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Database: PDB
Entry: 4TZZ
LinkDB: 4TZZ
Original site: 4TZZ 
HEADER    RIBOSOMAL PROTEIN/RNA                   11-JUL-14   4TZZ              
TITLE     CO-CRYSTALS OF THE TERNARY COMPLEX CONTAINING A T-BOX STEM I RNA, ITS 
TITLE    2 COGNATE TRNAGLY, AND B. SUBTILIS YBXF PROTEIN, TREATED BY REMOVING   
TITLE    3 LITHIUM SULFATE AND INCREASING PEG3350 CONCENTRATION FROM 20% TO 45% 
TITLE    4 POST CRYSTALLIZATION                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBOSOME-ASSOCIATED PROTEIN L7AE-LIKE;                     
COMPND   3 CHAIN: A, D, G, J;                                                   
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: ENGINEERED TRNAGLY;                                        
COMPND   7 CHAIN: B, E, H, K;                                                   
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: T-BOX STEM I RNA;                                          
COMPND  11 CHAIN: C, F, I, L;                                                   
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 GENE: RPLGB, YBAB, YBXF, BSU01090;                                   
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 SYNTHETIC: YES;                                                      
SOURCE  11 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE  12 ORGANISM_TAXID: 1423;                                                
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 SYNTHETIC: YES;                                                      
SOURCE  15 ORGANISM_SCIENTIFIC: OCEANOBACILLUS IHEYENSIS;                       
SOURCE  16 ORGANISM_TAXID: 182710                                               
KEYWDS    RNA, RIBOSWITCH, TRNA, T-BOX                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.ZHANG,A.R.FERRE-D'AMARE                                             
REVDAT   2   24-SEP-14 4TZZ    1       JRNL                                     
REVDAT   1   10-SEP-14 4TZZ    0                                                
JRNL        AUTH   J.ZHANG,A.R.FERRE-D'AMARE                                    
JRNL        TITL   DRAMATIC IMPROVEMENT OF CRYSTALS OF LARGE RNAS BY CATION     
JRNL        TITL 2 REPLACEMENT AND DEHYDRATION.                                 
JRNL        REF    STRUCTURE                     V.  22  1363 2014              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   25185828                                                     
JRNL        DOI    10.1016/J.STR.2014.07.011                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.64 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.2_1309)                   
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) : 3.64                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 70.61                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.370                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 24051                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.220                           
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.269                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.110                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1230                            
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 70.6270 -  7.5665    0.80     2415   152  0.1983 0.2439        
REMARK   3     2  7.5665 -  6.0068    0.83     2474   142  0.2118 0.2844        
REMARK   3     3  6.0068 -  5.2478    0.83     2525   119  0.1966 0.2797        
REMARK   3     4  5.2478 -  4.7681    0.85     2583   128  0.2286 0.2510        
REMARK   3     5  4.7681 -  4.4264    0.85     2502   144  0.2257 0.2844        
REMARK   3     6  4.4264 -  4.1655    0.85     2566   144  0.2350 0.2938        
REMARK   3     7  4.1655 -  3.9569    0.86     2614   128  0.2371 0.2854        
REMARK   3     8  3.9569 -  3.7846    0.87     2601   148  0.2559 0.2906        
REMARK   3     9  3.7846 -  3.6400    0.84     2541   125  0.2831 0.3135        
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)     : 0.500            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.760           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :  0.002          19077                                  
REMARK   3   ANGLE     :  0.493          29338                                  
REMARK   3   CHIRALITY :  0.023           3930                                  
REMARK   3   PLANARITY :  0.002           1060                                  
REMARK   3   DIHEDRAL  : 16.705           9142                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 4TZZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUL-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000202588.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-NOV-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5-7.0                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : KOHZU HLD8-24 MONOCHROMATOR        
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24059                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.640                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 70.610                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 84.5                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : 0.07400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.64                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.77                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 4LCK                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.22                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50 MM BIS-TRIS (HCL) PH 6.5, 300 MM      
REMARK 280  LI2SO4, AND 20% (W/V) PEG3350, VAPOR DIFFUSION, HANGING DROP,       
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000      130.36650            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, F, E                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, I, H                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J, L, K                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     1                                                      
REMARK 465     GLY D     1                                                      
REMARK 465     GLY G     1                                                      
REMARK 465     GLY J     1                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASP A   4    CG   OD1  OD2                                       
REMARK 470     LYS A   5    CG   CD   CE   NZ                                   
REMARK 470     LYS A  10    CG   CD   CE   NZ                                   
REMARK 470     LYS A  17    CG   CD   CE   NZ                                   
REMARK 470     LYS A  21    CD   CE   NZ                                        
REMARK 470     LYS A  29    CG   CD   CE   NZ                                   
REMARK 470     LYS A  35    CD   CE   NZ                                        
REMARK 470     ASP A  38    CG   OD1  OD2                                       
REMARK 470     LEU A  48    CG   CD1  CD2                                       
REMARK 470     ASP A  51    CG   OD1  OD2                                       
REMARK 470     GLU A  60    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  63    CD   CE   NZ                                        
REMARK 470     LYS A  64    CD   CE   NZ                                        
REMARK 470     LYS A  67    CD   CE   NZ                                        
REMARK 470     ILE A  71    CG1  CG2  CD1                                       
REMARK 470     GLU A  72    CG   CD   OE1  OE2                                  
REMARK 470     ILE A  81    CG1  CG2  CD1                                       
REMARK 470       U B  16    N1   C2   O2   N3   C4   O4   C5                    
REMARK 470       U B  16    C6                                                  
REMARK 470       U B  46    N1   C2   O2   N3   C4   O4   C5                    
REMARK 470       U B  46    C6                                                  
REMARK 470     ASP D   4    CG   OD1  OD2                                       
REMARK 470     LYS D   5    CG   CD   CE   NZ                                   
REMARK 470     LYS D  10    CG   CD   CE   NZ                                   
REMARK 470     LYS D  17    CG   CD   CE   NZ                                   
REMARK 470     LYS D  21    CD   CE   NZ                                        
REMARK 470     LYS D  29    CG   CD   CE   NZ                                   
REMARK 470     LYS D  35    CD   CE   NZ                                        
REMARK 470     ASP D  38    CG   OD1  OD2                                       
REMARK 470     LEU D  48    CG   CD1  CD2                                       
REMARK 470     ASP D  51    CG   OD1  OD2                                       
REMARK 470     GLU D  60    CG   CD   OE1  OE2                                  
REMARK 470     LYS D  63    CD   CE   NZ                                        
REMARK 470     LYS D  64    CD   CE   NZ                                        
REMARK 470     LYS D  67    CD   CE   NZ                                        
REMARK 470     ILE D  71    CG1  CG2  CD1                                       
REMARK 470     GLU D  72    CG   CD   OE1  OE2                                  
REMARK 470     ILE D  81    CG1  CG2  CD1                                       
REMARK 470       U E  16    N1   C2   O2   N3   C4   O4   C5                    
REMARK 470       U E  16    C6                                                  
REMARK 470       U E  46    N1   C2   O2   N3   C4   O4   C5                    
REMARK 470       U E  46    C6                                                  
REMARK 470     ASP G   4    CG   OD1  OD2                                       
REMARK 470     LYS G   5    CG   CD   CE   NZ                                   
REMARK 470     LYS G  10    CG   CD   CE   NZ                                   
REMARK 470     LYS G  17    CG   CD   CE   NZ                                   
REMARK 470     LYS G  21    CD   CE   NZ                                        
REMARK 470     LYS G  29    CG   CD   CE   NZ                                   
REMARK 470     LYS G  35    CD   CE   NZ                                        
REMARK 470     ASP G  38    CG   OD1  OD2                                       
REMARK 470     LEU G  48    CG   CD1  CD2                                       
REMARK 470     ASP G  51    CG   OD1  OD2                                       
REMARK 470     GLU G  60    CG   CD   OE1  OE2                                  
REMARK 470     LYS G  63    CD   CE   NZ                                        
REMARK 470     LYS G  64    CD   CE   NZ                                        
REMARK 470     LYS G  67    CD   CE   NZ                                        
REMARK 470     ILE G  71    CG1  CG2  CD1                                       
REMARK 470     GLU G  72    CG   CD   OE1  OE2                                  
REMARK 470     ILE G  81    CG1  CG2  CD1                                       
REMARK 470       U H  16    N1   C2   O2   N3   C4   O4   C5                    
REMARK 470       U H  16    C6                                                  
REMARK 470       U H  46    N1   C2   O2   N3   C4   O4   C5                    
REMARK 470       U H  46    C6                                                  
REMARK 470     ASP J   4    CG   OD1  OD2                                       
REMARK 470     LYS J   5    CG   CD   CE   NZ                                   
REMARK 470     LYS J  10    CG   CD   CE   NZ                                   
REMARK 470     LYS J  17    CG   CD   CE   NZ                                   
REMARK 470     LYS J  21    CD   CE   NZ                                        
REMARK 470     LYS J  29    CG   CD   CE   NZ                                   
REMARK 470     LYS J  35    CD   CE   NZ                                        
REMARK 470     ASP J  38    CG   OD1  OD2                                       
REMARK 470     LEU J  48    CG   CD1  CD2                                       
REMARK 470     ASP J  51    CG   OD1  OD2                                       
REMARK 470     GLU J  60    CG   CD   OE1  OE2                                  
REMARK 470     LYS J  63    CD   CE   NZ                                        
REMARK 470     LYS J  64    CD   CE   NZ                                        
REMARK 470     LYS J  67    CD   CE   NZ                                        
REMARK 470     ILE J  71    CG1  CG2  CD1                                       
REMARK 470     GLU J  72    CG   CD   OE1  OE2                                  
REMARK 470     ILE J  81    CG1  CG2  CD1                                       
REMARK 470       U K  16    N1   C2   O2   N3   C4   O4   C5                    
REMARK 470       U K  16    C6                                                  
REMARK 470       C K  34    N4                                                  
REMARK 470       U K  46    N1   C2   O2   N3   C4   O4   C5                    
REMARK 470       U K  46    C6                                                  
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   O2'    U K    32     OP2    C K    34              1.95            
REMARK 500   O2'    U B    32     OP2    C B    34              2.13            
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      U H  31   C3' -  O3' -  P   ANGL. DEV. =   8.3 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    GLN A   8     -130.23   -110.36                                   
REMARK 500    ALA A   9      160.30     66.79                                   
REMARK 500    LYS A  10      -70.03    -79.73                                   
REMARK 500    LYS A  24        3.52    -69.63                                   
REMARK 500    ARG A  25       10.60   -141.65                                   
REMARK 500    ASP A  36       27.81    -74.93                                   
REMARK 500    GLN D   8     -134.49   -107.46                                   
REMARK 500    ALA D   9      161.88     63.85                                   
REMARK 500    LYS D  24        2.53    -68.00                                   
REMARK 500    ASP D  36       28.52    -73.25                                   
REMARK 500    GLN G   8     -133.97   -107.22                                   
REMARK 500    ALA G   9      158.19     64.85                                   
REMARK 500    LYS G  10      -71.07    -82.79                                   
REMARK 500    ASP G  36       26.91    -76.57                                   
REMARK 500    GLN J   8     -134.31   -109.15                                   
REMARK 500    ALA J   9      156.16     63.50                                   
REMARK 500    LYS J  10      -72.78    -85.32                                   
REMARK 500    ARG J  25       10.69   -143.05                                   
REMARK 500    ASP J  36       27.87    -75.06                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 202  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   C C 102   O3'                                                    
REMARK 620 2   C C 102   O2'  64.6                                              
REMARK 620 3   A F  39   OP2  31.9  58.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 101  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A E   9   OP2                                                    
REMARK 620 2   U E  12   OP2 147.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 104  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   U E  46   O2'                                                    
REMARK 620 2   C E  47   OP1  79.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 102  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A E  74   OP1                                                    
REMARK 620 2   A E  74   OP2  55.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG F 201  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   C F 102   O3'                                                    
REMARK 620 2   C F 102   O2'  59.7                                              
REMARK 620 3   A C  39   OP2  19.8  55.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG H 105  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   U H   8   O3'                                                    
REMARK 620 2   A H   9   OP1  62.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG L 201  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A I  39   OP2                                                    
REMARK 620 2   C L 102   O3'  66.1                                              
REMARK 620 3   C L 102   O2' 135.0  69.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG I 201  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   C I 102   O3'                                                    
REMARK 620 2   C I 102   O2'  75.4                                              
REMARK 620 3   A L  39   OP2  51.7  27.2                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG C 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG E 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG E 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG E 103                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG E 104                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG E 105                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG E 106                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG F 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG F 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG F 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG H 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG H 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG H 103                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG H 104                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG H 105                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 203                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG I 205                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG L 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG L 202                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4LCK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4TZP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4TZV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4TZW   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4TZX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4TZY   RELATED DB: PDB                                   
DBREF  4TZZ A    2    82  UNP    P46350   RXL7_BACSU       2     82             
DBREF  4TZZ B    5    79  PDB    4TZZ     4TZZ             5     79             
DBREF  4TZZ C    1   102  PDB    4TZZ     4TZZ             1    102             
DBREF  4TZZ D    2    82  UNP    P46350   RXL7_BACSU       2     82             
DBREF  4TZZ E    5    79  PDB    4TZZ     4TZZ             5     79             
DBREF  4TZZ F    1   102  PDB    4TZZ     4TZZ             1    102             
DBREF  4TZZ G    2    82  UNP    P46350   RXL7_BACSU       2     82             
DBREF  4TZZ H    5    79  PDB    4TZZ     4TZZ             5     79             
DBREF  4TZZ I    1   102  PDB    4TZZ     4TZZ             1    102             
DBREF  4TZZ J    2    82  UNP    P46350   RXL7_BACSU       2     82             
DBREF  4TZZ K    5    79  PDB    4TZZ     4TZZ             5     79             
DBREF  4TZZ L    1   102  PDB    4TZZ     4TZZ             1    102             
SEQADV 4TZZ GLY A    1  UNP  P46350              EXPRESSION TAG                 
SEQADV 4TZZ GLY D    1  UNP  P46350              EXPRESSION TAG                 
SEQADV 4TZZ GLY G    1  UNP  P46350              EXPRESSION TAG                 
SEQADV 4TZZ GLY J    1  UNP  P46350              EXPRESSION TAG                 
SEQRES   1 A   82  GLY SER TYR ASP LYS VAL SER GLN ALA LYS SER ILE ILE          
SEQRES   2 A   82  ILE GLY THR LYS GLN THR VAL LYS ALA LEU LYS ARG GLY          
SEQRES   3 A   82  SER VAL LYS GLU VAL VAL VAL ALA LYS ASP ALA ASP PRO          
SEQRES   4 A   82  ILE LEU THR SER SER VAL VAL SER LEU ALA GLU ASP GLN          
SEQRES   5 A   82  GLY ILE SER VAL SER MSE VAL GLU SER MSE LYS LYS LEU          
SEQRES   6 A   82  GLY LYS ALA CYS GLY ILE GLU VAL GLY ALA ALA ALA VAL          
SEQRES   7 A   82  ALA ILE ILE LEU                                              
SEQRES   1 B   75    G   A   G   U   A   G   U   U   C   A   G   U   G          
SEQRES   2 B   75    G   U   A   G   A   A   C   A   C   C   A   C   C          
SEQRES   3 B   75    U   U   G   C   C   A   A   G   G   U   G   G   G          
SEQRES   4 B   75    G   G   U   C   G   C   G   G   G   U   U   C   G          
SEQRES   5 B   75    A   A   U   C   C   C   G   U   C   U   C   G   G          
SEQRES   6 B   75    G   C   G   A   A   A   G   C   C   C                      
SEQRES   1 C  102    G   G   G   U   G   C   G   A   U   G   A   G   A          
SEQRES   2 C  102    A   G   A   A   G   A   G   U   A   U   U   A   A          
SEQRES   3 C  102    G   G   A   U   U   U   A   C   U   A   U   G   A          
SEQRES   4 C  102    U   U   A   G   C   G   A   C   U   C   U   A   G          
SEQRES   5 C  102    G   A   U   A   G   U   G   A   A   A   G   C   U          
SEQRES   6 C  102    A   G   A   G   G   A   U   A   G   U   A   A   C          
SEQRES   7 C  102    C   U   U   A   A   G   A   A   G   G   C   A   C          
SEQRES   8 C  102    U   U   C   G   A   G   C   A   C   C   C                  
SEQRES   1 D   82  GLY SER TYR ASP LYS VAL SER GLN ALA LYS SER ILE ILE          
SEQRES   2 D   82  ILE GLY THR LYS GLN THR VAL LYS ALA LEU LYS ARG GLY          
SEQRES   3 D   82  SER VAL LYS GLU VAL VAL VAL ALA LYS ASP ALA ASP PRO          
SEQRES   4 D   82  ILE LEU THR SER SER VAL VAL SER LEU ALA GLU ASP GLN          
SEQRES   5 D   82  GLY ILE SER VAL SER MSE VAL GLU SER MSE LYS LYS LEU          
SEQRES   6 D   82  GLY LYS ALA CYS GLY ILE GLU VAL GLY ALA ALA ALA VAL          
SEQRES   7 D   82  ALA ILE ILE LEU                                              
SEQRES   1 E   75    G   A   G   U   A   G   U   U   C   A   G   U   G          
SEQRES   2 E   75    G   U   A   G   A   A   C   A   C   C   A   C   C          
SEQRES   3 E   75    U   U   G   C   C   A   A   G   G   U   G   G   G          
SEQRES   4 E   75    G   G   U   C   G   C   G   G   G   U   U   C   G          
SEQRES   5 E   75    A   A   U   C   C   C   G   U   C   U   C   G   G          
SEQRES   6 E   75    G   C   G   A   A   A   G   C   C   C                      
SEQRES   1 F  102    G   G   G   U   G   C   G   A   U   G   A   G   A          
SEQRES   2 F  102    A   G   A   A   G   A   G   U   A   U   U   A   A          
SEQRES   3 F  102    G   G   A   U   U   U   A   C   U   A   U   G   A          
SEQRES   4 F  102    U   U   A   G   C   G   A   C   U   C   U   A   G          
SEQRES   5 F  102    G   A   U   A   G   U   G   A   A   A   G   C   U          
SEQRES   6 F  102    A   G   A   G   G   A   U   A   G   U   A   A   C          
SEQRES   7 F  102    C   U   U   A   A   G   A   A   G   G   C   A   C          
SEQRES   8 F  102    U   U   C   G   A   G   C   A   C   C   C                  
SEQRES   1 G   82  GLY SER TYR ASP LYS VAL SER GLN ALA LYS SER ILE ILE          
SEQRES   2 G   82  ILE GLY THR LYS GLN THR VAL LYS ALA LEU LYS ARG GLY          
SEQRES   3 G   82  SER VAL LYS GLU VAL VAL VAL ALA LYS ASP ALA ASP PRO          
SEQRES   4 G   82  ILE LEU THR SER SER VAL VAL SER LEU ALA GLU ASP GLN          
SEQRES   5 G   82  GLY ILE SER VAL SER MSE VAL GLU SER MSE LYS LYS LEU          
SEQRES   6 G   82  GLY LYS ALA CYS GLY ILE GLU VAL GLY ALA ALA ALA VAL          
SEQRES   7 G   82  ALA ILE ILE LEU                                              
SEQRES   1 H   75    G   A   G   U   A   G   U   U   C   A   G   U   G          
SEQRES   2 H   75    G   U   A   G   A   A   C   A   C   C   A   C   C          
SEQRES   3 H   75    U   U   G   C   C   A   A   G   G   U   G   G   G          
SEQRES   4 H   75    G   G   U   C   G   C   G   G   G   U   U   C   G          
SEQRES   5 H   75    A   A   U   C   C   C   G   U   C   U   C   G   G          
SEQRES   6 H   75    G   C   G   A   A   A   G   C   C   C                      
SEQRES   1 I  102    G   G   G   U   G   C   G   A   U   G   A   G   A          
SEQRES   2 I  102    A   G   A   A   G   A   G   U   A   U   U   A   A          
SEQRES   3 I  102    G   G   A   U   U   U   A   C   U   A   U   G   A          
SEQRES   4 I  102    U   U   A   G   C   G   A   C   U   C   U   A   G          
SEQRES   5 I  102    G   A   U   A   G   U   G   A   A   A   G   C   U          
SEQRES   6 I  102    A   G   A   G   G   A   U   A   G   U   A   A   C          
SEQRES   7 I  102    C   U   U   A   A   G   A   A   G   G   C   A   C          
SEQRES   8 I  102    U   U   C   G   A   G   C   A   C   C   C                  
SEQRES   1 J   82  GLY SER TYR ASP LYS VAL SER GLN ALA LYS SER ILE ILE          
SEQRES   2 J   82  ILE GLY THR LYS GLN THR VAL LYS ALA LEU LYS ARG GLY          
SEQRES   3 J   82  SER VAL LYS GLU VAL VAL VAL ALA LYS ASP ALA ASP PRO          
SEQRES   4 J   82  ILE LEU THR SER SER VAL VAL SER LEU ALA GLU ASP GLN          
SEQRES   5 J   82  GLY ILE SER VAL SER MSE VAL GLU SER MSE LYS LYS LEU          
SEQRES   6 J   82  GLY LYS ALA CYS GLY ILE GLU VAL GLY ALA ALA ALA VAL          
SEQRES   7 J   82  ALA ILE ILE LEU                                              
SEQRES   1 K   75    G   A   G   U   A   G   U   U   C   A   G   U   G          
SEQRES   2 K   75    G   U   A   G   A   A   C   A   C   C   A   C   C          
SEQRES   3 K   75    U   U   G   C   C   A   A   G   G   U   G   G   G          
SEQRES   4 K   75    G   G   U   C   G   C   G   G   G   U   U   C   G          
SEQRES   5 K   75    A   A   U   C   C   C   G   U   C   U   C   G   G          
SEQRES   6 K   75    G   C   G   A   A   A   G   C   C   C                      
SEQRES   1 L  102    G   G   G   U   G   C   G   A   U   G   A   G   A          
SEQRES   2 L  102    A   G   A   A   G   A   G   U   A   U   U   A   A          
SEQRES   3 L  102    G   G   A   U   U   U   A   C   U   A   U   G   A          
SEQRES   4 L  102    U   U   A   G   C   G   A   C   U   C   U   A   G          
SEQRES   5 L  102    G   A   U   A   G   U   G   A   A   A   G   C   U          
SEQRES   6 L  102    A   G   A   G   G   A   U   A   G   U   A   A   C          
SEQRES   7 L  102    C   U   U   A   A   G   A   A   G   G   C   A   C          
SEQRES   8 L  102    U   U   C   G   A   G   C   A   C   C   C                  
MODRES 4TZZ MSE A   58  MET  MODIFIED RESIDUE                                   
MODRES 4TZZ MSE A   62  MET  MODIFIED RESIDUE                                   
MODRES 4TZZ MSE D   58  MET  MODIFIED RESIDUE                                   
MODRES 4TZZ MSE D   62  MET  MODIFIED RESIDUE                                   
MODRES 4TZZ MSE G   58  MET  MODIFIED RESIDUE                                   
MODRES 4TZZ MSE G   62  MET  MODIFIED RESIDUE                                   
MODRES 4TZZ MSE J   58  MET  MODIFIED RESIDUE                                   
MODRES 4TZZ MSE J   62  MET  MODIFIED RESIDUE                                   
HET    MSE  A  58       8                                                       
HET    MSE  A  62       8                                                       
HET    MSE  D  58       8                                                       
HET    MSE  D  62       8                                                       
HET    MSE  G  58       8                                                       
HET    MSE  G  62       8                                                       
HET    MSE  J  58       8                                                       
HET    MSE  J  62       8                                                       
HET     MG  B 101       1                                                       
HET     MG  B 102       1                                                       
HET     MG  C 201       1                                                       
HET     MG  C 202       1                                                       
HET     MG  C 203       1                                                       
HET     MG  C 204       1                                                       
HET     MG  E 101       1                                                       
HET     MG  E 102       1                                                       
HET     MG  E 103       1                                                       
HET     MG  E 104       1                                                       
HET     MG  E 105       1                                                       
HET     MG  E 106       1                                                       
HET     MG  E 107       1                                                       
HET     MG  F 201       1                                                       
HET     MG  F 202       1                                                       
HET     MG  F 203       1                                                       
HET     MG  F 204       1                                                       
HET     MG  H 101       1                                                       
HET     MG  H 102       1                                                       
HET     MG  H 103       1                                                       
HET     MG  H 104       1                                                       
HET     MG  H 105       1                                                       
HET     MG  I 201       1                                                       
HET     MG  I 202       1                                                       
HET     MG  I 203       1                                                       
HET     MG  I 204       1                                                       
HET     MG  I 205       1                                                       
HET     MG  L 201       1                                                       
HET     MG  L 202       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   1  MSE    8(C5 H11 N O2 SE)                                            
FORMUL  13   MG    29(MG 2+)                                                    
HELIX    1 AA1 SER A    2  SER A    7  1                                   6    
HELIX    2 AA2 GLY A   15  LYS A   24  1                                  10    
HELIX    3 AA3 ASP A   38  GLY A   53  1                                  16    
HELIX    4 AA4 SER A   61  GLY A   70  1                                  10    
HELIX    5 AA5 TYR D    3  GLN D    8  1                                   6    
HELIX    6 AA6 GLY D   15  LYS D   24  1                                  10    
HELIX    7 AA7 ASP D   38  GLY D   53  1                                  16    
HELIX    8 AA8 SER D   61  CYS D   69  1                                   9    
HELIX    9 AA9 TYR G    3  GLN G    8  1                                   6    
HELIX   10 AB1 GLY G   15  LYS G   24  1                                  10    
HELIX   11 AB2 ASP G   38  GLY G   53  1                                  16    
HELIX   12 AB3 SER G   61  CYS G   69  1                                   9    
HELIX   13 AB4 TYR J    3  SER J    7  1                                   5    
HELIX   14 AB5 GLY J   15  LYS J   24  1                                  10    
HELIX   15 AB6 ASP J   38  GLY J   53  1                                  16    
HELIX   16 AB7 SER J   61  GLY J   70  1                                  10    
SHEET    1 AA1 4 ILE A  13  ILE A  14  0                                        
SHEET    2 AA1 4 ALA A  77  ILE A  80 -1  O  ALA A  79   N  ILE A  13           
SHEET    3 AA1 4 GLU A  30  ALA A  34 -1  N  GLU A  30   O  ILE A  80           
SHEET    4 AA1 4 VAL A  56  VAL A  59  1  O  VAL A  59   N  VAL A  33           
SHEET    1 AA2 3 ILE D  13  ILE D  14  0                                        
SHEET    2 AA2 3 ALA D  77  ALA D  79 -1  O  ALA D  79   N  ILE D  13           
SHEET    3 AA2 3 VAL D  32  VAL D  33 -1  N  VAL D  32   O  VAL D  78           
SHEET    1 AA3 4 ILE G  12  ILE G  14  0                                        
SHEET    2 AA3 4 ALA G  77  ILE G  80 -1  O  ALA G  79   N  ILE G  13           
SHEET    3 AA3 4 GLU G  30  ALA G  34 -1  N  VAL G  32   O  VAL G  78           
SHEET    4 AA3 4 SER G  55  VAL G  59  1  O  SER G  57   N  VAL G  31           
SHEET    1 AA4 4 ILE J  12  ILE J  14  0                                        
SHEET    2 AA4 4 ALA J  77  ILE J  80 -1  O  ALA J  79   N  ILE J  13           
SHEET    3 AA4 4 GLU J  30  ALA J  34 -1  N  VAL J  32   O  VAL J  78           
SHEET    4 AA4 4 SER J  55  VAL J  59  1  O  SER J  55   N  VAL J  31           
LINK         C   SER A  57                 N   MSE A  58     1555   1555  1.33  
LINK         C   MSE A  58                 N   VAL A  59     1555   1555  1.33  
LINK         C   SER A  61                 N   MSE A  62     1555   1555  1.33  
LINK         C   MSE A  62                 N   LYS A  63     1555   1555  1.33  
LINK         OP2   A C  11                MG    MG C 203     1555   1555  2.38  
LINK         O3'   C C 102                MG    MG C 202     1555   1555  2.79  
LINK         O2'   C C 102                MG    MG C 202     1555   1555  2.25  
LINK         C   SER D  57                 N   MSE D  58     1555   1555  1.33  
LINK         C   MSE D  58                 N   VAL D  59     1555   1555  1.33  
LINK         C   SER D  61                 N   MSE D  62     1555   1555  1.33  
LINK         C   MSE D  62                 N   LYS D  63     1555   1555  1.33  
LINK         OP2   A E   9                MG    MG E 101     1555   1555  2.99  
LINK         OP2   U E  12                MG    MG E 101     1555   1555  2.49  
LINK         OP2   A E  14                MG    MG E 106     1555   1555  2.29  
LINK         O6    G E  44                MG    MG E 103     1555   1555  2.81  
LINK         O2'   U E  46                MG    MG E 104     1555   1555  2.82  
LINK         OP1   C E  47                MG    MG E 104     1555   1555  2.59  
LINK         OP1   A E  74                MG    MG E 102     1555   1555  2.43  
LINK         OP2   A E  74                MG    MG E 102     1555   1555  2.96  
LINK         O4    U F  37                MG    MG F 203     1555   1555  2.33  
LINK         O3'   C F 102                MG    MG F 201     1555   1555  2.86  
LINK         O2'   C F 102                MG    MG F 201     1555   1555  2.60  
LINK         C   SER G  57                 N   MSE G  58     1555   1555  1.33  
LINK         C   MSE G  58                 N   VAL G  59     1555   1555  1.33  
LINK         C   SER G  61                 N   MSE G  62     1555   1555  1.33  
LINK         C   MSE G  62                 N   LYS G  63     1555   1555  1.33  
LINK         O3'   U H   8                MG    MG H 105     1555   1555  2.60  
LINK         OP1   A H   9                MG    MG H 105     1555   1555  2.17  
LINK         OP2   A H  37                MG    MG H 102     1555   1555  2.01  
LINK         OP2   A I  11                MG    MG I 203     1555   1555  2.86  
LINK         OP2   A I  39                MG    MG L 201     1555   1555  2.41  
LINK         OP2   A I  83                MG    MG I 202     1555   1555  2.47  
LINK         O3'   C I 102                MG    MG I 201     1555   1555  2.19  
LINK         O2'   C I 102                MG    MG I 201     1555   1555  2.27  
LINK         C   SER J  57                 N   MSE J  58     1555   1555  1.33  
LINK         C   MSE J  58                 N   VAL J  59     1555   1555  1.33  
LINK         C   SER J  61                 N   MSE J  62     1555   1555  1.33  
LINK         C   MSE J  62                 N   LYS J  63     1555   1555  1.33  
LINK         OP2   A L  11                MG    MG L 202     1555   1555  2.81  
LINK         O3'   C L 102                MG    MG L 201     1555   1555  2.33  
LINK         O2'   C L 102                MG    MG L 201     1555   1555  2.46  
LINK         OP2   A C  39                MG    MG F 201     1555   1455  2.00  
LINK         OP2   A F  39                MG    MG C 202     1555   1556  2.94  
LINK         OP2   A L  39                MG    MG I 201     1555   1454  2.97  
SITE     1 AC1  1   G C  15                                                     
SITE     1 AC2  2   C C 102    A F  39                                          
SITE     1 AC3  2   A C  11    G C  12                                          
SITE     1 AC4  3   A E   9    U E  11    U E  12                               
SITE     1 AC5  2   G E  72    A E  74                                          
SITE     1 AC6  2   G E  43    G E  44                                          
SITE     1 AC7  4   U E  46    C E  47    C E  49    G E  50                    
SITE     1 AC8  1   G E  72                                                     
SITE     1 AC9  2   U E   8    A E  14                                          
SITE     1 AD1  3   A C  39    A C  46    C F 102                               
SITE     1 AD2  1   G F  59                                                     
SITE     1 AD3  3   A F  36    U F  37    A F  71                               
SITE     1 AD4  1   G H  41                                                     
SITE     1 AD5  1   A H  37                                                     
SITE     1 AD6  1   G H  52                                                     
SITE     1 AD7  1   C H  27                                                     
SITE     1 AD8  2   U H   8    A H   9                                          
SITE     1 AD9  3   C I 102    A L  39    A L  46                               
SITE     1 AE1  2   A I  83    G I  84                                          
SITE     1 AE2  2   A I  11    G I  12                                          
SITE     1 AE3  1   G I  67                                                     
SITE     1 AE4  3   A I  39    A I  46    C L 102                               
SITE     1 AE5  2   A L  11    G L  12                                          
CRYST1   70.641  260.733   70.698  90.00  92.80  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014156  0.000000  0.000692        0.00000                         
SCALE2      0.000000  0.003835  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014162        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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