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Database: PDB
Entry: 4IWX
LinkDB: 4IWX
Original site: 4IWX 
HEADER    LIGASE                                  24-JAN-13   4IWX              
TITLE     RIMK STRUCTURE AT 2.85A                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN;                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 GENE: B0852, JW0836, RIMK;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    ATP-GRASP FOLD, LIGASE                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.SHI,G.ZHAO,Z.JIN,N.M.ALLEWELL,M.TUCHMAN                             
REVDAT   3   15-NOV-17 4IWX    1       REMARK                                   
REVDAT   2   09-OCT-13 4IWX    1       JRNL                                     
REVDAT   1   08-MAY-13 4IWX    0                                                
JRNL        AUTH   G.ZHAO,Z.JIN,Y.WANG,N.M.ALLEWELL,M.TUCHMAN,D.SHI             
JRNL        TITL   STRUCTURE AND FUNCTION OF ESCHERICHIA COLI RIMK, AN          
JRNL        TITL 2 ATP-GRASP FOLD, L-GLUTAMYL LIGASE ENZYME.                    
JRNL        REF    PROTEINS                      V.  81  1847 2013              
JRNL        REFN                   ISSN 0887-3585                               
JRNL        PMID   23609986                                                     
JRNL        DOI    10.1002/PROT.24311                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.1_1168                                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.99                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 20062                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.218                           
REMARK   3   R VALUE            (WORKING SET) : 0.216                           
REMARK   3   FREE R VALUE                     : 0.257                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.980                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 999                             
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 46.9926 -  5.4570    0.99     2966   156  0.2225 0.2541        
REMARK   3     2  5.4570 -  4.3324    1.00     2799   148  0.1743 0.1765        
REMARK   3     3  4.3324 -  3.7850    1.00     2756   145  0.1867 0.2636        
REMARK   3     4  3.7850 -  3.4391    0.99     2716   142  0.2206 0.2668        
REMARK   3     5  3.4391 -  3.1926    1.00     2726   142  0.2573 0.3253        
REMARK   3     6  3.1926 -  3.0044    0.99     2671   138  0.2875 0.3444        
REMARK   3     7  3.0044 -  2.8540    0.90     2429   128  0.3215 0.4019        
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              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.420            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.890           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 75.23                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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      :  0.010           2345                                  
REMARK   3   ANGLE     :  1.475           3180                                  
REMARK   3   CHIRALITY :  0.097            366                                  
REMARK   3   PLANARITY :  0.009            407                                  
REMARK   3   DIHEDRAL  : 17.386            886                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID -1:99)                              
REMARK   3    ORIGIN FOR THE GROUP (A): -18.8388  74.2455  73.7926              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3849 T22:   0.4364                                     
REMARK   3      T33:   0.4084 T12:  -0.0588                                     
REMARK   3      T13:  -0.0279 T23:  -0.0473                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6669 L22:   3.3692                                     
REMARK   3      L33:   3.1749 L12:  -2.5502                                     
REMARK   3      L13:   0.1570 L23:  -1.2761                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1093 S12:  -0.2217 S13:   0.0026                       
REMARK   3      S21:   0.0991 S22:   0.1846 S23:   0.0201                       
REMARK   3      S31:  -0.2513 S32:   0.1826 S33:  -0.0948                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 100:115)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.5355  56.1094  59.8183              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5876 T22:   0.4319                                     
REMARK   3      T33:   0.4838 T12:  -0.0200                                     
REMARK   3      T13:  -0.0028 T23:  -0.0382                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9464 L22:   4.8873                                     
REMARK   3      L33:   3.3964 L12:  -2.2657                                     
REMARK   3      L13:   1.8467 L23:  -1.2041                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1806 S12:  -0.2176 S13:   0.4494                       
REMARK   3      S21:  -0.7466 S22:  -0.1907 S23:  -0.0973                       
REMARK   3      S31:  -0.3715 S32:   0.2394 S33:   0.0644                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 116:180)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -15.1672  42.8492  54.8023              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4712 T22:   0.3833                                     
REMARK   3      T33:   0.5164 T12:   0.0317                                     
REMARK   3      T13:  -0.0488 T23:  -0.0234                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8139 L22:   3.7744                                     
REMARK   3      L33:   4.2049 L12:   2.8434                                     
REMARK   3      L13:  -0.0394 L23:   0.4132                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1331 S12:   0.1776 S13:  -0.4416                       
REMARK   3      S21:  -0.6184 S22:   0.2537 S23:   0.1268                       
REMARK   3      S31:   0.0284 S32:   0.1470 S33:  -0.3211                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 181:276)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.3755  51.5287  75.1133              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4513 T22:   0.6990                                     
REMARK   3      T33:   0.5699 T12:  -0.0271                                     
REMARK   3      T13:  -0.0755 T23:   0.0119                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6218 L22:   2.5162                                     
REMARK   3      L33:   4.2076 L12:  -0.8247                                     
REMARK   3      L13:  -0.3169 L23:   0.6092                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0293 S12:  -0.0645 S13:  -0.3166                       
REMARK   3      S21:   0.0055 S22:  -0.0039 S23:   0.1833                       
REMARK   3      S31:   0.4418 S32:  -0.1750 S33:  -0.0888                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 277:292)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.0968  72.2769  81.9804              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5404 T22:   0.6513                                     
REMARK   3      T33:   0.5982 T12:  -0.0055                                     
REMARK   3      T13:  -0.0454 T23:  -0.1617                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.9952 L22:   2.1450                                     
REMARK   3      L33:   6.1593 L12:   0.0995                                     
REMARK   3      L13:  -1.3035 L23:  -1.4529                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2880 S12:  -0.1144 S13:   0.0025                       
REMARK   3      S21:   0.9595 S22:   0.7121 S23:  -1.5364                       
REMARK   3      S31:  -0.8372 S32:   0.5831 S33:  -0.5917                       
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 4IWX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JAN-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000077312.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JUL-12                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20166                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 15.70                              
REMARK 200  R MERGE                    (I) : 0.11100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.63900                            
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: SHELXS                                                
REMARK 200 STARTING MODEL: 4IWY                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 79.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES, AND 1.8 M AMMONIUM         
REMARK 280  SULFATE , PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z+1/3                                            
REMARK 290       6555   X-Y,X,Z+2/3                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+1/3                                            
REMARK 290      11555   -X+Y,Y,-Z                                               
REMARK 290      12555   X,X-Y,-Z+2/3                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       57.07967            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      114.15933            
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  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       57.07967            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000      114.15933            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       57.07967            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      114.15933            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       57.07967            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      114.15933            
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 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 19590 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 43100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -409.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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   BIOMT1   2 -1.000000  0.000000  0.000000      -64.90100            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      112.41183            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   3 -0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000      114.15933            
REMARK 350   BIOMT1   4  0.500000  0.866025  0.000000      -64.90100            
REMARK 350   BIOMT2   4  0.866025 -0.500000  0.000000      112.41183            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000      114.15933            
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   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     GLU A   293                                                      
REMARK 465     TYR A   294                                                      
REMARK 465     CYS A   295                                                      
REMARK 465     LEU A   296                                                      
REMARK 465     LYS A   297                                                      
REMARK 465     THR A   298                                                      
REMARK 465     GLY A   299                                                      
REMARK 465     GLY A   300                                                      
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    GLN A    24     N    GLY A    26              2.10            
REMARK 500   NH1  ARG A   102     OE2  GLU A   402              2.18            
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    HIS A   0       83.89     47.94                                   
REMARK 500    ARG A  25       35.97     -6.23                                   
REMARK 500    ASN A  42     -136.00    -70.82                                   
REMARK 500    PRO A  43       84.69    -22.25                                   
REMARK 500    ALA A  44      136.34    -18.93                                   
REMARK 500    ALA A  45     -107.21     75.67                                   
REMARK 500    SER A  46      141.35     65.29                                   
REMARK 500    HIS A  57      106.43     79.07                                   
REMARK 500    ARG A  64       53.69   -150.20                                   
REMARK 500    ILE A  69       20.45   -143.81                                   
REMARK 500    ASN A  89      107.02     76.85                                   
REMARK 500    HIS A 121      -60.33   -140.86                                   
REMARK 500    ASP A 124      -23.32     68.64                                   
REMARK 500    VAL A 133      -28.26     76.36                                   
REMARK 500    VAL A 143      -54.89   -128.75                                   
REMARK 500    GLU A 144       91.44     62.76                                   
REMARK 500    THR A 146       70.93   -155.05                                   
REMARK 500    GLN A 147      -77.36   -143.92                                   
REMARK 500    LEU A 170      -17.77    -45.31                                   
REMARK 500    ASN A 171        4.05    -55.02                                   
REMARK 500    HIS A 173     -162.46     61.78                                   
REMARK 500    ILE A 174      144.36    -38.48                                   
REMARK 500    GLU A 182      -93.20    -63.13                                   
REMARK 500    ALA A 183     -125.68     42.44                                   
REMARK 500    GLN A 184       60.35    162.05                                   
REMARK 500    ASP A 209     -129.86     27.14                                   
REMARK 500    PHE A 210      -90.28   -119.93                                   
REMARK 500    ARG A 211     -142.01     52.50                                   
REMARK 500    SER A 212      -10.67    156.20                                   
REMARK 500    LEU A 214      -64.34    -15.28                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASN A   42     PRO A   43                 -141.57                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLU A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 407                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4IWY   RELATED DB: PDB                                   
DBREF  4IWX A    1   300  UNP    P0C0U4   RIMK_ECOLI       1    300             
SEQADV 4IWX MET A  -19  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWX GLY A  -18  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWX SER A  -17  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWX SER A  -16  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWX HIS A  -15  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWX HIS A  -14  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWX HIS A  -13  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWX HIS A  -12  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWX HIS A  -11  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWX HIS A  -10  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWX SER A   -9  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWX SER A   -8  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWX GLY A   -7  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWX LEU A   -6  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWX VAL A   -5  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWX PRO A   -4  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWX ARG A   -3  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWX GLY A   -2  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWX SER A   -1  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWX HIS A    0  UNP  P0C0U4              EXPRESSION TAG                 
SEQRES   1 A  320  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  320  LEU VAL PRO ARG GLY SER HIS MET LYS ILE ALA ILE LEU          
SEQRES   3 A  320  SER ARG ASP GLY THR LEU TYR SER CYS LYS ARG LEU ARG          
SEQRES   4 A  320  GLU ALA ALA ILE GLN ARG GLY HIS LEU VAL GLU ILE LEU          
SEQRES   5 A  320  ASP PRO LEU SER CYS TYR MET ASN ILE ASN PRO ALA ALA          
SEQRES   6 A  320  SER SER ILE HIS TYR LYS GLY ARG LYS LEU PRO HIS PHE          
SEQRES   7 A  320  ASP ALA VAL ILE PRO ARG ILE GLY THR ALA ILE THR PHE          
SEQRES   8 A  320  TYR GLY THR ALA ALA LEU ARG GLN PHE GLU MET LEU GLY          
SEQRES   9 A  320  SER TYR PRO LEU ASN GLU SER VAL ALA ILE ALA ARG ALA          
SEQRES  10 A  320  ARG ASP LYS LEU ARG SER MET GLN LEU LEU ALA ARG GLN          
SEQRES  11 A  320  GLY ILE ASP LEU PRO VAL THR GLY ILE ALA HIS SER PRO          
SEQRES  12 A  320  ASP ASP THR SER ASP LEU ILE ASP MET VAL GLY GLY ALA          
SEQRES  13 A  320  PRO LEU VAL VAL LYS LEU VAL GLU GLY THR GLN GLY ILE          
SEQRES  14 A  320  GLY VAL VAL LEU ALA GLU THR ARG GLN ALA ALA GLU SER          
SEQRES  15 A  320  VAL ILE ASP ALA PHE ARG GLY LEU ASN ALA HIS ILE LEU          
SEQRES  16 A  320  VAL GLN GLU TYR ILE LYS GLU ALA GLN GLY CYS ASP ILE          
SEQRES  17 A  320  ARG CYS LEU VAL VAL GLY ASP GLU VAL VAL ALA ALA ILE          
SEQRES  18 A  320  GLU ARG ARG ALA LYS GLU GLY ASP PHE ARG SER ASN LEU          
SEQRES  19 A  320  HIS ARG GLY GLY ALA ALA SER VAL ALA SER ILE THR PRO          
SEQRES  20 A  320  GLN GLU ARG GLU ILE ALA ILE LYS ALA ALA ARG THR MET          
SEQRES  21 A  320  ALA LEU ASP VAL ALA GLY VAL ASP ILE LEU ARG ALA ASN          
SEQRES  22 A  320  ARG GLY PRO LEU VAL MET GLU VAL ASN ALA SER PRO GLY          
SEQRES  23 A  320  LEU GLU GLY ILE GLU LYS THR THR GLY ILE ASP ILE ALA          
SEQRES  24 A  320  GLY LYS MET ILE ARG TRP ILE GLU ARG HIS ALA THR THR          
SEQRES  25 A  320  GLU TYR CYS LEU LYS THR GLY GLY                              
HET    ADP  A 401      27                                                       
HET    GLU  A 402      10                                                       
HET    SO4  A 403       5                                                       
HET    SO4  A 404       5                                                       
HET    SO4  A 405       5                                                       
HET    SO4  A 406       5                                                       
HET    SO4  A 407       5                                                       
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     GLU GLUTAMIC ACID                                                    
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2  ADP    C10 H15 N5 O10 P2                                            
FORMUL   3  GLU    C5 H9 N O4                                                   
FORMUL   4  SO4    5(O4 S 2-)                                                   
FORMUL   9  HOH   *(H2 O)                                                       
HELIX    1   1 THR A   11  GLN A   24  1                                  14    
HELIX    2   2 ARG A   25  HIS A   27  5                                   3    
HELIX    3   3 ASP A   33  LEU A   35  5                                   3    
HELIX    4   4 ILE A   69  LEU A   83  1                                  15    
HELIX    5   5 GLU A   90  ASP A   99  1                                  10    
HELIX    6   6 ASP A   99  GLN A  110  1                                  12    
HELIX    7   7 ASP A  125  MET A  132  1                                   8    
HELIX    8   8 THR A  156  GLY A  169  1                                  14    
HELIX    9   9 LEU A  170  HIS A  173  5                                   4    
HELIX   10  10 THR A  226  MET A  240  1                                  15    
HELIX   11  11 LEU A  267  GLY A  275  1                                   9    
HELIX   12  12 ASP A  277  ALA A  290  1                                  14    
SHEET    1   A 4 LEU A  28  LEU A  32  0                                        
SHEET    2   A 4 LYS A   2  LEU A   6  1  N  ILE A   3   O  LEU A  28           
SHEET    3   A 4 ALA A  60  PRO A  63  1  O  ILE A  62   N  ALA A   4           
SHEET    4   A 4 TYR A  86  PRO A  87  1  O  TYR A  86   N  VAL A  61           
SHEET    1   B 3 CYS A  37  MET A  39  0                                        
SHEET    2   B 3 ILE A  48  TYR A  50 -1  O  HIS A  49   N  TYR A  38           
SHEET    3   B 3 ARG A  53  LYS A  54 -1  O  ARG A  53   N  TYR A  50           
SHEET    1   C 4 THR A 117  ALA A 120  0                                        
SHEET    2   C 4 LEU A 175  TYR A 179 -1  O  GLN A 177   N  GLY A 118           
SHEET    3   C 4 LEU A 138  LEU A 142 -1  N  VAL A 139   O  GLU A 178           
SHEET    4   C 4 GLY A 150  ALA A 154 -1  O  ALA A 154   N  LEU A 138           
SHEET    1   D 5 ALA A 219  VAL A 222  0                                        
SHEET    2   D 5 GLU A 196  ARG A 204 -1  N  GLU A 202   O  SER A 221           
SHEET    3   D 5 ASP A 187  VAL A 193 -1  N  ARG A 189   O  ILE A 201           
SHEET    4   D 5 VAL A 244  ALA A 252 -1  O  ILE A 249   N  ILE A 188           
SHEET    5   D 5 GLY A 255  ASN A 262 -1  O  MET A 259   N  ASP A 248           
SITE     1 AC1 12 LYS A 141  GLU A 178  TYR A 179  ILE A 180                    
SITE     2 AC1 12 LYS A 181  ASP A 187  ARG A 211  SER A 212                    
SITE     3 AC1 12 ASN A 213  ASP A 248  MET A 259  GLU A 260                    
SITE     1 AC2  8 ARG A  78  MET A  82  VAL A  92  ARG A  96                    
SITE     2 AC2  8 ARG A 102  GLN A 105  LEU A 106  ARG A 109                    
SITE     1 AC3  5 ARG A 189  LEU A 214  ASN A 262  PRO A 265                    
SITE     2 AC3  5 GLY A 266                                                     
SITE     1 AC4  6 THR A  67  ARG A  98  LYS A 100  ASN A 262                    
SITE     2 AC4  6 ALA A 263  SER A 264                                          
SITE     1 AC5  2 LYS A  51  ARG A  53                                          
SITE     1 AC6  3 SER A  46  SER A  47  LYS A  54                               
SITE     1 AC7  2 ARG A 284  ARG A 288                                          
CRYST1  129.802  129.802  171.239  90.00  90.00 120.00 P 64 2 2     12          
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      0.007704  0.004448  0.000000        0.00000                         
SCALE2      0.000000  0.008896  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005840        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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