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Database: PDB
Entry: 2Y0U
LinkDB: 2Y0U
Original site: 2Y0U 
HEADER    RIBOSOME                                07-DEC-10   2Y0U              
TITLE     THE CRYSTAL STRUCTURE OF EF-TU AND A9C-TRNA-TRP BOUND TO A            
TITLE    2 NEAR-COGNATE CODON ON THE 70S RIBOSOME                               
SPLIT      2Y0U 2Y0V 2Y0W 2Y0X                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 16S RRNA;                                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 OTHER_DETAILS: CHAIN A (16S RNA) HAS E.COLI NUMBERING, BASED ON A    
COMPND   5  STRUCTURAL ALIGNMENT WITH THE CORRESPONDING E. COLI STRUCTURE IN    
COMPND   6  2AVY.;                                                              
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: 30S RIBOSOMAL PROTEIN S2;                                  
COMPND   9 CHAIN: B;                                                            
COMPND  10 MOL_ID: 3;                                                           
COMPND  11 MOLECULE: 30S RIBOSOMAL PROTEIN S3;                                  
COMPND  12 CHAIN: C;                                                            
COMPND  13 MOL_ID: 4;                                                           
COMPND  14 MOLECULE: 30S RIBOSOMAL PROTEIN S4;                                  
COMPND  15 CHAIN: D;                                                            
COMPND  16 MOL_ID: 5;                                                           
COMPND  17 MOLECULE: 30S RIBOSOMAL PROTEIN S5;                                  
COMPND  18 CHAIN: E;                                                            
COMPND  19 MOL_ID: 6;                                                           
COMPND  20 MOLECULE: 30S RIBOSOMAL PROTEIN S6;                                  
COMPND  21 CHAIN: F;                                                            
COMPND  22 MOL_ID: 7;                                                           
COMPND  23 MOLECULE: 30S RIBOSOMAL PROTEIN S7;                                  
COMPND  24 CHAIN: G;                                                            
COMPND  25 MOL_ID: 8;                                                           
COMPND  26 MOLECULE: 30S RIBOSOMAL PROTEIN S8;                                  
COMPND  27 CHAIN: H;                                                            
COMPND  28 MOL_ID: 9;                                                           
COMPND  29 MOLECULE: 30S RIBOSOMAL PROTEIN S9;                                  
COMPND  30 CHAIN: I;                                                            
COMPND  31 MOL_ID: 10;                                                          
COMPND  32 MOLECULE: 30S RIBOSOMAL PROTEIN S10;                                 
COMPND  33 CHAIN: J;                                                            
COMPND  34 MOL_ID: 11;                                                          
COMPND  35 MOLECULE: 30S RIBOSOMAL PROTEIN S11;                                 
COMPND  36 CHAIN: K;                                                            
COMPND  37 MOL_ID: 12;                                                          
COMPND  38 MOLECULE: 30S RIBOSOMAL PROTEIN S12;                                 
COMPND  39 CHAIN: L;                                                            
COMPND  40 MOL_ID: 13;                                                          
COMPND  41 MOLECULE: 30S RIBOSOMAL PROTEIN S13;                                 
COMPND  42 CHAIN: M;                                                            
COMPND  43 MOL_ID: 14;                                                          
COMPND  44 MOLECULE: 30S RIBOSOMAL PROTEIN S14;                                 
COMPND  45 CHAIN: N;                                                            
COMPND  46 MOL_ID: 15;                                                          
COMPND  47 MOLECULE: 30S RIBOSOMAL PROTEIN S15;                                 
COMPND  48 CHAIN: O;                                                            
COMPND  49 MOL_ID: 16;                                                          
COMPND  50 MOLECULE: 30S RIBOSOMAL PROTEIN S16;                                 
COMPND  51 CHAIN: P;                                                            
COMPND  52 MOL_ID: 17;                                                          
COMPND  53 MOLECULE: 30S RIBOSOMAL PROTEIN S17;                                 
COMPND  54 CHAIN: Q;                                                            
COMPND  55 MOL_ID: 18;                                                          
COMPND  56 MOLECULE: 30S RIBOSOMAL PROTEIN S18;                                 
COMPND  57 CHAIN: R;                                                            
COMPND  58 MOL_ID: 19;                                                          
COMPND  59 MOLECULE: 30S RIBOSOMAL PROTEIN S19;                                 
COMPND  60 CHAIN: S;                                                            
COMPND  61 MOL_ID: 20;                                                          
COMPND  62 MOLECULE: 30S RIBOSOMAL PROTEIN S20;                                 
COMPND  63 CHAIN: T;                                                            
COMPND  64 MOL_ID: 21;                                                          
COMPND  65 MOLECULE: 30S RIBOSOMAL PROTEIN THX;                                 
COMPND  66 CHAIN: U;                                                            
COMPND  67 MOL_ID: 22;                                                          
COMPND  68 MOLECULE: E-SITE TRNA PHE OR P-SITE TRNA PHE;                        
COMPND  69 CHAIN: V, W;                                                         
COMPND  70 MOL_ID: 23;                                                          
COMPND  71 MOLECULE: MRNA;                                                      
COMPND  72 CHAIN: X;                                                            
COMPND  73 MOL_ID: 24;                                                          
COMPND  74 MOLECULE: A-SITE TRNA A9C TRP-TRNA TRP;                              
COMPND  75 CHAIN: Y;                                                            
COMPND  76 OTHER_DETAILS: MUTATION AT A9C;                                      
COMPND  77 MOL_ID: 25;                                                          
COMPND  78 MOLECULE: ELONGATION FACTOR TU;                                      
COMPND  79 CHAIN: Z                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE   3 ORGANISM_TAXID: 300852;                                              
SOURCE   4 STRAIN: HB8 - MRC - MSAW1;                                           
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE   7 ORGANISM_TAXID: 300852;                                              
SOURCE   8 STRAIN: HB8 - MRC - MSAW1;                                           
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  11 ORGANISM_TAXID: 300852;                                              
SOURCE  12 STRAIN: HB8 - MRC - MSAW1;                                           
SOURCE  13 MOL_ID: 4;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  15 ORGANISM_TAXID: 300852;                                              
SOURCE  16 STRAIN: HB8 - MRC - MSAW1;                                           
SOURCE  17 MOL_ID: 5;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  19 ORGANISM_TAXID: 300852;                                              
SOURCE  20 STRAIN: HB8 - MRC - MSAW1;                                           
SOURCE  21 MOL_ID: 6;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  23 ORGANISM_TAXID: 300852;                                              
SOURCE  24 STRAIN: HB8 - MRC - MSAW1;                                           
SOURCE  25 MOL_ID: 7;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  27 ORGANISM_TAXID: 300852;                                              
SOURCE  28 STRAIN: HB8 - MRC - MSAW1;                                           
SOURCE  29 MOL_ID: 8;                                                           
SOURCE  30 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  31 ORGANISM_TAXID: 300852;                                              
SOURCE  32 STRAIN: HB8 - MRC - MSAW1;                                           
SOURCE  33 MOL_ID: 9;                                                           
SOURCE  34 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  35 ORGANISM_TAXID: 300852;                                              
SOURCE  36 STRAIN: HB8 - MRC - MSAW1;                                           
SOURCE  37 MOL_ID: 10;                                                          
SOURCE  38 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  39 ORGANISM_TAXID: 300852;                                              
SOURCE  40 STRAIN: HB8 - MRC - MSAW1;                                           
SOURCE  41 MOL_ID: 11;                                                          
SOURCE  42 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  43 ORGANISM_TAXID: 300852;                                              
SOURCE  44 STRAIN: HB8 - MRC - MSAW1;                                           
SOURCE  45 MOL_ID: 12;                                                          
SOURCE  46 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  47 ORGANISM_TAXID: 300852;                                              
SOURCE  48 STRAIN: HB8 - MRC - MSAW1;                                           
SOURCE  49 MOL_ID: 13;                                                          
SOURCE  50 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  51 ORGANISM_TAXID: 300852;                                              
SOURCE  52 STRAIN: HB8 - MRC - MSAW1;                                           
SOURCE  53 MOL_ID: 14;                                                          
SOURCE  54 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  55 ORGANISM_TAXID: 300852;                                              
SOURCE  56 STRAIN: HB8 - MRC - MSAW1;                                           
SOURCE  57 MOL_ID: 15;                                                          
SOURCE  58 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  59 ORGANISM_TAXID: 300852;                                              
SOURCE  60 STRAIN: HB8 - MRC - MSAW1;                                           
SOURCE  61 MOL_ID: 16;                                                          
SOURCE  62 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  63 ORGANISM_TAXID: 300852;                                              
SOURCE  64 STRAIN: HB8 - MRC - MSAW1;                                           
SOURCE  65 MOL_ID: 17;                                                          
SOURCE  66 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  67 ORGANISM_TAXID: 300852;                                              
SOURCE  68 STRAIN: HB8 - MRC - MSAW1;                                           
SOURCE  69 MOL_ID: 18;                                                          
SOURCE  70 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  71 ORGANISM_TAXID: 300852;                                              
SOURCE  72 STRAIN: HB8 - MRC - MSAW1;                                           
SOURCE  73 MOL_ID: 19;                                                          
SOURCE  74 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  75 ORGANISM_TAXID: 300852;                                              
SOURCE  76 STRAIN: HB8 - MRC - MSAW1;                                           
SOURCE  77 MOL_ID: 20;                                                          
SOURCE  78 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  79 ORGANISM_TAXID: 300852;                                              
SOURCE  80 STRAIN: HB8 - MRC - MSAW1;                                           
SOURCE  81 MOL_ID: 21;                                                          
SOURCE  82 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  83 ORGANISM_TAXID: 300852;                                              
SOURCE  84 STRAIN: HB8 - MRC - MSAW1;                                           
SOURCE  85 MOL_ID: 22;                                                          
SOURCE  86 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  87 ORGANISM_TAXID: 83333;                                               
SOURCE  88 STRAIN: K-12;                                                        
SOURCE  89 MOL_ID: 23;                                                          
SOURCE  90 SYNTHETIC: YES;                                                      
SOURCE  91 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  92 ORGANISM_TAXID: 562;                                                 
SOURCE  93 MOL_ID: 24;                                                          
SOURCE  94 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  95 ORGANISM_TAXID: 83333;                                               
SOURCE  96 STRAIN: K-12;                                                        
SOURCE  97 MOL_ID: 25;                                                          
SOURCE  98 ORGANISM_SCIENTIFIC: THERMUS THERMOPHILUS;                           
SOURCE  99 ORGANISM_TAXID: 300852;                                              
SOURCE 100 STRAIN: HB8                                                          
KEYWDS    RIBOSOME                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.M.SCHMEING,R.M.VOORHEES,V.RAMAKRISHNAN                              
REVDAT   2   27-APR-11 2Y0U    1       JRNL                                     
REVDAT   1   09-MAR-11 2Y0U    0                                                
JRNL        AUTH   T.M.SCHMEING,R.M.VOORHEES,A.C.KELLEY,                        
JRNL        AUTH 2 V.RAMAKRISHNAN                                               
JRNL        TITL   HOW MUTATIONS IN TRNA DISTANT FROM THE ANTICODON             
JRNL        TITL 2 AFFECT THE FIDELITY OF DECODING.                             
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  18   432 2011              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   21378964                                                     
JRNL        DOI    10.1038/NSMB.2003                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.2                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.1                            
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.0                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0                              
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 14988406                       
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 1090696                        
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : INHERITED FROM 2WRN             
REMARK   3   R VALUE            (WORKING SET) : 0.243                           
REMARK   3   FREE R VALUE                     : 0.267                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 54315                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.001                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.29                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.5                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 168155                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.333                        
REMARK   3   BIN FREE R VALUE                    : 0.346                        
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.9                          
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 8615                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.004                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 22129                                   
REMARK   3   NUCLEIC ACID ATOMS       : 37693                                   
REMARK   3   HETEROGEN ATOMS          : 89                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 52.2                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 77.9                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.25                                                 
REMARK   3    B22 (A**2) : -0.84                                                
REMARK   3    B33 (A**2) : -4.41                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : -10.64                                               
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.42                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.61                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.46                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.64                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.2                             
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 29.0                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.51                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) :  NULL ;  NULL                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) :  NULL ;  NULL                
REMARK   3   SIDE-CHAIN BOND              (A**2) :  NULL ;  NULL                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) :  NULL ;  NULL                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.3                                                  
REMARK   3   BSOL        : 32.0063                                              
REMARK   3                                                                      
REMARK   3  NCS MODEL : RESTRAINTS                                              
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) :  NULL ;  NULL                
REMARK   3   GROUP  1  B-FACTOR           (A**2) :  NULL ;  NULL                
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : KIR.PAR                                        
REMARK   3  PARAMETER FILE  2  : GDP.PAR                                        
REMARK   3  PARAMETER FILE  3  : DNA-RNA_TRP_MODS.PARAM                         
REMARK   3  PARAMETER FILE  4  : PROTEIN_REP_TRP.PARAM                          
REMARK   3  PARAMETER FILE  5  : ION.PARAM                                      
REMARK   3  TOPOLOGY FILE  1   : KIR.TOP                                        
REMARK   3  TOPOLOGY FILE  2   : GDP.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : DNA-RNA_TRP_MODS.TOP                           
REMARK   3  TOPOLOGY FILE  4   : PROTEIN_REP_TRP.TOP                            
REMARK   3  TOPOLOGY FILE  5   : ION.TOP                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: THIS IS PART 1 OF A 4 PART                
REMARK   3    DEPOSITION                                                        
REMARK   4                                                                      
REMARK   4 2Y0U COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-DEC-10.                  
REMARK 100 THE PDBE ID CODE IS EBI-44521.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-APR-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.93950                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 1090696                            
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.10                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.7                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 5.0                                
REMARK 200  R MERGE                    (I) : 0.02                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.48                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.4                                
REMARK 200  R MERGE FOR SHELL          (I) : 1.03                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.69                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 2WRN                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES PH 6.3, 60-100 MM             
REMARK 280  KCL, 50 MM SUCROSE, 1% GLYCEROL, 5.2% (W/V) PEG20K                  
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      134.25000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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: 26-MERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: K, L, M, N, O, P, Q, R, S,            
REMARK 350                    AND CHAINS: T, U, V, W, X, Y, Z                   
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       U A     0                                                      
REMARK 465       U A     1                                                      
REMARK 465       U A     2                                                      
REMARK 465       G A     3                                                      
REMARK 465       U A     4                                                      
REMARK 465       C A  1538                                                      
REMARK 465       C A  1539                                                      
REMARK 465       U A  1540                                                      
REMARK 465       U A  1541                                                      
REMARK 465       U A  1542                                                      
REMARK 465       C A  1543                                                      
REMARK 465       U A  1544                                                      
REMARK 465     MET B     1                                                      
REMARK 465     PRO B     2                                                      
REMARK 465     VAL B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     ILE B     5                                                      
REMARK 465     THR B     6                                                      
REMARK 465     GLU B   241                                                      
REMARK 465     ALA B   242                                                      
REMARK 465     GLU B   243                                                      
REMARK 465     ALA B   244                                                      
REMARK 465     THR B   245                                                      
REMARK 465     GLU B   246                                                      
REMARK 465     THR B   247                                                      
REMARK 465     PRO B   248                                                      
REMARK 465     GLU B   249                                                      
REMARK 465     GLY B   250                                                      
REMARK 465     GLU B   251                                                      
REMARK 465     SER B   252                                                      
REMARK 465     GLU B   253                                                      
REMARK 465     VAL B   254                                                      
REMARK 465     GLU B   255                                                      
REMARK 465     ALA B   256                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ILE C   208                                                      
REMARK 465     GLY C   209                                                      
REMARK 465     GLY C   210                                                      
REMARK 465     GLN C   211                                                      
REMARK 465     LYS C   212                                                      
REMARK 465     PRO C   213                                                      
REMARK 465     LYS C   214                                                      
REMARK 465     ALA C   215                                                      
REMARK 465     ARG C   216                                                      
REMARK 465     PRO C   217                                                      
REMARK 465     GLU C   218                                                      
REMARK 465     LEU C   219                                                      
REMARK 465     PRO C   220                                                      
REMARK 465     LYS C   221                                                      
REMARK 465     ALA C   222                                                      
REMARK 465     GLU C   223                                                      
REMARK 465     GLU C   224                                                      
REMARK 465     ARG C   225                                                      
REMARK 465     PRO C   226                                                      
REMARK 465     ARG C   227                                                      
REMARK 465     ARG C   228                                                      
REMARK 465     ARG C   229                                                      
REMARK 465     ARG C   230                                                      
REMARK 465     PRO C   231                                                      
REMARK 465     ALA C   232                                                      
REMARK 465     VAL C   233                                                      
REMARK 465     ARG C   234                                                      
REMARK 465     VAL C   235                                                      
REMARK 465     LYS C   236                                                      
REMARK 465     LYS C   237                                                      
REMARK 465     GLU C   238                                                      
REMARK 465     GLU C   239                                                      
REMARK 465     MET D     1                                                      
REMARK 465     MET E     1                                                      
REMARK 465     PRO E     2                                                      
REMARK 465     GLU E     3                                                      
REMARK 465     THR E     4                                                      
REMARK 465     GLU E   155                                                      
REMARK 465     ALA E   156                                                      
REMARK 465     HIS E   157                                                      
REMARK 465     ALA E   158                                                      
REMARK 465     GLN E   159                                                      
REMARK 465     ALA E   160                                                      
REMARK 465     GLN E   161                                                      
REMARK 465     GLY E   162                                                      
REMARK 465     MET G     1                                                      
REMARK 465     MET I     1                                                      
REMARK 465     MET J     1                                                      
REMARK 465     PRO J     2                                                      
REMARK 465     VAL J   101                                                      
REMARK 465     GLY J   102                                                      
REMARK 465     GLY J   103                                                      
REMARK 465     GLY J   104                                                      
REMARK 465     ARG J   105                                                      
REMARK 465     MET K     1                                                      
REMARK 465     ALA K     2                                                      
REMARK 465     LYS K     3                                                      
REMARK 465     LYS K     4                                                      
REMARK 465     PRO K     5                                                      
REMARK 465     SER K     6                                                      
REMARK 465     LYS K     7                                                      
REMARK 465     LYS K     8                                                      
REMARK 465     LYS K     9                                                      
REMARK 465     VAL K    10                                                      
REMARK 465     MET L     1                                                      
REMARK 465     VAL L     2                                                      
REMARK 465     ALA L     3                                                      
REMARK 465     LEU L     4                                                      
REMARK 465     ALA L   129                                                      
REMARK 465     LYS L   130                                                      
REMARK 465     THR L   131                                                      
REMARK 465     ALA L   132                                                      
REMARK 465     ALA L   133                                                      
REMARK 465     LYS L   134                                                      
REMARK 465     LYS L   135                                                      
REMARK 465     MET M     1                                                      
REMARK 465     LYS M   126                                                      
REMARK 465     MET N     1                                                      
REMARK 465     MET O     1                                                      
REMARK 465     ALA P    84                                                      
REMARK 465     ARG P    85                                                      
REMARK 465     GLU P    86                                                      
REMARK 465     GLY P    87                                                      
REMARK 465     ALA P    88                                                      
REMARK 465     MET Q     1                                                      
REMARK 465     ARG Q   101                                                      
REMARK 465     GLY Q   102                                                      
REMARK 465     GLY Q   103                                                      
REMARK 465     LYS Q   104                                                      
REMARK 465     ALA Q   105                                                      
REMARK 465     MET R     1                                                      
REMARK 465     SER R     2                                                      
REMARK 465     THR R     3                                                      
REMARK 465     LYS R     4                                                      
REMARK 465     ASN R     5                                                      
REMARK 465     ALA R     6                                                      
REMARK 465     LYS R     7                                                      
REMARK 465     PRO R     8                                                      
REMARK 465     LYS R     9                                                      
REMARK 465     LYS R    10                                                      
REMARK 465     GLU R    11                                                      
REMARK 465     ALA R    12                                                      
REMARK 465     GLN R    13                                                      
REMARK 465     ARG R    14                                                      
REMARK 465     ARG R    15                                                      
REMARK 465     PRO R    16                                                      
REMARK 465     SER R    17                                                      
REMARK 465     ARG R    18                                                      
REMARK 465     MET S     1                                                      
REMARK 465     PRO S     2                                                      
REMARK 465     ARG S     3                                                      
REMARK 465     GLY S    82                                                      
REMARK 465     HIS S    83                                                      
REMARK 465     GLY S    84                                                      
REMARK 465     LYS S    85                                                      
REMARK 465     GLU S    86                                                      
REMARK 465     ALA S    87                                                      
REMARK 465     LYS S    88                                                      
REMARK 465     ALA S    89                                                      
REMARK 465     THR S    90                                                      
REMARK 465     LYS S    91                                                      
REMARK 465     LYS S    92                                                      
REMARK 465     LYS S    93                                                      
REMARK 465     MET T     1                                                      
REMARK 465     ALA T     2                                                      
REMARK 465     GLN T     3                                                      
REMARK 465     LYS T     4                                                      
REMARK 465     LYS T     5                                                      
REMARK 465     PRO T     6                                                      
REMARK 465     LYS T     7                                                      
REMARK 465     MET U     1                                                      
REMARK 465     LYS U    26                                                      
REMARK 465     LYS U    27                                                      
REMARK 465       G X     1                                                      
REMARK 465       G X     2                                                      
REMARK 465       C X     3                                                      
REMARK 465       A X     4                                                      
REMARK 465       A X     5                                                      
REMARK 465       G X     6                                                      
REMARK 465       G X     7                                                      
REMARK 465       A X     8                                                      
REMARK 465       G X     9                                                      
REMARK 465       G X    10                                                      
REMARK 465     GLU Z    43                                                      
REMARK 465     VAL Z    44                                                      
REMARK 465     LYS Z    45                                                      
REMARK 465     ASP Z    46                                                      
REMARK 465     TYR Z    47                                                      
REMARK 465     GLY Z    48                                                      
REMARK 465     ASP Z    49                                                      
REMARK 465     ILE Z    50                                                      
REMARK 465     ASP Z    51                                                      
REMARK 465     LYS Z    52                                                      
REMARK 465     ALA Z    53                                                      
REMARK 465     PRO Z    54                                                      
REMARK 465     GLU Z    55                                                      
REMARK 465     GLU Z    56                                                      
REMARK 465     ARG Z    57                                                      
REMARK 465     ALA Z    58                                                      
REMARK 465     ARG Z    59                                                      
REMARK 465     GLY Z    60                                                      
REMARK 465     ILE Z    61                                                      
REMARK 465     THR Z    62                                                      
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       U A   5    P    OP1  OP2                                       
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   O3'    A Y    76     C    TRP Y    77              1.33            
REMARK 500   NH1  ARG B   178     O    GLY H    71              2.12            
REMARK 500   O    ALA G   145     N    ALA G   147              2.15            
REMARK 500   O    GLU S    43     N    VAL S    45              2.16            
REMARK 500   OP1    G A   542     NH2  ARG D    10              2.18            
REMARK 500   O2'    U A   961     O5'    C A   962              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500      G A 858   C5      G A 858   C6     -0.079                       
REMARK 500      A Y   1   P       A Y   1   OP3    -0.086                       
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      A A  60   C2' -  C3' -  O3' ANGL. DEV. =  10.3 DEGREES          
REMARK 500      A A 109   C2' -  C3' -  O3' ANGL. DEV. =  13.5 DEGREES          
REMARK 500      A A 243   C2' -  C3' -  O3' ANGL. DEV. =  14.2 DEGREES          
REMARK 500      G A 347   N9  -  C1' -  C2' ANGL. DEV. =  -8.0 DEGREES          
REMARK 500      C A 369   N1  -  C1' -  C2' ANGL. DEV. =  -7.4 DEGREES          
REMARK 500      C A 508   C2' -  C3' -  O3' ANGL. DEV. =  17.2 DEGREES          
REMARK 500      A A 687   C2' -  C3' -  O3' ANGL. DEV. =  14.5 DEGREES          
REMARK 500      U A 772   C5' -  C4' -  C3' ANGL. DEV. =  -9.7 DEGREES          
REMARK 500      A A 792   C2' -  C3' -  O3' ANGL. DEV. =  14.4 DEGREES          
REMARK 500      U A 961   N1  -  C1' -  C2' ANGL. DEV. =  -8.2 DEGREES          
REMARK 500      U A 982   C2' -  C3' -  O3' ANGL. DEV. =   9.7 DEGREES          
REMARK 500      C A 995   N1  -  C1' -  C2' ANGL. DEV. =  -6.7 DEGREES          
REMARK 500      U A1049   C2' -  C3' -  O3' ANGL. DEV. =  14.3 DEGREES          
REMARK 500      G A1050   N9  -  C1' -  C2' ANGL. DEV. =  -7.7 DEGREES          
REMARK 500      C A1054   N1  -  C1' -  C2' ANGL. DEV. =   8.5 DEGREES          
REMARK 500      A A1101   C2' -  C3' -  O3' ANGL. DEV. =  12.6 DEGREES          
REMARK 500      G A1181   N9  -  C1' -  C2' ANGL. DEV. =   8.1 DEGREES          
REMARK 500      A A1239   C2' -  C3' -  O3' ANGL. DEV. =  15.2 DEGREES          
REMARK 500      U A1498   C2' -  C3' -  O3' ANGL. DEV. =  19.3 DEGREES          
REMARK 500      A A1502   N9  -  C1' -  C2' ANGL. DEV. =   7.9 DEGREES          
REMARK 500      G A1504   C4' -  C3' -  O3' ANGL. DEV. =  13.1 DEGREES          
REMARK 500      G A1504   C2' -  C3' -  O3' ANGL. DEV. =  13.1 DEGREES          
REMARK 500      G A1505   O3' -  P   -  OP2 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    PRO B 232   C   -  N   -  CA  ANGL. DEV. =  11.0 DEGREES          
REMARK 500    PRO C 174   C   -  N   -  CA  ANGL. DEV. =   9.6 DEGREES          
REMARK 500    CYS D  12   CA  -  CB  -  SG  ANGL. DEV. =   6.9 DEGREES          
REMARK 500    PRO M 113   C   -  N   -  CA  ANGL. DEV. =   9.5 DEGREES          
REMARK 500    PRO N  14   C   -  N   -  CA  ANGL. DEV. =  11.3 DEGREES          
REMARK 500      A W  76   C4' -  C3' -  O3' ANGL. DEV. =  17.2 DEGREES          
REMARK 500      A W  76   C2' -  C3' -  O3' ANGL. DEV. =  11.4 DEGREES          
REMARK 500      C Y  69   C2' -  C3' -  O3' ANGL. DEV. =  13.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS B   8      -99.09    -91.21                                   
REMARK 500    GLU B   9      -30.14    -39.84                                   
REMARK 500    VAL B  15       57.48   -179.52                                   
REMARK 500    HIS B  16       40.77   -146.51                                   
REMARK 500    HIS B  19      170.95    178.37                                   
REMARK 500    GLU B  20      148.74     57.91                                   
REMARK 500    ARG B  23       14.36   -146.66                                   
REMARK 500    PRO B  26       -2.37    -45.87                                   
REMARK 500    ASP B  43       97.76    -67.35                                   
REMARK 500    LYS B  75      -38.11    -37.12                                   
REMARK 500    ALA B  77       -5.32   -154.21                                   
REMARK 500    ARG B  87       42.47    -71.94                                   
REMARK 500    ALA B  88      -18.98   -153.54                                   
REMARK 500    GLN B  95     -104.10    -82.04                                   
REMARK 500    LEU B 102      -54.26   -121.11                                   
REMARK 500    GLN B 110       -7.00    -54.55                                   
REMARK 500    GLU B 126       -7.93    -57.10                                   
REMARK 500    ILE B 127      -71.49    -48.51                                   
REMARK 500    ARG B 130      147.56     60.76                                   
REMARK 500    PRO B 131      169.70    -49.11                                   
REMARK 500    VAL B 136      -70.60   -117.73                                   
REMARK 500    PHE B 152      -43.05     62.39                                   
REMARK 500    ARG B 157      146.06   -178.47                                   
REMARK 500    VAL B 165      -94.85    -90.38                                   
REMARK 500    GLU B 170       36.04    -99.84                                   
REMARK 500    THR B 190       76.58    -37.79                                   
REMARK 500    ASP B 191      -11.19    168.68                                   
REMARK 500    ASN B 204      127.49    -36.24                                   
REMARK 500    ALA B 225      -13.43    -47.15                                   
REMARK 500    VAL B 230     -116.39   -158.66                                   
REMARK 500    PRO B 232     -175.83    -55.05                                   
REMARK 500    PRO B 234       67.32    -19.21                                   
REMARK 500    ALA B 237      -42.81    -26.00                                   
REMARK 500    LEU B 238      -32.34   -169.98                                   
REMARK 500    VAL B 239       71.81     32.74                                   
REMARK 500    ASN C   3      -84.68   -157.12                                   
REMARK 500    LYS C   4      113.26     75.92                                   
REMARK 500    LEU C  12      -63.39    -17.34                                   
REMARK 500    THR C  15      -68.96     49.36                                   
REMARK 500    LYS C  26      -52.56    -25.35                                   
REMARK 500    GLN C  28     -144.58    -96.15                                   
REMARK 500    TYR C  29      -77.88     74.82                                   
REMARK 500    ARG C  30      -35.43    -39.65                                   
REMARK 500    LYS C  45      -70.22    -58.98                                   
REMARK 500    LEU C  47       17.93     97.14                                   
REMARK 500    ALA C  50      -13.87     72.77                                   
REMARK 500    ALA C  61      108.71    160.56                                   
REMARK 500    ASP C  62       11.36     58.90                                   
REMARK 500    ALA C  65      -78.19    -70.29                                   
REMARK 500    VAL C  66       85.70     62.60                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     396 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500      U A  14         0.08    SIDE CHAIN                              
REMARK 500      G A  21         0.06    SIDE CHAIN                              
REMARK 500      G A 108         0.05    SIDE CHAIN                              
REMARK 500      G A 189G        0.05    SIDE CHAIN                              
REMARK 500      G A 189H        0.06    SIDE CHAIN                              
REMARK 500      A A 197         0.06    SIDE CHAIN                              
REMARK 500      G A 198         0.08    SIDE CHAIN                              
REMARK 500      C A 245         0.12    SIDE CHAIN                              
REMARK 500      A A 250         0.05    SIDE CHAIN                              
REMARK 500      G A 251         0.06    SIDE CHAIN                              
REMARK 500      U A 323         0.07    SIDE CHAIN                              
REMARK 500      G A 347         0.06    SIDE CHAIN                              
REMARK 500      C A 369         0.07    SIDE CHAIN                              
REMARK 500      G A 428         0.06    SIDE CHAIN                              
REMARK 500      U A 498         0.09    SIDE CHAIN                              
REMARK 500      G A 557         0.06    SIDE CHAIN                              
REMARK 500      G A 570         0.06    SIDE CHAIN                              
REMARK 500      U A 571         0.07    SIDE CHAIN                              
REMARK 500      A A 573         0.06    SIDE CHAIN                              
REMARK 500      C A 586         0.08    SIDE CHAIN                              
REMARK 500      U A 603         0.07    SIDE CHAIN                              
REMARK 500      G A 727         0.07    SIDE CHAIN                              
REMARK 500      G A 741         0.05    SIDE CHAIN                              
REMARK 500      G A 774         0.05    SIDE CHAIN                              
REMARK 500      G A 803         0.05    SIDE CHAIN                              
REMARK 500      C A 808         0.07    SIDE CHAIN                              
REMARK 500      G A 898         0.05    SIDE CHAIN                              
REMARK 500      U A 961         0.22    SIDE CHAIN                              
REMARK 500      A A 977         0.06    SIDE CHAIN                              
REMARK 500      C A 995         0.08    SIDE CHAIN                              
REMARK 500      G A1050         0.09    SIDE CHAIN                              
REMARK 500      A A1055         0.05    SIDE CHAIN                              
REMARK 500      G A1077         0.12    SIDE CHAIN                              
REMARK 500      C A1153         0.09    SIDE CHAIN                              
REMARK 500      A A1157         0.05    SIDE CHAIN                              
REMARK 500      G A1181         0.09    SIDE CHAIN                              
REMARK 500      U A1278         0.09    SIDE CHAIN                              
REMARK 500      U A1281         0.09    SIDE CHAIN                              
REMARK 500      G A1283         0.10    SIDE CHAIN                              
REMARK 500      A A1299         0.06    SIDE CHAIN                              
REMARK 500      U A1348         0.07    SIDE CHAIN                              
REMARK 500      C A1397         0.06    SIDE CHAIN                              
REMARK 500      A A1398         0.08    SIDE CHAIN                              
REMARK 500      U A1406         0.08    SIDE CHAIN                              
REMARK 500      U A1414         0.07    SIDE CHAIN                              
REMARK 500      U A1472         0.06    SIDE CHAIN                              
REMARK 500      G A1494         0.06    SIDE CHAIN                              
REMARK 500      U A1512         0.08    SIDE CHAIN                              
REMARK 500      G A1516         0.06    SIDE CHAIN                              
REMARK 500      U W  39         0.08    SIDE CHAIN                              
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                              ZN 1   4  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS D  12   SG                                                     
REMARK 620 2 CYS D  26   SG   80.0                                              
REMARK 620 3 CYS D  31   SG   77.2  70.8                                        
REMARK 620 4 CYS D   9   SG   93.8 147.4 139.3                                  
REMARK 620 5 CYS D  31   O    86.7 141.1  70.6  69.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN 1   5  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS N  24   SG                                                     
REMARK 620 2 CYS N  40   SG  103.5                                              
REMARK 620 3 CYS N  43   SG  113.2 101.1                                        
REMARK 620 4 CYS N  27   SG  104.5 112.9 120.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "LA" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  5-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 700                                                                      
REMARK 700 THE SHEETS PRESENTED AS "QA" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  5-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1IBK   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE THERMUS THERMOPHILUS 30S                           
REMARK 900  RIBOSOMAL SUBUNITIN COMPLEX WITH THE                                
REMARK 900  ANTIBIOTIC PAROMOMYCIN                                              
REMARK 900 RELATED ID: 1IBL   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE THERMUS THERMOPHILUS 30S                           
REMARK 900  RIBOSOMAL SUBUNITIN COMPLEX WITH A MESSENGER                        
REMARK 900  RNA FRAGMENT AND COGNATETRANSFER RNA ANTICODON                      
REMARK 900   STEM-LOOP BOUND AT THE A SITE ANDWITH                              
REMARK 900  THE ANTIBIOTIC PAROMOMYCIN                                          
REMARK 900 RELATED ID: 2UUC   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE THERMUS THERMOPHILUS 30S                           
REMARK 900  RIBOSOMAL SUBUNIT COMPLEXED WITH A VALINE-                          
REMARK 900  ASL WITH CMO5U IN POSITION 34 BOUND TO                              
REMARK 900  AN MRNA WITH A GUA-CODON IN THE A-SITE                              
REMARK 900   AND PAROMOMYCIN.                                                   
REMARK 900 RELATED ID: 2WDK   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE THERMUS THERMOPHILUS 70S                           
REMARK 900  RIBOSOME IN COMPLEX WITH MRNA, PAROMOMYCIN,                         
REMARK 900  ACYLATED A- AND P-SITE TRNAS, AND E-SITE                            
REMARK 900   TRNA. THIS FILE CONTAINS THE 30S SUBUNIT                           
REMARK 900  A-,P-, AND E-SITE TRNAS AND PAROMOMYCIN                             
REMARK 900  FOR MOLECULE I.                                                     
REMARK 900 RELATED ID: 2J02   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE THERMUS THERMOPHILUS 70S                           
REMARK 900  RIBOSOME COMPLEXED WITH MRNA, TRNA AND                              
REMARK 900  PAROMOMYCIN (PART 3 OF 4) THIS FILE                                 
REMARK 900  CONTAINS THE 30S SUBUNIT, MRNA, A-, P- AND                          
REMARK 900   E-SITE TRNAS AND PAROMOMYCIN FOR MOLECULE                          
REMARK 900   II.                                                                
REMARK 900 RELATED ID: 1J5E   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE THERMUS THERMOPHILUS 30S                           
REMARK 900  RIBOSOMAL SUBUNIT                                                   
REMARK 900 RELATED ID: 2WRQ   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF THE 70S RIBOSOME                           
REMARK 900  BOUND TO EF-TU AND TRNA (PART 3 OF 4).                              
REMARK 900 RELATED ID: 1HNX   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE THERMUS THERMOPHILUS 30S                           
REMARK 900  RIBOSOMAL SUBUNITIN COMPLEX WITH PACTAMYCIN                         
REMARK 900 RELATED ID: 2J00   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE THERMUS THERMOPHILUS 70S                           
REMARK 900  RIBOSOME COMPLEXED WITH MRNA, TRNA AND                              
REMARK 900  PAROMOMYCIN (PART 1 OF 4). THIS FILE                                
REMARK 900  CONTAINS THE 30S SUBUNIT, MRNA, A-, P- AND                          
REMARK 900   E-SITE TRNAS AND PAROMOMYCIN FOR MOLECULE I.                       
REMARK 900 RELATED ID: 2B9O   RELATED DB: PDB                                   
REMARK 900  30S RIBOSOMAL SUBUNIT, TRNAS AND MRNA FROM                          
REMARK 900  A CRYSTALSTRUCTURE OF THE WHOLE RIBOSOMAL                           
REMARK 900  COMPLEX WITH A STOP CODONIN THE A-SITE.                             
REMARK 900  THIS FILE CONTAINS THE 30S SUBUNIT, TRNASAND                        
REMARK 900   MRNA FROM A CRYSTAL STRUCTURE OF THE                               
REMARK 900  WHOLE RIBOSOMALCOMPLEX WITH A STOP CODON IN                         
REMARK 900   THE A-SITE AND IS DESCRIBEDIN REMARK 400.                          
REMARK 900 RELATED ID: 2X9T   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE 70S RIBOSOME BOUND TO                              
REMARK 900  RELEASE FACTOR 2 AND A SUBSTRATE ANALOG                             
REMARK 900  PROVIDES INSIGHTS INTO CATALYSIS OF PEPTIDE                         
REMARK 900  RELEASE                                                             
REMARK 900 RELATED ID: 2WH3   RELATED DB: PDB                                   
REMARK 900  INSIGHTS INTO TRANSLATIONAL TERMINATION FROM                        
REMARK 900  THE STRUCTURE OF RF2 BOUND TO THE RIBOSOME                          
REMARK 900 RELATED ID: 2UUB   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE THERMUS THERMOPHILUS 30S                           
REMARK 900  RIBOSOMAL SUBUNIT COMPLEXED WITH A VALINE-                          
REMARK 900  ASL WITH CMO5U IN POSITION 34 BOUND TO                              
REMARK 900  AN MRNA WITH A GUU-CODON IN THE A-SITE                              
REMARK 900   AND PAROMOMYCIN.                                                   
REMARK 900 RELATED ID: 1VOV   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF FIVE 70S RIBOSOMES FROM                        
REMARK 900   ESCHERICHIACOLI IN COMPLEX WITH PROTEIN Y.                         
REMARK 900  THIS FILE CONTAINS THE 30SSUBUNIT OF ONE                            
REMARK 900  70S RIBOSOME. THE ENTIRE CRYSTAL                                    
REMARK 900  STRUCTURECONTAINS FIVE 70S RIBOSOMES AND IS                         
REMARK 900  DESCRIBED IN REMARK 400.                                            
REMARK 900 RELATED ID: 1EMI   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF 16S RRNA IN THE REGION AROUND                          
REMARK 900   RIBOSOMALPROTEIN S8.                                               
REMARK 900 RELATED ID: 2XQD   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF EF-TU AND AMINOACYL-TRNA                           
REMARK 900   BOUND TO THE 70S RIBOSOME WITH A GTP ANALOG                        
REMARK 900 RELATED ID: 1PNX   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE WILD TYPE RIBOSOME                         
REMARK 900   FROM E. COLI,30S SUBUNIT OF 70S RIBOSOME                           
REMARK 900  . THIS FILE, 1PNX, CONTAINSONLY MOLECULES OF                        
REMARK 900   THE 30S RIBOSOMAL SUBUNIT. THE 50SSUBUNIT                          
REMARK 900  IS IN THE PDB FILE 1PNY.                                            
REMARK 900 RELATED ID: 2V46   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE RIBOSOME RECYCLING FACTOR                          
REMARK 900  BOUND TO THE THERMUS THERMOPHILUS 70S                               
REMARK 900  RIBOSOME WITH MRNA, ASL-PHE AND TRNA-FMET                           
REMARK 900   (PART 1 OF 4). THIS FILE CONTAINS THE                              
REMARK 900  30S SUBUNIT, MRNA, P-SITE ASL, E-SITE                               
REMARK 900  TRNA AND RRF FOR MOLECULE 1.                                        
REMARK 900 RELATED ID: 2VQF   RELATED DB: PDB                                   
REMARK 900  MODIFIED URIDINES WITH C5-METHYLENE                                 
REMARK 900  SUBSTITUENTS AT THE FIRST POSITION OF THE                           
REMARK 900  TRNA ANTICODON STABILIZE U-G WOBBLE PAIRING                         
REMARK 900   DURING DECODING                                                    
REMARK 900 RELATED ID: 2WH1   RELATED DB: PDB                                   
REMARK 900  INSIGHTS INTO TRANSLATIONAL TERMINATION FROM                        
REMARK 900  THE STRUCTURE OF RF2 BOUND TO THE RIBOSOME                          
REMARK 900 RELATED ID: 1N32   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE THERMUS THERMOPHILUS 30S                           
REMARK 900  RIBOSOMAL SUBUNITBOUND TO CODON AND NEAR-                           
REMARK 900  COGNATE TRANSFER RNA ANTICODONSTEM-LOOP                             
REMARK 900  MISMATCHED AT THE FIRST CODON POSITION AT                           
REMARK 900  THE ASITE WITH PAROMOMYCIN                                          
REMARK 900 RELATED ID: 2WRN   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF THE 70S RIBOSOME                           
REMARK 900  BOUND TO EF-TU AND TRNA (PART 1 OF 4).                              
REMARK 900 RELATED ID: 2F4V   RELATED DB: PDB                                   
REMARK 900  30S RIBOSOME + DESIGNER ANTIBIOTIC                                  
REMARK 900 RELATED ID: 2JL5   RELATED DB: PDB                                   
REMARK 900  INSIGHTS INTO TRANSLATIONAL TERMINATION FROM                        
REMARK 900  THE STRUCTURE OF RF2 BOUND TO THE RIBOSOME                          
REMARK 900   (PART 1 OF 4). THIS FILE CONTAINS THE                              
REMARK 900  30S SUBUNIT.                                                        
REMARK 900 RELATED ID: 1TWT   RELATED DB: PDB                                   
REMARK 900  MODEL STRUCTURE OF THE T. THERMOPHILUS 70S                          
REMARK 900  RIBOSOME, 30SSUBUNIT OF 70S ROBOSOME. THIS                          
REMARK 900  FILE, 1TWT, CONTAINS ONLYMOLECULES OF THE                           
REMARK 900  30S RIBOSOMAL SUBUNIT. THE 50S SUBUNIT ISIN                         
REMARK 900   THE PDB FILE 1TWV.                                                 
REMARK 900 RELATED ID: 1QZC   RELATED DB: PDB                                   
REMARK 900  COORDINATES OF S12, SH44, LH69 AND SRL                              
REMARK 900  SEPARATELY FITTEDINTO THE CRYO-EM MAP OF                            
REMARK 900  EF-TU TERNARY COMPLEX(GDP.KIRROMYCIN) BOUND                         
REMARK 900   70S RIBOSOME                                                       
REMARK 900 RELATED ID: 2UXD   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF AN EXTENDED TRNA                               
REMARK 900  ANTICODON STEM LOOP IN COMPLEX WITH ITS                             
REMARK 900  COGNATE MRNA CGGG IN THE CONTEXT OF THE                             
REMARK 900  THERMUS THERMOPHILUS 30S SUBUNIT.                                   
REMARK 900 RELATED ID: 1FKA   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF FUNCTIONALLY ACTIVATED SMALL                           
REMARK 900  RIBOSOMAL SUBUNITAT 3.3 A RESOLUTION                                
REMARK 900 RELATED ID: 1FJG   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE THERMUS THERMOPHILUS 30S                           
REMARK 900  RIBOSOMAL SUBUNITIN COMPLEX WITH THE                                
REMARK 900  ANTIBIOTICS STREPTOMYCIN, SPECTINOMYCIN,AND                         
REMARK 900  PAROMOMYCIN                                                         
REMARK 900 RELATED ID: 1N36   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE THERMUS THERMOPHILUS 30S                           
REMARK 900  RIBOSOMAL SUBUNITIN THE PRESENCE OF                                 
REMARK 900  CRYSTALLOGRAPHICALLY DISORDERED CODONAND NEAR-                      
REMARK 900  COGNATE TRANSFER RNA ANTICODON STEM-                                
REMARK 900  LOOPMISMATCHED AT THE SECOND CODON POSITION                         
REMARK 900 RELATED ID: 2UXC   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF AN EXTENDED TRNA                               
REMARK 900  ANTICODON STEM LOOP IN COMPLEX WITH ITS                             
REMARK 900  COGNATE MRNA UCGU IN THE CONTEXT OF THE                             
REMARK 900  THERMUS THERMOPHILUS 30S SUBUNIT.                                   
REMARK 900 RELATED ID: 1HNW   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE THERMUS THERMOPHILUS 30S                           
REMARK 900  RIBOSOMAL SUBUNITIN COMPLEX WITH TETRACYCLINE                       
REMARK 900 RELATED ID: 1L1U   RELATED DB: PDB                                   
REMARK 900  TERNARY COMPLEX DOCKED IN THE DECODING SITE                         
REMARK 900   OF THE 30SRIBOSOMAL SUBUNIT                                        
REMARK 900 RELATED ID: 1HR0   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF INITIATION FACTOR IF1                          
REMARK 900  BOUND TO THE 30SRIBOSOMAL SUBUNIT                                   
REMARK 900 RELATED ID: 2XUY   RELATED DB: PDB                                   
REMARK 900  TRNA TRANLOCATION ON THE 70S RIBOSOME: THE                          
REMARK 900  POST-TRANSLOCATIONAL TRANSLOCATION INTERMEDIATE                     
REMARK 900  TI(POST)                                                            
REMARK 900 RELATED ID: 2V48   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE RIBOSOME RECYCLING FACTOR                          
REMARK 900  BOUND TO THE THERMUS THERMOPHILUS 70S                               
REMARK 900  RIBOSOME WITH MRNA, ASL-PHE AND TRNA-FMET                           
REMARK 900   (PART 3 OF 4). THIS FILE CONTAINS THE                              
REMARK 900  30S SUBUNIT, MRNA, P-SITE ASL, E-SITE                               
REMARK 900  TRNA AND RRF FOR MOLECULE 2.                                        
REMARK 900 RELATED ID: 1XMQ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF T6A37-ASLLYSUUU AAA-                           
REMARK 900  MRNA BOUND TO THEDECODING CENTER                                    
REMARK 900 RELATED ID: 2B64   RELATED DB: PDB                                   
REMARK 900  30S RIBOSOMAL SUBUNIT, TRNAS, MRNA AND                              
REMARK 900  RELEASE FACTOR RF1FROM A CRYSTAL STRUCTURE                          
REMARK 900  OF THE WHOLE RIBOSOMAL COMPLEX.THIS FILE                            
REMARK 900  CONTAINS THE 30S SUBUNIT, TRNAS, MRNA                               
REMARK 900  ANDRELEASE FACTOR RF1 FROM A CRYSTAL                                
REMARK 900  STRUCTURE OF THE WHOLERIBOSOMAL COMPLEX". THE                       
REMARK 900   ENTIRE CRYSTAL STRUCTURE CONTAINSONE 70S                           
REMARK 900  RIBOSOME, TRNAS, MRNA AND RELEASE FACTOR RF1                        
REMARK 900   ANDIS DESCRIBED IN REMARK 400.                                     
REMARK 900 RELATED ID: 2B9M   RELATED DB: PDB                                   
REMARK 900  30S RIBOSOMAL SUBUNIT, TRNAS, MRNA AND                              
REMARK 900  RELEASE FACTOR RF2FROM A CRYSTAL STRUCTURE                          
REMARK 900  OF THE WHOLE RIBOSOMAL COMPLEX.THIS FILE                            
REMARK 900  CONTAINS THE 30S RIBOSOMAL SUBUNIT, TRNAS,                          
REMARK 900  MRNAAND RELEASE FACTOR RF2 FROM A CRYSTAL                           
REMARK 900  STRUCTURE OF THEWHOLE RIBOSOMAL COMPLEX". THE                       
REMARK 900   ENTIRE CRYSTAL STRUCTURECONTAINS ONE 70S                           
REMARK 900  RIBOSOME, TRNAS, MRNA AND RELEASE FACTORRF2                         
REMARK 900  AND IS DESCRIBED IN REMARK 400.                                     
REMARK 900 RELATED ID: 1PN8   RELATED DB: PDB                                   
REMARK 900  COORDINATES OF S12, L11 PROTEINS AND E-                             
REMARK 900  SITE TRNA FROM 70SCRYSTAL STRUCTURE SEPARATELY                      
REMARK 900   FITTED INTO THE CRYO-EM MAPOF E.COLI                               
REMARK 900  70S.EF-G.GDPNP COMPLEX. THE ATOMIC                                  
REMARK 900  COORDINATESORIGINALLY FROM THE E-SITE TRNA                          
REMARK 900  WERE FITTED IN THEPOSITION OF THE HYBRID P                          
REMARK 900  /E-SITE TRNA.                                                       
REMARK 900 RELATED ID: 2WDG   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE THERMUS THERMOPHILUS 70S                           
REMARK 900  RIBOSOME IN COMPLEX WITH MRNA, PAROMOMYCIN,                         
REMARK 900  ACYLATED A-SITE TRNA, DEACYLATED P-SITE                             
REMARK 900  TRNA, AND E-SITE TRNA. THIS FILE CONTAINS                           
REMARK 900   THE 30S SUBUNIT A-,P-, AND E-SITE                                  
REMARK 900  TRNAS AND PAROMOMYCIN FOR MOLECULE I.                               
REMARK 900 RELATED ID: 1XNR   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF AN INOSINE-CYTOSINE                            
REMARK 900  WOBBLE BASE PAIRIN THE CONTEXT OF THE                               
REMARK 900  DECODING CENTER                                                     
REMARK 900 RELATED ID: 1DV4   RELATED DB: PDB                                   
REMARK 900  PARTIAL STRUCTURE OF 16S RIBONUCLEIC ACID OF                        
REMARK 900   THE SMALL RIBOSOMAL SUBUNIT FROM THERMUS                           
REMARK 900  THERMOPHILUS                                                        
REMARK 900 RELATED ID: 1HNZ   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE THERMUS THERMOPHILUS 30S                           
REMARK 900  RIBOSOMAL SUBUNITIN COMPLEX WITH HYGROMYCIN B                       
REMARK 900 RELATED ID: 1RSS   RELATED DB: PDB                                   
REMARK 900  RIBOSOMAL PROTEIN S7 FROM THERMUS THERMOPHILUS                      
REMARK 900 RELATED ID: 2WDH   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE THERMUS THERMOPHILUS 70S                           
REMARK 900  RIBOSOME IN COMPLEX WITH MRNA, PAROMOMYCIN,                         
REMARK 900  ACYLATED A-SITE TRNA, DEACYLATED P-SITE                             
REMARK 900  TRNA, AND E-SITE TRNA. THIS FILE CONTAINS                           
REMARK 900   THE 30S SUBUNIT A-,P-, AND E-SITE                                  
REMARK 900  TRNAS AND PAROMOMYCIN FOR MOLECULE II.                              
REMARK 900 RELATED ID: 1JGQ   RELATED DB: PDB                                   
REMARK 900  THE PATH OF MESSENGER RNA THROUGH THE                               
REMARK 900  RIBOSOME. THIS FILE,1JGQ, CONTAINS THE 30S                          
REMARK 900  RIBOSOME SUBUNIT, THREE TRNA, ANDMRNA                               
REMARK 900  MOLECULES. 50S RIBOSOME SUBUNIT IS IN THE                           
REMARK 900  FILE 1GIY                                                           
REMARK 900 RELATED ID: 1I94   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURES OF THE SMALL RIBOSOMAL                           
REMARK 900  SUBUNIT WITHTETRACYCLINE, EDEINE AND IF3                            
REMARK 900 RELATED ID: 1I96   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE 30S RIBOSOMAL                              
REMARK 900  SUBUNIT FROM THERMUSTHERMOPHILUS IN COMPLEX                         
REMARK 900  WITH THE TRANSLATION INITIATIONFACTOR IF3 (C-                       
REMARK 900  TERMINAL DOMAIN)                                                    
REMARK 900 RELATED ID: 2XSY   RELATED DB: PDB                                   
REMARK 900  TRNA TRANLOCATION ON THE 70S RIBOSOME: THE                          
REMARK 900  PRE-TRANSLOCATIONAL TRANSLOCATION INTERMEDIATE                      
REMARK 900  TI(PRE)                                                             
REMARK 900 RELATED ID: 2UU9   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE THERMUS THERMOPHILUS 30S                           
REMARK 900  RIBOSOMAL SUBUNIT COMPLEXED WITH A VALINE-                          
REMARK 900  ASL WITH CMO5U IN POSITION 34 BOUND TO                              
REMARK 900  AN MRNA WITH A GUG-CODON IN THE A-SITE                              
REMARK 900   AND PAROMOMYCIN.                                                   
REMARK 900 RELATED ID: 1PN7   RELATED DB: PDB                                   
REMARK 900  COORDINATES OF S12, L11 PROTEINS AND P-                             
REMARK 900  TRNA, FROM THE 70S X-RAY STRUCTURE ALIGNED                          
REMARK 900   TO THE 70S CRYO-EM MAP OF E.                                       
REMARK 900  COLIRIBOSOME                                                        
REMARK 900 RELATED ID: 1EG0   RELATED DB: PDB                                   
REMARK 900  FITTING OF COMPONENTS WITH KNOWN STRUCTURE                          
REMARK 900  INTO AN 11.5 A CRYO-EM MAP OF THE E                                 
REMARK 900  .COLI 70S RIBOSOME                                                  
REMARK 900 RELATED ID: 1IBM   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE THERMUS THERMOPHILUS 30S                           
REMARK 900  RIBOSOMAL SUBUNITIN COMPLEX WITH A MESSENGER                        
REMARK 900  RNA FRAGMENT AND COGNATETRANSFER RNA ANTICODON                      
REMARK 900   STEM-LOOP BOUND AT THE A SITE                                      
REMARK 900 RELATED ID: 2UXB   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF AN EXTENDED TRNA                               
REMARK 900  ANTICODON STEM LOOP IN COMPLEX WITH ITS                             
REMARK 900  COGNATE MRNA GGGU IN THE CONTEXT OF THE                             
REMARK 900  THERMUS THERMOPHILUS 30S SUBUNIT.                                   
REMARK 900 RELATED ID: 2VQE   RELATED DB: PDB                                   
REMARK 900  MODIFIED URIDINES WITH C5-METHYLENE                                 
REMARK 900  SUBSTITUENTS AT THE FIRST POSITION OF THE                           
REMARK 900  TRNA ANTICODON STABILIZE U-G WOBBLE PAIRING                         
REMARK 900   DURING DECODING                                                    
REMARK 900 RELATED ID: 1G1X   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF RIBOSOMAL PROTEINS S15, S6, S18                        
REMARK 900  , AND 16SRIBOSOMAL RNA                                              
REMARK 900 RELATED ID: 1HA3   RELATED DB: PDB                                   
REMARK 900  ELONGATION FACTOR TU IN COMPLEX WITH AURODOX                        
REMARK 900 RELATED ID: 1I95   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE 30S RIBOSOMAL                              
REMARK 900  SUBUNIT FROM THERMUSTHERMOPHILUS IN COMPLEX                         
REMARK 900  WITH EDEINE                                                         
REMARK 900 RELATED ID: 2UUA   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE THERMUS THERMOPHILUS 30S                           
REMARK 900  RIBOSOMAL SUBUNIT COMPLEXED WITH A VALINE-                          
REMARK 900  ASL WITH CMO5U IN POSITION 34 BOUND TO                              
REMARK 900  AN MRNA WITH A GUC-CODON IN THE A-SITE                              
REMARK 900   AND PAROMOMYCIN.                                                   
REMARK 900 RELATED ID: 1XNQ   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF AN INOSINE-ADENINE WOBBLE BASE                         
REMARK 900   PAIR COMPLEX INTHE CONTEXT OF THE DECODING                         
REMARK 900   CENTER                                                             
REMARK 900 RELATED ID: 2XFZ   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF CYTOTOXIC DOMAIN OF COLICIN E3                         
REMARK 900   BOUND TO THE 70S RIBOSOME (PART 1 OF 4)                            
REMARK 900 RELATED ID: 1QD7   RELATED DB: PDB                                   
REMARK 900  PARTIAL MODEL FOR 30S RIBOSOMAL SUBUNIT                             
REMARK 900 RELATED ID: 1GIX   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE RIBOSOME AT 5.5                            
REMARK 900  A RESOLUTION. THISFILE, 1GIX, CONTAINS THE                          
REMARK 900  30S RIBOSOME SUBUNIT, THREE TRNA,AND MRNA                           
REMARK 900  MOLECULES. 50S RIBOSOME SUBUNIT IS IN THE                           
REMARK 900  FILE 1GIY                                                           
REMARK 900 RELATED ID: 1JGO   RELATED DB: PDB                                   
REMARK 900  THE PATH OF MESSENGER RNA THROUGH THE                               
REMARK 900  RIBOSOME. THIS FILE,1JGO, CONTAINS THE 30S                          
REMARK 900  RIBOSOME SUBUNIT, THREE TRNA, ANDMRNA                               
REMARK 900  MOLECULES. 50S RIBOSOME SUBUNIT IS IN THE                           
REMARK 900  FILE 1GIY                                                           
REMARK 900 RELATED ID: 1JGP   RELATED DB: PDB                                   
REMARK 900  THE PATH OF MESSENGER RNA THROUGH THE                               
REMARK 900  RIBOSOME. THIS FILE,1JGP, CONTAINS THE 30S                          
REMARK 900  RIBOSOME SUBUNIT, THREE TRNA, ANDMRNA                               
REMARK 900  MOLECULES. 50S RIBOSOME SUBUNIT IS IN THE                           
REMARK 900  FILE 1GIY                                                           
REMARK 900 RELATED ID: 2XG1   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF CYTOTOXIC DOMAIN OF COLICIN E3                         
REMARK 900   BOUND TO THE 70S RIBOSOME (PART 3 OF 4)                            
REMARK 900 RELATED ID: 2C78   RELATED DB: PDB                                   
REMARK 900  EF-TU COMPLEXED WITH A GTP ANALOG AND                               
REMARK 900  THE ANTIBIOTIC PULVOMYCIN                                           
REMARK 900 RELATED ID: 2X9R   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE 70S RIBOSOME BOUND TO                              
REMARK 900  RELEASE FACTOR 2 AND A SUBSTRATE ANALOG                             
REMARK 900  PROVIDES INSIGHTS INTO CATALYSIS OF PEPTIDE                         
REMARK 900  RELEASE                                                             
REMARK 900 RELATED ID: 1N34   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE THERMUS THERMOPHILUS 30S                           
REMARK 900  RIBOSOMAL SUBUNITIN THE PRESENCE OF CODON                           
REMARK 900  AND CRYSTALLOGRAPHICALLYDISORDERED NEAR-COGNATE                     
REMARK 900  TRANSFER RNA ANTICODON STEM-LOOPMISMATCHED AT                       
REMARK 900   THE FIRST CODON POSITION                                           
REMARK 900 RELATED ID: 1N33   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE THERMUS THERMOPHILUS 30S                           
REMARK 900  RIBOSOMAL SUBUNITBOUND TO CODON AND NEAR-                           
REMARK 900  COGNATE TRANSFER RNA ANTICODONSTEM-LOOP                             
REMARK 900  MISMATCHED AT THE SECOND CODON POSITION AT                          
REMARK 900  THE ASITE WITH PAROMOMYCIN                                          
REMARK 900 RELATED ID: 1PNS   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF A STREPTOMYCIN DEPENDENT                       
REMARK 900   RIBOSOME FROME. COLI, 30S SUBUNIT OF 70S                           
REMARK 900  RIBOSOME. THIS FILE, 1PNS,CONTAINS THE 30S                          
REMARK 900  SUBUNIT, TWO TRNAS, AND ONE MRNAMOLECULE.                           
REMARK 900  THE 50S RIBOSOMAL SUBUNIT IS IN FILE 1PNU.                          
REMARK 900 RELATED ID: 2JL7   RELATED DB: PDB                                   
REMARK 900  INSIGHTS INTO TRANSLATIONAL TERMINATION FROM                        
REMARK 900  THE STRUCTURE OF RF2 BOUND TO THE RIBOSOME                          
REMARK 900   (PART 3 OF 4). THIS FILE CONTAINS THE                              
REMARK 900  30S SUBUNIT.                                                        
REMARK 900 RELATED ID: 1YL4   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF 70S RIBOSOME WITH THRS                         
REMARK 900   OPERATOR ANDTRNAS. 30S SUBUNIT. THE                                
REMARK 900  COORDINATES FOR THE 50S SUBUNITARE IN THE                           
REMARK 900  PDB ENTRY 1YL3                                                      
REMARK 900 RELATED ID: 2WDM   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE THERMUS THERMOPHILUS 70S                           
REMARK 900  RIBOSOME IN COMPLEX WITH MRNA, PAROMOMYCIN,                         
REMARK 900  ACYLATED A- AND P-SITE TRNAS, AND E-SITE                            
REMARK 900   TRNA. THIS FILE CONTAINS THE 30S SUBUNIT                           
REMARK 900  A-,P-, AND E-SITE TRNAS AND PAROMOMYCIN                             
REMARK 900  FOR MOLECULE II.                                                    
REMARK 900 RELATED ID: 1XMO   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF MNM5U34T6A37-TRNALYSUUU                        
REMARK 900  COMPLEXED WITHAAG-MRNA IN THE DECODING CENTER                       
REMARK 900 RELATED ID: 1I97   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE 30S RIBOSOMAL                              
REMARK 900  SUBUNIT FROM THERMUSTHERMOPHILUS IN COMPLEX                         
REMARK 900  WITH TETRACYCLINE                                                   
REMARK 900 RELATED ID: 2Y12   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF EF-TU AND G24A-                            
REMARK 900  TRNA-TRP BOUND TO A NEAR-COGNATE CODON                              
REMARK 900  ON THE 70S RIBOSOME                                                 
REMARK 900 RELATED ID: 2Y13   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF EF-TU AND G24A-                            
REMARK 900  TRNA-TRP BOUND TO A NEAR-COGNATE CODON                              
REMARK 900  ON THE 70S RIBOSOME                                                 
REMARK 900 RELATED ID: 2Y16   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF EF-TU AND G24A-                            
REMARK 900  TRNA-TRP BOUND TO A COGNATE CODON ON THE                            
REMARK 900   70S RIBOSOME.                                                      
REMARK 900 RELATED ID: 2Y0Z   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF EF-TU AND G24A-                            
REMARK 900  TRNA-TRP BOUND TO A NEAR-COGNATE CODON                              
REMARK 900  ON THE 70S RIBOSOME                                                 
REMARK 900 RELATED ID: 2Y0W   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF EF-TU AND A9C-                             
REMARK 900  TRNA-TRP BOUND TO A NEAR-COGNATE CODON                              
REMARK 900  ON THE 70S RIBOSOME                                                 
REMARK 900 RELATED ID: 2Y0Y   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF EF-TU AND G24A-                            
REMARK 900  TRNA-TRP BOUND TO A NEAR-COGNATE CODON                              
REMARK 900  ON THE 70S RIBOSOME                                                 
REMARK 900 RELATED ID: 2Y15   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF EF-TU AND G24A-                            
REMARK 900  TRNA-TRP BOUND TO A COGNATE CODON ON THE                            
REMARK 900   70S RIBOSOME.                                                      
REMARK 900 RELATED ID: 2Y10   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF EF-TU AND TRP-                             
REMARK 900  TRNA-TRP BOUND TO A COGNATE CODON ON THE                            
REMARK 900   70S RIBOSOME.                                                      
REMARK 900 RELATED ID: 2Y0V   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF EF-TU AND A9C-                             
REMARK 900  TRNA-TRP BOUND TO A NEAR-COGNATE CODON                              
REMARK 900  ON THE 70S RIBOSOME                                                 
REMARK 900 RELATED ID: 2Y0X   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF EF-TU AND A9C-                             
REMARK 900  TRNA-TRP BOUND TO A NEAR-COGNATE CODON                              
REMARK 900  ON THE 70S RIBOSOME                                                 
REMARK 900 RELATED ID: 2Y11   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF EF-TU AND TRP-                             
REMARK 900  TRNA-TRP BOUND TO A COGNATE CODON ON THE                            
REMARK 900   70S RIBOSOME.                                                      
REMARK 900 RELATED ID: 2Y14   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF EF-TU AND G24A-                            
REMARK 900  TRNA-TRP BOUND TO A COGNATE CODON ON THE                            
REMARK 900   70S RIBOSOME.                                                      
REMARK 900 RELATED ID: 2Y17   RELATED DB: PDB                                   
REMARK 900  EF-TU COMPLEX 3                                                     
REMARK 900 RELATED ID: 2Y19   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF EF-TU AND TRP-                             
REMARK 900  TRNA-TRP BOUND TO A COGNATE CODON ON THE                            
REMARK 900   70S RIBOSOME.                                                      
REMARK 900 RELATED ID: 2Y18   RELATED DB: PDB                                   
REMARK 900  THE CRYSTAL STRUCTURE OF EF-TU AND TRP-                             
REMARK 900  TRNA-TRP BOUND TO A COGNATE CODON ON THE                            
REMARK 900   70S RIBOSOME.                                                      
DBREF1 2Y0U A    0  1544  GB                   NC_006461                        
DBREF2 2Y0U A     55979969                       131300      132821             
DBREF  2Y0U B    1   256  UNP    P80371   RS2_THET8        1    256             
DBREF  2Y0U C    1   239  UNP    P80372   RS3_THET8        1    239             
DBREF  2Y0U D    1   209  UNP    P80373   RS4_THET8        1    209             
DBREF  2Y0U E    1   162  UNP    Q5SHQ5   RS5_THET8        1    162             
DBREF  2Y0U F    1   101  UNP    Q5SLP8   RS6_THET8        1    101             
DBREF  2Y0U G    1   156  UNP    P17291   RS7_THET8        1    156             
DBREF  2Y0U H    1   138  UNP    Q5SHQ2   RS8_THET8        1    138             
DBREF  2Y0U I    1   128  UNP    P80374   RS9_THET8        1    128             
DBREF  2Y0U J    1   105  UNP    Q5SHN7   RS10_THET8       1    105             
DBREF  2Y0U K    1   129  UNP    P80376   RS11_THET8       1    129             
DBREF  2Y0U L    5   135  UNP    Q5SHN3   RS12_THET8       2    132             
DBREF  2Y0U M    1   126  UNP    P80377   RS13_THET8       1    126             
DBREF  2Y0U N    1    61  UNP    Q5SHQ1   RS14Z_THET8      1     61             
DBREF  2Y0U O    1    89  UNP    Q5SJ76   RS15_THET8       1     89             
DBREF  2Y0U P    1    88  UNP    Q5SJH3   RS16_THET8       1     88             
DBREF  2Y0U Q    1   105  UNP    Q5SHP7   RS17_THET8       1    105             
DBREF  2Y0U R    1    88  UNP    Q5SLQ0   RS18_THET8       1     88             
DBREF  2Y0U S    1    93  UNP    Q5SHP2   RS19_THET8       1     93             
DBREF  2Y0U T    1   106  UNP    P80380   RS20_THET8       1    106             
DBREF  2Y0U U    1    27  UNP    Q5SIH3   RSHX_THET8       1     27             
DBREF  2Y0U V    1    76  PDB    2Y0U     2Y0U             1     76             
DBREF  2Y0U W    1    76  PDB    2Y0U     2Y0U             1     76             
DBREF  2Y0U X    1    27  PDB    2Y0U     2Y0U             1     27             
DBREF  2Y0U Y    1    77  PDB    2Y0U     2Y0U             1     77             
DBREF  2Y0U Z    1   405  UNP    Q5SHN6   EFTU1_THET8      2    406             
SEQADV 2Y0U MET L    1  UNP  Q5SHN3              EXPRESSION TAG                 
SEQADV 2Y0U VAL L    2  UNP  Q5SHN3              EXPRESSION TAG                 
SEQADV 2Y0U ALA L    3  UNP  Q5SHN3              EXPRESSION TAG                 
SEQADV 2Y0U LEU L    4  UNP  Q5SHN3              EXPRESSION TAG                 
SEQADV 2Y0U ILE Z    6  UNP  Q5SHN6    VAL     7 CONFLICT                       
SEQADV 2Y0U LYS Z  264  UNP  Q5SHN6    ARG   265 CONFLICT                       
SEQRES   1 A 1522    U   U   U   G   U   U   G   G   A   G   A   G   U          
SEQRES   2 A 1522    U   U   G   A   U   C   C   U   G   G   C   U   C          
SEQRES   3 A 1522    A   G   G   G   U   G   A   A   C   G   C   U   G          
SEQRES   4 A 1522    G   C   G   G   C   G   U   G   C   C   U   A   A          
SEQRES   5 A 1522    G   A   C   A   U   G   C   A   A   G   U   C   G          
SEQRES   6 A 1522    U   G   C   G   G   G   C   C   G   C   G   G   G          
SEQRES   7 A 1522    G   U   U   U   U   A   C   U   C   C   G   U   G          
SEQRES   8 A 1522    G   U   C   A   G   C   G   G   C   G   G   A   C          
SEQRES   9 A 1522    G   G   G   U   G   A   G   U   A   A   C   G   C          
SEQRES  10 A 1522    G   U   G   G   G   U   G   A   C   C   U   A   C          
SEQRES  11 A 1522    C   C   G   G   A   A   G   A   G   G   G   G   G          
SEQRES  12 A 1522    A   C   A   A   C   C   C   G   G   G   G   A   A          
SEQRES  13 A 1522    A   C   U   C   G   G   G   C   U   A   A   U   C          
SEQRES  14 A 1522    C   C   C   C   A   U   G   U   G   G   A   C   C          
SEQRES  15 A 1522    C   G   C   C   C   C   U   U   G   G   G   G   U          
SEQRES  16 A 1522    G   U   G   U   C   C   A   A   A   G   G   G   C          
SEQRES  17 A 1522    U   U   U   G   C   C   C   G   C   U   U   C   C          
SEQRES  18 A 1522    G   G   A   U   G   G   G   C   C   C   G   C   G          
SEQRES  19 A 1522    U   C   C   C   A   U   C   A   G   C   U   A   G          
SEQRES  20 A 1522    U   U   G   G   U   G   G   G   G   U   A   A   U          
SEQRES  21 A 1522    G   G   C   C   C   A   C   C   A   A   G   G   C          
SEQRES  22 A 1522    G   A   C   G   A   C   G   G   G   U   A   G   C          
SEQRES  23 A 1522    C   G   G   U   C   U   G   A   G   A   G   G   A          
SEQRES  24 A 1522    U   G   G   C   C   G   G   C   C   A   C   A   G          
SEQRES  25 A 1522    G   G   G   C   A   C   U   G   A   G   A   C   A          
SEQRES  26 A 1522    C   G   G   G   C   C   C   C   A   C   U   C   C          
SEQRES  27 A 1522    U   A   C   G   G   G   A   G   G   C   A   G   C          
SEQRES  28 A 1522    A   G   U   U   A   G   G   A   A   U   C   U   U          
SEQRES  29 A 1522    C   C   G   C   A   A   U   G   G   G   C   G   C          
SEQRES  30 A 1522    A   A   G   C   C   U   G   A   C   G   G   A   G          
SEQRES  31 A 1522    C   G   A   C   G   C   C   G   C   U   U   G   G          
SEQRES  32 A 1522    A   G   G   A   A   G   A   A   G   C   C   C   U          
SEQRES  33 A 1522    U   C   G   G   G   G   U   G   U   A   A   A   C          
SEQRES  34 A 1522    U   C   C   U   G   A   A   C   C   C   G   G   G          
SEQRES  35 A 1522    A   C   G   A   A   A   C   C   C   C   C   G   A          
SEQRES  36 A 1522    C   G   A   G   G   G   G   A   C   U   G   A   C          
SEQRES  37 A 1522    G   G   U   A   C   C   G   G   G   G   U   A   A          
SEQRES  38 A 1522    U   A   G   C   G   C   C   G   G   C   C   A   A          
SEQRES  39 A 1522    C   U   C   C   G   U   G   C   C   A   G   C   A          
SEQRES  40 A 1522    G   C   C   G   C   G   G   U   A   A   U   A   C          
SEQRES  41 A 1522    G   G   A   G   G   G   C   G   C   G   A   G   C          
SEQRES  42 A 1522    G   U   U   A   C   C   C   G   G   A   U   U   C          
SEQRES  43 A 1522    A   C   U   G   G   G   C   G   U   A   A   A   G          
SEQRES  44 A 1522    G   G   C   G   U   G   U   A   G   G   C   G   G          
SEQRES  45 A 1522    C   C   U   G   G   G   G   C   G   U   C   C   C          
SEQRES  46 A 1522    A   U   G   U   G   A   A   A   G   A   C   C   A          
SEQRES  47 A 1522    C   G   G   C   U   C   A   A   C   C   G   U   G          
SEQRES  48 A 1522    G   G   G   G   A   G   C   G   U   G   G   G   A          
SEQRES  49 A 1522    U   A   C   G   C   U   C   A   G   G   C   U   A          
SEQRES  50 A 1522    G   A   C   G   G   U   G   G   G   A   G   A   G          
SEQRES  51 A 1522    G   G   U   G   G   U   G   G   A   A   U   U   C          
SEQRES  52 A 1522    C   C   G   G   A   G   U   A   G   C   G   G   U          
SEQRES  53 A 1522    G   A   A   A   U   G   C   G   C   A   G   A   U          
SEQRES  54 A 1522    A   C   C   G   G   G   A   G   G   A   A   C   G          
SEQRES  55 A 1522    C   C   G   A   U   G   G   C   G   A   A   G   G          
SEQRES  56 A 1522    C   A   G   C   C   A   C   C   U   G   G   U   C          
SEQRES  57 A 1522    C   A   C   C   C   G   U   G   A   C   G   C   U          
SEQRES  58 A 1522    G   A   G   G   C   G   C   G   A   A   A   G   C          
SEQRES  59 A 1522    G   U   G   G   G   G   A   G   C   A   A   A   C          
SEQRES  60 A 1522    C   G   G   A   U   U   A   G   A   U   A   C   C          
SEQRES  61 A 1522    C   G   G   G   U   A   G   U   C   C   A   C   G          
SEQRES  62 A 1522    C   C   C   U   A   A   A   C   G   A   U   G   C          
SEQRES  63 A 1522    G   C   G   C   U   A   G   G   U   C   U   C   U          
SEQRES  64 A 1522    G   G   G   U   C   U   C   C   U   G   G   G   G          
SEQRES  65 A 1522    G   C   C   G   A   A   G   C   U   A   A   C   G          
SEQRES  66 A 1522    C   G   U   U   A   A   G   C   G   C   G   C   C          
SEQRES  67 A 1522    G   C   C   U   G   G   G   G   A   G   U   A   C          
SEQRES  68 A 1522    G   G   C   C   G   C   A   A   G   G   C   U   G          
SEQRES  69 A 1522    A   A   A   C   U   C   A   A   A   G   G   A   A          
SEQRES  70 A 1522    U   U   G   A   C   G   G   G   G   G   C   C   C          
SEQRES  71 A 1522    G   C   A   C   A   A   G   C   G   G   U   G   G          
SEQRES  72 A 1522    A   G   C   A   U   G   U   G   G   U   U   U   A          
SEQRES  73 A 1522    A   U   U   C   G   A   A   G   C   A   A   C   G          
SEQRES  74 A 1522    C   G   A   A   G   A   A   C   C   U   U   A   C          
SEQRES  75 A 1522    C   A   G   G   C   C   U   U   G   A   C   A   U          
SEQRES  76 A 1522    G   C   U   A   G   G   G   A   A   C   C   C   G          
SEQRES  77 A 1522    G   G   U   G   A   A   A   G   C   C   U   G   G          
SEQRES  78 A 1522    G   G   U   G   C   C   C   C   G   C   G   A   G          
SEQRES  79 A 1522    G   G   G   A   G   C   C   C   U   A   G   C   A          
SEQRES  80 A 1522    C   A   G   G   U   G   C   U   G   C   A   U   G          
SEQRES  81 A 1522    G   C   C   G   U   C   G   U   C   A   G   C   U          
SEQRES  82 A 1522    C   G   U   G   C   C   G   U   G   A   G   G   U          
SEQRES  83 A 1522    G   U   U   G   G   G   U   U   A   A   G   U   C          
SEQRES  84 A 1522    C   C   G   C   A   A   C   G   A   G   C   G   C          
SEQRES  85 A 1522    A   A   C   C   C   C   C   G   C   C   G   U   U          
SEQRES  86 A 1522    A   G   U   U   G   C   C   A   G   C   G   G   U          
SEQRES  87 A 1522    U   C   G   G   C   C   G   G   G   C   A   C   U          
SEQRES  88 A 1522    C   U   A   A   C   G   G   G   A   C   U   G   C          
SEQRES  89 A 1522    C   C   G   C   G   A   A   A   G   C   G   G   G          
SEQRES  90 A 1522    A   G   G   A   A   G   G   A   G   G   G   G   A          
SEQRES  91 A 1522    C   G   A   C   G   U   C   U   G   G   U   C   A          
SEQRES  92 A 1522    G   C   A   U   G   G   C   C   C   U   U   A   C          
SEQRES  93 A 1522    G   G   C   C   U   G   G   G   C   G   A   C   A          
SEQRES  94 A 1522    C   A   C   G   U   G   C   U   A   C   A   A   U          
SEQRES  95 A 1522    G   C   C   C   A   C   U   A   C   A   A   A   G          
SEQRES  96 A 1522    C   G   A   U   G   C   C   A   C   C   C   G   G          
SEQRES  97 A 1522    C   A   A   C   G   G   G   G   A   G   C   U   A          
SEQRES  98 A 1522    A   U   C   G   C   A   A   A   A   A   G   G   U          
SEQRES  99 A 1522    G   G   G   C   C   C   A   G   U   U   C   G   G          
SEQRES 100 A 1522    A   U   U   G   G   G   G   U   C   U   G   C   A          
SEQRES 101 A 1522    A   C   C   C   G   A   C   C   C   C   A   U   G          
SEQRES 102 A 1522    A   A   G   C   C   G   G   A   A   U   C   G   C          
SEQRES 103 A 1522    U   A   G   U   A   A   U   C   G   C   G   G   A          
SEQRES 104 A 1522    U   C   A   G   C   C   A   U   G   C   C   G   C          
SEQRES 105 A 1522    G   G   U   G   A   A   U   A   C   G   U   U   C          
SEQRES 106 A 1522    C   C   G   G   G   C   C   U   U   G   U   A   C          
SEQRES 107 A 1522    A   C   A   C   C   G   C   C   C   G   U   C   A          
SEQRES 108 A 1522    C   G   C   C   A   U   G   G   G   A   G   C   G          
SEQRES 109 A 1522    G   G   C   U   C   U   A   C   C   C   G   A   A          
SEQRES 110 A 1522    G   U   C   G   C   C   G   G   G   A   G   C   C          
SEQRES 111 A 1522    U   A   C   G   G   G   C   A   G   G   C   G   C          
SEQRES 112 A 1522    C   G   A   G   G   G   U   A   G   G   G   C   C          
SEQRES 113 A 1522    C   G   U   G   A   C   U   G   G   G   G   C   G          
SEQRES 114 A 1522    A   A   G   U   C   G   U   A   A   C   A   A   G          
SEQRES 115 A 1522    G   U   A   G   C   U   G   U   A   C   C   G   G          
SEQRES 116 A 1522    A   A   G   G   U   G   C   G   G   C   U   G   G          
SEQRES 117 A 1522    A   U   C   A   C   C   U   C   C   U   U   U   C          
SEQRES 118 A 1522    U                                                          
SEQRES   1 B  256  MET PRO VAL GLU ILE THR VAL LYS GLU LEU LEU GLU ALA          
SEQRES   2 B  256  GLY VAL HIS PHE GLY HIS GLU ARG LYS ARG TRP ASN PRO          
SEQRES   3 B  256  LYS PHE ALA ARG TYR ILE TYR ALA GLU ARG ASN GLY ILE          
SEQRES   4 B  256  HIS ILE ILE ASP LEU GLN LYS THR MET GLU GLU LEU GLU          
SEQRES   5 B  256  ARG THR PHE ARG PHE ILE GLU ASP LEU ALA MET ARG GLY          
SEQRES   6 B  256  GLY THR ILE LEU PHE VAL GLY THR LYS LYS GLN ALA GLN          
SEQRES   7 B  256  ASP ILE VAL ARG MET GLU ALA GLU ARG ALA GLY MET PRO          
SEQRES   8 B  256  TYR VAL ASN GLN ARG TRP LEU GLY GLY MET LEU THR ASN          
SEQRES   9 B  256  PHE LYS THR ILE SER GLN ARG VAL HIS ARG LEU GLU GLU          
SEQRES  10 B  256  LEU GLU ALA LEU PHE ALA SER PRO GLU ILE GLU GLU ARG          
SEQRES  11 B  256  PRO LYS LYS GLU GLN VAL ARG LEU LYS HIS GLU LEU GLU          
SEQRES  12 B  256  ARG LEU GLN LYS TYR LEU SER GLY PHE ARG LEU LEU LYS          
SEQRES  13 B  256  ARG LEU PRO ASP ALA ILE PHE VAL VAL ASP PRO THR LYS          
SEQRES  14 B  256  GLU ALA ILE ALA VAL ARG GLU ALA ARG LYS LEU PHE ILE          
SEQRES  15 B  256  PRO VAL ILE ALA LEU ALA ASP THR ASP SER ASP PRO ASP          
SEQRES  16 B  256  LEU VAL ASP TYR ILE ILE PRO GLY ASN ASP ASP ALA ILE          
SEQRES  17 B  256  ARG SER ILE GLN LEU ILE LEU SER ARG ALA VAL ASP LEU          
SEQRES  18 B  256  ILE ILE GLN ALA ARG GLY GLY VAL VAL GLU PRO SER PRO          
SEQRES  19 B  256  SER TYR ALA LEU VAL GLN GLU ALA GLU ALA THR GLU THR          
SEQRES  20 B  256  PRO GLU GLY GLU SER GLU VAL GLU ALA                          
SEQRES   1 C  239  MET GLY ASN LYS ILE HIS PRO ILE GLY PHE ARG LEU GLY          
SEQRES   2 C  239  ILE THR ARG ASP TRP GLU SER ARG TRP TYR ALA GLY LYS          
SEQRES   3 C  239  LYS GLN TYR ARG HIS LEU LEU LEU GLU ASP GLN ARG ILE          
SEQRES   4 C  239  ARG GLY LEU LEU GLU LYS GLU LEU TYR SER ALA GLY LEU          
SEQRES   5 C  239  ALA ARG VAL ASP ILE GLU ARG ALA ALA ASP ASN VAL ALA          
SEQRES   6 C  239  VAL THR VAL HIS VAL ALA LYS PRO GLY VAL VAL ILE GLY          
SEQRES   7 C  239  ARG GLY GLY GLU ARG ILE ARG VAL LEU ARG GLU GLU LEU          
SEQRES   8 C  239  ALA LYS LEU THR GLY LYS ASN VAL ALA LEU ASN VAL GLN          
SEQRES   9 C  239  GLU VAL GLN ASN PRO ASN LEU SER ALA PRO LEU VAL ALA          
SEQRES  10 C  239  GLN ARG VAL ALA GLU GLN ILE GLU ARG ARG PHE ALA VAL          
SEQRES  11 C  239  ARG ARG ALA ILE LYS GLN ALA VAL GLN ARG VAL MET GLU          
SEQRES  12 C  239  SER GLY ALA LYS GLY ALA LYS VAL ILE VAL SER GLY ARG          
SEQRES  13 C  239  ILE GLY GLY ALA GLU GLN ALA ARG THR GLU TRP ALA ALA          
SEQRES  14 C  239  GLN GLY ARG VAL PRO LEU HIS THR LEU ARG ALA ASN ILE          
SEQRES  15 C  239  ASP TYR GLY PHE ALA LEU ALA ARG THR THR TYR GLY VAL          
SEQRES  16 C  239  LEU GLY VAL LYS ALA TYR ILE PHE LEU GLY GLU VAL ILE          
SEQRES  17 C  239  GLY GLY GLN LYS PRO LYS ALA ARG PRO GLU LEU PRO LYS          
SEQRES  18 C  239  ALA GLU GLU ARG PRO ARG ARG ARG ARG PRO ALA VAL ARG          
SEQRES  19 C  239  VAL LYS LYS GLU GLU                                          
SEQRES   1 D  209  MET GLY ARG TYR ILE GLY PRO VAL CYS ARG LEU CYS ARG          
SEQRES   2 D  209  ARG GLU GLY VAL LYS LEU TYR LEU LYS GLY GLU ARG CYS          
SEQRES   3 D  209  TYR SER PRO LYS CYS ALA MET GLU ARG ARG PRO TYR PRO          
SEQRES   4 D  209  PRO GLY GLN HIS GLY GLN LYS ARG ALA ARG ARG PRO SER          
SEQRES   5 D  209  ASP TYR ALA VAL ARG LEU ARG GLU LYS GLN LYS LEU ARG          
SEQRES   6 D  209  ARG ILE TYR GLY ILE SER GLU ARG GLN PHE ARG ASN LEU          
SEQRES   7 D  209  PHE GLU GLU ALA SER LYS LYS LYS GLY VAL THR GLY SER          
SEQRES   8 D  209  VAL PHE LEU GLY LEU LEU GLU SER ARG LEU ASP ASN VAL          
SEQRES   9 D  209  VAL TYR ARG LEU GLY PHE ALA VAL SER ARG ARG GLN ALA          
SEQRES  10 D  209  ARG GLN LEU VAL ARG HIS GLY HIS ILE THR VAL ASN GLY          
SEQRES  11 D  209  ARG ARG VAL ASP LEU PRO SER TYR ARG VAL ARG PRO GLY          
SEQRES  12 D  209  ASP GLU ILE ALA VAL ALA GLU LYS SER ARG ASN LEU GLU          
SEQRES  13 D  209  LEU ILE ARG GLN ASN LEU GLU ALA MET LYS GLY ARG LYS          
SEQRES  14 D  209  VAL GLY PRO TRP LEU SER LEU ASP VAL GLU GLY MET LYS          
SEQRES  15 D  209  GLY LYS PHE LEU ARG LEU PRO ASP ARG GLU ASP LEU ALA          
SEQRES  16 D  209  LEU PRO VAL ASN GLU GLN LEU VAL ILE GLU PHE TYR SER          
SEQRES  17 D  209  ARG                                                          
SEQRES   1 E  162  MET PRO GLU THR ASP PHE GLU GLU LYS MET ILE LEU ILE          
SEQRES   2 E  162  ARG ARG THR ALA ARG MET GLN ALA GLY GLY ARG ARG PHE          
SEQRES   3 E  162  ARG PHE GLY ALA LEU VAL VAL VAL GLY ASP ARG GLN GLY          
SEQRES   4 E  162  ARG VAL GLY LEU GLY PHE GLY LYS ALA PRO GLU VAL PRO          
SEQRES   5 E  162  LEU ALA VAL GLN LYS ALA GLY TYR TYR ALA ARG ARG ASN          
SEQRES   6 E  162  MET VAL GLU VAL PRO LEU GLN ASN GLY THR ILE PRO HIS          
SEQRES   7 E  162  GLU ILE GLU VAL GLU PHE GLY ALA SER LYS ILE VAL LEU          
SEQRES   8 E  162  LYS PRO ALA ALA PRO GLY THR GLY VAL ILE ALA GLY ALA          
SEQRES   9 E  162  VAL PRO ARG ALA ILE LEU GLU LEU ALA GLY VAL THR ASP          
SEQRES  10 E  162  ILE LEU THR LYS GLU LEU GLY SER ARG ASN PRO ILE ASN          
SEQRES  11 E  162  ILE ALA TYR ALA THR MET GLU ALA LEU ARG GLN LEU ARG          
SEQRES  12 E  162  THR LYS ALA ASP VAL GLU ARG LEU ARG LYS GLY GLU ALA          
SEQRES  13 E  162  HIS ALA GLN ALA GLN GLY                                      
SEQRES   1 F  101  MET ARG ARG TYR GLU VAL ASN ILE VAL LEU ASN PRO ASN          
SEQRES   2 F  101  LEU ASP GLN SER GLN LEU ALA LEU GLU LYS GLU ILE ILE          
SEQRES   3 F  101  GLN ARG ALA LEU GLU ASN TYR GLY ALA ARG VAL GLU LYS          
SEQRES   4 F  101  VAL GLU GLU LEU GLY LEU ARG ARG LEU ALA TYR PRO ILE          
SEQRES   5 F  101  ALA LYS ASP PRO GLN GLY TYR PHE LEU TRP TYR GLN VAL          
SEQRES   6 F  101  GLU MET PRO GLU ASP ARG VAL ASN ASP LEU ALA ARG GLU          
SEQRES   7 F  101  LEU ARG ILE ARG ASP ASN VAL ARG ARG VAL MET VAL VAL          
SEQRES   8 F  101  LYS SER GLN GLU PRO PHE LEU ALA ASN ALA                      
SEQRES   1 G  156  MET ALA ARG ARG ARG ARG ALA GLU VAL ARG GLN LEU GLN          
SEQRES   2 G  156  PRO ASP LEU VAL TYR GLY ASP VAL LEU VAL THR ALA PHE          
SEQRES   3 G  156  ILE ASN LYS ILE MET ARG ASP GLY LYS LYS ASN LEU ALA          
SEQRES   4 G  156  ALA ARG ILE PHE TYR ASP ALA CYS LYS ILE ILE GLN GLU          
SEQRES   5 G  156  LYS THR GLY GLN GLU PRO LEU LYS VAL PHE LYS GLN ALA          
SEQRES   6 G  156  VAL GLU ASN VAL LYS PRO ARG MET GLU VAL ARG SER ARG          
SEQRES   7 G  156  ARG VAL GLY GLY ALA ASN TYR GLN VAL PRO MET GLU VAL          
SEQRES   8 G  156  SER PRO ARG ARG GLN GLN SER LEU ALA LEU ARG TRP LEU          
SEQRES   9 G  156  VAL GLN ALA ALA ASN GLN ARG PRO GLU ARG ARG ALA ALA          
SEQRES  10 G  156  VAL ARG ILE ALA HIS GLU LEU MET ASP ALA ALA GLU GLY          
SEQRES  11 G  156  LYS GLY GLY ALA VAL LYS LYS LYS GLU ASP VAL GLU ARG          
SEQRES  12 G  156  MET ALA GLU ALA ASN ARG ALA TYR ALA HIS TYR ARG TRP          
SEQRES   1 H  138  MET LEU THR ASP PRO ILE ALA ASP MET LEU THR ARG ILE          
SEQRES   2 H  138  ARG ASN ALA THR ARG VAL TYR LYS GLU SER THR ASP VAL          
SEQRES   3 H  138  PRO ALA SER ARG PHE LYS GLU GLU ILE LEU ARG ILE LEU          
SEQRES   4 H  138  ALA ARG GLU GLY PHE ILE LYS GLY TYR GLU ARG VAL ASP          
SEQRES   5 H  138  VAL ASP GLY LYS PRO TYR LEU ARG VAL TYR LEU LYS TYR          
SEQRES   6 H  138  GLY PRO ARG ARG GLN GLY PRO ASP PRO ARG PRO GLU GLN          
SEQRES   7 H  138  VAL ILE HIS HIS ILE ARG ARG ILE SER LYS PRO GLY ARG          
SEQRES   8 H  138  ARG VAL TYR VAL GLY VAL LYS GLU ILE PRO ARG VAL ARG          
SEQRES   9 H  138  ARG GLY LEU GLY ILE ALA ILE LEU SER THR SER LYS GLY          
SEQRES  10 H  138  VAL LEU THR ASP ARG GLU ALA ARG LYS LEU GLY VAL GLY          
SEQRES  11 H  138  GLY GLU LEU ILE CYS GLU VAL TRP                              
SEQRES   1 I  128  MET GLU GLN TYR TYR GLY THR GLY ARG ARG LYS GLU ALA          
SEQRES   2 I  128  VAL ALA ARG VAL PHE LEU ARG PRO GLY ASN GLY LYS VAL          
SEQRES   3 I  128  THR VAL ASN GLY GLN ASP PHE ASN GLU TYR PHE GLN GLY          
SEQRES   4 I  128  LEU VAL ARG ALA VAL ALA ALA LEU GLU PRO LEU ARG ALA          
SEQRES   5 I  128  VAL ASP ALA LEU GLY HIS PHE ASP ALA TYR ILE THR VAL          
SEQRES   6 I  128  ARG GLY GLY GLY LYS SER GLY GLN ILE ASP ALA ILE LYS          
SEQRES   7 I  128  LEU GLY ILE ALA ARG ALA LEU VAL GLN TYR ASN PRO ASP          
SEQRES   8 I  128  TYR ARG ALA LYS LEU LYS PRO LEU GLY PHE LEU THR ARG          
SEQRES   9 I  128  ASP ALA ARG VAL VAL GLU ARG LYS LYS TYR GLY LYS HIS          
SEQRES  10 I  128  LYS ALA ARG ARG ALA PRO GLN TYR SER LYS ARG                  
SEQRES   1 J  105  MET PRO LYS ILE ARG ILE LYS LEU ARG GLY PHE ASP HIS          
SEQRES   2 J  105  LYS THR LEU ASP ALA SER ALA GLN LYS ILE VAL GLU ALA          
SEQRES   3 J  105  ALA ARG ARG SER GLY ALA GLN VAL SER GLY PRO ILE PRO          
SEQRES   4 J  105  LEU PRO THR ARG VAL ARG ARG PHE THR VAL ILE ARG GLY          
SEQRES   5 J  105  PRO PHE LYS HIS LYS ASP SER ARG GLU HIS PHE GLU LEU          
SEQRES   6 J  105  ARG THR HIS ASN ARG LEU VAL ASP ILE ILE ASN PRO ASN          
SEQRES   7 J  105  ARG LYS THR ILE GLU GLN LEU MET THR LEU ASP LEU PRO          
SEQRES   8 J  105  THR GLY VAL GLU ILE GLU ILE LYS THR VAL GLY GLY GLY          
SEQRES   9 J  105  ARG                                                          
SEQRES   1 K  129  MET ALA LYS LYS PRO SER LYS LYS LYS VAL LYS ARG GLN          
SEQRES   2 K  129  VAL ALA SER GLY ARG ALA TYR ILE HIS ALA SER TYR ASN          
SEQRES   3 K  129  ASN THR ILE VAL THR ILE THR ASP PRO ASP GLY ASN PRO          
SEQRES   4 K  129  ILE THR TRP SER SER GLY GLY VAL ILE GLY TYR LYS GLY          
SEQRES   5 K  129  SER ARG LYS GLY THR PRO TYR ALA ALA GLN LEU ALA ALA          
SEQRES   6 K  129  LEU ASP ALA ALA LYS LYS ALA MET ALA TYR GLY MET GLN          
SEQRES   7 K  129  SER VAL ASP VAL ILE VAL ARG GLY THR GLY ALA GLY ARG          
SEQRES   8 K  129  GLU GLN ALA ILE ARG ALA LEU GLN ALA SER GLY LEU GLN          
SEQRES   9 K  129  VAL LYS SER ILE VAL ASP ASP THR PRO VAL PRO HIS ASN          
SEQRES  10 K  129  GLY CYS ARG PRO LYS LYS LYS PHE ARG LYS ALA SER              
SEQRES   1 L  135  MET VAL ALA LEU PRO THR ILE ASN GLN LEU VAL ARG LYS          
SEQRES   2 L  135  GLY ARG GLU LYS VAL ARG LYS LYS SER LYS VAL PRO ALA          
SEQRES   3 L  135  LEU LYS GLY ALA PRO PHE ARG ARG GLY VAL CYS THR VAL          
SEQRES   4 L  135  VAL ARG THR VAL THR PRO LYS LYS PRO ASN SER ALA LEU          
SEQRES   5 L  135  ARG LYS VAL ALA LYS VAL ARG LEU THR SER GLY TYR GLU          
SEQRES   6 L  135  VAL THR ALA TYR ILE PRO GLY GLU GLY HIS ASN LEU GLN          
SEQRES   7 L  135  GLU HIS SER VAL VAL LEU ILE ARG GLY GLY ARG VAL LYS          
SEQRES   8 L  135  ASP LEU PRO GLY VAL ARG TYR HIS ILE VAL ARG GLY VAL          
SEQRES   9 L  135  TYR ASP ALA ALA GLY VAL LYS ASP ARG LYS LYS SER ARG          
SEQRES  10 L  135  SER LYS TYR GLY THR LYS LYS PRO LYS GLU ALA ALA LYS          
SEQRES  11 L  135  THR ALA ALA LYS LYS                                          
SEQRES   1 M  126  MET ALA ARG ILE ALA GLY VAL GLU ILE PRO ARG ASN LYS          
SEQRES   2 M  126  ARG VAL ASP VAL ALA LEU THR TYR ILE TYR GLY ILE GLY          
SEQRES   3 M  126  LYS ALA ARG ALA LYS GLU ALA LEU GLU LYS THR GLY ILE          
SEQRES   4 M  126  ASN PRO ALA THR ARG VAL LYS ASP LEU THR GLU ALA GLU          
SEQRES   5 M  126  VAL VAL ARG LEU ARG GLU TYR VAL GLU ASN THR TRP LYS          
SEQRES   6 M  126  LEU GLU GLY GLU LEU ARG ALA GLU VAL ALA ALA ASN ILE          
SEQRES   7 M  126  LYS ARG LEU MET ASP ILE GLY CYS TYR ARG GLY LEU ARG          
SEQRES   8 M  126  HIS ARG ARG GLY LEU PRO VAL ARG GLY GLN ARG THR ARG          
SEQRES   9 M  126  THR ASN ALA ARG THR ARG LYS GLY PRO ARG LYS THR VAL          
SEQRES  10 M  126  ALA GLY LYS LYS LYS ALA PRO ARG LYS                          
SEQRES   1 N   61  MET ALA ARG LYS ALA LEU ILE GLU LYS ALA LYS ARG THR          
SEQRES   2 N   61  PRO LYS PHE LYS VAL ARG ALA TYR THR ARG CYS VAL ARG          
SEQRES   3 N   61  CYS GLY ARG ALA ARG SER VAL TYR ARG PHE PHE GLY LEU          
SEQRES   4 N   61  CYS ARG ILE CYS LEU ARG GLU LEU ALA HIS LYS GLY GLN          
SEQRES   5 N   61  LEU PRO GLY VAL ARG LYS ALA SER TRP                          
SEQRES   1 O   89  MET PRO ILE THR LYS GLU GLU LYS GLN LYS VAL ILE GLN          
SEQRES   2 O   89  GLU PHE ALA ARG PHE PRO GLY ASP THR GLY SER THR GLU          
SEQRES   3 O   89  VAL GLN VAL ALA LEU LEU THR LEU ARG ILE ASN ARG LEU          
SEQRES   4 O   89  SER GLU HIS LEU LYS VAL HIS LYS LYS ASP HIS HIS SER          
SEQRES   5 O   89  HIS ARG GLY LEU LEU MET MET VAL GLY GLN ARG ARG ARG          
SEQRES   6 O   89  LEU LEU ARG TYR LEU GLN ARG GLU ASP PRO GLU ARG TYR          
SEQRES   7 O   89  ARG ALA LEU ILE GLU LYS LEU GLY ILE ARG GLY                  
SEQRES   1 P   88  MET VAL LYS ILE ARG LEU ALA ARG PHE GLY SER LYS HIS          
SEQRES   2 P   88  ASN PRO HIS TYR ARG ILE VAL VAL THR ASP ALA ARG ARG          
SEQRES   3 P   88  LYS ARG ASP GLY LYS TYR ILE GLU LYS ILE GLY TYR TYR          
SEQRES   4 P   88  ASP PRO ARG LYS THR THR PRO ASP TRP LEU LYS VAL ASP          
SEQRES   5 P   88  VAL GLU ARG ALA ARG TYR TRP LEU SER VAL GLY ALA GLN          
SEQRES   6 P   88  PRO THR ASP THR ALA ARG ARG LEU LEU ARG GLN ALA GLY          
SEQRES   7 P   88  VAL PHE ARG GLN GLU ALA ARG GLU GLY ALA                      
SEQRES   1 Q  105  MET PRO LYS LYS VAL LEU THR GLY VAL VAL VAL SER ASP          
SEQRES   2 Q  105  LYS MET GLN LYS THR VAL THR VAL LEU VAL GLU ARG GLN          
SEQRES   3 Q  105  PHE PRO HIS PRO LEU TYR GLY LYS VAL ILE LYS ARG SER          
SEQRES   4 Q  105  LYS LYS TYR LEU ALA HIS ASP PRO GLU GLU LYS TYR LYS          
SEQRES   5 Q  105  LEU GLY ASP VAL VAL GLU ILE ILE GLU SER ARG PRO ILE          
SEQRES   6 Q  105  SER LYS ARG LYS ARG PHE ARG VAL LEU ARG LEU VAL GLU          
SEQRES   7 Q  105  SER GLY ARG MET ASP LEU VAL GLU LYS TYR LEU ILE ARG          
SEQRES   8 Q  105  ARG GLN ASN TYR GLU SER LEU SER LYS ARG GLY GLY LYS          
SEQRES   9 Q  105  ALA                                                          
SEQRES   1 R   88  MET SER THR LYS ASN ALA LYS PRO LYS LYS GLU ALA GLN          
SEQRES   2 R   88  ARG ARG PRO SER ARG LYS ALA LYS VAL LYS ALA THR LEU          
SEQRES   3 R   88  GLY GLU PHE ASP LEU ARG ASP TYR ARG ASN VAL GLU VAL          
SEQRES   4 R   88  LEU LYS ARG PHE LEU SER GLU THR GLY LYS ILE LEU PRO          
SEQRES   5 R   88  ARG ARG ARG THR GLY LEU SER ALA LYS GLU GLN ARG ILE          
SEQRES   6 R   88  LEU ALA LYS THR ILE LYS ARG ALA ARG ILE LEU GLY LEU          
SEQRES   7 R   88  LEU PRO PHE THR GLU LYS LEU VAL ARG LYS                      
SEQRES   1 S   93  MET PRO ARG SER LEU LYS LYS GLY VAL PHE VAL ASP ASP          
SEQRES   2 S   93  HIS LEU LEU GLU LYS VAL LEU GLU LEU ASN ALA LYS GLY          
SEQRES   3 S   93  GLU LYS ARG LEU ILE LYS THR TRP SER ARG ARG SER THR          
SEQRES   4 S   93  ILE VAL PRO GLU MET VAL GLY HIS THR ILE ALA VAL TYR          
SEQRES   5 S   93  ASN GLY LYS GLN HIS VAL PRO VAL TYR ILE THR GLU ASN          
SEQRES   6 S   93  MET VAL GLY HIS LYS LEU GLY GLU PHE ALA PRO THR ARG          
SEQRES   7 S   93  THR TYR ARG GLY HIS GLY LYS GLU ALA LYS ALA THR LYS          
SEQRES   8 S   93  LYS LYS                                                      
SEQRES   1 T  106  MET ALA GLN LYS LYS PRO LYS ARG ASN LEU SER ALA LEU          
SEQRES   2 T  106  LYS ARG HIS ARG GLN SER LEU LYS ARG ARG LEU ARG ASN          
SEQRES   3 T  106  LYS ALA LYS LYS SER ALA ILE LYS THR LEU SER LYS LYS          
SEQRES   4 T  106  ALA ILE GLN LEU ALA GLN GLU GLY LYS ALA GLU GLU ALA          
SEQRES   5 T  106  LEU LYS ILE MET ARG LYS ALA GLU SER LEU ILE ASP LYS          
SEQRES   6 T  106  ALA ALA LYS GLY SER THR LEU HIS LYS ASN ALA ALA ALA          
SEQRES   7 T  106  ARG ARG LYS SER ARG LEU MET ARG LYS VAL ARG GLN LEU          
SEQRES   8 T  106  LEU GLU ALA ALA GLY ALA PRO LEU ILE GLY GLY GLY LEU          
SEQRES   9 T  106  SER ALA                                                      
SEQRES   1 U   27  MET GLY LYS GLY ASP ARG ARG THR ARG ARG GLY LYS ILE          
SEQRES   2 U   27  TRP ARG GLY THR TYR GLY LYS TYR ARG PRO ARG LYS LYS          
SEQRES   3 U   27  LYS                                                          
SEQRES   1 V   76    G   C   C   C   G   G   A   U   A   G   C   U   C          
SEQRES   2 V   76    A   G   U   C   G   G   U   A   G   A   G   C   A          
SEQRES   3 V   76    G   G   G   G   A   U   U   G   A   A   A   A   U          
SEQRES   4 V   76    C   C   C   C   G   U   G   U   C   C   U   U   G          
SEQRES   5 V   76    G   U   U   C   G   A   U   U   C   C   G   A   G          
SEQRES   6 V   76    U   C   C   G   G   G   C   A   C   C   A                  
SEQRES   1 W   76    G   C   C   C   G   G   A   U   A   G   C   U   C          
SEQRES   2 W   76    A   G   U   C   G   G   U   A   G   A   G   C   A          
SEQRES   3 W   76    G   G   G   G   A   U   U   G   A   A   A   A   U          
SEQRES   4 W   76    C   C   C   C   G   U   G   U   C   C   U   U   G          
SEQRES   5 W   76    G   U   U   C   G   A   U   U   C   C   G   A   G          
SEQRES   6 W   76    U   C   C   G   G   G   C   A   C   C   A                  
SEQRES   1 X   27    G   G   C   A   A   G   G   A   G   G   U   A   A          
SEQRES   2 X   27    A   A   A   U   G   U   U   C   U   G   A   A   A          
SEQRES   3 X   27    A                                                          
SEQRES   1 Y   77    A   G   G   G   G   C   G 4SU   C   G   U   U   C          
SEQRES   2 Y   77    A   A H2U H2U   G   G H2U   A   G   A   G   C   A          
SEQRES   3 Y   77    C   C   G   G   U OMC   U   C   C   A MIA   A   A          
SEQRES   4 Y   77    C   C   G   G   G   U 7MG   U   U   G   G   G   A          
SEQRES   5 Y   77    G 5MU PSU   C   G   A   G   U   C   U   C   U   C          
SEQRES   6 Y   77    C   G   C   C   C   C   U   G   C   C   A TRP              
SEQRES   1 Z  405  ALA LYS GLY GLU PHE ILE ARG THR LYS PRO HIS VAL ASN          
SEQRES   2 Z  405  VAL GLY THR ILE GLY HIS VAL ASP HIS GLY LYS THR THR          
SEQRES   3 Z  405  LEU THR ALA ALA LEU THR TYR VAL ALA ALA ALA GLU ASN          
SEQRES   4 Z  405  PRO ASN VAL GLU VAL LYS ASP TYR GLY ASP ILE ASP LYS          
SEQRES   5 Z  405  ALA PRO GLU GLU ARG ALA ARG GLY ILE THR ILE ASN THR          
SEQRES   6 Z  405  ALA HIS VAL GLU TYR GLU THR ALA LYS ARG HIS TYR SER          
SEQRES   7 Z  405  HIS VAL ASP CYS PRO GLY HIS ALA ASP TYR ILE LYS ASN          
SEQRES   8 Z  405  MET ILE THR GLY ALA ALA GLN MET ASP GLY ALA ILE LEU          
SEQRES   9 Z  405  VAL VAL SER ALA ALA ASP GLY PRO MET PRO GLN THR ARG          
SEQRES  10 Z  405  GLU HIS ILE LEU LEU ALA ARG GLN VAL GLY VAL PRO TYR          
SEQRES  11 Z  405  ILE VAL VAL PHE MET ASN LYS VAL ASP MET VAL ASP ASP          
SEQRES  12 Z  405  PRO GLU LEU LEU ASP LEU VAL GLU MET GLU VAL ARG ASP          
SEQRES  13 Z  405  LEU LEU ASN GLN TYR GLU PHE PRO GLY ASP GLU VAL PRO          
SEQRES  14 Z  405  VAL ILE ARG GLY SER ALA LEU LEU ALA LEU GLU GLN MET          
SEQRES  15 Z  405  HIS ARG ASN PRO LYS THR ARG ARG GLY GLU ASN GLU TRP          
SEQRES  16 Z  405  VAL ASP LYS ILE TRP GLU LEU LEU ASP ALA ILE ASP GLU          
SEQRES  17 Z  405  TYR ILE PRO THR PRO VAL ARG ASP VAL ASP LYS PRO PHE          
SEQRES  18 Z  405  LEU MET PRO VAL GLU ASP VAL PHE THR ILE THR GLY ARG          
SEQRES  19 Z  405  GLY THR VAL ALA THR GLY ARG ILE GLU ARG GLY LYS VAL          
SEQRES  20 Z  405  LYS VAL GLY ASP GLU VAL GLU ILE VAL GLY LEU ALA PRO          
SEQRES  21 Z  405  GLU THR ARG LYS THR VAL VAL THR GLY VAL GLU MET HIS          
SEQRES  22 Z  405  ARG LYS THR LEU GLN GLU GLY ILE ALA GLY ASP ASN VAL          
SEQRES  23 Z  405  GLY VAL LEU LEU ARG GLY VAL SER ARG GLU GLU VAL GLU          
SEQRES  24 Z  405  ARG GLY GLN VAL LEU ALA LYS PRO GLY SER ILE THR PRO          
SEQRES  25 Z  405  HIS THR LYS PHE GLU ALA SER VAL TYR VAL LEU LYS LYS          
SEQRES  26 Z  405  GLU GLU GLY GLY ARG HIS THR GLY PHE PHE SER GLY TYR          
SEQRES  27 Z  405  ARG PRO GLN PHE TYR PHE ARG THR THR ASP VAL THR GLY          
SEQRES  28 Z  405  VAL VAL GLN LEU PRO PRO GLY VAL GLU MET VAL MET PRO          
SEQRES  29 Z  405  GLY ASP ASN VAL THR PHE THR VAL GLU LEU ILE LYS PRO          
SEQRES  30 Z  405  VAL ALA LEU GLU GLU GLY LEU ARG PHE ALA ILE ARG GLU          
SEQRES  31 Z  405  GLY GLY ARG THR VAL GLY ALA GLY VAL VAL THR LYS ILE          
SEQRES  32 Z  405  LEU GLU                                                      
MODRES 2Y0U 4SU Y    8    U  4-THIOURIDINE-5'-MONOPHOSPHATE                     
MODRES 2Y0U H2U Y   16    U  5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE                
MODRES 2Y0U H2U Y   17    U  5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE                
MODRES 2Y0U H2U Y   20    U  5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE                
MODRES 2Y0U OMC Y   32    C  O2'-METHYLYCYTIDINE-5'-MONOPHOSPHATE               
MODRES 2Y0U MIA Y   37    A  MODIFIED ADENOSINE                                 
MODRES 2Y0U 7MG Y   46    G  7-METHYL GUANOSINE                                 
MODRES 2Y0U 5MU Y   54    U  5-METHYLURIDINE 5'-MONOPHOSPHATE                   
MODRES 2Y0U PSU Y   55    U  PSEUDOURIDINE-5'-MONOPHOSPHATE                     
HET    4SU  Y   8      20                                                       
HET    H2U  Y  16      20                                                       
HET    H2U  Y  17      20                                                       
HET    H2U  Y  20      20                                                       
HET    OMC  Y  32      21                                                       
HET    MIA  Y  37      29                                                       
HET    7MG  Y  46      24                                                       
HET    5MU  Y  54      21                                                       
HET    PSU  Y  55      20                                                       
HET    GDP  1   1      28                                                       
HET    KIR  1   2      57                                                       
HET     ZN  1   3       1                                                       
HET     ZN  1   4       1                                                       
HET     ZN  1   5       1                                                       
HET     ZN  1   6       1                                                       
HETNAM     4SU 4-THIOURIDINE-5'-MONOPHOSPHATE                                   
HETNAM     H2U 5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE                              
HETNAM     OMC O2'-METHYLYCYTIDINE-5'-MONOPHOSPHATE                             
HETNAM     MIA 2-METHYLTHIO-N6-ISOPENTENYL-ADENOSINE-5'-MONOPHOSPHATE           
HETNAM     7MG 7N-METHYL-8-HYDROGUANOSINE-5'-MONOPHOSPHATE                      
HETNAM     5MU 5-METHYLURIDINE 5'-MONOPHOSPHATE                                 
HETNAM     PSU PSEUDOURIDINE-5'-MONOPHOSPHATE                                   
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM     KIR KIRROMYCIN                                                       
HETNAM      ZN ZINC ION                                                         
HETSYN     KIR MOCIMYCIN; DELVOMYCIN; MYC-8003                                  
FORMUL  25  4SU    C9 H13 N2 O8 P S                                             
FORMUL  26  H2U    3(C9 H15 N2 O9 P)                                            
FORMUL  27  OMC    C10 H16 N3 O8 P                                              
FORMUL  28  MIA    C16 H26 N5 O7 P S                                            
FORMUL  29  7MG    C11 H18 N5 O8 P                                              
FORMUL  30  5MU    C10 H15 N2 O9 P                                              
FORMUL  31  PSU    C9 H13 N2 O9 P                                               
FORMUL  32  GDP    C10 H15 N5 O11 P2                                            
FORMUL  33  KIR    C43 H60 N2 O12                                               
FORMUL  34   ZN    4(ZN 2+)                                                     
HELIX    1   1 LYS B    8  HIS B   16  1                                   9    
HELIX    2   2 LYS B   27  ILE B   32  5                                   6    
HELIX    3   3 ASP B   43  GLY B   65  1                                  23    
HELIX    4   4 ALA B   77  ARG B   87  1                                  11    
HELIX    5   5 ASN B  104  ALA B  123  1                                  20    
HELIX    6   6 SER B  124  GLU B  128  5                                   5    
HELIX    7   7 LYS B  133  LEU B  149  1                                  17    
HELIX    8   8 GLU B  170  LEU B  180  1                                  11    
HELIX    9   9 ASP B  193  VAL B  197  5                                   5    
HELIX   10  10 ALA B  207  GLY B  227  1                                  21    
HELIX   11  11 TYR C   29  GLU C   46  1                                  18    
HELIX   12  12 LYS C   72  GLY C   78  1                                   7    
HELIX   13  13 GLY C   81  LEU C   94  1                                  14    
HELIX   14  14 ASN C  108  LEU C  111  5                                   4    
HELIX   15  15 SER C  112  ARG C  126  1                                  15    
HELIX   16  16 ALA C  129  SER C  144  1                                  16    
HELIX   17  17 ARG C  156  ALA C  160  5                                   5    
HELIX   18  18 VAL D    8  GLU D   15  1                                   8    
HELIX   19  19 SER D   52  TYR D   68  1                                  17    
HELIX   20  20 SER D   71  LYS D   85  1                                  15    
HELIX   21  21 VAL D   88  ARG D  100  1                                  13    
HELIX   22  22 ARG D  100  ARG D  107  1                                   8    
HELIX   23  23 SER D  113  HIS D  123  1                                  11    
HELIX   24  24 LEU D  155  ALA D  164  1                                  10    
HELIX   25  25 ASN D  199  GLU D  205  1                                   7    
HELIX   26  26 GLU E   50  ARG E   63  1                                  14    
HELIX   27  27 GLY E  103  GLY E  114  1                                  12    
HELIX   28  28 ASN E  127  GLN E  141  1                                  15    
HELIX   29  29 THR E  144  LYS E  153  1                                  10    
HELIX   30  30 ASP F   15  TYR F   33  1                                  19    
HELIX   31  31 ARG F   71  ILE F   81  1                                  11    
HELIX   32  32 ASP G   20  MET G   31  1                                  12    
HELIX   33  33 LYS G   35  GLU G   52  1                                  18    
HELIX   34  34 GLU G   57  LYS G   70  1                                  14    
HELIX   35  35 SER G   92  ASN G  109  1                                  18    
HELIX   36  36 ARG G  115  GLY G  130  1                                  16    
HELIX   37  37 GLY G  132  ASN G  148  1                                  17    
HELIX   38  38 ARG G  149  ARG G  155  5                                   7    
HELIX   39  39 ASP H    4  ARG H   18  1                                  15    
HELIX   40  40 SER H   29  GLU H   42  1                                  14    
HELIX   41  41 ARG H  102  LEU H  107  5                                   6    
HELIX   42  42 ASP H  121  LEU H  127  1                                   7    
HELIX   43  43 ASP I   32  PHE I   37  1                                   6    
HELIX   44  44 ARG I   42  ALA I   46  5                                   5    
HELIX   45  45 GLU I   48  ALA I   52  5                                   5    
HELIX   46  46 GLY I   69  TYR I   88  1                                  20    
HELIX   47  47 LEU I   96  GLY I  100  5                                   5    
HELIX   48  48 ASP J   12  SER J   19  1                                   8    
HELIX   49  49 SER J   19  VAL J   24  1                                   6    
HELIX   50  50 VAL J   24  ARG J   29  1                                   6    
HELIX   51  51 ASN J   78  GLU J   83  1                                   6    
HELIX   52  52 GLN J   84  LEU J   88  5                                   5    
HELIX   53  53 SER K   53  GLY K   56  5                                   4    
HELIX   54  54 THR K   57  ALA K   74  1                                  18    
HELIX   55  55 ALA K   89  ALA K  100  1                                  12    
HELIX   56  56 THR L    6  GLY L   14  1                                   9    
HELIX   57  57 VAL L   24  LYS L   28  5                                   5    
HELIX   58  58 ARG M   14  LEU M   19  1                                   6    
HELIX   59  59 GLY M   26  LEU M   34  1                                   9    
HELIX   60  60 VAL M   45  LEU M   48  5                                   4    
HELIX   61  61 THR M   49  TRP M   64  1                                  16    
HELIX   62  62 GLY M   68  LEU M   81  1                                  14    
HELIX   63  63 CYS M   86  GLY M   95  1                                  10    
HELIX   64  64 LYS N    4  ALA N   10  1                                   7    
HELIX   65  65 CYS N   40  GLY N   51  1                                  12    
HELIX   66  66 THR O    4  ALA O   16  1                                  13    
HELIX   67  67 SER O   24  HIS O   46  1                                  23    
HELIX   68  68 ASP O   49  ASP O   74  1                                  26    
HELIX   69  69 ASP O   74  GLY O   86  1                                  13    
HELIX   70  70 ASP P   52  SER P   61  1                                  10    
HELIX   71  71 THR P   67  ALA P   77  1                                  11    
HELIX   72  72 ARG Q   81  TYR Q   95  1                                  15    
HELIX   73  73 GLU Q   96  SER Q   99  5                                   4    
HELIX   74  74 LYS R   21  LEU R   26  5                                   6    
HELIX   75  75 ASN R   36  LYS R   41  1                                   6    
HELIX   76  76 PRO R   52  GLY R   57  1                                   6    
HELIX   77  77 SER R   59  GLY R   77  1                                  19    
HELIX   78  78 ASP S   12  ALA S   24  1                                  13    
HELIX   79  79 LEU S   71  ALA S   75  5                                   5    
HELIX   80  80 ALA T   12  GLN T   45  1                                  34    
HELIX   81  81 LYS T   48  LYS T   68  1                                  21    
HELIX   82  82 ASN T   75  MET T   85  1                                  11    
HELIX   83  83 VAL T   88  GLU T   93  1                                   6    
HELIX   84  84 THR U    8  GLY U   16  1                                   9    
HELIX   85  85 LEU Z   27  THR Z   32  1                                   6    
HELIX   86  86 ILE Z   89  MET Z   99  1                                  11    
HELIX   87  87 MET Z  113  VAL Z  126  1                                  14    
HELIX   88  88 GLU Z  145  ASN Z  159  1                                  15    
HELIX   89  89 GLN Z  160  GLU Z  162  5                                   3    
HELIX   90  90 PRO Z  164  VAL Z  168  5                                   5    
HELIX   91  91 SER Z  174  GLN Z  181  1                                   8    
HELIX   92  92 LYS Z  198  LEU Z  203  1                                   6    
HELIX   93  93 LYS Z  324  GLY Z  328  5                                   5    
SHEET    1  BA 2 ALA B  34  ARG B  36  0                                        
SHEET    2  BA 2 ILE B  39  ILE B  41 -1  O  ILE B  39   N  ARG B  36           
SHEET    1  BB 5 TYR B  92  VAL B  93  0                                        
SHEET    2  BB 5 ILE B  68  VAL B  71  1  O  PHE B  70   N  VAL B  93           
SHEET    3  BB 5 ALA B 161  VAL B 164  1  O  ALA B 161   N  LEU B  69           
SHEET    4  BB 5 VAL B 184  ALA B 188  1  O  ILE B 185   N  VAL B 164           
SHEET    5  BB 5 TYR B 199  PRO B 202  1  O  TYR B 199   N  ALA B 186           
SHEET    1  CA 4 SER C  20  ARG C  21  0                                        
SHEET    2  CA 4 LEU C  52  GLU C  58  1  O  ILE C  57   N  ARG C  21           
SHEET    3  CA 4 THR C  67  VAL C  70 -1  O  THR C  67   N  ASP C  56           
SHEET    4  CA 4 ASN C 102  GLU C 105  1  O  ASN C 102   N  VAL C  68           
SHEET    1  CB 2 ASN C  63  VAL C  64  0                                        
SHEET    2  CB 2 ASN C  98  VAL C  99  1  O  ASN C  98   N  VAL C  64           
SHEET    1  CC 2 ARG C 164  GLU C 166  0                                        
SHEET    2  CC 2 GLY C 148  GLY C 155 -1  O  VAL C 153   N  GLU C 166           
SHEET    1  CD 2 ALA C 169  GLY C 171  0                                        
SHEET    2  CD 2 GLY C 148  GLY C 155 -1  O  ALA C 149   N  GLN C 170           
SHEET    1  CE 4 ILE C 182  THR C 191  0                                        
SHEET    2  CE 4 GLY C 194  PHE C 203 -1  O  GLY C 194   N  THR C 191           
SHEET    3  CE 4 GLY C 148  GLY C 155 -1  O  GLY C 148   N  PHE C 203           
SHEET    4  CE 4 ARG C 164  GLU C 166 -1  O  ARG C 164   N  GLY C 155           
SHEET    1  CF 4 ILE C 182  THR C 191  0                                        
SHEET    2  CF 4 GLY C 194  PHE C 203 -1  O  GLY C 194   N  THR C 191           
SHEET    3  CF 4 GLY C 148  GLY C 155 -1  O  GLY C 148   N  PHE C 203           
SHEET    4  CF 4 ALA C 169  GLY C 171 -1  O  GLN C 170   N  ALA C 149           
SHEET    1  DA 2 ILE D 126  THR D 127  0                                        
SHEET    2  DA 2 ALA D 147  VAL D 148 -1  O  ALA D 147   N  THR D 127           
SHEET    1  EA 3 LYS E   9  GLN E  20  0                                        
SHEET    2  EA 3 GLY E  23  GLY E  35 -1  O  GLY E  23   N  GLN E  20           
SHEET    3  EA 3 VAL E  41  ALA E  48 -1  O  GLY E  42   N  VAL E  34           
SHEET    1  EB 4 ILE E  80  PHE E  84  0                                        
SHEET    2  EB 4 SER E  87  PRO E  93 -1  O  SER E  87   N  PHE E  84           
SHEET    3  EB 4 ASP E 117  GLY E 124 -1  O  LEU E 119   N  LYS E  92           
SHEET    4  EB 4 GLY E  99  ILE E 101  1  O  GLY E  99   N  ILE E 118           
SHEET    1  FA 5 VAL F  37  VAL F  40  0                                        
SHEET    2  FA 5 TYR F  63  MET F  67 -1  O  GLN F  64   N  GLU F  38           
SHEET    3  FA 5 ARG F   2  LEU F  10 -1  O  ARG F   2   N  MET F  67           
SHEET    4  FA 5 ASP F  55  PHE F  60 -1  O  TYR F  59   N  LEU F  10           
SHEET    5  FA 5 GLY F  44  ILE F  52 -1  O  GLY F  44   N  PHE F  60           
SHEET    1  FB 4 VAL F  37  VAL F  40  0                                        
SHEET    2  FB 4 TYR F  63  MET F  67 -1  O  GLN F  64   N  GLU F  38           
SHEET    3  FB 4 ARG F   2  LEU F  10 -1  O  ARG F   2   N  MET F  67           
SHEET    4  FB 4 VAL F  85  LYS F  92 -1  N  ARG F  86   O  VAL F   9           
SHEET    1  FC 2 LEU F  98  ALA F  99  0                                        
SHEET    2  FC 2 PHE R  29  ASP R  30 -1  O  PHE R  29   N  ALA F  99           
SHEET    1  GA 2 MET G  73  SER G  77  0                                        
SHEET    2  GA 2 GLN G  86  GLU G  90 -1  O  VAL G  87   N  ARG G  76           
SHEET    1  HA 3 SER H  23  PRO H  27  0                                        
SHEET    2  HA 3 LYS H  56  LEU H  63 -1  O  LEU H  59   N  VAL H  26           
SHEET    3  HA 3 ILE H  45  VAL H  53 -1  N  LYS H  46   O  TYR H  62           
SHEET    1  HB 2 HIS H  82  ARG H  85  0                                        
SHEET    2  HB 2 GLY H 131  TRP H 138 -1  O  GLU H 136   N  ARG H  84           
SHEET    1  HC 2 TYR H  94  VAL H  95  0                                        
SHEET    2  HC 2 GLY H 131  TRP H 138  1  O  GLY H 131   N  VAL H  95           
SHEET    1  HD 4 GLY H 117  THR H 120  0                                        
SHEET    2  HD 4 ILE H 109  THR H 114 -1  O  LEU H 112   N  LEU H 119           
SHEET    3  HD 4 GLY H 131  TRP H 138 -1  O  GLU H 132   N  SER H 113           
SHEET    4  HD 4 TYR H  94  VAL H  95  1  O  VAL H  95   N  GLY H 131           
SHEET    1  HE 4 GLY H 117  THR H 120  0                                        
SHEET    2  HE 4 ILE H 109  THR H 114 -1  O  LEU H 112   N  LEU H 119           
SHEET    3  HE 4 GLY H 131  TRP H 138 -1  O  GLU H 132   N  SER H 113           
SHEET    4  HE 4 HIS H  82  ARG H  85 -1  O  HIS H  82   N  TRP H 138           
SHEET    1  IA 4 GLY I   6  ARG I  10  0                                        
SHEET    2  IA 4 ALA I  13  VAL I  17 -1  O  ALA I  13   N  ARG I  10           
SHEET    3  IA 4 ALA I  61  ARG I  66 -1  O  THR I  64   N  ARG I  16           
SHEET    4  IA 4 VAL I  26  THR I  27  1  O  THR I  27   N  ILE I  63           
SHEET    1  JA 4 VAL J  34  ARG J  43  0                                        
SHEET    2  JA 4 THR J  67  ILE J  74 -1  O  THR J  67   N  ARG J  43           
SHEET    3  JA 4 ILE J   4  GLY J  10 -1  O  ILE J   4   N  ILE J  74           
SHEET    4  JA 4 VAL J  94  ILE J  98 -1  O  GLU J  95   N  ARG J   9           
SHEET    1  JB 3 ARG J  46  ILE J  50  0                                        
SHEET    2  JB 3 ARG J  60  LEU J  65 -1  O  GLU J  61   N  VAL J  49           
SHEET    3  JB 3 VAL N  56  LYS N  58 -1  O  ARG N  57   N  GLU J  64           
SHEET    1  KA 6 PRO K  39  SER K  44  0                                        
SHEET    2  KA 6 THR K  28  THR K  33 -1  O  VAL K  30   N  SER K  43           
SHEET    3  KA 6 SER K  16  ALA K  23 -1  O  ARG K  18   N  THR K  33           
SHEET    4  KA 6 SER K  79  GLY K  86  1  O  SER K  79   N  GLY K  17           
SHEET    5  KA 6 GLN K 104  ASP K 110  1  O  GLN K 104   N  VAL K  80           
SHEET    6  KA 6 LEU R  85  VAL R  86 -1  O  LEU R  85   N  ASP K 110           
SHEET    1  LA 6 PHE L  32  VAL L  43  0                                        
SHEET    2  LA 6 VAL L  82  GLY L  87 -1  O  VAL L  83   N  GLY L  35           
SHEET    3  LA 6 TYR L  98  ILE L 100 -1  O  HIS L  99   N  ARG L  86           
SHEET    4  LA 6 GLU L  65  TYR L  69  1  O  TYR L  69   N  ILE L 100           
SHEET    5  LA 6 ARG L  53  LEU L  60 -1  O  ALA L  56   N  ALA L  68           
SHEET    6  LA 6 PHE L  32  VAL L  43 -1  O  VAL L  36   N  ARG L  59           
SHEET    1  PA 5 LEU P  49  VAL P  51  0                                        
SHEET    2  PA 5 LYS P  35  TYR P  39 -1  O  TYR P  38   N  LYS P  50           
SHEET    3  PA 5 HIS P  16  VAL P  20 -1  O  TYR P  17   N  TYR P  39           
SHEET    4  PA 5 LYS P   3  PHE P   9 -1  O  ARG P   5   N  VAL P  20           
SHEET    5  PA 5 GLN P  65  PRO P  66  1  O  GLN P  65   N  ILE P   4           
SHEET    1  QA 6 VAL Q   5  SER Q  12  0                                        
SHEET    2  QA 6 VAL Q  56  GLU Q  61 -1  O  VAL Q  57   N  GLY Q   8           
SHEET    3  QA 6 PHE Q  71  GLU Q  78 -1  O  ARG Q  72   N  ILE Q  60           
SHEET    4  QA 6 VAL Q  35  HIS Q  45  1  O  LEU Q  43   N  PHE Q  71           
SHEET    5  QA 6 THR Q  18  PRO Q  28 -1  O  VAL Q  19   N  ALA Q  44           
SHEET    6  QA 6 VAL Q   5  SER Q  12 -1  O  VAL Q   9   N  LEU Q  22           
SHEET    1  SA 3 LEU S  30  LYS S  32  0                                        
SHEET    2  SA 3 THR S  48  TYR S  52  1  O  THR S  48   N  ILE S  31           
SHEET    3  SA 3 HIS S  57  TYR S  61 -1  O  VAL S  58   N  VAL S  51           
SHEET    1  ZA 2 HIS Z  11  VAL Z  12  0                                        
SHEET    2  ZA 2 HIS Z  76  TYR Z  77  1  O  HIS Z  76   N  VAL Z  12           
SHEET    1  ZB 6 ALA Z  66  HIS Z  67  0                                        
SHEET    2  ZB 6 VAL Z  80  ASP Z  81 -1  O  ASP Z  81   N  ALA Z  66           
SHEET    3  ZB 6 VAL Z  14  GLY Z  18  1  O  VAL Z  14   N  VAL Z  80           
SHEET    4  ZB 6 GLY Z 101  SER Z 107  1  O  GLY Z 101   N  GLY Z  15           
SHEET    5  ZB 6 PHE Z 134  ASN Z 136  1  O  PHE Z 134   N  VAL Z 106           
SHEET    6  ZB 6 ILE Z 171  ARG Z 172  1  O  ILE Z 171   N  MET Z 135           
SHEET    1  ZC 5 LEU Z 222  PRO Z 224  0                                        
SHEET    2  ZC 5 VAL Z 303  ALA Z 305 -1  O  LEU Z 304   N  MET Z 223           
SHEET    3  ZC 5 GLU Z 252  VAL Z 256 -1  O  GLU Z 254   N  ALA Z 305           
SHEET    4  ZC 5 ARG Z 263  MET Z 272 -1  O  ARG Z 263   N  ILE Z 255           
SHEET    5  ZC 5 LYS Z 275  THR Z 276 -1  O  LYS Z 275   N  MET Z 272           
SHEET    1  ZD 7 LEU Z 222  PRO Z 224  0                                        
SHEET    2  ZD 7 VAL Z 303  ALA Z 305 -1  O  LEU Z 304   N  MET Z 223           
SHEET    3  ZD 7 GLU Z 252  VAL Z 256 -1  O  GLU Z 254   N  ALA Z 305           
SHEET    4  ZD 7 ARG Z 263  MET Z 272 -1  O  ARG Z 263   N  ILE Z 255           
SHEET    5  ZD 7 GLY Z 287  LEU Z 290 -1  O  GLY Z 287   N  GLU Z 271           
SHEET    6  ZD 7 GLY Z 235  ALA Z 238 -1  O  THR Z 236   N  LEU Z 290           
SHEET    7  ZD 7 VAL Z 228  ILE Z 231 -1  O  PHE Z 229   N  VAL Z 237           
SHEET    1  ZE 2 LYS Z 275  THR Z 276  0                                        
SHEET    2  ZE 2 ARG Z 263  MET Z 272 -1  O  MET Z 272   N  LYS Z 275           
SHEET    1  ZF 2 LYS Z 246  VAL Z 247  0                                        
SHEET    2  ZF 2 GLY Z 280  ILE Z 281 -1  O  GLY Z 280   N  VAL Z 247           
SHEET    1  ZG 2 HIS Z 313  GLU Z 317  0                                        
SHEET    2  ZG 2 THR Z 371  VAL Z 378 -1  O  VAL Z 372   N  PHE Z 316           
SHEET    1  ZH 4 VAL Z 349  THR Z 350  0                                        
SHEET    2  ZH 4 GLN Z 341  PHE Z 342 -1  O  PHE Z 342   N  VAL Z 349           
SHEET    3  ZH 4 ARG Z 385  ARG Z 389 -1  O  ARG Z 389   N  GLN Z 341           
SHEET    4  ZH 4 THR Z 394  VAL Z 399 -1  O  GLY Z 396   N  ILE Z 388           
LINK        ZN    ZN 1   4                 SG  CYS D  12     1555   1555  2.48  
LINK        ZN    ZN 1   4                 SG  CYS D  26     1555   1555  2.35  
LINK        ZN    ZN 1   4                 SG  CYS D  31     1555   1555  2.29  
LINK        ZN    ZN 1   4                 SG  CYS D   9     1555   1555  1.92  
LINK        ZN    ZN 1   4                 O   CYS D  31     1555   1555  2.58  
LINK        ZN    ZN 1   5                 SG  CYS N  24     1555   1555  2.53  
LINK        ZN    ZN 1   5                 SG  CYS N  40     1555   1555  2.19  
LINK        ZN    ZN 1   5                 SG  CYS N  43     1555   1555  2.08  
LINK        ZN    ZN 1   5                 SG  CYS N  27     1555   1555  2.21  
LINK         O3'   G A  73                 P     C A  76     1555   1555  1.61  
LINK         O3'   U A  84                 P     A A  88     1555   1555  1.61  
LINK         O3'   G A  93                 P     U A  96     1555   1555  1.61  
LINK         O3'   U A 204                 P     G A 216     1555   1555  1.61  
LINK         O3'   A A 439                 P     A A 441     1555   1555  1.61  
LINK         O3'   C A 458                 P     G A 460     1555   1555  1.60  
LINK         O3'   A A 461                 P     C A 470     1555   1555  1.60  
LINK         O3'   A A 477                 P     C A 479     1555   1555  1.61  
LINK         O3'   A A 496                 P     U A 498     1555   1555  1.61  
LINK         O3'   U A 841                 P     C A 848     1555   1555  1.62  
LINK         O3'   G A1166                 P     A A1168     1555   1555  1.60  
LINK         O3'   A A1447                 P     C A1452     1555   1555  1.62  
LINK         O3'   C A1452                 P     G A1456     1555   1555  1.61  
LINK         O3'   G Y   7                 P   4SU Y   8     1555   1555  1.61  
LINK         O3' 4SU Y   8                 P     C Y   9     1555   1555  1.61  
LINK         O3'   A Y  15                 P   H2U Y  16     1555   1555  1.62  
LINK         O3' H2U Y  16                 P   H2U Y  17     1555   1555  1.62  
LINK         O3' H2U Y  17                 P     G Y  18     1555   1555  1.62  
LINK         O3'   G Y  19                 P   H2U Y  20     1555   1555  1.61  
LINK         O3' H2U Y  20                 P     A Y  21     1555   1555  1.61  
LINK         O3'   U Y  31                 P   OMC Y  32     1555   1555  1.61  
LINK         O3' OMC Y  32                 P     U Y  33     1555   1555  1.61  
LINK         O3'   A Y  36                 P   MIA Y  37     1555   1555  1.60  
LINK         O3' MIA Y  37                 P     A Y  38     1555   1555  1.61  
LINK         O3'   U Y  45                 P   7MG Y  46     1555   1555  1.62  
LINK         O3' 7MG Y  46                 P     U Y  47     1555   1555  1.61  
LINK         O3'   G Y  53                 P   5MU Y  54     1555   1555  1.61  
LINK         O3' 5MU Y  54                 P   PSU Y  55     1555   1555  1.61  
LINK         O3' PSU Y  55                 P     C Y  56     1555   1555  1.62  
CRYST1  289.900  268.500  403.600  90.00  91.62  90.00 P 1 21 1      2          
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      0.003449  0.000000  0.000098        0.00000                         
SCALE2      0.000000  0.003724  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002479        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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