                                  13    
HELIX    8   8 SER A  108  ARG A  123  1                                  16    
HELIX    9   9 SER A  148  MET A  151  5                                   4    
HELIX   10  10 GLY A  152  GLY A  157  1                                   6    
HELIX   11  11 TRP A  169  ALA A  172  5                                   4    
HELIX   12  12 TYR A  173  GLN A  178  1                                   6    
HELIX   13  13 ARG A  180  VAL A  192  1                                  13    
HELIX   14  14 ASN A  193  LYS A  204  1                                  12    
HELIX   15  15 ASP B   19  LYS B   29  1                                  11    
HELIX   16  16 LYS B   29  GLU B   43  1                                  15    
HELIX   17  17 LEU B   45  ASN B   50  1                                   6    
HELIX   18  18 PRO B   52  ILE B   57  1                                   6    
HELIX   19  19 THR B   58  LEU B   63  5                                   6    
HELIX   20  20 PRO B   64  ASP B   66  5                                   3    
HELIX   21  21 LYS B   67  GLY B   87  1                                  21    
HELIX   22  22 GLN B   95  GLY B  107  1                                  13    
HELIX   23  23 SER B  108  ARG B  123  1                                  16    
HELIX   24  24 SER B  148  MET B  151  5                                   4    
HELIX   25  25 GLY B  152  GLY B  157  1                                   6    
HELIX   26  26 TRP B  169  ALA B  172  5                                   4    
HELIX   27  27 TYR B  173  GLN B  178  1                                   6    
HELIX   28  28 ARG B  180  VAL B  192  1                                  13    
HELIX   29  29 ASN B  193  LYS B  204  1                                  12    
HELIX   30  30 ASP C   19  LYS C   29  1                                  11    
HELIX   31  31 LYS C   29  GLU C   43  1                                  15    
HELIX   32  32 LEU C   45  ASN C   50  1                                   6    
HELIX   33  33 PRO C   52  ILE C   57  1                                   6    
HELIX   34  34 THR C   58  LEU C   63  5                                   6    
HELIX   35  35 PRO C   64  ASP C   66  5                                   3    
HELIX   36  36 LYS C   67  GLY C   87  1                                  21    
HELIX   37  37 GLN C   95  GLY C  107  1                                  13    
HELIX   38  38 SER C  108  ARG C  123  1                                  16    
HELIX   39  39 SER C  148  MET C  151  5                                   4    
HELIX   40  40 GLY C  152  GLY C  157  1                                   6    
HELIX   41  41 TRP C  169  ALA C  172  5                                   4    
HELIX   42  42 TYR C  173  GLN C  178  1                                   6    
HELIX   43  43 ARG C  180  TRP C  189  1                                  10    
HELIX   44  44 ASN C  193  LYS C  204  1                                  12    
HELIX   45  45 ASP D   19  LYS D   29  1                                  11    
HELIX   46  46 LYS D   29  GLU D   43  1                                  15    
HELIX   47  47 LEU D   45  ASN D   50  1                                   6    
HELIX   48  48 PRO D   52  ILE D   57  1                                   6    
HELIX   49  49 THR D   58  LEU D   63  5                                   6    
HELIX   50  50 PRO D   64  GLY D   87  1                                  24    
HELIX   51  51 GLN D   95  GLY D  107  1                                  13    
HELIX   52  52 SER D  108  ARG D  123  1                                  16    
HELIX   53  53 SER D  148  MET D  151  5                                   4    
HELIX   54  54 GLY D  152  GLY D  157  1                                   6    
HELIX   55  55 TRP D  169  ALA D  172  5                                   4    
HELIX   56  56 TYR D  173  GLN D  178  1                                   6    
HELIX   57  57 ARG D  180  TRP D  189  1                                  10    
HELIX   58  58 ASN D  193  LYS D  204  1                                  12    
SHEET    1   A 3 LYS A 137  ALA A 144  0                                        
SHEET    2   A 3 GLY A 127  LYS A 134 -1  N  TRP A 130   O  VAL A 141           
SHEET    3   A 3 PHE A 161  ASP A 167 -1  O  ILE A 163   N  LEU A 131           
SHEET    1   B 3 LYS B 137  ALA B 144  0                                        
SHEET    2   B 3 GLY B 127  LYS B 134 -1  N  TRP B 130   O  VAL B 141           
SHEET    3   B 3 PHE B 161  ASP B 167 -1  O  ILE B 163   N  LEU B 131           
SHEET    1   C 3 LYS C 137  ALA C 144  0                                        
SHEET    2   C 3 GLY C 127  LYS C 134 -1  N  TRP C 130   O  VAL C 141           
SHEET    3   C 3 PHE C 161  ASP C 167 -1  O  ILE C 163   N  LEU C 131           
SHEET    1   D 3 LYS D 137  ALA D 144  0                                        
SHEET    2   D 3 GLY D 127  LYS D 134 -1  N  TRP D 130   O  VAL D 141           
SHEET    3   D 3 PHE D 161  ASP D 167 -1  O  ILE D 163   N  LEU D 131           
CISPEP   1 GLU A   15    PRO A   16          0         1.08                     
CISPEP   2 GLU B   15    PRO B   16          0         0.18                     
CISPEP   3 GLU C   15    PRO C   16          0         4.48                     
CISPEP   4 GLU D   15    PRO D   16          0        -0.13                     
CRYST1   94.875  106.548  178.033  90.00  90.00  90.00 C 2 2 21     32          
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      0.010540  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009385  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005617        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system