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Database: PDB
Entry: 3FIH
LinkDB: 3FIH
Original site: 3FIH 
HEADER    RIBOSOME                                11-DEC-08   3FIH              
TITLE     TERNARY COMPLEX-BOUND E.COLI 70S RIBOSOME. THIS ENTRY CONSISTS OF THE 
TITLE    2 30S SUBUNIT, TRNAS AND THE TERNARY COMPLEX.                          
SPLIT      3FIK 3FIH                                                            
CAVEAT     3FIH    CHIRALITY ERRORS AT C1' CENTER OF C 17, C1' CENTER OF U 47,  
CAVEAT   2 3FIH     C3' CENTER OF G 70 IN CHAIN V AND C1' CENTER OF C17 IN      
CAVEAT   3 3FIH     CHAIN W. THE CHIRALITY ERRORS ARE INHERITED FROM STARTING   
CAVEAT   4 3FIH     MODEL 2J00                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 30S RIBOSOMAL PROTEIN S10;                                 
COMPND   3 CHAIN: J;                                                            
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: 30S RIBOSOMAL PROTEIN S11;                                 
COMPND   6 CHAIN: K;                                                            
COMPND   7 MOL_ID: 3;                                                           
COMPND   8 MOLECULE: 30S RIBOSOMAL PROTEIN S12;                                 
COMPND   9 CHAIN: L;                                                            
COMPND  10 MOL_ID: 4;                                                           
COMPND  11 MOLECULE: 30S RIBOSOMAL PROTEIN S13;                                 
COMPND  12 CHAIN: M;                                                            
COMPND  13 MOL_ID: 5;                                                           
COMPND  14 MOLECULE: 30S RIBOSOMAL PROTEIN S14;                                 
COMPND  15 CHAIN: N;                                                            
COMPND  16 MOL_ID: 6;                                                           
COMPND  17 MOLECULE: 30S RIBOSOMAL PROTEIN S15;                                 
COMPND  18 CHAIN: O;                                                            
COMPND  19 MOL_ID: 7;                                                           
COMPND  20 MOLECULE: 30S RIBOSOMAL PROTEIN S16;                                 
COMPND  21 CHAIN: P;                                                            
COMPND  22 MOL_ID: 8;                                                           
COMPND  23 MOLECULE: 30S RIBOSOMAL PROTEIN S17;                                 
COMPND  24 CHAIN: Q;                                                            
COMPND  25 MOL_ID: 9;                                                           
COMPND  26 MOLECULE: 30S RIBOSOMAL PROTEIN S18;                                 
COMPND  27 CHAIN: R;                                                            
COMPND  28 MOL_ID: 10;                                                          
COMPND  29 MOLECULE: 30S RIBOSOMAL PROTEIN S19;                                 
COMPND  30 CHAIN: S;                                                            
COMPND  31 MOL_ID: 11;                                                          
COMPND  32 MOLECULE: 30S RIBOSOMAL PROTEIN S20;                                 
COMPND  33 CHAIN: T;                                                            
COMPND  34 MOL_ID: 12;                                                          
COMPND  35 MOLECULE: 30S RIBOSOMAL PROTEIN S21;                                 
COMPND  36 CHAIN: U;                                                            
COMPND  37 MOL_ID: 13;                                                          
COMPND  38 MOLECULE: 30S RIBOSOMAL PROTEIN S2;                                  
COMPND  39 CHAIN: B;                                                            
COMPND  40 MOL_ID: 14;                                                          
COMPND  41 MOLECULE: 30S RIBOSOMAL PROTEIN S3;                                  
COMPND  42 CHAIN: C;                                                            
COMPND  43 MOL_ID: 15;                                                          
COMPND  44 MOLECULE: 30S RIBOSOMAL PROTEIN S4;                                  
COMPND  45 CHAIN: D;                                                            
COMPND  46 MOL_ID: 16;                                                          
COMPND  47 MOLECULE: 30S RIBOSOMAL PROTEIN S5;                                  
COMPND  48 CHAIN: E;                                                            
COMPND  49 MOL_ID: 17;                                                          
COMPND  50 MOLECULE: 30S RIBOSOMAL PROTEIN S6;                                  
COMPND  51 CHAIN: F;                                                            
COMPND  52 MOL_ID: 18;                                                          
COMPND  53 MOLECULE: 30S RIBOSOMAL PROTEIN S7;                                  
COMPND  54 CHAIN: G;                                                            
COMPND  55 MOL_ID: 19;                                                          
COMPND  56 MOLECULE: 30S RIBOSOMAL PROTEIN S8;                                  
COMPND  57 CHAIN: H;                                                            
COMPND  58 MOL_ID: 20;                                                          
COMPND  59 MOLECULE: 30S RIBOSOMAL PROTEIN S9;                                  
COMPND  60 CHAIN: I;                                                            
COMPND  61 MOL_ID: 21;                                                          
COMPND  62 MOLECULE: 16S RRNA;                                                  
COMPND  63 CHAIN: A;                                                            
COMPND  64 MOL_ID: 22;                                                          
COMPND  65 MOLECULE: A/T-SITE TRNA PHE;                                         
COMPND  66 CHAIN: Y;                                                            
COMPND  67 ENGINEERED: YES;                                                     
COMPND  68 MOL_ID: 23;                                                          
COMPND  69 MOLECULE: P-SITE TRNA FMET (UNMODIFIED BASES EXCEPT FOR THYMINE 54); 
COMPND  70 CHAIN: W;                                                            
COMPND  71 MOL_ID: 24;                                                          
COMPND  72 MOLECULE: MRNA;                                                      
COMPND  73 CHAIN: X;                                                            
COMPND  74 ENGINEERED: YES;                                                     
COMPND  75 MOL_ID: 25;                                                          
COMPND  76 MOLECULE: ELONGATION FACTOR TU;                                      
COMPND  77 CHAIN: Z;                                                            
COMPND  78 MOL_ID: 26;                                                          
COMPND  79 MOLECULE: E-SITE TRNA PHE;                                           
COMPND  80 CHAIN: V                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   6 ORGANISM_TAXID: 562;                                                 
SOURCE   7 MOL_ID: 3;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   9 ORGANISM_TAXID: 562;                                                 
SOURCE  10 MOL_ID: 4;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  12 ORGANISM_TAXID: 562;                                                 
SOURCE  13 MOL_ID: 5;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  15 ORGANISM_TAXID: 562;                                                 
SOURCE  16 MOL_ID: 6;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  18 ORGANISM_TAXID: 562;                                                 
SOURCE  19 MOL_ID: 7;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  21 ORGANISM_TAXID: 562;                                                 
SOURCE  22 MOL_ID: 8;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  24 ORGANISM_TAXID: 562;                                                 
SOURCE  25 MOL_ID: 9;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  27 ORGANISM_TAXID: 562;                                                 
SOURCE  28 MOL_ID: 10;                                                          
SOURCE  29 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  30 ORGANISM_TAXID: 562;                                                 
SOURCE  31 MOL_ID: 11;                                                          
SOURCE  32 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  33 ORGANISM_TAXID: 562;                                                 
SOURCE  34 MOL_ID: 12;                                                          
SOURCE  35 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  36 ORGANISM_TAXID: 562;                                                 
SOURCE  37 MOL_ID: 13;                                                          
SOURCE  38 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  39 ORGANISM_TAXID: 562;                                                 
SOURCE  40 MOL_ID: 14;                                                          
SOURCE  41 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  42 ORGANISM_TAXID: 562;                                                 
SOURCE  43 MOL_ID: 15;                                                          
SOURCE  44 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  45 ORGANISM_TAXID: 562;                                                 
SOURCE  46 MOL_ID: 16;                                                          
SOURCE  47 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  48 ORGANISM_TAXID: 562;                                                 
SOURCE  49 MOL_ID: 17;                                                          
SOURCE  50 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  51 ORGANISM_TAXID: 562;                                                 
SOURCE  52 MOL_ID: 18;                                                          
SOURCE  53 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  54 ORGANISM_TAXID: 562;                                                 
SOURCE  55 MOL_ID: 19;                                                          
SOURCE  56 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  57 ORGANISM_TAXID: 562;                                                 
SOURCE  58 MOL_ID: 20;                                                          
SOURCE  59 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  60 ORGANISM_TAXID: 562;                                                 
SOURCE  61 MOL_ID: 21;                                                          
SOURCE  62 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  63 ORGANISM_TAXID: 562;                                                 
SOURCE  64 MOL_ID: 22;                                                          
SOURCE  65 SYNTHETIC: YES;                                                      
SOURCE  66 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN YEAST.;             
SOURCE  67 MOL_ID: 23;                                                          
SOURCE  68 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  69 ORGANISM_TAXID: 562;                                                 
SOURCE  70 MOL_ID: 24;                                                          
SOURCE  71 SYNTHETIC: YES;                                                      
SOURCE  72 OTHER_DETAILS: MRNA WAS SYNTHETICALLY CONTSTRUCTED;                  
SOURCE  73 MOL_ID: 25;                                                          
SOURCE  74 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  75 ORGANISM_TAXID: 562;                                                 
SOURCE  76 MOL_ID: 26;                                                          
SOURCE  77 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  78 ORGANISM_TAXID: 562                                                  
KEYWDS    RIBOSOME, TERNARY COMPLEX, FLEXIBLE FITTING, CRYO-EM, 30S, 50S, TRNA, 
KEYWDS   2 MRNA, EF-TU, 70S, RIBONUCLEOPROTEIN, RIBOSOMAL PROTEIN, RNA-BINDING, 
KEYWDS   3 RRNA-BINDING, ANTIBIOTIC RESISTANCE, REPRESSOR, TRANSCRIPTION,       
KEYWDS   4 TRANSCRIPTION REGULATION, TRANSCRIPTION TERMINATION, TRANSLATION     
KEYWDS   5 REGULATION, TRNA-BINDING, METHYLATION, ENDONUCLEASE, HYDROLASE,      
KEYWDS   6 NUCLEASE, CELL MEMBRANE, ELONGATION FACTOR, GTP-BINDING, MEMBRANE,   
KEYWDS   7 NUCLEOTIDE-BINDING, PHOSPHOPROTEIN, PROTEIN BIOSYNTHESIS             
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    E.VILLA,J.SENGUPTA,L.G.TRABUCO,J.LEBARRON,W.T.BAXTER,T.R.SHAIKH,      
AUTHOR   2 R.A.GRASSUCCI,P.NISSEN,M.EHRENBERG,K.SCHULTEN,J.FRANK                
REVDAT   3   15-FEB-12 3FIH    1       REMARK VERSN                             
REVDAT   2   02-JUN-09 3FIH    1       ATOM                                     
REVDAT   1   03-MAR-09 3FIH    0                                                
JRNL        AUTH   E.VILLA,J.SENGUPTA,L.G.TRABUCO,J.LEBARRON,W.T.BAXTER,        
JRNL        AUTH 2 T.R.SHAIKH,R.A.GRASSUCCI,P.NISSEN,M.EHRENBERG,K.SCHULTEN,    
JRNL        AUTH 3 J.FRANK                                                      
JRNL        TITL   RIBOSOME-INDUCED CHANGES IN ELONGATION FACTOR TU             
JRNL        TITL 2 CONFORMATION CONTROL GTP HYDROLYSIS                          
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 106  1063 2009              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   19122150                                                     
JRNL        DOI    10.1073/PNAS.0811370106                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   L.TRABUCO,E.VILLA,K.MITRA,J.FRANK,K.SCHULTEN                 
REMARK   1  TITL   FLEXIBLE FITTING OF ATOMIC STRUCTURES INTO ELECTRON          
REMARK   1  TITL 2 MICROSCOPY MAPS USING MOLECULAR DYNAMICS.                    
REMARK   1  REF    STRUCTURE                     V.  16   673 2008              
REMARK   1  REFN                   ISSN 0969-2126                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   J.LEBARRON,R.A.GRASSUCCI,T.R.SHAIKH,W.T.BAXTER,J.SENGUPTA,   
REMARK   1  AUTH 2 J.FRANK                                                      
REMARK   1  TITL   EXPLORATION OF PARAMETERS IN CRYO-EM LEADING TO AN IMPROVED  
REMARK   1  TITL 2 DENSITY MAP OF THE E. COLI RIBOSOME                          
REMARK   1  REF    J.STRUCT.BIOL.                V. 164    24 2008              
REMARK   1  REFN                   ISSN 1047-8477                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    6.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : MOLECULAR DYNAMICS FLEXIBLE FITTING       
REMARK   3                            (MDFF)                                    
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 2I2U, 2I2V, 2J00, 1OB2              
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : FLEXIBLE FITTING                    
REMARK   3   REFINEMENT TARGET            : CROSS CORRELATION, ROOT-MEAN        
REMARK   3                                  SQUARE DEVIATION                    
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : SEE TRABUCO ET AL., STRUCTURE 16 (2008) 673-     
REMARK   3  683.                                                                
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : 1.200                          
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 6.700                          
REMARK   3   NUMBER OF PARTICLES               : NULL                           
REMARK   3   CTF CORRECTION METHOD             : CORRECTION OF RECONSTRUCTION   
REMARK   3                                       OF EACH DEFOCUS GROUP          
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: SEE LEBARRON ET AL., JSB 164 (2008) 24-32.            
REMARK   4                                                                      
REMARK   4 3FIH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB050631.                                      
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : VITREOUS ICE (CRYO EM)            
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : ASYMMETRIC                        
REMARK 245   NAME OF SAMPLE                 : E. COLI RIBOSOME IN COMPLEX       
REMARK 245                                    WITH THE TERNARY COMPLEX EF-TU    
REMARK 245                                    AMINOACYL-TRNA GDP                
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 0.08                              
REMARK 245   SAMPLE SUPPORT DETAILS         : THIN CARBON ON 300 MESH           
REMARK 245                                    QUANTIFOIL R2/4                   
REMARK 245   SAMPLE VITRIFICATION DETAILS   : VITRIFICATION USING FEI           
REMARK 245                                    VITROBOT; BLOT 3 SECONDS BEFORE   
REMARK 245                                    PLUNGING WITH AN OFFSET OF -1MM   
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.50                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : 31-AUG-06                      
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : 84.00                          
REMARK 245   MICROSCOPE MODEL                  : FEI POLARA 300                 
REMARK 245   DETECTOR TYPE                     : KODAK SO163 FILM               
REMARK 245   MINIMUM DEFOCUS (NM)              : 4520.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 1200.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : NULL                           
REMARK 245   IMAGING MODE                      : MAGNIFICATION                  
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 20.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 59000                          
REMARK 245   CALIBRATED MAGNIFICATION          : 58279                          
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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: J, K, L, M, N, O, P, Q, R,            
REMARK 350                    AND CHAINS: S, T, U, B, C, D, E, F, G,            
REMARK 350                    AND CHAINS: H, I, A, Y, W, X, Z, V                
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 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     SER Z   1    OG                                                  
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    ARG J  45   CZ    ARG J  45   NH2     0.092                       
REMARK 500    HIS J  56   CG    HIS J  56   CD2     0.084                       
REMARK 500    ARG J  62   NE    ARG J  62   CZ      0.105                       
REMARK 500    TYR J  65   CZ    TYR J  65   OH      0.107                       
REMARK 500    ARG J  72   CZ    ARG J  72   NH2     0.085                       
REMARK 500    SER J 101   CA    SER J 101   CB      0.110                       
REMARK 500    HIS K  23   CG    HIS K  23   CD2     0.059                       
REMARK 500    ARG K  52   NE    ARG K  52   CZ      0.087                       
REMARK 500    ARG K 121   CZ    ARG K 121   NH2     0.091                       
REMARK 500    PRO K 123   CD    PRO K 123   N      -0.094                       
REMARK 500    ARG K 127   NE    ARG K 127   CZ      0.083                       
REMARK 500    ARG L  55   NE    ARG L  55   CZ      0.089                       
REMARK 500    ARG L  98   CZ    ARG L  98   NH2     0.092                       
REMARK 500    ARG M  78   NE    ARG M  78   CZ      0.099                       
REMARK 500    TYR M  85   CE1   TYR M  85   CZ      0.091                       
REMARK 500    ARG M 100   CZ    ARG M 100   NH2     0.079                       
REMARK 500    ARG N  12   CZ    ARG N  12   NH2     0.080                       
REMARK 500    ARG N  84   NE    ARG N  84   CZ      0.084                       
REMARK 500    PRO N  93   N     PRO N  93   CA     -0.104                       
REMARK 500    ARG O  76   NE    ARG O  76   CZ      0.096                       
REMARK 500    ARG O  87   CZ    ARG O  87   NH2     0.083                       
REMARK 500    ARG P   8   NE    ARG P   8   CZ      0.085                       
REMARK 500    ARG P  25   CD    ARG P  25   NE      0.116                       
REMARK 500    ARG P  31   CZ    ARG P  31   NH1     0.098                       
REMARK 500    GLY P  37   CA    GLY P  37   C      -0.120                       
REMARK 500    PHE P  39   CG    PHE P  39   CD2     0.112                       
REMARK 500    ARG P  51   CZ    ARG P  51   NH1     0.092                       
REMARK 500    ARG P  56   NE    ARG P  56   CZ      0.085                       
REMARK 500    ARG Q   5   CD    ARG Q   5   NE      0.105                       
REMARK 500    ARG Q  26   CZ    ARG Q  26   NH2     0.078                       
REMARK 500    ARG Q  61   CZ    ARG Q  61   NH2     0.097                       
REMARK 500    GLU Q  79   CG    GLU Q  79   CD      0.100                       
REMARK 500    TYR R  50   CG    TYR R  50   CD2     0.107                       
REMARK 500    TYR R  69   CZ    TYR R  69   CE2     0.079                       
REMARK 500    ARG S  31   CZ    ARG S  31   NH2     0.082                       
REMARK 500    ARG S  36   CD    ARG S  36   NE      0.111                       
REMARK 500    ARG S  36   CZ    ARG S  36   NH2     0.104                       
REMARK 500    ARG S  77   CZ    ARG S  77   NH2     0.078                       
REMARK 500    ARG S  80   CD    ARG S  80   NE      0.120                       
REMARK 500    ARG T   9   CZ    ARG T   9   NH2     0.080                       
REMARK 500    ARG T  17   CZ    ARG T  17   NH2     0.089                       
REMARK 500    ARG T  73   CD    ARG T  73   NE      0.122                       
REMARK 500    GLU U   7   CG    GLU U   7   CD      0.100                       
REMARK 500    ARG U  32   NE    ARG U  32   CZ      0.084                       
REMARK 500    ARG U  34   NE    ARG U  34   CZ      0.088                       
REMARK 500    TYR U  37   CG    TYR U  37   CD2     0.081                       
REMARK 500    ARG B  34   NE    ARG B  34   CZ      0.084                       
REMARK 500    SER B  85   CA    SER B  85   CB      0.091                       
REMARK 500    ARG B 136   CD    ARG B 136   NE      0.127                       
REMARK 500    ASP B 166   CA    ASP B 166   CB      0.134                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS    4090 BOND DEVIATIONS.                              
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    ARG J   5   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG J   9   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG J   9   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    PHE J  49   CB  -  CG  -  CD2 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    TYR J  65   CD1 -  CG  -  CD2 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    TYR J  65   CB  -  CG  -  CD1 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    TYR J  65   CG  -  CD2 -  CE2 ANGL. DEV. =  -7.8 DEGREES          
REMARK 500    ARG K  12   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ALA K  24   N   -  CA  -  CB  ANGL. DEV. =   9.6 DEGREES          
REMARK 500    THR K  32   N   -  CA  -  CB  ANGL. DEV. =  12.9 DEGREES          
REMARK 500    ARG K  36   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    PHE K  51   CB  -  CG  -  CD2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ARG K  55   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG K  68   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    MET K  84   CG  -  SD  -  CE  ANGL. DEV. = -11.1 DEGREES          
REMARK 500    ARG K  97   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG K 121   NE  -  CZ  -  NH1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ARG K 121   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ARG K 126   NH1 -  CZ  -  NH2 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ARG K 126   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ARG L   8   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG L  13   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG L  13   NE  -  CZ  -  NH2 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG L  30   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG L  35   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG L  49   CB  -  CG  -  CD  ANGL. DEV. =  16.1 DEGREES          
REMARK 500    TYR L  65   CB  -  CG  -  CD1 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ARG L  85   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    ARG L  85   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG L 109   NE  -  CZ  -  NH1 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    ARG L 109   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG L 113   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.1 DEGREES          
REMARK 500    TYR L 116   CZ  -  CE2 -  CD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ARG M   2   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    TYR M  22   CG  -  CD2 -  CE2 ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    ARG M  28   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    GLU M  46   CB  -  CA  -  C   ANGL. DEV. = -12.0 DEGREES          
REMARK 500    ARG M  56   NE  -  CZ  -  NH2 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG M  69   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG M  69   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ARG M  78   N   -  CA  -  CB  ANGL. DEV. =  11.1 DEGREES          
REMARK 500    ARG M  78   NH1 -  CZ  -  NH2 ANGL. DEV. =   7.6 DEGREES          
REMARK 500    ARG M  78   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ARG M  86   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ARG M  91   NE  -  CZ  -  NH1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG M  97   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    ARG M 106   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG M 108   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG N  12   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG N  12   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS    7521 ANGLE DEVIATIONS.                             
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    ARG J  16       41.66    -70.31                                   
REMARK 500    LEU J  17      -50.72   -175.72                                   
REMARK 500    THR J  22      -11.50   -149.32                                   
REMARK 500    ALA J  34       -2.25   -157.25                                   
REMARK 500    PRO J  41      179.87    -54.19                                   
REMARK 500    ARG J  48      134.38   -175.35                                   
REMARK 500    HIS J  56      128.96    179.15                                   
REMARK 500    VAL J  57     -146.46     46.94                                   
REMARK 500    ASN J  58       73.71     44.12                                   
REMARK 500    ILE J  67       93.08   -176.04                                   
REMARK 500    VAL J  74      -80.17     87.01                                   
REMARK 500    ASP J  75       61.99     82.96                                   
REMARK 500    ASP J  85      -77.01    -48.04                                   
REMARK 500    SER K  16      -35.50     79.85                                   
REMARK 500    ASP K  35     -173.92    -56.40                                   
REMARK 500    LEU K  41      -53.25   -135.79                                   
REMARK 500    PHE K  51     -129.07   -142.62                                   
REMARK 500    ARG K  52     -119.66    -85.29                                   
REMARK 500    SER K  54        7.33   -154.50                                   
REMARK 500    SER K  57      -18.51   -150.57                                   
REMARK 500    LYS K  79       -9.64   -148.65                                   
REMARK 500    ALA K 101       28.41    -63.60                                   
REMARK 500    ALA K 102       16.11   -146.96                                   
REMARK 500    THR K 107       -3.76   -143.68                                   
REMARK 500    ILE K 109      -24.41   -142.59                                   
REMARK 500    ASN K 118      120.02    106.33                                   
REMARK 500    CYS K 120      162.98    -44.23                                   
REMARK 500    LYS K 125      175.68     57.54                                   
REMARK 500    ALA L  22        0.85   -151.33                                   
REMARK 500    GLU L  24     -148.42     29.45                                   
REMARK 500    ALA L  25        7.34   -162.18                                   
REMARK 500    ARG L  35      149.28   -170.89                                   
REMARK 500    LYS L  43      148.21     80.62                                   
REMARK 500    VAL L  62     -175.89    -53.02                                   
REMARK 500    ALA L 100      152.29     63.65                                   
REMARK 500    LEU L 101     -149.14     60.68                                   
REMARK 500    TYR L 116       -6.28     76.09                                   
REMARK 500    ARG M   2      -19.22   -148.32                                   
REMARK 500    ILE M   3      -78.49     96.14                                   
REMARK 500    ALA M   4      -21.24   -150.56                                   
REMARK 500    ILE M   6      114.78     64.42                                   
REMARK 500    ILE M  16      -70.18    -37.47                                   
REMARK 500    THR M  19     -161.88     49.35                                   
REMARK 500    ILE M  21       59.80   -152.65                                   
REMARK 500    TYR M  22      110.53     71.32                                   
REMARK 500    VAL M  24      107.31   -161.61                                   
REMARK 500    SER M  29      -89.33    -59.83                                   
REMARK 500    ASP M  41       57.38   -109.05                                   
REMARK 500    GLU M  65     -154.11     44.68                                   
REMARK 500    CYS M  84      160.05    -46.14                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     345 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY K   89     PRO K   90                 -142.68                    
REMARK 500 VAL L   20     PRO L   21                 -140.66                    
REMARK 500 ASN M  104     ALA M  105                 -147.22                    
REMARK 500 ASP O   20     THR O   21                 -146.29                    
REMARK 500 PHE B   68     VAL B   69                 -148.63                    
REMARK 500 TYR C  167     ARG C  168                  139.38                    
REMARK 500 ASP G   14     PRO G   15                 -147.85                    
REMARK 500 ILE H  125     CYS H  126                 -149.88                    
REMARK 500 ASN Z   51     ALA Z   52                  -32.03                    
REMARK 500 TYR Z  160     ASP Z  161                  147.04                    
REMARK 500 LYS Z  208     PRO Z  209                  141.42                    
REMARK 500 ASP Z  354     ASN Z  355                  149.88                    
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    ARG J   9         0.13    SIDE CHAIN                              
REMARK 500    ARG J  16         0.10    SIDE CHAIN                              
REMARK 500    ARG J  68         0.10    SIDE CHAIN                              
REMARK 500    PHE K  26         0.08    SIDE CHAIN                              
REMARK 500    ARG K  55         0.08    SIDE CHAIN                              
REMARK 500    ARG K  97         0.10    SIDE CHAIN                              
REMARK 500    ARG L  13         0.10    SIDE CHAIN                              
REMARK 500    ARG L  30         0.11    SIDE CHAIN                              
REMARK 500    ARG L  49         0.11    SIDE CHAIN                              
REMARK 500    ARG L  53         0.12    SIDE CHAIN                              
REMARK 500    TYR L  65         0.12    SIDE CHAIN                              
REMARK 500    ARG L  93         0.09    SIDE CHAIN                              
REMARK 500    ARG M   2         0.09    SIDE CHAIN                              
REMARK 500    TYR M  22         0.09    SIDE CHAIN                              
REMARK 500    ARG M 100         0.22    SIDE CHAIN                              
REMARK 500    ARG N  12         0.11    SIDE CHAIN                              
REMARK 500    ARG N  52         0.13    SIDE CHAIN                              
REMARK 500    ARG N  62         0.09    SIDE CHAIN                              
REMARK 500    ARG N  68         0.09    SIDE CHAIN                              
REMARK 500    ARG N  84         0.10    SIDE CHAIN                              
REMARK 500    ARG O  16         0.10    SIDE CHAIN                              
REMARK 500    ARG O  57         0.12    SIDE CHAIN                              
REMARK 500    ARG O  62         0.09    SIDE CHAIN                              
REMARK 500    ARG O  79         0.13    SIDE CHAIN                              
REMARK 500    HIS P   9         0.07    SIDE CHAIN                              
REMARK 500    TYR P  17         0.07    SIDE CHAIN                              
REMARK 500    ARG P  25         0.11    SIDE CHAIN                              
REMARK 500    HIS Q  30         0.10    SIDE CHAIN                              
REMARK 500    TYR R  22         0.12    SIDE CHAIN                              
REMARK 500    TYR R  31         0.10    SIDE CHAIN                              
REMARK 500    ARG R  47         0.10    SIDE CHAIN                              
REMARK 500    TYR R  69         0.07    SIDE CHAIN                              
REMARK 500    TYR S  79         0.07    SIDE CHAIN                              
REMARK 500    ARG T   9         0.09    SIDE CHAIN                              
REMARK 500    ARG T  17         0.12    SIDE CHAIN                              
REMARK 500    ARG T  24         0.10    SIDE CHAIN                              
REMARK 500    ARG U   6         0.10    SIDE CHAIN                              
REMARK 500    ARG U  20         0.10    SIDE CHAIN                              
REMARK 500    TYR U  37         0.12    SIDE CHAIN                              
REMARK 500    ARG U  44         0.09    SIDE CHAIN                              
REMARK 500    ARG U  46         0.12    SIDE CHAIN                              
REMARK 500    PHE B  29         0.10    SIDE CHAIN                              
REMARK 500    PHE B  89         0.08    SIDE CHAIN                              
REMARK 500    ARG B 107         0.09    SIDE CHAIN                              
REMARK 500    ARG C  53         0.10    SIDE CHAIN                              
REMARK 500    ARG C  71         0.08    SIDE CHAIN                              
REMARK 500    ARG C 155         0.12    SIDE CHAIN                              
REMARK 500    ARG C 163         0.13    SIDE CHAIN                              
REMARK 500    PHE D  19         0.08    SIDE CHAIN                              
REMARK 500    TYR D  50         0.14    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     908 PLANE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ARG M 108        -11.20                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500      U A 137       -45.3      D          D   OUTSIDE RANGE           
REMARK 500      A A1394       -45.2      D          D   OUTSIDE RANGE           
REMARK 500      C W  17        33.5      D          L   WRONG HAND              
REMARK 500      U W  47        33.0      D          L   WRONG HAND              
REMARK 500    VAL J  57        22.6      L          L   OUTSIDE RANGE           
REMARK 500    VAL L  62        23.8      L          L   OUTSIDE RANGE           
REMARK 500    ALA L 100        24.6      L          L   OUTSIDE RANGE           
REMARK 500    TYR L 116        22.7      L          L   OUTSIDE RANGE           
REMARK 500    ILE M   6        23.7      L          L   OUTSIDE RANGE           
REMARK 500    TYR M  22        24.8      L          L   OUTSIDE RANGE           
REMARK 500    ILE M  52        22.8      L          L   OUTSIDE RANGE           
REMARK 500    ARG M  78        24.5      L          L   OUTSIDE RANGE           
REMARK 500    VAL N  44        22.6      L          L   OUTSIDE RANGE           
REMARK 500    ASP N  53        23.3      L          L   OUTSIDE RANGE           
REMARK 500    ILE O  35        24.1      L          L   OUTSIDE RANGE           
REMARK 500    HIS O  45        22.3      L          L   OUTSIDE RANGE           
REMARK 500    GLU O  82        20.1      L          L   OUTSIDE RANGE           
REMARK 500    LEU O  86        24.9      L          L   OUTSIDE RANGE           
REMARK 500    GLU P  48        23.5      L          L   OUTSIDE RANGE           
REMARK 500    LYS Q  18        23.8      L          L   OUTSIDE RANGE           
REMARK 500    HIS S  13        24.8      L          L   OUTSIDE RANGE           
REMARK 500    GLN T  54        24.1      L          L   OUTSIDE RANGE           
REMARK 500    VAL U  31        24.9      L          L   OUTSIDE RANGE           
REMARK 500    LEU B 213        23.9      L          L   OUTSIDE RANGE           
REMARK 500    ASP C  82        23.9      L          L   OUTSIDE RANGE           
REMARK 500    ASP C 111        23.9      L          L   OUTSIDE RANGE           
REMARK 500    ASN E  69        24.2      L          L   OUTSIDE RANGE           
REMARK 500    VAL E 116        23.5      L          L   OUTSIDE RANGE           
REMARK 500    VAL F  18        23.7      L          L   OUTSIDE RANGE           
REMARK 500    ARG G 118        24.9      L          L   OUTSIDE RANGE           
REMARK 500    GLN I  49        23.1      L          L   OUTSIDE RANGE           
REMARK 500    ASP I  55        24.7      L          L   OUTSIDE RANGE           
REMARK 500    ILE Z  31        24.8      L          L   OUTSIDE RANGE           
REMARK 500    ILE Z  49        22.3      L          L   OUTSIDE RANGE           
REMARK 500    TYR Z  76        24.6      L          L   OUTSIDE RANGE           
REMARK 500    ILE Z  92        24.1      L          L   OUTSIDE RANGE           
REMARK 500    MET Z  98        20.2      L          L   OUTSIDE RANGE           
REMARK 500    VAL Z 149        22.5      L          L   OUTSIDE RANGE           
REMARK 500    MET Z 151        22.1      L          L   OUTSIDE RANGE           
REMARK 500    ILE Z 281        23.8      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP Z 1397                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-5036   RELATED DB: EMDB                              
REMARK 900 6.7-A CRYO-EM MAP ON WHICH THIS MODEL IS BASED                       
REMARK 900 RELATED ID: 2I2U   RELATED DB: PDB                                   
REMARK 900 INITIAL COORDINATES USED FOR FITTING THE 30S INTO THE CRYO-          
REMARK 900 EM MAP                                                               
REMARK 900 RELATED ID: 2I2V   RELATED DB: PDB                                   
REMARK 900 INITIAL COORDINATES USED FOR FITTING THE 50S INTO THE CRYO-          
REMARK 900 EM MAP                                                               
REMARK 900 RELATED ID: 2J00   RELATED DB: PDB                                   
REMARK 900 INITIAL COORDINATES USED FOR FITTING P- AND E-SITE TRNAS             
REMARK 900 INTO THE CRYO-EM MAP                                                 
REMARK 900 RELATED ID: 1OB2   RELATED DB: PDB                                   
REMARK 900 INITIAL COORDINATES USED FOR FITTING THE TERNARY COMPLEX             
REMARK 900 INTO THE CRYO-EM MAP                                                 
DBREF  3FIH J    5   102  UNP    P0A7R5   RS10_ECOLI       5    102             
DBREF  3FIH K   12   128  UNP    P0A7R9   RS11_ECOLI      13    129             
DBREF  3FIH L    1   123  UNP    P0A7S3   RS12_ECOLI       2    124             
DBREF  3FIH M    1   113  UNP    P0A7S9   RS13_ECOLI       2    114             
DBREF  3FIH N    1   100  UNP    P0AG59   RS14_ECOLI       2    101             
DBREF  3FIH O    1    88  UNP    Q8X9M2   RS15_ECO57       2     89             
DBREF  3FIH P    1    80  UNP    P0A7T3   RS16_ECOLI       1     80             
DBREF  3FIH Q    3    82  UNP    P0AG63   RS17_ECOLI       4     83             
DBREF  3FIH R   19    73  UNP    P0A7T7   RS18_ECOLI      20     74             
DBREF  3FIH S    2    80  UNP    P0A7U3   RS19_ECOLI       3     81             
DBREF  3FIH T    2    86  UNP    P0A7U7   RS20_ECOLI       3     87             
DBREF  3FIH U    3    53  UNP    P68679   RS21_ECOLI       4     54             
DBREF  3FIH B    8   225  UNP    P0A7V0   RS2_ECOLI        9    226             
DBREF  3FIH C    1   206  UNP    P0A7V3   RS3_ECOLI        2    207             
DBREF  3FIH D    1   205  UNP    P0A7V8   RS4_ECOLI        2    206             
DBREF  3FIH E    9   158  UNP    P0A7W1   RS5_ECOLI       10    159             
DBREF  3FIH F    1   100  UNP    P02358   RS6_ECOLI        1    100             
DBREF  3FIH G    2   151  UNP    P02359   RS7_ECOLI        3    152             
DBREF  3FIH H    1   129  UNP    P0A7W7   RS8_ECOLI        2    130             
DBREF  3FIH I    3   129  UNP    P0A7X3   RS9_ECOLI        4    130             
DBREF  3FIH A    5  1534  GB     83754040 2AVY_A           5   1534             
DBREF  3FIH Z    1   393  UNP    P0A6N1   EFTU_ECOLI       2    394             
SEQADV 3FIH     N       UNP  P0AG59    SER    37 DELETION                       
SEQADV 3FIH     N       UNP  P0AG59    ASP    38 DELETION                       
SEQADV 3FIH     N       UNP  P0AG59    GLU    39 DELETION                       
SEQADV 3FIH     N       UNP  P0AG59    ASP    40 DELETION                       
SEQRES   1 J   98  ARG ILE ARG ILE ARG LEU LYS ALA PHE ASP HIS ARG LEU          
SEQRES   2 J   98  ILE ASP GLN ALA THR ALA GLU ILE VAL GLU THR ALA LYS          
SEQRES   3 J   98  ARG THR GLY ALA GLN VAL ARG GLY PRO ILE PRO LEU PRO          
SEQRES   4 J   98  THR ARG LYS GLU ARG PHE THR VAL LEU ILE SER PRO HIS          
SEQRES   5 J   98  VAL ASN LYS ASP ALA ARG ASP GLN TYR GLU ILE ARG THR          
SEQRES   6 J   98  HIS LEU ARG LEU VAL ASP ILE VAL GLU PRO THR GLU LYS          
SEQRES   7 J   98  THR VAL ASP ALA LEU MET ARG LEU ASP LEU ALA ALA GLY          
SEQRES   8 J   98  VAL ASP VAL GLN ILE SER LEU                                  
SEQRES   1 K  117  ARG LYS GLN VAL SER ASP GLY VAL ALA HIS ILE HIS ALA          
SEQRES   2 K  117  SER PHE ASN ASN THR ILE VAL THR ILE THR ASP ARG GLN          
SEQRES   3 K  117  GLY ASN ALA LEU GLY TRP ALA THR ALA GLY GLY SER GLY          
SEQRES   4 K  117  PHE ARG GLY SER ARG LYS SER THR PRO PHE ALA ALA GLN          
SEQRES   5 K  117  VAL ALA ALA GLU ARG CYS ALA ASP ALA VAL LYS GLU TYR          
SEQRES   6 K  117  GLY ILE LYS ASN LEU GLU VAL MET VAL LYS GLY PRO GLY          
SEQRES   7 K  117  PRO GLY ARG GLU SER THR ILE ARG ALA LEU ASN ALA ALA          
SEQRES   8 K  117  GLY PHE ARG ILE THR ASN ILE THR ASP VAL THR PRO ILE          
SEQRES   9 K  117  PRO HIS ASN GLY CYS ARG PRO PRO LYS LYS ARG ARG VAL          
SEQRES   1 L  123  ALA THR VAL ASN GLN LEU VAL ARG LYS PRO ARG ALA ARG          
SEQRES   2 L  123  LYS VAL ALA LYS SER ASN VAL PRO ALA LEU GLU ALA CYS          
SEQRES   3 L  123  PRO GLN LYS ARG GLY VAL CYS THR ARG VAL TYR THR THR          
SEQRES   4 L  123  THR PRO LYS LYS PRO ASN SER ALA LEU ARG LYS VAL CYS          
SEQRES   5 L  123  ARG VAL ARG LEU THR ASN GLY PHE GLU VAL THR SER TYR          
SEQRES   6 L  123  ILE GLY GLY GLU GLY HIS ASN LEU GLN GLU HIS SER VAL          
SEQRES   7 L  123  ILE LEU ILE ARG GLY GLY ARG VAL LYS ASP LEU PRO GLY          
SEQRES   8 L  123  VAL ARG TYR HIS THR VAL ARG GLY ALA LEU ASP CYS SER          
SEQRES   9 L  123  GLY VAL LYS ASP ARG LYS GLN ALA ARG SER LYS TYR GLY          
SEQRES  10 L  123  VAL LYS ARG PRO LYS ALA                                      
SEQRES   1 M  113  ALA ARG ILE ALA GLY ILE ASN ILE PRO ASP HIS LYS HIS          
SEQRES   2 M  113  ALA VAL ILE ALA LEU THR SER ILE TYR GLY VAL GLY LYS          
SEQRES   3 M  113  THR ARG SER LYS ALA ILE LEU ALA ALA ALA GLY ILE ALA          
SEQRES   4 M  113  GLU ASP VAL LYS ILE SER GLU LEU SER GLU GLY GLN ILE          
SEQRES   5 M  113  ASP THR LEU ARG ASP GLU VAL ALA LYS PHE VAL VAL GLU          
SEQRES   6 M  113  GLY ASP LEU ARG ARG GLU ILE SER MET SER ILE LYS ARG          
SEQRES   7 M  113  LEU MET ASP LEU GLY CYS TYR ARG GLY LEU ARG HIS ARG          
SEQRES   8 M  113  ARG GLY LEU PRO VAL ARG GLY GLN ARG THR LYS THR ASN          
SEQRES   9 M  113  ALA ARG THR ARG LYS GLY PRO ARG LYS                          
SEQRES   1 N   96  ALA LYS GLN SER MET LYS ALA ARG GLU VAL LYS ARG VAL          
SEQRES   2 N   96  ALA LEU ALA ASP LYS TYR PHE ALA LYS ARG ALA GLU LEU          
SEQRES   3 N   96  LYS ALA ILE ILE SER ASP VAL ASN ALA ARG TRP ASN ALA          
SEQRES   4 N   96  VAL LEU LYS LEU GLN THR LEU PRO ARG ASP SER SER PRO          
SEQRES   5 N   96  SER ARG GLN ARG ASN ARG CYS ARG GLN THR GLY ARG PRO          
SEQRES   6 N   96  HIS GLY PHE LEU ARG LYS PHE GLY LEU SER ARG ILE LYS          
SEQRES   7 N   96  VAL ARG GLU ALA ALA MET ARG GLY GLU ILE PRO GLY LEU          
SEQRES   8 N   96  LYS LYS ALA SER TRP                                          
SEQRES   1 O   88  SER LEU SER THR GLU ALA THR ALA LYS ILE VAL SER GLU          
SEQRES   2 O   88  PHE GLY ARG ASP ALA ASN ASP THR GLY SER THR GLU VAL          
SEQRES   3 O   88  GLN VAL ALA LEU LEU THR ALA GLN ILE ASN HIS LEU GLN          
SEQRES   4 O   88  GLY HIS PHE ALA GLU HIS LYS LYS ASP HIS HIS SER ARG          
SEQRES   5 O   88  ARG GLY LEU LEU ARG MET VAL SER GLN ARG ARG LYS LEU          
SEQRES   6 O   88  LEU ASP TYR LEU LYS ARG LYS ASP VAL ALA ARG TYR THR          
SEQRES   7 O   88  ARG LEU ILE GLU ARG LEU GLY LEU ARG ARG                      
SEQRES   1 P   80  MET VAL THR ILE ARG LEU ALA ARG HIS GLY ALA LYS LYS          
SEQRES   2 P   80  ARG PRO PHE TYR GLN VAL VAL VAL ALA ASP SER ARG ASN          
SEQRES   3 P   80  ALA ARG ASN GLY ARG PHE ILE GLU ARG VAL GLY PHE PHE          
SEQRES   4 P   80  ASN PRO ILE ALA SER GLU LYS GLU GLU GLY THR ARG LEU          
SEQRES   5 P   80  ASP LEU ASP ARG ILE ALA HIS TRP VAL GLY GLN GLY ALA          
SEQRES   6 P   80  THR ILE SER ASP ARG VAL ALA ALA LEU ILE LYS GLU VAL          
SEQRES   7 P   80  ASN LYS                                                      
SEQRES   1 Q   80  LYS ILE ARG THR LEU GLN GLY ARG VAL VAL SER ASP LYS          
SEQRES   2 Q   80  MET GLU LYS SER ILE VAL VAL ALA ILE GLU ARG PHE VAL          
SEQRES   3 Q   80  LYS HIS PRO ILE TYR GLY LYS PHE ILE LYS ARG THR THR          
SEQRES   4 Q   80  LYS LEU HIS VAL HIS ASP GLU ASN ASN GLU CYS GLY ILE          
SEQRES   5 Q   80  GLY ASP VAL VAL GLU ILE ARG GLU CYS ARG PRO LEU SER          
SEQRES   6 Q   80  LYS THR LYS SER TRP THR LEU VAL ARG VAL VAL GLU LYS          
SEQRES   7 Q   80  ALA VAL                                                      
SEQRES   1 R   55  GLU ILE ASP TYR LYS ASP ILE ALA THR LEU LYS ASN TYR          
SEQRES   2 R   55  ILE THR GLU SER GLY LYS ILE VAL PRO SER ARG ILE THR          
SEQRES   3 R   55  GLY THR ARG ALA LYS TYR GLN ARG GLN LEU ALA ARG ALA          
SEQRES   4 R   55  ILE LYS ARG ALA ARG TYR LEU SER LEU LEU PRO TYR THR          
SEQRES   5 R   55  ASP ARG HIS                                                  
SEQRES   1 S   79  ARG SER LEU LYS LYS GLY PRO PHE ILE ASP LEU HIS LEU          
SEQRES   2 S   79  LEU LYS LYS VAL GLU LYS ALA VAL GLU SER GLY ASP LYS          
SEQRES   3 S   79  LYS PRO LEU ARG THR TRP SER ARG ARG SER THR ILE PHE          
SEQRES   4 S   79  PRO ASN MET ILE GLY LEU THR ILE ALA VAL HIS ASN GLY          
SEQRES   5 S   79  ARG GLN HIS VAL PRO VAL PHE VAL THR ASP GLU MET VAL          
SEQRES   6 S   79  GLY HIS LYS LEU GLY GLU PHE ALA PRO THR ARG THR TYR          
SEQRES   7 S   79  ARG                                                          
SEQRES   1 T   85  ASN ILE LYS SER ALA LYS LYS ARG ALA ILE GLN SER GLU          
SEQRES   2 T   85  LYS ALA ARG LYS HIS ASN ALA SER ARG ARG SER MET MET          
SEQRES   3 T   85  ARG THR PHE ILE LYS LYS VAL TYR ALA ALA ILE GLU ALA          
SEQRES   4 T   85  GLY ASP LYS ALA ALA ALA GLN LYS ALA PHE ASN GLU MET          
SEQRES   5 T   85  GLN PRO ILE VAL ASP ARG GLN ALA ALA LYS GLY LEU ILE          
SEQRES   6 T   85  HIS LYS ASN LYS ALA ALA ARG HIS LYS ALA ASN LEU THR          
SEQRES   7 T   85  ALA GLN ILE ASN LYS LEU ALA                                  
SEQRES   1 U   51  ILE LYS VAL ARG GLU ASN GLU PRO PHE ASP VAL ALA LEU          
SEQRES   2 U   51  ARG ARG PHE LYS ARG SER CYS GLU LYS ALA GLY VAL LEU          
SEQRES   3 U   51  ALA GLU VAL ARG ARG ARG GLU PHE TYR GLU LYS PRO THR          
SEQRES   4 U   51  THR GLU ARG LYS ARG ALA LYS ALA SER ALA VAL LYS              
SEQRES   1 B  218  MET LEU LYS ALA GLY VAL HIS PHE GLY HIS GLN THR ARG          
SEQRES   2 B  218  TYR TRP ASN PRO LYS MET LYS PRO PHE ILE PHE GLY ALA          
SEQRES   3 B  218  ARG ASN LYS VAL HIS ILE ILE ASN LEU GLU LYS THR VAL          
SEQRES   4 B  218  PRO MET PHE ASN GLU ALA LEU ALA GLU LEU ASN LYS ILE          
SEQRES   5 B  218  ALA SER ARG LYS GLY LYS ILE LEU PHE VAL GLY THR LYS          
SEQRES   6 B  218  ARG ALA ALA SER GLU ALA VAL LYS ASP ALA ALA LEU SER          
SEQRES   7 B  218  CYS ASP GLN PHE PHE VAL ASN HIS ARG TRP LEU GLY GLY          
SEQRES   8 B  218  MET LEU THR ASN TRP LYS THR VAL ARG GLN SER ILE LYS          
SEQRES   9 B  218  ARG LEU LYS ASP LEU GLU THR GLN SER GLN ASP GLY THR          
SEQRES  10 B  218  PHE ASP LYS LEU THR LYS LYS GLU ALA LEU MET ARG THR          
SEQRES  11 B  218  ARG GLU LEU GLU LYS LEU GLU ASN SER LEU GLY GLY ILE          
SEQRES  12 B  218  LYS ASP MET GLY GLY LEU PRO ASP ALA LEU PHE VAL ILE          
SEQRES  13 B  218  ASP ALA ASP HIS GLU HIS ILE ALA ILE LYS GLU ALA ASN          
SEQRES  14 B  218  ASN LEU GLY ILE PRO VAL PHE ALA ILE VAL ASP THR ASN          
SEQRES  15 B  218  SER ASP PRO ASP GLY VAL ASP PHE VAL ILE PRO GLY ASN          
SEQRES  16 B  218  ASP ASP ALA ILE ARG ALA VAL THR LEU TYR LEU GLY ALA          
SEQRES  17 B  218  VAL ALA ALA THR VAL ARG GLU GLY ARG SER                      
SEQRES   1 C  206  GLY GLN LYS VAL HIS PRO ASN GLY ILE ARG LEU GLY ILE          
SEQRES   2 C  206  VAL LYS PRO TRP ASN SER THR TRP PHE ALA ASN THR LYS          
SEQRES   3 C  206  GLU PHE ALA ASP ASN LEU ASP SER ASP PHE LYS VAL ARG          
SEQRES   4 C  206  GLN TYR LEU THR LYS GLU LEU ALA LYS ALA SER VAL SER          
SEQRES   5 C  206  ARG ILE VAL ILE GLU ARG PRO ALA LYS SER ILE ARG VAL          
SEQRES   6 C  206  THR ILE HIS THR ALA ARG PRO GLY ILE VAL ILE GLY LYS          
SEQRES   7 C  206  LYS GLY GLU ASP VAL GLU LYS LEU ARG LYS VAL VAL ALA          
SEQRES   8 C  206  ASP ILE ALA GLY VAL PRO ALA GLN ILE ASN ILE ALA GLU          
SEQRES   9 C  206  VAL ARG LYS PRO GLU LEU ASP ALA LYS LEU VAL ALA ASP          
SEQRES  10 C  206  SER ILE THR SER GLN LEU GLU ARG ARG VAL MET PHE ARG          
SEQRES  11 C  206  ARG ALA MET LYS ARG ALA VAL GLN ASN ALA MET ARG LEU          
SEQRES  12 C  206  GLY ALA LYS GLY ILE LYS VAL GLU VAL SER GLY ARG LEU          
SEQRES  13 C  206  GLY GLY ALA GLU ILE ALA ARG THR GLU TRP TYR ARG GLU          
SEQRES  14 C  206  GLY ARG VAL PRO LEU HIS THR LEU ARG ALA ASP ILE ASP          
SEQRES  15 C  206  TYR ASN THR SER GLU ALA HIS THR THR TYR GLY VAL ILE          
SEQRES  16 C  206  GLY VAL LYS VAL TRP ILE PHE LYS GLY GLU ILE                  
SEQRES   1 D  205  ALA ARG TYR LEU GLY PRO LYS LEU LYS LEU SER ARG ARG          
SEQRES   2 D  205  GLU GLY THR ASP LEU PHE LEU LYS SER GLY VAL ARG ALA          
SEQRES   3 D  205  ILE ASP THR LYS CYS LYS ILE GLU GLN ALA PRO GLY GLN          
SEQRES   4 D  205  HIS GLY ALA ARG LYS PRO ARG LEU SER ASP TYR GLY VAL          
SEQRES   5 D  205  GLN LEU ARG GLU LYS GLN LYS VAL ARG ARG ILE TYR GLY          
SEQRES   6 D  205  VAL LEU GLU ARG GLN PHE ARG ASN TYR TYR LYS GLU ALA          
SEQRES   7 D  205  ALA ARG LEU LYS GLY ASN THR GLY GLU ASN LEU LEU ALA          
SEQRES   8 D  205  LEU LEU GLU GLY ARG LEU ASP ASN VAL VAL TYR ARG MET          
SEQRES   9 D  205  GLY PHE GLY ALA THR ARG ALA GLU ALA ARG GLN LEU VAL          
SEQRES  10 D  205  SER HIS LYS ALA ILE MET VAL ASN GLY ARG VAL VAL ASN          
SEQRES  11 D  205  ILE ALA SER TYR GLN VAL SER PRO ASN ASP VAL VAL SER          
SEQRES  12 D  205  ILE ARG GLU LYS ALA LYS LYS GLN SER ARG VAL LYS ALA          
SEQRES  13 D  205  ALA LEU GLU LEU ALA GLU GLN ARG GLU LYS PRO THR TRP          
SEQRES  14 D  205  LEU GLU VAL ASP ALA GLY LYS MET GLU GLY THR PHE LYS          
SEQRES  15 D  205  ARG LYS PRO GLU ARG SER ASP LEU SER ALA ASP ILE ASN          
SEQRES  16 D  205  GLU HIS LEU ILE VAL GLU LEU TYR SER LYS                      
SEQRES   1 E  150  GLU LEU GLN GLU LYS LEU ILE ALA VAL ASN ARG VAL SER          
SEQRES   2 E  150  LYS THR VAL LYS GLY GLY ARG ILE PHE SER PHE THR ALA          
SEQRES   3 E  150  LEU THR VAL VAL GLY ASP GLY ASN GLY ARG VAL GLY PHE          
SEQRES   4 E  150  GLY TYR GLY LYS ALA ARG GLU VAL PRO ALA ALA ILE GLN          
SEQRES   5 E  150  LYS ALA MET GLU LYS ALA ARG ARG ASN MET ILE ASN VAL          
SEQRES   6 E  150  ALA LEU ASN ASN GLY THR LEU GLN HIS PRO VAL LYS GLY          
SEQRES   7 E  150  VAL HIS THR GLY SER ARG VAL PHE MET GLN PRO ALA SER          
SEQRES   8 E  150  GLU GLY THR GLY ILE ILE ALA GLY GLY ALA MET ARG ALA          
SEQRES   9 E  150  VAL LEU GLU VAL ALA GLY VAL HIS ASN VAL LEU ALA LYS          
SEQRES  10 E  150  ALA TYR GLY SER THR ASN PRO ILE ASN VAL VAL ARG ALA          
SEQRES  11 E  150  THR ILE ASP GLY LEU GLU ASN MET ASN SER PRO GLU MET          
SEQRES  12 E  150  VAL ALA ALA LYS ARG GLY LYS                                  
SEQRES   1 F  100  MET ARG HIS TYR GLU ILE VAL PHE MET VAL HIS PRO ASP          
SEQRES   2 F  100  GLN SER GLU GLN VAL PRO GLY MET ILE GLU ARG TYR THR          
SEQRES   3 F  100  ALA ALA ILE THR GLY ALA GLU GLY LYS ILE HIS ARG LEU          
SEQRES   4 F  100  GLU ASP TRP GLY ARG ARG GLN LEU ALA TYR PRO ILE ASN          
SEQRES   5 F  100  LYS LEU HIS LYS ALA HIS TYR VAL LEU MET ASN VAL GLU          
SEQRES   6 F  100  ALA PRO GLN GLU VAL ILE ASP GLU LEU GLU THR THR PHE          
SEQRES   7 F  100  ARG PHE ASN ASP ALA VAL ILE ARG SER MET VAL MET ARG          
SEQRES   8 F  100  THR LYS HIS ALA VAL THR GLU ALA SER                          
SEQRES   1 G  150  ARG ARG ARG VAL ILE GLY GLN ARG LYS ILE LEU PRO ASP          
SEQRES   2 G  150  PRO LYS PHE GLY SER GLU LEU LEU ALA LYS PHE VAL ASN          
SEQRES   3 G  150  ILE LEU MET VAL ASP GLY LYS LYS SER THR ALA GLU SER          
SEQRES   4 G  150  ILE VAL TYR SER ALA LEU GLU THR LEU ALA GLN ARG SER          
SEQRES   5 G  150  GLY LYS SER GLU LEU GLU ALA PHE GLU VAL ALA LEU GLU          
SEQRES   6 G  150  ASN VAL ARG PRO THR VAL GLU VAL LYS SER ARG ARG VAL          
SEQRES   7 G  150  GLY GLY SER THR TYR GLN VAL PRO VAL GLU VAL ARG PRO          
SEQRES   8 G  150  VAL ARG ARG ASN ALA LEU ALA MET ARG TRP ILE VAL GLU          
SEQRES   9 G  150  ALA ALA ARG LYS ARG GLY ASP LYS SER MET ALA LEU ARG          
SEQRES  10 G  150  LEU ALA ASN GLU LEU SER ASP ALA ALA GLU ASN LYS GLY          
SEQRES  11 G  150  THR ALA VAL LYS LYS ARG GLU ASP VAL HIS ARG MET ALA          
SEQRES  12 G  150  GLU ALA ASN LYS ALA PHE ALA                                  
SEQRES   1 H  129  SER MET GLN ASP PRO ILE ALA ASP MET LEU THR ARG ILE          
SEQRES   2 H  129  ARG ASN GLY GLN ALA ALA ASN LYS ALA ALA VAL THR MET          
SEQRES   3 H  129  PRO SER SER LYS LEU LYS VAL ALA ILE ALA ASN VAL LEU          
SEQRES   4 H  129  LYS GLU GLU GLY PHE ILE GLU ASP PHE LYS VAL GLU GLY          
SEQRES   5 H  129  ASP THR LYS PRO GLU LEU GLU LEU THR LEU LYS TYR PHE          
SEQRES   6 H  129  GLN GLY LYS ALA VAL VAL GLU SER ILE GLN ARG VAL SER          
SEQRES   7 H  129  ARG PRO GLY LEU ARG ILE TYR LYS ARG LYS ASP GLU LEU          
SEQRES   8 H  129  PRO LYS VAL MET ALA GLY LEU GLY ILE ALA VAL VAL SER          
SEQRES   9 H  129  THR SER LYS GLY VAL MET THR ASP ARG ALA ALA ARG GLN          
SEQRES  10 H  129  ALA GLY LEU GLY GLY GLU ILE ILE CYS TYR VAL ALA              
SEQRES   1 I  127  ASN GLN TYR TYR GLY THR GLY ARG ARG LYS SER SER ALA          
SEQRES   2 I  127  ALA ARG VAL PHE ILE LYS PRO GLY ASN GLY LYS ILE VAL          
SEQRES   3 I  127  ILE ASN GLN ARG SER LEU GLU GLN TYR PHE GLY ARG GLU          
SEQRES   4 I  127  THR ALA ARG MET VAL VAL ARG GLN PRO LEU GLU LEU VAL          
SEQRES   5 I  127  ASP MET VAL GLU LYS LEU ASP LEU TYR ILE THR VAL LYS          
SEQRES   6 I  127  GLY GLY GLY ILE SER GLY GLN ALA GLY ALA ILE ARG HIS          
SEQRES   7 I  127  GLY ILE THR ARG ALA LEU MET GLU TYR ASP GLU SER LEU          
SEQRES   8 I  127  ARG SER GLU LEU ARG LYS ALA GLY PHE VAL THR ARG ASP          
SEQRES   9 I  127  ALA ARG GLN VAL GLU ARG LYS LYS VAL GLY LEU ARG LYS          
SEQRES  10 I  127  ALA ARG ARG ARG PRO GLN PHE SER LYS ARG                      
SEQRES   1 A 1530    U   G   A   A   G   A   G   U   U   U   G   A   U          
SEQRES   2 A 1530    C   A   U   G   G   C   U   C   A   G   A   U   U          
SEQRES   3 A 1530    G   A   A   C   G   C   U   G   G   C   G   G   C          
SEQRES   4 A 1530    A   G   G   C   C   U   A   A   C   A   C   A   U          
SEQRES   5 A 1530    G   C   A   A   G   U   C   G   A   A   C   G   G          
SEQRES   6 A 1530    U   A   A   C   A   G   G   A   A   G   A   A   G          
SEQRES   7 A 1530    C   U   U   G   C   U   U   C   U   U   U   G   C          
SEQRES   8 A 1530    U   G   A   C   G   A   G   U   G   G   C   G   G          
SEQRES   9 A 1530    A   C   G   G   G   U   G   A   G   U   A   A   U          
SEQRES  10 A 1530    G   U   C   U   G   G   G   A   A   A   C   U   G          
SEQRES  11 A 1530    C   C   U   G   A   U   G   G   A   G   G   G   G          
SEQRES  12 A 1530    G   A   U   A   A   C   U   A   C   U   G   G   A          
SEQRES  13 A 1530    A   A   C   G   G   U   A   G   C   U   A   A   U          
SEQRES  14 A 1530    A   C   C   G   C   A   U   A   A   C   G   U   C          
SEQRES  15 A 1530    G   C   A   A   G   A   C   C   A   A   A   G   A          
SEQRES  16 A 1530    G   G   G   G   G   A   C   C   U   U   C   G   G          
SEQRES  17 A 1530    G   C   C   U   C   U   U   G   C   C   A   U   C          
SEQRES  18 A 1530    G   G   A   U   G   U   G   C   C   C   A   G   A          
SEQRES  19 A 1530    U   G   G   G   A   U   U   A   G   C   U   A   G          
SEQRES  20 A 1530    U   A   G   G   U   G   G   G   G   U   A   A   C          
SEQRES  21 A 1530    G   G   C   U   C   A   C   C   U   A   G   G   C          
SEQRES  22 A 1530    G   A   C   G   A   U   C   C   C   U   A   G   C          
SEQRES  23 A 1530    U   G   G   U   C   U   G   A   G   A   G   G   A          
SEQRES  24 A 1530    U   G   A   C   C   A   G   C   C   A   C   A   C          
SEQRES  25 A 1530    U   G   G   A   A   C   U   G   A   G   A   C   A          
SEQRES  26 A 1530    C   G   G   U   C   C   A   G   A   C   U   C   C          
SEQRES  27 A 1530    U   A   C   G   G   G   A   G   G   C   A   G   C          
SEQRES  28 A 1530    A   G   U   G   G   G   G   A   A   U   A   U   U          
SEQRES  29 A 1530    G   C   A   C   A   A   U   G   G   G   C   G   C          
SEQRES  30 A 1530    A   A   G   C   C   U   G   A   U   G   C   A   G          
SEQRES  31 A 1530    C   C   A   U   G   C   C   G   C   G   U   G   U          
SEQRES  32 A 1530    A   U   G   A   A   G   A   A   G   G   C   C   U          
SEQRES  33 A 1530    U   C   G   G   G   U   U   G   U   A   A   A   G          
SEQRES  34 A 1530    U   A   C   U   U   U   C   A   G   C   G   G   G          
SEQRES  35 A 1530    G   A   G   G   A   A   G   G   G   A   G   U   A          
SEQRES  36 A 1530    A   A   G   U   U   A   A   U   A   C   C   U   U          
SEQRES  37 A 1530    U   G   C   U   C   A   U   U   G   A   C   G   U          
SEQRES  38 A 1530    U   A   C   C   C   G   C   A   G   A   A   G   A          
SEQRES  39 A 1530    A   G   C   A   C   C   G   G   C   U   A   A   C          
SEQRES  40 A 1530    U   C   C   G   U   G   C   C   A   G   C   A   G          
SEQRES  41 A 1530    C   C   G   C   G   G   U   A   A   U   A   C   G          
SEQRES  42 A 1530    G   A   G   G   G   U   G   C   A   A   G   C   G          
SEQRES  43 A 1530    U   U   A   A   U   C   G   G   A   A   U   U   A          
SEQRES  44 A 1530    C   U   G   G   G   C   G   U   A   A   A   G   C          
SEQRES  45 A 1530    G   C   A   C   G   C   A   G   G   C   G   G   U          
SEQRES  46 A 1530    U   U   G   U   U   A   A   G   U   C   A   G   A          
SEQRES  47 A 1530    U   G   U   G   A   A   A   U   C   C   C   C   G          
SEQRES  48 A 1530    G   G   C   U   C   A   A   C   C   U   G   G   G          
SEQRES  49 A 1530    A   A   C   U   G   C   A   U   C   U   G   A   U          
SEQRES  50 A 1530    A   C   U   G   G   C   A   A   G   C   U   U   G          
SEQRES  51 A 1530    A   G   U   C   U   C   G   U   A   G   A   G   G          
SEQRES  52 A 1530    G   G   G   G   U   A   G   A   A   U   U   C   C          
SEQRES  53 A 1530    A   G   G   U   G   U   A   G   C   G   G   U   G          
SEQRES  54 A 1530    A   A   A   U   G   C   G   U   A   G   A   G   A          
SEQRES  55 A 1530    U   C   U   G   G   A   G   G   A   A   U   A   C          
SEQRES  56 A 1530    C   G   G   U   G   G   C   G   A   A   G   G   C          
SEQRES  57 A 1530    G   G   C   C   C   C   C   U   G   G   A   C   G          
SEQRES  58 A 1530    A   A   G   A   C   U   G   A   C   G   C   U   C          
SEQRES  59 A 1530    A   G   G   U   G   C   G   A   A   A   G   C   G          
SEQRES  60 A 1530    U   G   G   G   G   A   G   C   A   A   A   C   A          
SEQRES  61 A 1530    G   G   A   U   U   A   G   A   U   A   C   C   C          
SEQRES  62 A 1530    U   G   G   U   A   G   U   C   C   A   C   G   C          
SEQRES  63 A 1530    C   G   U   A   A   A   C   G   A   U   G   U   C          
SEQRES  64 A 1530    G   A   C   U   U   G   G   A   G   G   U   U   G          
SEQRES  65 A 1530    U   G   C   C   C   U   U   G   A   G   G   C   G          
SEQRES  66 A 1530    U   G   G   C   U   U   C   C   G   G   A   G   C          
SEQRES  67 A 1530    U   A   A   C   G   C   G   U   U   A   A   G   U          
SEQRES  68 A 1530    C   G   A   C   C   G   C   C   U   G   G   G   G          
SEQRES  69 A 1530    A   G   U   A   C   G   G   C   C   G   C   A   A          
SEQRES  70 A 1530    G   G   U   U   A   A   A   A   C   U   C   A   A          
SEQRES  71 A 1530    A   U   G   A   A   U   U   G   A   C   G   G   G          
SEQRES  72 A 1530    G   G   C   C   C   G   C   A   C   A   A   G   C          
SEQRES  73 A 1530    G   G   U   G   G   A   G   C   A   U   G   U   G          
SEQRES  74 A 1530    G   U   U   U   A   A   U   U   C   G   A   U   G          
SEQRES  75 A 1530    C   A   A   C   G   C   G   A   A   G   A   A   C          
SEQRES  76 A 1530    C   U   U   A   C   C   U   G   G   U   C   U   U          
SEQRES  77 A 1530    G   A   C   A   U   C   C   A   C   G   G   A   A          
SEQRES  78 A 1530    G   U   U   U   U   C   A   G   A   G   A   U   G          
SEQRES  79 A 1530    A   G   A   A   U   G   U   G   C   C   U   U   C          
SEQRES  80 A 1530    G   G   G   A   A   C   C   G   U   G   A   G   A          
SEQRES  81 A 1530    C   A   G   G   U   G   C   U   G   C   A   U   G          
SEQRES  82 A 1530    G   C   U   G   U   C   G   U   C   A   G   C   U          
SEQRES  83 A 1530    C   G   U   G   U   U   G   U   G   A   A   A   U          
SEQRES  84 A 1530    G   U   U   G   G   G   U   U   A   A   G   U   C          
SEQRES  85 A 1530    C   C   G   C   A   A   C   G   A   G   C   G   C          
SEQRES  86 A 1530    A   A   C   C   C   U   U   A   U   C   C   U   U          
SEQRES  87 A 1530    U   G   U   U   G   C   C   A   G   C   G   G   U          
SEQRES  88 A 1530    C   C   G   G   C   C   G   G   G   A   A   C   U          
SEQRES  89 A 1530    C   A   A   A   G   G   A   G   A   C   U   G   C          
SEQRES  90 A 1530    C   A   G   U   G   A   U   A   A   A   C   U   G          
SEQRES  91 A 1530    G   A   G   G   A   A   G   G   U   G   G   G   G          
SEQRES  92 A 1530    A   U   G   A   C   G   U   C   A   A   G   U   C          
SEQRES  93 A 1530    A   U   C   A   U   G   G   C   C   C   U   U   A          
SEQRES  94 A 1530    C   G   A   C   C   A   G   G   G   C   U   A   C          
SEQRES  95 A 1530    A   C   A   C   G   U   G   C   U   A   C   A   A          
SEQRES  96 A 1530    U   G   G   C   G   C   A   U   A   C   A   A   A          
SEQRES  97 A 1530    G   A   G   A   A   G   C   G   A   C   C   U   C          
SEQRES  98 A 1530    G   C   G   A   G   A   G   C   A   A   G   C   G          
SEQRES  99 A 1530    G   A   C   C   U   C   A   U   A   A   A   G   U          
SEQRES 100 A 1530    G   C   G   U   C   G   U   A   G   U   C   C   G          
SEQRES 101 A 1530    G   A   U   U   G   G   A   G   U   C   U   G   C          
SEQRES 102 A 1530    A   A   C   U   C   G   A   C   U   C   C   A   U          
SEQRES 103 A 1530    G   A   A   G   U   C   G   G   A   A   U   C   G          
SEQRES 104 A 1530    C   U   A   G   U   A   A   U   C   G   U   G   G          
SEQRES 105 A 1530    A   U   C   A   G   A   A   U   G   C   C   A   C          
SEQRES 106 A 1530    G   G   U   G   A   A   U   A   C   G   U   U   C          
SEQRES 107 A 1530    C   C   G   G   G   C   C   U   U   G   U   A   C          
SEQRES 108 A 1530    A   C   A   C   C   G   C   C   C   G   U   C   A          
SEQRES 109 A 1530    C   A   C   C   A   U   G   G   G   A   G   U   G          
SEQRES 110 A 1530    G   G   U   U   G   C   A   A   A   A   G   A   A          
SEQRES 111 A 1530    G   U   A   G   G   U   A   G   C   U   U   A   A          
SEQRES 112 A 1530    C   C   U   U   C   G   G   G   A   G   G   G   C          
SEQRES 113 A 1530    G   C   U   U   A   C   C   A   C   U   U   U   G          
SEQRES 114 A 1530    U   G   A   U   U   C   A   U   G   A   C   U   G          
SEQRES 115 A 1530    G   G   G   U   G   A   A   G   U   C   G   U   A          
SEQRES 116 A 1530    A   C   A   A   G   G   U   A   A   C   C   G   U          
SEQRES 117 A 1530    A   G   G   G   G   A   A   C   C   U   G   C   G          
SEQRES 118 A 1530    G   U   U   G   G   A   U   C   A                          
SEQRES   1 Y   76    G   C   G   G   A   U   U   U   A   G   C   U   C          
SEQRES   2 Y   76    A   G   U   U   G   G   G   A   G   A   G   C   G          
SEQRES   3 Y   76    C   C   A   G   A   C   U   G   A   A   G   A   U          
SEQRES   4 Y   76    C   U   G   G   A   G   G   U   C   C   U   G   U          
SEQRES   5 Y   76    G   U   U   C   G   A   U   C   C   A   C   A   G          
SEQRES   6 Y   76    A   A   U   U   C   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   11    A   A   A   A   A   U   G   U   U   C   A                  
SEQRES   1 Z  393  SER LYS GLU LYS PHE GLU ARG THR LYS PRO HIS VAL ASN          
SEQRES   2 Z  393  VAL GLY THR ILE GLY HIS VAL ASP HIS GLY LYS THR THR          
SEQRES   3 Z  393  LEU THR ALA ALA ILE THR THR VAL LEU ALA LYS THR TYR          
SEQRES   4 Z  393  GLY GLY ALA ALA ARG ALA PHE ASP GLN ILE ASP ASN ALA          
SEQRES   5 Z  393  PRO GLU GLU LYS ALA ARG GLY ILE THR ILE ASN THR SER          
SEQRES   6 Z  393  HIS VAL GLU TYR ASP THR PRO THR ARG HIS TYR ALA HIS          
SEQRES   7 Z  393  VAL ASP CYS PRO GLY HIS ALA ASP TYR VAL LYS ASN MET          
SEQRES   8 Z  393  ILE THR GLY ALA ALA GLN MET ASP GLY ALA ILE LEU VAL          
SEQRES   9 Z  393  VAL ALA ALA THR ASP GLY PRO MET PRO GLN THR ARG GLU          
SEQRES  10 Z  393  HIS ILE LEU LEU GLY ARG GLN VAL GLY VAL PRO TYR ILE          
SEQRES  11 Z  393  ILE VAL PHE LEU ASN LYS CYS ASP MET VAL ASP ASP GLU          
SEQRES  12 Z  393  GLU LEU LEU GLU LEU VAL GLU MET GLU VAL ARG GLU LEU          
SEQRES  13 Z  393  LEU SER GLN TYR ASP PHE PRO GLY ASP ASP THR PRO ILE          
SEQRES  14 Z  393  VAL ARG GLY SER ALA LEU LYS ALA LEU GLU GLY ASP ALA          
SEQRES  15 Z  393  GLU TRP GLU ALA LYS ILE LEU GLU LEU ALA GLY PHE LEU          
SEQRES  16 Z  393  ASP SER TYR ILE PRO GLU PRO GLU ARG ALA ILE ASP LYS          
SEQRES  17 Z  393  PRO PHE LEU LEU PRO ILE GLU ASP VAL PHE SER ILE SER          
SEQRES  18 Z  393  GLY ARG GLY THR VAL VAL THR GLY ARG VAL GLU ARG GLY          
SEQRES  19 Z  393  ILE ILE LYS VAL GLY GLU GLU VAL GLU ILE VAL GLY ILE          
SEQRES  20 Z  393  LYS GLU THR GLN LYS SER THR CYS THR GLY VAL GLU MET          
SEQRES  21 Z  393  PHE ARG LYS LEU LEU ASP GLU GLY ARG ALA GLY GLU ASN          
SEQRES  22 Z  393  VAL GLY VAL LEU LEU ARG GLY ILE LYS ARG GLU GLU ILE          
SEQRES  23 Z  393  GLU ARG GLY GLN VAL LEU ALA LYS PRO GLY THR ILE LYS          
SEQRES  24 Z  393  PRO HIS THR LYS PHE GLU SER GLU VAL TYR ILE LEU SER          
SEQRES  25 Z  393  LYS ASP GLU GLY GLY ARG HIS THR PRO PHE PHE LYS GLY          
SEQRES  26 Z  393  TYR ARG PRO GLN PHE TYR PHE ARG THR THR ASP VAL THR          
SEQRES  27 Z  393  GLY THR ILE GLU LEU PRO GLU GLY VAL GLU MET VAL MET          
SEQRES  28 Z  393  PRO GLY ASP ASN ILE LYS MET VAL VAL THR LEU ILE HIS          
SEQRES  29 Z  393  PRO ILE ALA MET ASP ASP GLY LEU ARG PHE ALA ILE ARG          
SEQRES  30 Z  393  GLU GLY GLY ARG THR VAL GLY ALA GLY VAL VAL ALA LYS          
SEQRES  31 Z  393  VAL LEU SER                                                  
SEQRES   1 V   77    C   G   C   G   G   G   G   U   G   G   A   G   C          
SEQRES   2 V   77    A   G   C   C   U   G   G   U   A   G   C   U   C          
SEQRES   3 V   77    G   U   C   G   G   G   C   U   C   A   U   A   A          
SEQRES   4 V   77    C   C   C   G   A   A   G   G   U   C   G   U   C          
SEQRES   5 V   77    G   G 5MU   U   C   A   A   A   U   C   C   G   G          
SEQRES   6 V   77    C   C   C   C   C   G   C   A   A   C   C   A              
MODRES 3FIH 5MU V   54    U  5-METHYLURIDINE 5'-MONOPHOSPHATE                   
HET    5MU  V  54      21                                                       
HET    GDP  Z1397      28                                                       
HETNAM     5MU 5-METHYLURIDINE 5'-MONOPHOSPHATE                                 
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
FORMUL  26  5MU    C10 H15 N2 O9 P                                              
FORMUL  27  GDP    C10 H15 N5 O11 P2                                            
HELIX    1   1 ASP J   14  ASP J   19  1                                   6    
HELIX    2   2 THR J   22  GLY J   33  1                                  12    
HELIX    3   3 THR J   83  ARG J   89  1                                   7    
HELIX    4   4 ALA K   46  GLY K   50  1                                   5    
HELIX    5   5 THR K   58  LYS K   74  1                                  17    
HELIX    6   6 GLU K   93  ALA K  101  1                                   9    
HELIX    7   7 THR L    2  VAL L    7  1                                   6    
HELIX    8   8 HIS M   13  THR M   19  1                                   7    
HELIX    9   9 GLY M   25  GLY M   37  1                                  13    
HELIX   10  10 GLY M   50  ALA M   60  1                                  11    
HELIX   11  11 VAL M   64  GLY M   83  1                                  20    
HELIX   12  12 CYS M   84  ARG M   89  1                                   6    
HELIX   13  13 LYS N    2  ALA N   16  1                                  15    
HELIX   14  14 ALA N   28  ASP N   32  5                                   5    
HELIX   15  15 TRP N   41  LEU N   47  1                                   7    
HELIX   16  16 ARG N   80  GLY N   90  1                                  11    
HELIX   17  17 SER O    3  PHE O   14  1                                  12    
HELIX   18  18 SER O   23  ASN O   36  1                                  14    
HELIX   19  19 GLN O   39  GLU O   44  1                                   6    
HELIX   20  20 ASP O   48  LYS O   70  1                                  23    
HELIX   21  21 ASP O   73  GLY O   85  1                                  13    
HELIX   22  22 SER P   68  ALA P   73  1                                   6    
HELIX   23  23 ASP R   24  LYS R   29  1                                   6    
HELIX   24  24 ARG R   47  TYR R   63  1                                  17    
HELIX   25  25 LEU S   70  ALA S   74  5                                   5    
HELIX   26  26 LYS T    8  ALA T   16  1                                   9    
HELIX   27  27 LYS T   18  GLU T   39  1                                  22    
HELIX   28  28 MET T   53  ALA T   62  1                                  10    
HELIX   29  29 LEU T   78  ALA T   86  1                                   9    
HELIX   30  30 ALA U   29  ARG U   33  5                                   5    
HELIX   31  31 LYS B   44  ALA B   52  1                                   9    
HELIX   32  32 VAL B   79  LEU B   84  1                                   6    
HELIX   33  33 ASN B  102  LYS B  111  1                                  10    
HELIX   34  34 ASP B  115  SER B  120  1                                   6    
HELIX   35  35 GLN B  121  ASP B  126  5                                   6    
HELIX   36  36 THR B  129  LYS B  142  1                                  14    
HELIX   37  37 GLU B  168  ALA B  175  1                                   8    
HELIX   38  38 ALA B  208  LEU B  213  1                                   6    
HELIX   39  39 GLY B  214  VAL B  216  5                                   3    
HELIX   40  40 LYS C   26  LEU C   46  1                                  21    
HELIX   41  41 ASP C   82  ALA C   94  1                                  13    
HELIX   42  42 ALA C  112  GLU C  124  1                                  13    
HELIX   43  43 MET C  128  LEU C  143  1                                  16    
HELIX   44  44 ARG C  155  ALA C  159  5                                   5    
HELIX   45  45 PRO D    6  GLY D   15  1                                  10    
HELIX   46  46 SER D   48  ILE D   63  1                                  16    
HELIX   47  47 LEU D   67  ALA D   79  1                                  13    
HELIX   48  48 ASN D   84  LEU D   93  1                                  10    
HELIX   49  49 ARG D   96  ARG D  103  1                                   8    
HELIX   50  50 THR D  109  HIS D  119  1                                  11    
HELIX   51  51 GLU D  146  LYS D  149  5                                   4    
HELIX   52  52 GLN D  151  ALA D  156  1                                   6    
HELIX   53  53 ALA D  157  LEU D  158  5                                   2    
HELIX   54  54 GLU D  159  ARG D  164  5                                   6    
HELIX   55  55 ASN D  195  SER D  204  1                                  10    
HELIX   56  56 PRO E   56  LYS E   65  1                                  10    
HELIX   57  57 GLY E  108  ARG E  111  5                                   4    
HELIX   58  58 ALA E  112  ALA E  117  1                                   6    
HELIX   59  59 ASN E  131  VAL E  136  1                                   6    
HELIX   60  60 ARG E  137  ALA E  138  5                                   2    
HELIX   61  61 THR E  139  LEU E  143  5                                   5    
HELIX   62  62 SER E  148  GLY E  157  1                                  10    
HELIX   63  63 GLN F   17  GLY F   31  1                                  15    
HELIX   64  64 PRO F   67  ARG F   79  1                                  13    
HELIX   65  65 SER G   19  PHE G   25  1                                   7    
HELIX   66  66 LYS G   35  SER G   53  1                                  19    
HELIX   67  67 LEU G   58  ASN G   67  1                                  10    
HELIX   68  68 ARG G   91  ALA G  106  1                                  16    
HELIX   69  69 SER G  114  SER G  124  1                                  11    
HELIX   70  70 GLY G  131  ALA G  144  1                                  14    
HELIX   71  71 ASP H    4  ALA H   18  1                                  15    
HELIX   72  72 SER H   29  GLU H   42  1                                  14    
HELIX   73  73 VAL H   94  LEU H   98  5                                   5    
HELIX   74  74 ASP H  112  ALA H  118  1                                   7    
HELIX   75  75 SER I   33  PHE I   38  1                                   6    
HELIX   76  76 THR I   42  VAL I   47  1                                   6    
HELIX   77  77 ARG I   48  GLU I   52  5                                   5    
HELIX   78  78 ILE I   71  THR I   83  1                                  13    
HELIX   79  79 ARG I   94  LYS I   99  1                                   6    
HELIX   80  80 GLY Z   23  LEU Z   35  1                                  13    
HELIX   81  81 LEU Z   35  GLY Z   40  1                                   6    
HELIX   82  82 ALA Z   52  GLY Z   59  1                                   8    
HELIX   83  83 HIS Z   84  ASP Z   86  5                                   3    
HELIX   84  84 TYR Z   87  ALA Z   96  1                                  10    
HELIX   85  85 MET Z  112  GLY Z  126  1                                  15    
HELIX   86  86 ASP Z  142  SER Z  158  1                                  17    
HELIX   87  87 SER Z  173  ASP Z  181  1                                   9    
HELIX   88  88 ASP Z  181  TYR Z  198  1                                  18    
HELIX   89  89 LYS Z  282  ILE Z  286  5                                   5    
SHEET    1   A 2 ILE J   8  ALA J  12  0                                        
SHEET    2   A 2 VAL J  96  ILE J 100 -1  O  ASP J  97   N  LYS J  11           
SHEET    1   B 3 THR J  50  VAL J  51  0                                        
SHEET    2   B 3 ASP J  63  GLU J  66 -1  O  ASP J  63   N  VAL J  51           
SHEET    3   B 3 LYS N  96  LYS N  97 -1  O  LYS N  96   N  GLU J  66           
SHEET    1   C 4 ALA K  40  THR K  45  0                                        
SHEET    2   C 4 ASN K  28  THR K  34 -1  N  ILE K  33   O  GLY K  42           
SHEET    3   C 4 SER K  16  SER K  25 -1  N  VAL K  19   O  THR K  34           
SHEET    4   C 4 ILE K  78  MET K  84  1  O  GLU K  82   N  ALA K  20           
SHEET    1   D 6 LYS L  29  THR L  39  0                                        
SHEET    2   D 6 ARG L  49  ARG L  55 -1  O  ARG L  55   N  VAL L  32           
SHEET    3   D 6 THR L  63  ILE L  66 -1  O  SER L  64   N  CYS L  52           
SHEET    4   D 6 TYR L  94  VAL L  97  1  O  THR L  96   N  TYR L  65           
SHEET    5   D 6 ILE L  79  ILE L  81 -1  N  LEU L  80   O  VAL L  97           
SHEET    6   D 6 LYS L  29  THR L  39 -1  N  GLY L  31   O  ILE L  79           
SHEET    1   E 3 VAL P   2  ARG P   8  0                                        
SHEET    2   E 3 TYR P  17  ASP P  23 -1  O  ALA P  22   N  THR P   3           
SHEET    3   E 3 PHE P  32  PHE P  39 -1  O  GLU P  34   N  VAL P  21           
SHEET    1   F 5 PHE Q  36  HIS Q  46  0                                        
SHEET    2   F 5 SER Q  19  LYS Q  29 -1  N  VAL Q  28   O  ILE Q  37           
SHEET    3   F 5 LEU Q   7  ASP Q  14 -1  N  ARG Q  10   O  ALA Q  23           
SHEET    4   F 5 ILE Q  54  GLU Q  62 -1  O  GLY Q  55   N  VAL Q  11           
SHEET    5   F 5 TRP Q  72  VAL Q  77 -1  O  VAL Q  75   N  GLU Q  59           
SHEET    1   G 3 LEU S  30  THR S  32  0                                        
SHEET    2   G 3 THR S  47  HIS S  51  1  O  THR S  47   N  LEU S  30           
SHEET    3   G 3 HIS S  56  PHE S  60 -1  O  VAL S  59   N  ILE S  48           
SHEET    1   H 2 THR C  66  THR C  69  0                                        
SHEET    2   H 2 ASN C 101  GLU C 104  1  O  ALA C 103   N  ILE C  67           
SHEET    1   I 3 ILE C 148  VAL C 152  0                                        
SHEET    2   I 3 ILE C 195  ILE C 201 -1  O  TRP C 200   N  LYS C 149           
SHEET    3   I 3 ASP C 182  ALA C 188 -1  N  ASP C 182   O  ILE C 201           
SHEET    1   J 3 ARG D 127  VAL D 128  0                                        
SHEET    2   J 3 ILE D 122  VAL D 124 -1  N  VAL D 124   O  ARG D 127           
SHEET    3   J 3 VAL D 142  ILE D 144 -1  O  SER D 143   N  MET D 123           
SHEET    1   K 2 GLN E  11  LEU E  14  0                                        
SHEET    2   K 2 THR E  36  GLY E  39 -1  O  VAL E  37   N  LYS E  13           
SHEET    1   L 2 ASN E  18  VAL E  20  0                                        
SHEET    2   L 2 SER E  31  THR E  33 -1  O  THR E  33   N  ASN E  18           
SHEET    1   M 3 VAL E  84  LYS E  85  0                                        
SHEET    2   M 3 ARG E  92  GLN E  96 -1  O  MET E  95   N  VAL E  84           
SHEET    3   M 3 LEU E 123  TYR E 127 -1  O  LYS E 125   N  PHE E  94           
SHEET    1   N 3 VAL F  60  LEU F  61  0                                        
SHEET    2   N 3 VAL F   7  VAL F  10 -1  N  PHE F   8   O  VAL F  60           
SHEET    3   N 3 VAL F  84  MET F  88 -1  O  ILE F  85   N  MET F   9           
SHEET    1   O 2 ARG G  77  VAL G  79  0                                        
SHEET    2   O 2 SER G  82  TYR G  84 -1  O  SER G  82   N  VAL G  79           
SHEET    1   P 3 ALA H  23  PRO H  27  0                                        
SHEET    2   P 3 GLU H  57  LEU H  62 -1  O  LEU H  58   N  MET H  26           
SHEET    3   P 3 ILE H  45  VAL H  50 -1  N  LYS H  49   O  GLU H  59           
SHEET    1   Q 2 VAL H 102  SER H 104  0                                        
SHEET    2   Q 2 VAL H 109  THR H 111 -1  O  MET H 110   N  VAL H 103           
SHEET    1   R 3 TYR I   5  GLY I   7  0                                        
SHEET    2   R 3 SER I  14  LYS I  21 -1  O  ILE I  20   N  TYR I   5           
SHEET    3   R 3 ARG I  10  ARG I  11 -1  N  ARG I  11   O  SER I  14           
SHEET    1   S 4 TYR I   5  GLY I   7  0                                        
SHEET    2   S 4 SER I  14  LYS I  21 -1  O  ILE I  20   N  TYR I   5           
SHEET    3   S 4 ASP I  61  VAL I  66 -1  O  ASP I  61   N  LYS I  21           
SHEET    4   S 4 LYS I  26  ILE I  29  1  N  VAL I  28   O  LEU I  62           
SHEET    1   T 2 GLU Z   3  LYS Z   4  0                                        
SHEET    2   T 2 LYS Z 263  LEU Z 264  1  O  LEU Z 264   N  GLU Z   3           
SHEET    1   U 3 HIS Z  11  VAL Z  14  0                                        
SHEET    2   U 3 HIS Z  75  HIS Z  78  1  O  ALA Z  77   N  VAL Z  12           
SHEET    3   U 3 VAL Z  67  ASP Z  70 -1  N  TYR Z  69   O  TYR Z  76           
SHEET    1   V 4 THR Z  16  ILE Z  17  0                                        
SHEET    2   V 4 ILE Z 102  ALA Z 106  1  O  ILE Z 102   N  ILE Z  17           
SHEET    3   V 4 ILE Z 131  ASN Z 135  1  O  PHE Z 133   N  VAL Z 105           
SHEET    4   V 4 VAL Z 170  GLY Z 172  1  O  GLY Z 172   N  LEU Z 134           
SHEET    1   W 6 ASP Z 216  SER Z 219  0                                        
SHEET    2   W 6 THR Z 225  ARG Z 230 -1  O  THR Z 228   N  ASP Z 216           
SHEET    3   W 6 ASN Z 273  ARG Z 279 -1  O  VAL Z 274   N  GLY Z 229           
SHEET    4   W 6 GLN Z 251  GLY Z 257 -1  N  GLY Z 257   O  LEU Z 277           
SHEET    5   W 6 GLU Z 240  VAL Z 245 -1  N  ILE Z 244   O  GLN Z 251           
SHEET    6   W 6 VAL Z 291  ALA Z 293 -1  O  VAL Z 291   N  VAL Z 245           
SHEET    1   X 8 ASN Z 355  ILE Z 356  0                                        
SHEET    2   X 8 PRO Z 300  ILE Z 310 -1  N  VAL Z 308   O  ILE Z 356           
SHEET    3   X 8 ARG Z 381  VAL Z 391 -1  O  LYS Z 390   N  GLU Z 305           
SHEET    4   X 8 ARG Z 373  GLU Z 378 -1  N  ILE Z 376   O  VAL Z 383           
SHEET    5   X 8 GLN Z 329  PHE Z 332 -1  N  GLN Z 329   O  ARG Z 377           
SHEET    6   X 8 THR Z 335  THR Z 340 -1  O  VAL Z 337   N  PHE Z 330           
SHEET    7   X 8 VAL Z 359  ALA Z 367 -1  O  ILE Z 363   N  THR Z 338           
SHEET    8   X 8 PRO Z 300  ILE Z 310 -1  N  PHE Z 304   O  VAL Z 360           
LINK         O3'   G V  53                 P   5MU V  54     1555   1555  1.58  
LINK         O3' 5MU V  54                 P     U V  55     1555   1555  1.61  
CISPEP   1 ILE Z  199    PRO Z  200          0       -12.07                     
SITE     1 AC1 14 VAL Z  20  ASP Z  21  HIS Z  22  GLY Z  23                    
SITE     2 AC1 14 LYS Z  24  THR Z  25  THR Z  26  HIS Z  84                    
SITE     3 AC1 14 ASN Z 135  MET Z 139  SER Z 173  ALA Z 174                    
SITE     4 AC1 14 LEU Z 175  LYS Z 176                                          
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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