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Database: PDB
Entry: 4IWY
LinkDB: 4IWY
Original site: 4IWY 
HEADER    LIGASE                                  24-JAN-13   4IWY              
TITLE     SEMET-SUBSTITUTED RIMK STRUCTURE                                      
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   24-JAN-18 4IWY    1       AUTHOR                                   
REVDAT   2   09-OCT-13 4IWY    1       JRNL                                     
REVDAT   1   08-MAY-13 4IWY    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.    2.90 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) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.56                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 18059                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.207                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1621                            
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 26.5590 -  6.6057    1.00     2801   141  0.1804 0.2125        
REMARK   3     2  6.6057 -  5.2565    1.00     2809   147  0.2183 0.2699        
REMARK   3     3  5.2565 -  4.5959    1.00     2787   146  0.1630 0.2093        
REMARK   3     4  4.5959 -  4.1775    1.00     2803   153  0.1579 0.2014        
REMARK   3     5  4.1775 -  3.8790    1.00     2788   145  0.1948 0.2474        
REMARK   3     6  3.8790 -  3.6509    1.00     2785   142  0.2083 0.2655        
REMARK   3     7  3.6509 -  3.4685    1.00     2794   149  0.2265 0.3117        
REMARK   3     8  3.4685 -  3.3178    1.00     2775   145  0.2526 0.2930        
REMARK   3     9  3.3178 -  3.1903    0.97     2730   146  0.2799 0.3375        
REMARK   3    10  3.1903 -  3.0804    0.86     2385   129  0.3004 0.3199        
REMARK   3    11  3.0804 -  2.9842    0.70     1931   104  0.3043 0.3269        
REMARK   3    12  2.9842 -  2.8990    0.50     1413    74  0.3190 0.3459        
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)     : 0.340            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.440           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 79.83                          
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      :  0.011           2349                                  
REMARK   3   ANGLE     :  1.589           3186                                  
REMARK   3   CHIRALITY :  0.099            366                                  
REMARK   3   PLANARITY :  0.008            407                                  
REMARK   3   DIHEDRAL  : 17.636            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): -18.6768  74.0092  73.6544              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3807 T22:   0.4514                                     
REMARK   3      T33:   0.3815 T12:  -0.0144                                     
REMARK   3      T13:  -0.0006 T23:  -0.0016                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5408 L22:   3.5171                                     
REMARK   3      L33:   3.4585 L12:  -2.4305                                     
REMARK   3      L13:   0.6976 L23:  -0.2057                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0971 S12:  -0.2920 S13:   0.0494                       
REMARK   3      S21:   0.0534 S22:   0.2260 S23:  -0.0433                       
REMARK   3      S31:  -0.1801 S32:   0.2034 S33:  -0.1263                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 100:115)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.5500  55.6888  59.8972              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6564 T22:   0.6113                                     
REMARK   3      T33:   0.5479 T12:  -0.0511                                     
REMARK   3      T13:   0.0335 T23:   0.0149                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5911 L22:   5.4357                                     
REMARK   3      L33:   4.0750 L12:  -1.5220                                     
REMARK   3      L13:   1.2814 L23:  -0.8046                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1177 S12:  -0.5821 S13:  -0.1639                       
REMARK   3      S21:  -0.4703 S22:  -0.0845 S23:  -0.2824                       
REMARK   3      S31:  -0.4310 S32:   0.5445 S33:   0.0333                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 116:180)                            
REMARK   3    ORIGIN FOR THE GROUP (A): -14.8888  42.4821  54.7934              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4544 T22:   0.3492                                     
REMARK   3      T33:   0.5126 T12:   0.0054                                     
REMARK   3      T13:  -0.0519 T23:  -0.0369                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5429 L22:   3.9936                                     
REMARK   3      L33:   5.1567 L12:   2.6485                                     
REMARK   3      L13:  -0.1830 L23:   0.0712                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0957 S12:   0.2473 S13:  -0.1850                       
REMARK   3      S21:  -0.4378 S22:   0.3026 S23:   0.1364                       
REMARK   3      S31:   0.0656 S32:   0.1374 S33:  -0.3593                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 181:276)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.3004  51.2419  75.0353              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4854 T22:   0.7477                                     
REMARK   3      T33:   0.5790 T12:  -0.0233                                     
REMARK   3      T13:  -0.1008 T23:   0.0252                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8133 L22:   2.3361                                     
REMARK   3      L33:   2.9308 L12:  -0.8186                                     
REMARK   3      L13:  -0.6169 L23:   1.0919                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0673 S12:  -0.1173 S13:  -0.2194                       
REMARK   3      S21:   0.0079 S22:   0.0043 S23:   0.1212                       
REMARK   3      S31:   0.4483 S32:  -0.1715 S33:  -0.0960                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 277:292)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.1839  71.7582  81.8850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5491 T22:   0.6661                                     
REMARK   3      T33:   0.6165 T12:   0.0129                                     
REMARK   3      T13:  -0.0828 T23:  -0.1375                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5984 L22:   6.5723                                     
REMARK   3      L33:   5.5082 L12:   1.0898                                     
REMARK   3      L13:  -1.6484 L23:  -0.7852                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2265 S12:   0.2183 S13:  -0.0310                       
REMARK   3      S21:   0.2231 S22:   0.5930 S23:  -0.8698                       
REMARK   3      S31:  -0.3870 S32:   0.3057 S33:  -0.3963                       
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 4IWY 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_1000077313.                                   
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-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97921, 0.97934, 0.97471          
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 : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18059                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
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     (%) : 93.4                               
REMARK 200  DATA REDUNDANCY                : 15.60                              
REMARK 200  R MERGE                    (I) : 0.12600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 53.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.80300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHELXS                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 79.06                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.87                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES, AND 1.8 M AMMONIUM         
REMARK 280  SULFATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K, PH 7.5    
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       57.07933            
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      114.15867            
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       57.07933            
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      114.15867            
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       57.07933            
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      114.15867            
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       57.07933            
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      114.15867            
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: 19430 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 42640 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -405.0 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      -64.51500            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      111.74326            
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      114.15867            
REMARK 350   BIOMT1   4  0.500000  0.866025  0.000000      -64.51500            
REMARK 350   BIOMT2   4  0.866025 -0.500000  0.000000      111.74326            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000      114.15867            
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 S    SO4 A 408  LIES ON A SPECIAL POSITION.                          
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     MSE 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   NH1  ARG A   102     OE2  GLU A   402              2.15            
REMARK 500   O    GLN A    24     N    GLY A    26              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A  18   CA  -  CB  -  CG  ANGL. DEV. =  14.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A   0       86.11     41.99                                   
REMARK 500    ILE A  23      -74.87    -63.82                                   
REMARK 500    ARG A  25       39.55     -3.81                                   
REMARK 500    ASN A  42     -132.10    -71.70                                   
REMARK 500    PRO A  43       87.56    -23.87                                   
REMARK 500    ALA A  44      127.80    -13.74                                   
REMARK 500    ALA A  45     -102.14     74.02                                   
REMARK 500    SER A  46      148.71     65.15                                   
REMARK 500    HIS A  57      105.55     77.51                                   
REMARK 500    ILE A  69       20.61   -142.59                                   
REMARK 500    ASN A  89      108.62     70.07                                   
REMARK 500    ASP A  99       92.16    -68.01                                   
REMARK 500    HIS A 121      -57.46   -137.48                                   
REMARK 500    ASP A 124      -20.84     77.49                                   
REMARK 500    VAL A 133      -31.95     74.05                                   
REMARK 500    VAL A 143      -54.03   -133.10                                   
REMARK 500    GLU A 144       94.40     61.68                                   
REMARK 500    THR A 146       80.67   -156.61                                   
REMARK 500    GLN A 147      -76.41   -153.85                                   
REMARK 500    ILE A 149       20.10   -147.49                                   
REMARK 500    ASN A 171        2.61    -53.63                                   
REMARK 500    HIS A 173     -165.57     58.17                                   
REMARK 500    ILE A 174      138.28    -32.64                                   
REMARK 500    GLU A 182      -98.64    -60.59                                   
REMARK 500    ALA A 183     -126.27     46.82                                   
REMARK 500    GLN A 184       71.37    161.36                                   
REMARK 500    ASP A 209     -148.43     36.36                                   
REMARK 500    PHE A 210      -91.92   -111.97                                   
REMARK 500    ARG A 211     -129.27     48.43                                   
REMARK 500    SER A 212      -17.94    151.91                                   
REMARK 500    ASN A 213      141.08    -35.27                                   
REMARK 500    LEU A 214      -64.57    -12.88                                   
REMARK 500    HIS A 289      -31.82   -130.40                                   
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                 -139.29                    
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 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 408                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4IWX   RELATED DB: PDB                                   
REMARK 900 SAME PROTEIN, BUT IT IS NATIVE STRUCTURE.                            
DBREF  4IWY A    2   300  UNP    P0C0U4   RIMK_ECOLI       2    300             
SEQADV 4IWY MSE A  -19  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWY GLY A  -18  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWY SER A  -17  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWY SER A  -16  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWY HIS A  -15  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWY HIS A  -14  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWY HIS A  -13  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWY HIS A  -12  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWY HIS A  -11  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWY HIS A  -10  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWY SER A   -9  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWY SER A   -8  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWY GLY A   -7  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWY LEU A   -6  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWY VAL A   -5  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWY PRO A   -4  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWY ARG A   -3  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWY GLY A   -2  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWY SER A   -1  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWY HIS A    0  UNP  P0C0U4              EXPRESSION TAG                 
SEQADV 4IWY MSE A    1  UNP  P0C0U4              EXPRESSION TAG                 
SEQRES   1 A  320  MSE GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  320  LEU VAL PRO ARG GLY SER HIS MSE 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 MSE 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 MSE 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 MSE 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 MSE 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 MSE          
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 MSE 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 MSE ILE ARG TRP ILE GLU ARG HIS ALA THR THR          
SEQRES  25 A  320  GLU TYR CYS LEU LYS THR GLY GLY                              
MODRES 4IWY MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 4IWY MSE A   39  MET  SELENOMETHIONINE                                   
MODRES 4IWY MSE A   82  MET  SELENOMETHIONINE                                   
MODRES 4IWY MSE A  104  MET  SELENOMETHIONINE                                   
MODRES 4IWY MSE A  132  MET  SELENOMETHIONINE                                   
MODRES 4IWY MSE A  240  MET  SELENOMETHIONINE                                   
MODRES 4IWY MSE A  259  MET  SELENOMETHIONINE                                   
MODRES 4IWY MSE A  282  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A  39       8                                                       
HET    MSE  A  82       8                                                       
HET    MSE  A 104       8                                                       
HET    MSE  A 132       8                                                       
HET    MSE  A 240       8                                                       
HET    MSE  A 259       8                                                       
HET    MSE  A 282       8                                                       
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                                                       
HET    SO4  A 408       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     GLU GLUTAMIC ACID                                                    
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  MSE    8(C5 H11 N O2 SE)                                            
FORMUL   2  ADP    C10 H15 N5 O10 P2                                            
FORMUL   3  GLU    C5 H9 N O4                                                   
FORMUL   4  SO4    6(O4 S 2-)                                                   
FORMUL  10  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  GLY A   84  1                                  16    
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  MSE 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  ALA A  241  1                                  16    
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  MSE 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 CYS A 186  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  LEU A 257   N  LEU A 250           
LINK         C   HIS A   0                 N   MSE A   1     1555   1555  1.33  
LINK         C   MSE A   1                 N   LYS A   2     1555   1555  1.33  
LINK         C   TYR A  38                 N   MSE A  39     1555   1555  1.33  
LINK         C   MSE A  39                 N   ASN A  40     1555   1555  1.33  
LINK         C   GLU A  81                 N   MSE A  82     1555   1555  1.34  
LINK         C   MSE A  82                 N   LEU A  83     1555   1555  1.33  
LINK         C   SER A 103                 N   MSE A 104     1555   1555  1.33  
LINK         C   MSE A 104                 N   GLN A 105     1555   1555  1.33  
LINK         C   ASP A 131                 N   MSE A 132     1555   1555  1.33  
LINK         C   MSE A 132                 N   VAL A 133     1555   1555  1.33  
LINK         C   THR A 239                 N   MSE A 240     1555   1555  1.33  
LINK         C   MSE A 240                 N   ALA A 241     1555   1555  1.33  
LINK         C   VAL A 258                 N   MSE A 259     1555   1555  1.32  
LINK         C   MSE A 259                 N   GLU A 260     1555   1555  1.33  
LINK         C   LYS A 281                 N   MSE A 282     1555   1555  1.33  
LINK         C   MSE A 282                 N   ILE A 283     1555   1555  1.33  
SITE     1 AC1 15 LYS A 141  GLU A 178  TYR A 179  ILE A 180                    
SITE     2 AC1 15 LYS A 181  ASP A 187  ARG A 203  PHE A 210                    
SITE     3 AC1 15 ARG A 211  SER A 212  ASN A 213  ASP A 248                    
SITE     4 AC1 15 LEU A 250  MSE A 259  GLU A 260                               
SITE     1 AC2  7 ARG A  78  VAL A  92  ARG A  96  ARG A 102                    
SITE     2 AC2  7 GLN A 105  LEU A 106  ARG A 109                               
SITE     1 AC3  6 ARG A 189  LEU A 214  ASN A 262  PRO A 265                    
SITE     2 AC3  6 GLY A 266  SO4 A 405                                          
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  4 TYR A  13  LEU A 214  GLY A 269  SO4 A 403                    
SITE     1 AC6  2 LYS A  51  ARG A  53                                          
SITE     1 AC7  3 SER A  46  SER A  47  LYS A  54                               
SITE     1 AC8  2 ARG A 284  ARG A 288                                          
CRYST1  129.030  129.030  171.238  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      0.007750  0.004475  0.000000        0.00000                         
SCALE2      0.000000  0.008949  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005840        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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