GenomeNet

Database: PDB
Entry: 3IZU
LinkDB: 3IZU
Original site: 3IZU 
HEADER    RIBOSOME                                07-JAN-11   3IZU              
TITLE     STRUCTURAL INSIGHTS INTO COGNATE VS. NEAR-COGNATE DISCRIMINATION      
TITLE    2 DURING DECODING. THIS ENTRY CONTAINS THE LARGE SUBUNIT OF A RIBOSOME 
TITLE    3 PROGRAMMED WITH A COGNATE CODON                                      
SPLIT      3IZU 3IZW                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBOSOMAL RNA 5S;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: RIBOSOMAL RNA 23S;                                         
COMPND   6 CHAIN: B;                                                            
COMPND   7 MOL_ID: 3;                                                           
COMPND   8 MOLECULE: 50S RIBOSOMAL PROTEIN L1;                                  
COMPND   9 CHAIN: C;                                                            
COMPND  10 MOL_ID: 4;                                                           
COMPND  11 MOLECULE: 50S RIBOSOMAL PROTEIN L2;                                  
COMPND  12 CHAIN: D;                                                            
COMPND  13 MOL_ID: 5;                                                           
COMPND  14 MOLECULE: 50S RIBOSOMAL PROTEIN L3;                                  
COMPND  15 CHAIN: E;                                                            
COMPND  16 MOL_ID: 6;                                                           
COMPND  17 MOLECULE: 50S RIBOSOMAL PROTEIN L4;                                  
COMPND  18 CHAIN: F;                                                            
COMPND  19 MOL_ID: 7;                                                           
COMPND  20 MOLECULE: 50S RIBOSOMAL PROTEIN L5;                                  
COMPND  21 CHAIN: G;                                                            
COMPND  22 MOL_ID: 8;                                                           
COMPND  23 MOLECULE: 50S RIBOSOMAL PROTEIN L6;                                  
COMPND  24 CHAIN: H;                                                            
COMPND  25 MOL_ID: 9;                                                           
COMPND  26 MOLECULE: 50S RIBOSOMAL PROTEIN L9;                                  
COMPND  27 CHAIN: I;                                                            
COMPND  28 MOL_ID: 10;                                                          
COMPND  29 MOLECULE: 50S RIBOSOMAL PROTEIN L11;                                 
COMPND  30 CHAIN: J;                                                            
COMPND  31 MOL_ID: 11;                                                          
COMPND  32 MOLECULE: 50S RIBOSOMAL PROTEIN L13;                                 
COMPND  33 CHAIN: K;                                                            
COMPND  34 MOL_ID: 12;                                                          
COMPND  35 MOLECULE: 50S RIBOSOMAL PROTEIN L14;                                 
COMPND  36 CHAIN: L;                                                            
COMPND  37 MOL_ID: 13;                                                          
COMPND  38 MOLECULE: 50S RIBOSOMAL PROTEIN L15;                                 
COMPND  39 CHAIN: M;                                                            
COMPND  40 MOL_ID: 14;                                                          
COMPND  41 MOLECULE: 50S RIBOSOMAL PROTEIN L16;                                 
COMPND  42 CHAIN: N;                                                            
COMPND  43 MOL_ID: 15;                                                          
COMPND  44 MOLECULE: 50S RIBOSOMAL PROTEIN L17;                                 
COMPND  45 CHAIN: O;                                                            
COMPND  46 MOL_ID: 16;                                                          
COMPND  47 MOLECULE: 50S RIBOSOMAL PROTEIN L18;                                 
COMPND  48 CHAIN: P;                                                            
COMPND  49 MOL_ID: 17;                                                          
COMPND  50 MOLECULE: 50S RIBOSOMAL PROTEIN L19;                                 
COMPND  51 CHAIN: Q;                                                            
COMPND  52 MOL_ID: 18;                                                          
COMPND  53 MOLECULE: 50S RIBOSOMAL PROTEIN L20;                                 
COMPND  54 CHAIN: R;                                                            
COMPND  55 MOL_ID: 19;                                                          
COMPND  56 MOLECULE: 50S RIBOSOMAL PROTEIN L21;                                 
COMPND  57 CHAIN: S;                                                            
COMPND  58 MOL_ID: 20;                                                          
COMPND  59 MOLECULE: 50S RIBOSOMAL PROTEIN L22;                                 
COMPND  60 CHAIN: T;                                                            
COMPND  61 MOL_ID: 21;                                                          
COMPND  62 MOLECULE: 50S RIBOSOMAL PROTEIN L23;                                 
COMPND  63 CHAIN: U;                                                            
COMPND  64 MOL_ID: 22;                                                          
COMPND  65 MOLECULE: 50S RIBOSOMAL PROTEIN L24;                                 
COMPND  66 CHAIN: V;                                                            
COMPND  67 MOL_ID: 23;                                                          
COMPND  68 MOLECULE: 50S RIBOSOMAL PROTEIN L25;                                 
COMPND  69 CHAIN: W;                                                            
COMPND  70 MOL_ID: 24;                                                          
COMPND  71 MOLECULE: 50S RIBOSOMAL PROTEIN L27;                                 
COMPND  72 CHAIN: X;                                                            
COMPND  73 MOL_ID: 25;                                                          
COMPND  74 MOLECULE: 50S RIBOSOMAL PROTEIN L28;                                 
COMPND  75 CHAIN: Y;                                                            
COMPND  76 MOL_ID: 26;                                                          
COMPND  77 MOLECULE: 50S RIBOSOMAL PROTEIN L29;                                 
COMPND  78 CHAIN: Z;                                                            
COMPND  79 MOL_ID: 27;                                                          
COMPND  80 MOLECULE: 50S RIBOSOMAL PROTEIN L30;                                 
COMPND  81 CHAIN: a;                                                            
COMPND  82 MOL_ID: 28;                                                          
COMPND  83 MOLECULE: 50S RIBOSOMAL PROTEIN L31;                                 
COMPND  84 CHAIN: b;                                                            
COMPND  85 MOL_ID: 29;                                                          
COMPND  86 MOLECULE: 50S RIBOSOMAL PROTEIN L32;                                 
COMPND  87 CHAIN: c;                                                            
COMPND  88 MOL_ID: 30;                                                          
COMPND  89 MOLECULE: 50S RIBOSOMAL PROTEIN L33;                                 
COMPND  90 CHAIN: d;                                                            
COMPND  91 MOL_ID: 31;                                                          
COMPND  92 MOLECULE: 50S RIBOSOMAL PROTEIN L34;                                 
COMPND  93 CHAIN: e;                                                            
COMPND  94 MOL_ID: 32;                                                          
COMPND  95 MOLECULE: 50S RIBOSOMAL PROTEIN L35;                                 
COMPND  96 CHAIN: f;                                                            
COMPND  97 MOL_ID: 33;                                                          
COMPND  98 MOLECULE: 50S RIBOSOMAL PROTEIN L36;                                 
COMPND  99 CHAIN: g                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   7 ORGANISM_TAXID: 83333;                                               
SOURCE   8 STRAIN: K12;                                                         
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  11 ORGANISM_TAXID: 83333;                                               
SOURCE  12 STRAIN: K12;                                                         
SOURCE  13 MOL_ID: 4;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  15 ORGANISM_TAXID: 83333;                                               
SOURCE  16 STRAIN: K12;                                                         
SOURCE  17 MOL_ID: 5;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  19 ORGANISM_TAXID: 83333;                                               
SOURCE  20 STRAIN: K12;                                                         
SOURCE  21 MOL_ID: 6;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  23 ORGANISM_TAXID: 83333;                                               
SOURCE  24 STRAIN: K12;                                                         
SOURCE  25 MOL_ID: 7;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  27 ORGANISM_TAXID: 83333;                                               
SOURCE  28 STRAIN: K12;                                                         
SOURCE  29 MOL_ID: 8;                                                           
SOURCE  30 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  31 ORGANISM_TAXID: 83333;                                               
SOURCE  32 STRAIN: K12;                                                         
SOURCE  33 MOL_ID: 9;                                                           
SOURCE  34 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  35 ORGANISM_TAXID: 83333;                                               
SOURCE  36 STRAIN: K12;                                                         
SOURCE  37 MOL_ID: 10;                                                          
SOURCE  38 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  39 ORGANISM_TAXID: 83333;                                               
SOURCE  40 STRAIN: K12;                                                         
SOURCE  41 MOL_ID: 11;                                                          
SOURCE  42 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  43 ORGANISM_TAXID: 83333;                                               
SOURCE  44 STRAIN: K12;                                                         
SOURCE  45 MOL_ID: 12;                                                          
SOURCE  46 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  47 ORGANISM_TAXID: 83333;                                               
SOURCE  48 STRAIN: K12;                                                         
SOURCE  49 MOL_ID: 13;                                                          
SOURCE  50 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  51 ORGANISM_TAXID: 83333;                                               
SOURCE  52 STRAIN: K12;                                                         
SOURCE  53 MOL_ID: 14;                                                          
SOURCE  54 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  55 ORGANISM_TAXID: 83333;                                               
SOURCE  56 STRAIN: K12;                                                         
SOURCE  57 MOL_ID: 15;                                                          
SOURCE  58 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  59 ORGANISM_TAXID: 83333;                                               
SOURCE  60 STRAIN: K12;                                                         
SOURCE  61 MOL_ID: 16;                                                          
SOURCE  62 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  63 ORGANISM_TAXID: 83333;                                               
SOURCE  64 STRAIN: K12;                                                         
SOURCE  65 MOL_ID: 17;                                                          
SOURCE  66 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  67 ORGANISM_TAXID: 83333;                                               
SOURCE  68 STRAIN: K12;                                                         
SOURCE  69 MOL_ID: 18;                                                          
SOURCE  70 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  71 ORGANISM_TAXID: 83333;                                               
SOURCE  72 STRAIN: K12;                                                         
SOURCE  73 MOL_ID: 19;                                                          
SOURCE  74 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  75 ORGANISM_TAXID: 83333;                                               
SOURCE  76 STRAIN: K12;                                                         
SOURCE  77 MOL_ID: 20;                                                          
SOURCE  78 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  79 ORGANISM_TAXID: 83333;                                               
SOURCE  80 STRAIN: K12;                                                         
SOURCE  81 MOL_ID: 21;                                                          
SOURCE  82 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  83 ORGANISM_TAXID: 83333;                                               
SOURCE  84 STRAIN: K12;                                                         
SOURCE  85 MOL_ID: 22;                                                          
SOURCE  86 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  87 ORGANISM_TAXID: 83333;                                               
SOURCE  88 STRAIN: K12;                                                         
SOURCE  89 MOL_ID: 23;                                                          
SOURCE  90 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  91 ORGANISM_TAXID: 83333;                                               
SOURCE  92 STRAIN: K12;                                                         
SOURCE  93 MOL_ID: 24;                                                          
SOURCE  94 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  95 ORGANISM_TAXID: 83333;                                               
SOURCE  96 STRAIN: K12;                                                         
SOURCE  97 MOL_ID: 25;                                                          
SOURCE  98 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  99 ORGANISM_TAXID: 83333;                                               
SOURCE 100 STRAIN: K12;                                                         
SOURCE 101 MOL_ID: 26;                                                          
SOURCE 102 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE 103 ORGANISM_TAXID: 83333;                                               
SOURCE 104 STRAIN: K12;                                                         
SOURCE 105 MOL_ID: 27;                                                          
SOURCE 106 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE 107 ORGANISM_TAXID: 83333;                                               
SOURCE 108 STRAIN: K12;                                                         
SOURCE 109 MOL_ID: 28;                                                          
SOURCE 110 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE 111 ORGANISM_TAXID: 83333;                                               
SOURCE 112 STRAIN: K12;                                                         
SOURCE 113 MOL_ID: 29;                                                          
SOURCE 114 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE 115 ORGANISM_TAXID: 83333;                                               
SOURCE 116 STRAIN: K12;                                                         
SOURCE 117 MOL_ID: 30;                                                          
SOURCE 118 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE 119 ORGANISM_TAXID: 83333;                                               
SOURCE 120 STRAIN: K12;                                                         
SOURCE 121 MOL_ID: 31;                                                          
SOURCE 122 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE 123 ORGANISM_TAXID: 83333;                                               
SOURCE 124 STRAIN: K12;                                                         
SOURCE 125 MOL_ID: 32;                                                          
SOURCE 126 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE 127 ORGANISM_TAXID: 83333;                                               
SOURCE 128 STRAIN: K12;                                                         
SOURCE 129 MOL_ID: 33;                                                          
SOURCE 130 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE 131 ORGANISM_TAXID: 83333;                                               
SOURCE 132 STRAIN: K12                                                          
KEYWDS    TRANSLATION, RIBOSOME, TERNARY COMPLEX, TRNA INCORPORATION, CRYOEM,   
KEYWDS   2 NEAR-COGNATE                                                         
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    X.AGIRREZABALA,E.SCHREINER,L.G.TRABUCO,J.LEI,R.F.ORTIZ-MEOZ,          
AUTHOR   2 K.SCHULTEN,R.GREEN,J.FRANK                                           
REVDAT   4   30-MAY-12 3IZU    1       REMARK                                   
REVDAT   3   01-FEB-12 3IZU    1       MODRES CRYST1 LINK   REMARK              
REVDAT   2   04-MAY-11 3IZU    1       JRNL                                     
REVDAT   1   23-MAR-11 3IZU    0                                                
JRNL        AUTH   X.AGIRREZABALA,E.SCHREINER,L.G.TRABUCO,J.LEI,R.F.ORTIZ-MEOZ, 
JRNL        AUTH 2 K.SCHULTEN,R.GREEN,J.FRANK                                   
JRNL        TITL   STRUCTURAL INSIGHTS INTO COGNATE VERSUS NEAR-COGNATE         
JRNL        TITL 2 DISCRIMINATION DURING DECODING.                              
JRNL        REF    EMBO J.                       V.  30  1497 2011              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   21378755                                                     
JRNL        DOI    10.1038/EMBOJ.2011.58                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    8.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : NAMD 2.7                                  
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 2I2V                                
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : NULL                                
REMARK   3   REFINEMENT TARGET            : RMSD < 0.1   A/NS                   
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : FLEXIBLE FITTING, MDFF                           
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 8.250                          
REMARK   3   NUMBER OF PARTICLES               : NULL                           
REMARK   3   CTF CORRECTION METHOD             : NULL                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 3IZU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JAN-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB160072.                                      
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                 : NULL                              
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : NULL                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : NULL                           
REMARK 245   DETECTOR TYPE                     : NULL                           
REMARK 245   MINIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MAXIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : NULL                           
REMARK 245   IMAGING MODE                      : NULL                           
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : NULL                           
REMARK 245   ILLUMINATION MODE                 : NULL                           
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : NULL                           
REMARK 245   ACCELERATION VOLTAGE (KV)         : NULL                           
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: 33-MERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I,            
REMARK 350                    AND CHAINS: J, K, L, M, N, O, P, Q, R,            
REMARK 350                    AND CHAINS: S, T, U, V, W, X, Y, Z, a,            
REMARK 350                    AND CHAINS: b, c, d, e, f, g                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET D     0                                                      
REMARK 465     MET G     0                                                      
REMARK 465     MET H     0                                                      
REMARK 465     MET J     0                                                      
REMARK 465     MET Q     0                                                      
REMARK 465     MET R     0                                                      
REMARK 465     MET V     0                                                      
REMARK 465     MET X     0                                                      
REMARK 465     MET Y     0                                                      
REMARK 465     MET a     0                                                      
REMARK 465     MET c     0                                                      
REMARK 465     MET d     0                                                      
REMARK 465     MET f     0                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500      U A   1   O4' -  C1' -  N1  ANGL. DEV. =   4.8 DEGREES          
REMARK 500      C A   3   C5' -  C4' -  O4' ANGL. DEV. =   5.7 DEGREES          
REMARK 500      C A   4   O4' -  C1' -  N1  ANGL. DEV. =   4.7 DEGREES          
REMARK 500      U A   5   O4' -  C1' -  N1  ANGL. DEV. =   4.5 DEGREES          
REMARK 500      C A  11   O4' -  C1' -  N1  ANGL. DEV. =   6.8 DEGREES          
REMARK 500      G A  13   N9  -  C1' -  C2' ANGL. DEV. =  -9.3 DEGREES          
REMARK 500      G A  13   O4' -  C1' -  N9  ANGL. DEV. =  11.9 DEGREES          
REMARK 500      U A  14   C5' -  C4' -  C3' ANGL. DEV. =  -9.0 DEGREES          
REMARK 500      G A  16   C8  -  N9  -  C4  ANGL. DEV. =  -2.4 DEGREES          
REMARK 500      G A  18   C5' -  C4' -  O4' ANGL. DEV. =   5.6 DEGREES          
REMARK 500      C A  19   O4' -  C1' -  N1  ANGL. DEV. =   4.9 DEGREES          
REMARK 500      C A  28   O4' -  C1' -  N1  ANGL. DEV. =   5.2 DEGREES          
REMARK 500      A A  29   O4' -  C1' -  N9  ANGL. DEV. =   4.3 DEGREES          
REMARK 500      C A  30   O4' -  C1' -  N1  ANGL. DEV. =   9.8 DEGREES          
REMARK 500      C A  31   C5' -  C4' -  O4' ANGL. DEV. =   6.8 DEGREES          
REMARK 500      U A  32   C3' -  C2' -  C1' ANGL. DEV. =  -4.4 DEGREES          
REMARK 500      U A  32   O4' -  C1' -  N1  ANGL. DEV. =   5.1 DEGREES          
REMARK 500      A A  34   C5' -  C4' -  O4' ANGL. DEV. =   7.3 DEGREES          
REMARK 500      C A  36   C5' -  C4' -  C3' ANGL. DEV. =  -8.9 DEGREES          
REMARK 500      C A  36   O4' -  C1' -  N1  ANGL. DEV. =   6.1 DEGREES          
REMARK 500      A A  39   O4' -  C1' -  N9  ANGL. DEV. =   4.3 DEGREES          
REMARK 500      G A  41   O4' -  C1' -  N9  ANGL. DEV. =   5.2 DEGREES          
REMARK 500      C A  42   O4' -  C1' -  N1  ANGL. DEV. =   4.9 DEGREES          
REMARK 500      C A  47   O4' -  C1' -  N1  ANGL. DEV. =   5.3 DEGREES          
REMARK 500      C A  49   O4' -  C1' -  N1  ANGL. DEV. =  10.0 DEGREES          
REMARK 500      A A  50   C5' -  C4' -  C3' ANGL. DEV. =  -8.6 DEGREES          
REMARK 500      A A  50   C5' -  C4' -  O4' ANGL. DEV. =   5.9 DEGREES          
REMARK 500      A A  52   O4' -  C1' -  N9  ANGL. DEV. =   7.3 DEGREES          
REMARK 500      G A  64   O4' -  C1' -  N9  ANGL. DEV. =   4.8 DEGREES          
REMARK 500      G A  67   C5' -  C4' -  O4' ANGL. DEV. =   6.9 DEGREES          
REMARK 500      G A  67   C8  -  N9  -  C4  ANGL. DEV. =  -2.7 DEGREES          
REMARK 500      C A  68   O4' -  C1' -  N1  ANGL. DEV. =   7.0 DEGREES          
REMARK 500      G A  69   O4' -  C1' -  N9  ANGL. DEV. =   5.1 DEGREES          
REMARK 500      C A  70   O4' -  C1' -  N1  ANGL. DEV. =   5.9 DEGREES          
REMARK 500      C A  71   O4' -  C1' -  N1  ANGL. DEV. =   4.9 DEGREES          
REMARK 500      G A  72   C5' -  C4' -  O4' ANGL. DEV. =   5.6 DEGREES          
REMARK 500      U A  74   O4' -  C1' -  N1  ANGL. DEV. =   4.9 DEGREES          
REMARK 500      G A  75   O5' -  C5' -  C4' ANGL. DEV. =  -7.6 DEGREES          
REMARK 500      U A  77   C5' -  C4' -  O4' ANGL. DEV. =   5.5 DEGREES          
REMARK 500      U A  77   C2' -  C3' -  O3' ANGL. DEV. =   9.7 DEGREES          
REMARK 500      G A  79   C8  -  N9  -  C4  ANGL. DEV. =  -2.4 DEGREES          
REMARK 500      G A  84   O4' -  C1' -  N9  ANGL. DEV. =   4.7 DEGREES          
REMARK 500      G A  85   O4' -  C1' -  N9  ANGL. DEV. =   5.1 DEGREES          
REMARK 500      G A  86   O4' -  C1' -  N9  ANGL. DEV. =   5.7 DEGREES          
REMARK 500      U A  89   O4' -  C1' -  N1  ANGL. DEV. =   5.7 DEGREES          
REMARK 500      C A  90   C1' -  O4' -  C4' ANGL. DEV. =  -5.3 DEGREES          
REMARK 500      C A  91   O4' -  C1' -  N1  ANGL. DEV. =   4.9 DEGREES          
REMARK 500      C A  92   O4' -  C1' -  N1  ANGL. DEV. =   5.0 DEGREES          
REMARK 500      C A  93   O4' -  C1' -  N1  ANGL. DEV. =   7.2 DEGREES          
REMARK 500      U A  95   C5' -  C4' -  C3' ANGL. DEV. =  -9.0 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS    1525 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    ASP C  16        7.70   -152.08                                   
REMARK 500    THR C  69       -6.57   -140.84                                   
REMARK 500    ASN C  83       92.18    -65.55                                   
REMARK 500    MET C  97      -34.58   -147.82                                   
REMARK 500    LEU C 131      -19.73   -149.96                                   
REMARK 500    PRO C 140      -12.85    -49.23                                   
REMARK 500    LYS C 141      -52.08   -128.22                                   
REMARK 500    ASN C 148       63.48   -102.41                                   
REMARK 500    ASP C 166      -52.95   -138.66                                   
REMARK 500    THR C 217      -86.34    -61.32                                   
REMARK 500    LEU C 229       26.20    -61.16                                   
REMARK 500    SER C 230       18.96   -151.18                                   
REMARK 500    PRO D   7       42.30    -86.26                                   
REMARK 500    ASN D  36       61.42   -161.11                                   
REMARK 500    ILE D  63       90.77    -66.21                                   
REMARK 500    VAL D 119       13.30    -59.39                                   
REMARK 500    PRO D 125      115.36    -35.35                                   
REMARK 500    VAL D 140     -131.63     51.13                                   
REMARK 500    HIS D 141      -53.76   -161.43                                   
REMARK 500    ALA D 154       73.47     46.27                                   
REMARK 500    ALA D 169        2.90    -67.33                                   
REMARK 500    THR D 190     -171.10     51.56                                   
REMARK 500    GLU D 193      158.50     57.77                                   
REMARK 500    ARG D 237      -19.09     56.78                                   
REMARK 500    LYS D 252       53.40   -152.47                                   
REMARK 500    SER D 258       15.13   -151.08                                   
REMARK 500    LYS D 260        4.64     47.25                                   
REMARK 500    ALA E  31       97.51    -68.19                                   
REMARK 500    ASN E  32       51.18    -93.57                                   
REMARK 500    ALA E  41       -0.53   -166.60                                   
REMARK 500    ASP E  43       25.48     36.12                                   
REMARK 500    ALA E  57       19.70     56.00                                   
REMARK 500    GLU E  88      -39.49   -144.03                                   
REMARK 500    SER E 113     -175.31     62.75                                   
REMARK 500    VAL E 122       -2.57     38.36                                   
REMARK 500    ARG E 124       -8.92   -152.86                                   
REMARK 500    SER E 137      100.07    -43.74                                   
REMARK 500    GLN E 150      -62.25     31.24                                   
REMARK 500    LYS E 157      109.55    -52.08                                   
REMARK 500    ALA E 162      167.74     69.80                                   
REMARK 500    ASN E 167       15.95   -146.49                                   
REMARK 500    ARG E 169      -99.00   -151.26                                   
REMARK 500    VAL E 170      143.00     58.63                                   
REMARK 500    GLU E 183      -29.88     73.89                                   
REMARK 500    ALA F  39        5.79    -67.20                                   
REMARK 500    GLN F  41      -33.84   -135.33                                   
REMARK 500    LYS F  57      157.82    -49.15                                   
REMARK 500    GLN F  62      141.89     63.10                                   
REMARK 500    THR F  65      -57.83   -151.17                                   
REMARK 500    ARG F  79       98.62    -60.25                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     208 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 ASP C   43     VAL C   44                  148.15                    
REMARK 500 VAL C   44     ALA C   45                  149.46                    
REMARK 500 ALA E   47     ILE E   48                  148.15                    
REMARK 500 ILE F   77     TRP F   78                  147.03                    
REMARK 500 ALA H   39     VAL H   40                 -149.94                    
REMARK 500 GLY H  107     PHE H  108                  147.28                    
REMARK 500 LEU I  117     PRO I  118                  145.75                    
REMARK 500 GLY K   51     ASP K   52                 -149.13                    
REMARK 500 LYS R    4     ARG R    5                 -143.40                    
REMARK 500 GLN e    6     PRO e    7                 -147.10                    
REMARK 500 SER e   45     LYS e   46                  149.12                    
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      G A   2         0.08    SIDE CHAIN                              
REMARK 500      G A   7         0.05    SIDE CHAIN                              
REMARK 500      G A  13         0.12    SIDE CHAIN                              
REMARK 500      U A  14         0.10    SIDE CHAIN                              
REMARK 500      A A  15         0.06    SIDE CHAIN                              
REMARK 500      C A  19         0.09    SIDE CHAIN                              
REMARK 500      C A  26         0.12    SIDE CHAIN                              
REMARK 500      C A  36         0.11    SIDE CHAIN                              
REMARK 500      C A  37         0.07    SIDE CHAIN                              
REMARK 500      U A  40         0.12    SIDE CHAIN                              
REMARK 500      G A  41         0.05    SIDE CHAIN                              
REMARK 500      U A  48         0.08    SIDE CHAIN                              
REMARK 500      A A  52         0.13    SIDE CHAIN                              
REMARK 500      C A  62         0.06    SIDE CHAIN                              
REMARK 500      G A  64         0.06    SIDE CHAIN                              
REMARK 500      U A  65         0.08    SIDE CHAIN                              
REMARK 500      A A  66         0.06    SIDE CHAIN                              
REMARK 500      G A  67         0.07    SIDE CHAIN                              
REMARK 500      G A  72         0.07    SIDE CHAIN                              
REMARK 500      U A  87         0.10    SIDE CHAIN                              
REMARK 500      C A  88         0.09    SIDE CHAIN                              
REMARK 500      U A  95         0.08    SIDE CHAIN                              
REMARK 500      A A  99         0.06    SIDE CHAIN                              
REMARK 500      U A 103         0.09    SIDE CHAIN                              
REMARK 500      G A 107         0.07    SIDE CHAIN                              
REMARK 500      A A 108         0.07    SIDE CHAIN                              
REMARK 500      A A 109         0.08    SIDE CHAIN                              
REMARK 500      G B   7         0.06    SIDE CHAIN                              
REMARK 500      G B  17         0.08    SIDE CHAIN                              
REMARK 500      C B  20         0.06    SIDE CHAIN                              
REMARK 500      C B  22         0.07    SIDE CHAIN                              
REMARK 500      G B  23         0.07    SIDE CHAIN                              
REMARK 500      G B  24         0.09    SIDE CHAIN                              
REMARK 500      U B  29         0.07    SIDE CHAIN                              
REMARK 500      C B  32         0.06    SIDE CHAIN                              
REMARK 500      C B  33         0.08    SIDE CHAIN                              
REMARK 500      U B  34         0.07    SIDE CHAIN                              
REMARK 500      G B  45         0.07    SIDE CHAIN                              
REMARK 500      C B  47         0.06    SIDE CHAIN                              
REMARK 500      G B  60         0.07    SIDE CHAIN                              
REMARK 500      U B  62         0.12    SIDE CHAIN                              
REMARK 500      U B  65         0.08    SIDE CHAIN                              
REMARK 500      G B  68         0.07    SIDE CHAIN                              
REMARK 500      A B  71         0.07    SIDE CHAIN                              
REMARK 500      U B  72         0.07    SIDE CHAIN                              
REMARK 500      A B  74         0.07    SIDE CHAIN                              
REMARK 500      G B  77         0.05    SIDE CHAIN                              
REMARK 500      G B  81         0.07    SIDE CHAIN                              
REMARK 500      A B  83         0.12    SIDE CHAIN                              
REMARK 500      G B  88         0.05    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     852 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    VAL E  24        -11.04                                           
REMARK 500    ALA E  47        -10.23                                           
REMARK 500    VAL I  31        -12.78                                           
REMARK 500    GLY b  54        -10.50                                           
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    VAL C  73        24.2      L          L   OUTSIDE RANGE           
REMARK 500    PHE O  80        24.7      L          L   OUTSIDE RANGE           
REMARK 500    ILE X  36        24.1      L          L   OUTSIDE RANGE           
REMARK 500    VAL Z  46        24.8      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-1849   RELATED DB: EMDB                              
REMARK 900 CRYO-EM MAP OF E. COLI RIBOSOME PROGRAMMED WITH COGNATE              
REMARK 900 CODON                                                                
DBREF1 3IZU A    1   120  GB                   AP012030.1                       
DBREF2 3IZU A     AP012030                       228757      228876             
DBREF1 3IZU B    1  2904  GB                   AP012030.1                       
DBREF2 3IZU B     AP012030                      4147746     4150649             
DBREF  3IZU C    1   234  UNP    P0A7L0   RL1_ECOLI        1    234             
DBREF  3IZU D    0   272  UNP    P60422   RL2_ECOLI        1    273             
DBREF  3IZU E    1   209  UNP    P60438   RL3_ECOLI        1    209             
DBREF  3IZU F    1   201  UNP    P60723   RL4_ECOLI        1    201             
DBREF  3IZU G    0   178  UNP    P62399   RL5_ECOLI        1    179             
DBREF  3IZU H    0   176  UNP    P0AG55   RL6_ECOLI        1    177             
DBREF  3IZU I    1   149  UNP    P0A7R1   RL9_ECOLI        1    149             
DBREF  3IZU J    0   141  UNP    P0A7J7   RL11_ECOLI       1    142             
DBREF  3IZU K    1   142  UNP    P0AA10   RL13_ECOLI       1    142             
DBREF  3IZU L    1   123  UNP    P0ADY3   RL14_ECOLI       1    123             
DBREF  3IZU M    1   144  UNP    P02413   RL15_ECOLI       1    144             
DBREF  3IZU N    1   136  UNP    P0ADY7   RL16_ECOLI       1    136             
DBREF  3IZU O    1   127  UNP    P0AG44   RL17_ECOLI       1    127             
DBREF  3IZU P    1   117  UNP    P0C018   RL18_ECOLI       1    117             
DBREF  3IZU Q    0   114  UNP    P0A7K6   RL19_ECOLI       1    115             
DBREF  3IZU R    0   117  UNP    P0A7L3   RL20_ECOLI       1    118             
DBREF  3IZU S    1   103  UNP    P0AG48   RL21_ECOLI       1    103             
DBREF  3IZU T    1   110  UNP    P61175   RL22_ECOLI       1    110             
DBREF  3IZU U    1   100  UNP    P0ADZ0   RL23_ECOLI       1    100             
DBREF  3IZU V    0   103  UNP    P60624   RL24_ECOLI       1    104             
DBREF  3IZU W    1    94  UNP    P68919   RL25_ECOLI       1     94             
DBREF  3IZU X    0    84  UNP    P0A7L8   RL27_ECOLI       1     85             
DBREF  3IZU Y    0    77  UNP    P0A7M2   RL28_ECOLI       1     78             
DBREF  3IZU Z    1    63  UNP    P0A7M6   RL29_ECOLI       1     63             
DBREF  3IZU a    0    58  UNP    P0AG51   RL30_ECOLI       1     59             
DBREF  3IZU b    1    70  UNP    P0A7M9   RL31_ECOLI       1     70             
DBREF  3IZU c    0    56  UNP    P0A7N4   RL32_ECOLI       1     57             
DBREF  3IZU d    0    54  UNP    P0A7N9   RL33_ECOLI       1     55             
DBREF  3IZU e    1    46  UNP    P0A7P5   RL34_ECOLI       1     46             
DBREF  3IZU f    0    64  UNP    P0A7Q1   RL35_ECOLI       1     65             
DBREF  3IZU g    1    38  GB     P0A7Q6   P0A7Q6           1     38             
SEQRES   1 A  120    U   G   C   C   U   G   G   C   G   G   C   C   G          
SEQRES   2 A  120    U   A   G   C   G   C   G   G   U   G   G   U   C          
SEQRES   3 A  120    C   C   A   C   C   U   G   A   C   C   C   C   A          
SEQRES   4 A  120    U   G   C   C   G   A   A   C   U   C   A   G   A          
SEQRES   5 A  120    A   G   U   G   A   A   A   C   G   C   C   G   U          
SEQRES   6 A  120    A   G   C   G   C   C   G   A   U   G   G   U   A          
SEQRES   7 A  120    G   U   G   U   G   G   G   G   U   C   U   C   C          
SEQRES   8 A  120    C   C   A   U   G   C   G   A   G   A   G   U   A          
SEQRES   9 A  120    G   G   G   A   A   C   U   G   C   C   A   G   G          
SEQRES  10 A  120    C   A   U                                                  
SEQRES   1 B 2904    G   G   U   U   A   A   G   C   G   A   C   U   A          
SEQRES   2 B 2904    A   G   C   G   U   A   C   A   C   G   G   U   G          
SEQRES   3 B 2904    G   A   U   G   C   C   C   U   G   G   C   A   G          
SEQRES   4 B 2904    U   C   A   G   A   G   G   C   G   A   U   G   A          
SEQRES   5 B 2904    A   G   G   A   C   G   U   G   C   U   A   A   U          
SEQRES   6 B 2904    C   U   G   C   G   A   U   A   A   G   C   G   U          
SEQRES   7 B 2904    C   G   G   U   A   A   G   G   U   G   A   U   A          
SEQRES   8 B 2904    U   G   A   A   C   C   G   U   U   A   U   A   A          
SEQRES   9 B 2904    C   C   G   G   C   G   A   U   U   U   C   C   G          
SEQRES  10 B 2904    A   A   U   G   G   G   G   A   A   A   C   C   C          
SEQRES  11 B 2904    A   G   U   G   U   G   U   U   U   C   G   A   C          
SEQRES  12 B 2904    A   C   A   C   U   A   U   C   A   U   U   A   A          
SEQRES  13 B 2904    C   U   G   A   A   U   C   C   A   U   A   G   G          
SEQRES  14 B 2904    U   U   A   A   U   G   A   G   G   C   G   A   A          
SEQRES  15 B 2904    C   C   G   G   G   G   G   A   A   C   U   G   A          
SEQRES  16 B 2904    A   A   C   A   U   C   U   A   A   G   U   A   C          
SEQRES  17 B 2904    C   C   C   G   A   G   G   A   A   A   A   G   A          
SEQRES  18 B 2904    A   A   U   C   A   A   C   C   G   A   G   A   U          
SEQRES  19 B 2904    U   C   C   C   C   C   A   G   U   A   G   C   G          
SEQRES  20 B 2904    G   C   G   A   G   C   G   A   A   C   G   G   G          
SEQRES  21 B 2904    G   A   G   C   A   G   C   C   C   A   G   A   G          
SEQRES  22 B 2904    C   C   U   G   A   A   U   C   A   G   U   G   U          
SEQRES  23 B 2904    G   U   G   U   G   U   U   A   G   U   G   G   A          
SEQRES  24 B 2904    A   G   C   G   U   C   U   G   G   A   A   A   G          
SEQRES  25 B 2904    G   C   G   C   G   C   G   A   U   A   C   A   G          
SEQRES  26 B 2904    G   G   U   G   A   C   A   G   C   C   C   C   G          
SEQRES  27 B 2904    U   A   C   A   C   A   A   A   A   A   U   G   C          
SEQRES  28 B 2904    A   C   A   U   G   C   U   G   U   G   A   G   C          
SEQRES  29 B 2904    U   C   G   A   U   G   A   G   U   A   G   G   G          
SEQRES  30 B 2904    C   G   G   G   A   C   A   C   G   U   G   G   U          
SEQRES  31 B 2904    A   U   C   C   U   G   U   C   U   G   A   A   U          
SEQRES  32 B 2904    A   U   G   G   G   G   G   G   A   C   C   A   U          
SEQRES  33 B 2904    C   C   U   C   C   A   A   G   G   C   U   A   A          
SEQRES  34 B 2904    A   U   A   C   U   C   C   U   G   A   C   U   G          
SEQRES  35 B 2904    A   C   C   G   A   U   A   G   U   G   A   A   C          
SEQRES  36 B 2904    C   A   G   U   A   C   C   G   U   G   A   G   G          
SEQRES  37 B 2904    G   A   A   A   G   G   C   G   A   A   A   A   G          
SEQRES  38 B 2904    A   A   C   C   C   C   G   G   C   G   A   G   G          
SEQRES  39 B 2904    G   G   A   G   U   G   A   A   A   A   A   G   A          
SEQRES  40 B 2904    A   C   C   U   G   A   A   A   C   C   G   U   G          
SEQRES  41 B 2904    U   A   C   G   U   A   C   A   A   G   C   A   G          
SEQRES  42 B 2904    U   G   G   G   A   G   C   A   C   G   C   U   U          
SEQRES  43 B 2904    A   G   G   C   G   U   G   U   G   A   C   U   G          
SEQRES  44 B 2904    C   G   U   A   C   C   U   U   U   U   G   U   A          
SEQRES  45 B 2904    U   A   A   U   G   G   G   U   C   A   G   C   G          
SEQRES  46 B 2904    A   C   U   U   A   U   A   U   U   C   U   G   U          
SEQRES  47 B 2904    A   G   C   A   A   G   G   U   U   A   A   C   C          
SEQRES  48 B 2904    G   A   A   U   A   G   G   G   G   A   G   C   C          
SEQRES  49 B 2904    G   A   A   G   G   G   A   A   A   C   C   G   A          
SEQRES  50 B 2904    G   U   C   U   U   A   A   C   U   G   G   G   C          
SEQRES  51 B 2904    G   U   U   A   A   G   U   U   G   C   A   G   G          
SEQRES  52 B 2904    G   U   A   U   A   G   A   C   C   C   G   A   A          
SEQRES  53 B 2904    A   C   C   C   G   G   U   G   A   U   C   U   A          
SEQRES  54 B 2904    G   C   C   A   U   G   G   G   C   A   G   G   U          
SEQRES  55 B 2904    U   G   A   A   G   G   U   U   G   G   G   U   A          
SEQRES  56 B 2904    A   C   A   C   U   A   A   C   U   G   G   A   G          
SEQRES  57 B 2904    G   A   C   C   G   A   A   C   C   G   A   C   U          
SEQRES  58 B 2904    A   A   U 1MG PSU 5MU   G   A   A   A   A   A   U          
SEQRES  59 B 2904    U   A   G   C   G   G   A   U   G   A   C   U   U          
SEQRES  60 B 2904    G   U   G   G   C   U   G   G   G   G   G   U   G          
SEQRES  61 B 2904    A   A   A   G   G   C   C   A   A   U   C   A   A          
SEQRES  62 B 2904    A   C   C   G   G   G   A   G   A   U   A   G   C          
SEQRES  63 B 2904    U   G   G   U   U   C   U   C   C   C   C   G   A          
SEQRES  64 B 2904    A   A   G   C   U   A   U   U   U   A   G   G   U          
SEQRES  65 B 2904    A   G   C   G   C   C   U   C   G   U   G   A   A          
SEQRES  66 B 2904    U   U   C   A   U   C   U   C   C   G   G   G   G          
SEQRES  67 B 2904    G   U   A   G   A   G   C   A   C   U   G   U   U          
SEQRES  68 B 2904    U   C   G   G   C   A   A   G   G   G   G   G   U          
SEQRES  69 B 2904    C   A   U   C   C   C   G   A   C   U   U   A   C          
SEQRES  70 B 2904    C   A   A   C   C   C   G   A   U   G   C   A   A          
SEQRES  71 B 2904    A   C   U   G   C   G   A   A   U   A   C   C   G          
SEQRES  72 B 2904    G   A   G   A   A   U   G   U   U   A   U   C   A          
SEQRES  73 B 2904    C   G   G   G   A   G   A   C   A   C   A   C   G          
SEQRES  74 B 2904    G   C   G   G   G PSU   G   C   U   A   A   C   G          
SEQRES  75 B 2904    U   C   C   G   U   C   G   U   G   A   A   G   A          
SEQRES  76 B 2904    G   G   G   A   A   A   C   A   A   C   C   C   A          
SEQRES  77 B 2904    G   A   C   C   G   C   C   A   G   C   U   A   A          
SEQRES  78 B 2904    G   G   U   C   C   C   A   A   A   G   U   C   A          
SEQRES  79 B 2904    U   G   G   U   U   A   A   G   U   G   G   G   A          
SEQRES  80 B 2904    A   A   C   G   A   U   G   U   G   G   G   A   A          
SEQRES  81 B 2904    G   G   C   C   C   A   G   A   C   A   G   C   C          
SEQRES  82 B 2904    A   G   G   A   U   G   U   U   G   G   C   U   U          
SEQRES  83 B 2904    A   G   A   A   G   C   A   G   C   C   A   U   C          
SEQRES  84 B 2904    A   U   U   U   A   A   A   G   A   A   A   G   C          
SEQRES  85 B 2904    G   U   A   A   U   A   G   C   U   C   A   C   U          
SEQRES  86 B 2904    G   G   U   C   G   A   G   U   C   G   G   C   C          
SEQRES  87 B 2904    U   G   C   G   C   G   G   A   A   G   A   U   G          
SEQRES  88 B 2904    U   A   A   C   G   G   G   G   C   U   A   A   A          
SEQRES  89 B 2904    C   C   A   U   G   C   A   C   C   G   A   A   G          
SEQRES  90 B 2904    C   U   G   C   G   G   C   A   G   C   G   A   C          
SEQRES  91 B 2904    G   C   U   U   A   U   G   C   G   U   U   G   U          
SEQRES  92 B 2904    U   G   G   G   U   A   G   G   G   G   A   G   C          
SEQRES  93 B 2904    G   U   U   C   U   G   U   A   A   G   C   C   U          
SEQRES  94 B 2904    G   C   G   A   A   G   G   U   G   U   G   C   U          
SEQRES  95 B 2904    G   U   G   A   G   G   C   A   U   G   C   U   G          
SEQRES  96 B 2904    G   A   G   G   U   A   U   C   A   G   A   A   G          
SEQRES  97 B 2904    U   G   C   G   A   A   U   G   C   U   G   A   C          
SEQRES  98 B 2904    A   U   A   A   G   U   A   A   C   G   A   U   A          
SEQRES  99 B 2904    A   A   G   C   G   G   G   U   G   A   A   A   A          
SEQRES 100 B 2904    G   C   C   C   G   C   U   C   G   C   C   G   G          
SEQRES 101 B 2904    A   A   G   A   C   C   A   A   G   G   G   U   U          
SEQRES 102 B 2904    C   C   U   G   U   C   C   A   A   C   G   U   U          
SEQRES 103 B 2904    A   A   U   C   G   G   G   G   C   A   G   G   G          
SEQRES 104 B 2904    U   G   A   G   U   C   G   A   C   C   C   C   U          
SEQRES 105 B 2904    A   A   G   G   C   G   A   G   G   C   C   G   A          
SEQRES 106 B 2904    A   A   G   G   C   G   U   A   G   U   C   G   A          
SEQRES 107 B 2904    U   G   G   G   A   A   A   C   A   G   G   U   U          
SEQRES 108 B 2904    A   A   U   A   U   U   C   C   U   G   U   A   C          
SEQRES 109 B 2904    U   U   G   G   U   G   U   U   A   C   U   G   C          
SEQRES 110 B 2904    G   A   A   G   G   G   G   G   G   A   C   G   G          
SEQRES 111 B 2904    A   G   A   A   G   G   C   U   A   U   G   U   U          
SEQRES 112 B 2904    G   G   C   C   G   G   G   C   G   A   C   G   G          
SEQRES 113 B 2904    U   U   G   U   C   C   C   G   G   U   U   U   A          
SEQRES 114 B 2904    A   G   C   G   U   G   U   A   G   G   C   U   G          
SEQRES 115 B 2904    G   U   U   U   U   C   C   A   G   G   C   A   A          
SEQRES 116 B 2904    A   U   C   C   G   G   A   A   A   A   U   C   A          
SEQRES 117 B 2904    A   G   G   C   U   G   A   G   G   C   G   U   G          
SEQRES 118 B 2904    A   U   G   A   C   G   A   G   G   C   A   C   U          
SEQRES 119 B 2904    A   C   G   G   U   G   C   U   G   A   A   G   C          
SEQRES 120 B 2904    A   A   C   A   A   A   U   G   C   C   C   U   G          
SEQRES 121 B 2904    C   U   U   C   C   A   G   G   A   A   A   A   G          
SEQRES 122 B 2904    C   C   U   C   U   A   A   G   C   A   U   C   A          
SEQRES 123 B 2904    G   G   U   A   A   C   A   U   C   A   A   A   U          
SEQRES 124 B 2904    C   G   U   A   C   C   C   C   A   A   A   C   C          
SEQRES 125 B 2904    G   A   C   A   C 6MZ   G   G   U   G   G   U   C          
SEQRES 126 B 2904    A   G   G   U   A   G   A   G   A   A   U   A   C          
SEQRES 127 B 2904    C   A   A   G   G   C   G   C   U   U   G   A   G          
SEQRES 128 B 2904    A   G   A   A   C   U   C   G   G   G   U   G   A          
SEQRES 129 B 2904    A   G   G   A   A   C   U   A   G   G   C   A   A          
SEQRES 130 B 2904    A   A   U   G   G   U   G   C   C   G   U   A   A          
SEQRES 131 B 2904    C   U   U   C   G   G   G   A   G   A   A   G   G          
SEQRES 132 B 2904    C   A   C   G   C   U   G   A   U   A   U   G   U          
SEQRES 133 B 2904    A   G   G   U   G   A   G   G   U   C   C   C   U          
SEQRES 134 B 2904    C   G   C   G   G   A   U   G   G   A   G   C   U          
SEQRES 135 B 2904    G   A   A   A   U   C   A   G   U   C   G   A   A          
SEQRES 136 B 2904    G   A   U   A   C   C   A   G   C   U   G   G   C          
SEQRES 137 B 2904    U   G   C   A   A   C   U   G   U   U   U   A   U          
SEQRES 138 B 2904    U   A   A   A   A   A   C   A   C   A   G   C   A          
SEQRES 139 B 2904    C   U   G   U   G   C   A   A   A   C   A   C   G          
SEQRES 140 B 2904    A   A   A   G   U   G   G   A   C   G   U   A   U          
SEQRES 141 B 2904    A   C   G   G   U   G   U   G   A   C   G   C   C          
SEQRES 142 B 2904    U 2MG   C   C   C   G   G   U   G   C   C   G   G          
SEQRES 143 B 2904    A   A   G   G   U   U   A   A   U   U   G   A   U          
SEQRES 144 B 2904    G   G   G   G   U   U   A   G   C   G   C   A   A          
SEQRES 145 B 2904    G   C   G   A   A   G   C   U   C   U   U   G   A          
SEQRES 146 B 2904    U   C   G   A   A   G   C   C   C   C   G   G   U          
SEQRES 147 B 2904    A   A   A   C   G   G   C   G   G   C   C   G PSU          
SEQRES 148 B 2904    A   A   C 3TD   A PSU   A   A   C   G   G   U   C          
SEQRES 149 B 2904    C   U   A   A   G   G   U   A   G   C   G   A   A          
SEQRES 150 B 2904    A 5MU   U   C   C   U   U   G   U   C   G   G   G          
SEQRES 151 B 2904    U   A   A   G   U   U   C   C   G   A   C 5MC   U          
SEQRES 152 B 2904    G   C   A   C   G   A   A   U   G   G   C   G   U          
SEQRES 153 B 2904    A   A   U   G   A   U   G   G   C   C   A   G   G          
SEQRES 154 B 2904    C   U   G   U   C   U   C   C   A   C   C   C   G          
SEQRES 155 B 2904    A   G   A   C   U   C   A   G   U   G   A   A   A          
SEQRES 156 B 2904    U   U   G   A   A   C   U   C   G   C   U   G   U          
SEQRES 157 B 2904    G 6MZ   A   G   A   U   G   C   A   G   U   G   U          
SEQRES 158 B 2904    A   C   C   C   G   C   G   G   C   A   A   G   A          
SEQRES 159 B 2904    C   G   G   A   A   A   G   A   C   C   C   C   G          
SEQRES 160 B 2904    U 7MG   A   A   C   C   U   U   U   A   C   U   A          
SEQRES 161 B 2904    U   A   G   C   U   U   G   A   C   A   C   U   G          
SEQRES 162 B 2904    A   A   C   A   U   U   G   A   G   C   C   U   U          
SEQRES 163 B 2904    G   A   U   G   U   G   U   A   G   G   A   U   A          
SEQRES 164 B 2904    G   G   U   G   G   G   A   G   G   C   U   U   U          
SEQRES 165 B 2904    G   A   A   G   U   G   U   G   G   A   C   G   C          
SEQRES 166 B 2904    C   A   G   U   C   U   G   C   A   U   G   G   A          
SEQRES 167 B 2904    G   C   C   G   A   C   C   U   U   G   A   A   A          
SEQRES 168 B 2904    U   A   C   C   A   C   C   C   U   U   U   A   A          
SEQRES 169 B 2904    U   G   U   U   U   G   A   U   G   U   U   C   U          
SEQRES 170 B 2904    A   A   C   G   U   U   G   A   C   C   C   G   U          
SEQRES 171 B 2904    A   A   U   C   C   G   G   G   U   U   G   C   G          
SEQRES 172 B 2904    G   A   C   A   G   U   G   U   C   U   G   G   U          
SEQRES 173 B 2904    G   G   G   U   A   G   U   U   U   G   A   C   U          
SEQRES 174 B 2904    G OMG   G   G   C   G   G   U   C   U   C   C   U          
SEQRES 175 B 2904    C   C   U   A   A   A   G   A   G   U   A   A   C          
SEQRES 176 B 2904    G   G   A   G   G   A   G   C   A   C   G   A   A          
SEQRES 177 B 2904    G   G   U   U   G   G   C   U   A   A   U   C   C          
SEQRES 178 B 2904    U   G   G   U   C   G   G   A   C   A   U   C   A          
SEQRES 179 B 2904    G   G   A   G   G   U   U   A   G   U   G   C   A          
SEQRES 180 B 2904    A   U   G   G   C   A   U   A   A   G   C   C   A          
SEQRES 181 B 2904    G   C   U   U   G   A   C   U   G   C   G   A   G          
SEQRES 182 B 2904    C   G   U   G   A   C   G   G   C   G   C   G   A          
SEQRES 183 B 2904    G   C   A   G   G   U   G   C   G   A   A   A   G          
SEQRES 184 B 2904    C   A   G   G   U   C   A   U   A   G   U   G   A          
SEQRES 185 B 2904    U   C   C   G   G   U   G   G   U   U   C   U   G          
SEQRES 186 B 2904    A   A   U   G   G   A   A   G   G   G   C   C   A          
SEQRES 187 B 2904    U   C   G   C   U   C   A   A   C   G   G   A   U          
SEQRES 188 B 2904    A   A   A   A   G   G   U   A   C   U   C   C   G          
SEQRES 189 B 2904  2MG   G   G   A H2U   A   A   C   A   G   G   C PSU          
SEQRES 190 B 2904    G   A   U   A   C   C   G   C   C   C   A   A   G          
SEQRES 191 B 2904    A   G   U   U   C   A   U   A   U   C   G   A   C          
SEQRES 192 B 2904    G   G   C   G   G   U   G   U   U   U   G   G   C          
SEQRES 193 B 2904    A OMC   C   U   C   G 2MA PSU   G   U   C   G   G          
SEQRES 194 B 2904    C   U   C   A   U   C   A   C   A   U   C   C   U          
SEQRES 195 B 2904    G   G   G   G   C   U   G   A   A   G   U   A   G          
SEQRES 196 B 2904    G   U   C   C   C   A   A   G   G   G   U   A   U          
SEQRES 197 B 2904    G   G   C OMU   G   U   U   C   G   C   C   A   U          
SEQRES 198 B 2904    U   U   A   A   A   G   U   G   G   U   A   C   G          
SEQRES 199 B 2904   CH   G   A   G   C PSU   G   G   G   U   U   U   A          
SEQRES 200 B 2904    G   A   A   C   G   U   C   G   U   G   A   G   A          
SEQRES 201 B 2904    C   A   G   U PSU   C   G   G   U   C   C   C   U          
SEQRES 202 B 2904    A   U   C   U   G   C   C   G   U   G   G   G   C          
SEQRES 203 B 2904    G   C   U   G   G   A   G   A   A   C   U   G   A          
SEQRES 204 B 2904    G   G   G   G   G   G   C   U   G   C   U   C   C          
SEQRES 205 B 2904    U   A   G   U   A   C   G   A   G   A   G   G   A          
SEQRES 206 B 2904    C   C   G   G   A   G   U   G   G   A   C   G   C          
SEQRES 207 B 2904    A   U   C   A   C   U   G   G   U   G   U   U   C          
SEQRES 208 B 2904    G   G   G   U   U   G   U   C   A   U   G   C   C          
SEQRES 209 B 2904    A   A   U   G   G   C   A   C   U   G   C   C   C          
SEQRES 210 B 2904    G   G   U   A   G   C   U   A   A   A   U   G   C          
SEQRES 211 B 2904    G   G   A   A   G   A   G   A   U   A   A   G   U          
SEQRES 212 B 2904    G   C   U   G   A   A   A   G   C   A   U   C   U          
SEQRES 213 B 2904    A   A   G   C   A   C   G   A   A   A   C   U   U          
SEQRES 214 B 2904    G   C   C   C   C   G   A   G   A   U   G   A   G          
SEQRES 215 B 2904    U   U   C   U   C   C   C   U   G   A   C   C   C          
SEQRES 216 B 2904    U   U   U   A   A   G   G   G   U   C   C   U   G          
SEQRES 217 B 2904    A   A   G   G   A   A   C   G   U   U   G   A   A          
SEQRES 218 B 2904    G   A   C   G   A   C   G   A   C   G   U   U   G          
SEQRES 219 B 2904    A   U   A   G   G   C   C   G   G   G   U   G   U          
SEQRES 220 B 2904    G   U   A   A   G   C   G   C   A   G   C   G   A          
SEQRES 221 B 2904    U   G   C   G   U   U   G   A   G   C   U   A   A          
SEQRES 222 B 2904    C   C   G   G   U   A   C   U   A   A   U   G   A          
SEQRES 223 B 2904    A   C   C   G   U   G   A   G   G   C   U   U   A          
SEQRES 224 B 2904    A   C   C   U   U                                          
SEQRES   1 C  234  MET ALA LYS LEU THR LYS ARG MET ARG VAL ILE ARG GLU          
SEQRES   2 C  234  LYS VAL ASP ALA THR LYS GLN TYR ASP ILE ASN GLU ALA          
SEQRES   3 C  234  ILE ALA LEU LEU LYS GLU LEU ALA THR ALA LYS PHE VAL          
SEQRES   4 C  234  GLU SER VAL ASP VAL ALA VAL ASN LEU GLY ILE ASP ALA          
SEQRES   5 C  234  ARG LYS SER ASP GLN ASN VAL ARG GLY ALA THR VAL LEU          
SEQRES   6 C  234  PRO HIS GLY THR GLY ARG SER VAL ARG VAL ALA VAL PHE          
SEQRES   7 C  234  THR GLN GLY ALA ASN ALA GLU ALA ALA LYS ALA ALA GLY          
SEQRES   8 C  234  ALA GLU LEU VAL GLY MET GLU ASP LEU ALA ASP GLN ILE          
SEQRES   9 C  234  LYS LYS GLY GLU MET ASN PHE ASP VAL VAL ILE ALA SER          
SEQRES  10 C  234  PRO ASP ALA MET ARG VAL VAL GLY GLN LEU GLY GLN VAL          
SEQRES  11 C  234  LEU GLY PRO ARG GLY LEU MET PRO ASN PRO LYS VAL GLY          
SEQRES  12 C  234  THR VAL THR PRO ASN VAL ALA GLU ALA VAL LYS ASN ALA          
SEQRES  13 C  234  LYS ALA GLY GLN VAL ARG TYR ARG ASN ASP LYS ASN GLY          
SEQRES  14 C  234  ILE ILE HIS THR THR ILE GLY LYS VAL ASP PHE ASP ALA          
SEQRES  15 C  234  ASP LYS LEU LYS GLU ASN LEU GLU ALA LEU LEU VAL ALA          
SEQRES  16 C  234  LEU LYS LYS ALA LYS PRO THR GLN ALA LYS GLY VAL TYR          
SEQRES  17 C  234  ILE LYS LYS VAL SER ILE SER THR THR MET GLY ALA GLY          
SEQRES  18 C  234  VAL ALA VAL ASP GLN ALA GLY LEU SER ALA SER VAL ASN          
SEQRES   1 D  273  MET ALA VAL VAL LYS CYS LYS PRO THR SER PRO GLY ARG          
SEQRES   2 D  273  ARG HIS VAL VAL LYS VAL VAL ASN PRO GLU LEU HIS LYS          
SEQRES   3 D  273  GLY LYS PRO PHE ALA PRO LEU LEU GLU LYS ASN SER LYS          
SEQRES   4 D  273  SER GLY GLY ARG ASN ASN ASN GLY ARG ILE THR THR ARG          
SEQRES   5 D  273  HIS ILE GLY GLY GLY HIS LYS GLN ALA TYR ARG ILE VAL          
SEQRES   6 D  273  ASP PHE LYS ARG ASN LYS ASP GLY ILE PRO ALA VAL VAL          
SEQRES   7 D  273  GLU ARG LEU GLU TYR ASP PRO ASN ARG SER ALA ASN ILE          
SEQRES   8 D  273  ALA LEU VAL LEU TYR LYS ASP GLY GLU ARG ARG TYR ILE          
SEQRES   9 D  273  LEU ALA PRO LYS GLY LEU LYS ALA GLY ASP GLN ILE GLN          
SEQRES  10 D  273  SER GLY VAL ASP ALA ALA ILE LYS PRO GLY ASN THR LEU          
SEQRES  11 D  273  PRO MET ARG ASN ILE PRO VAL GLY SER THR VAL HIS ASN          
SEQRES  12 D  273  VAL GLU MET LYS PRO GLY LYS GLY GLY GLN LEU ALA ARG          
SEQRES  13 D  273  SER ALA GLY THR TYR VAL GLN ILE VAL ALA ARG ASP GLY          
SEQRES  14 D  273  ALA TYR VAL THR LEU ARG LEU ARG SER GLY GLU MET ARG          
SEQRES  15 D  273  LYS VAL GLU ALA ASP CYS ARG ALA THR LEU GLY GLU VAL          
SEQRES  16 D  273  GLY ASN ALA GLU HIS MET LEU ARG VAL LEU GLY LYS ALA          
SEQRES  17 D  273  GLY ALA ALA ARG TRP ARG GLY VAL ARG PRO THR VAL ARG          
SEQRES  18 D  273  GLY THR ALA MET ASN PRO VAL ASP HIS PRO HIS GLY GLY          
SEQRES  19 D  273  GLY GLU GLY ARG ASN PHE GLY LYS HIS PRO VAL THR PRO          
SEQRES  20 D  273  TRP GLY VAL GLN THR LYS GLY LYS LYS THR ARG SER ASN          
SEQRES  21 D  273  LYS ARG THR ASP LYS PHE ILE VAL ARG ARG ARG SER LYS          
SEQRES   1 E  209  MET ILE GLY LEU VAL GLY LYS LYS VAL GLY MET THR ARG          
SEQRES   2 E  209  ILE PHE THR GLU ASP GLY VAL SER ILE PRO VAL THR VAL          
SEQRES   3 E  209  ILE GLU VAL GLU ALA ASN ARG VAL THR GLN VAL LYS ASP          
SEQRES   4 E  209  LEU ALA ASN ASP GLY TYR ARG ALA ILE GLN VAL THR THR          
SEQRES   5 E  209  GLY ALA LYS LYS ALA ASN ARG VAL THR LYS PRO GLU ALA          
SEQRES   6 E  209  GLY HIS PHE ALA LYS ALA GLY VAL GLU ALA GLY ARG GLY          
SEQRES   7 E  209  LEU TRP GLU PHE ARG LEU ALA GLU GLY GLU GLU PHE THR          
SEQRES   8 E  209  VAL GLY GLN SER ILE SER VAL GLU LEU PHE ALA ASP VAL          
SEQRES   9 E  209  LYS LYS VAL ASP VAL THR GLY THR SER LYS GLY LYS GLY          
SEQRES  10 E  209  PHE ALA GLY THR VAL LYS ARG TRP ASN PHE ARG THR GLN          
SEQRES  11 E  209  ASP ALA THR HIS GLY ASN SER LEU SER HIS ARG VAL PRO          
SEQRES  12 E  209  GLY SER ILE GLY GLN ASN GLN THR PRO GLY LYS VAL PHE          
SEQRES  13 E  209  LYS GLY LYS LYS MET ALA GLY GLN MET GLY ASN GLU ARG          
SEQRES  14 E  209  VAL THR VAL GLN SER LEU ASP VAL VAL ARG VAL ASP ALA          
SEQRES  15 E  209  GLU ARG ASN LEU LEU LEU VAL LYS GLY ALA VAL PRO GLY          
SEQRES  16 E  209  ALA THR GLY SER ASP LEU ILE VAL LYS PRO ALA VAL LYS          
SEQRES  17 E  209  ALA                                                          
SEQRES   1 F  201  MET GLU LEU VAL LEU LYS ASP ALA GLN SER ALA LEU THR          
SEQRES   2 F  201  VAL SER GLU THR THR PHE GLY ARG ASP PHE ASN GLU ALA          
SEQRES   3 F  201  LEU VAL HIS GLN VAL VAL VAL ALA TYR ALA ALA GLY ALA          
SEQRES   4 F  201  ARG GLN GLY THR ARG ALA GLN LYS THR ARG ALA GLU VAL          
SEQRES   5 F  201  THR GLY SER GLY LYS LYS PRO TRP ARG GLN LYS GLY THR          
SEQRES   6 F  201  GLY ARG ALA ARG SER GLY SER ILE LYS SER PRO ILE TRP          
SEQRES   7 F  201  ARG SER GLY GLY VAL THR PHE ALA ALA ARG PRO GLN ASP          
SEQRES   8 F  201  HIS SER GLN LYS VAL ASN LYS LYS MET TYR ARG GLY ALA          
SEQRES   9 F  201  LEU LYS SER ILE LEU SER GLU LEU VAL ARG GLN ASP ARG          
SEQRES  10 F  201  LEU ILE VAL VAL GLU LYS PHE SER VAL GLU ALA PRO LYS          
SEQRES  11 F  201  THR LYS LEU LEU ALA GLN LYS LEU LYS ASP MET ALA LEU          
SEQRES  12 F  201  GLU ASP VAL LEU ILE ILE THR GLY GLU LEU ASP GLU ASN          
SEQRES  13 F  201  LEU PHE LEU ALA ALA ARG ASN LEU HIS LYS VAL ASP VAL          
SEQRES  14 F  201  ARG ASP ALA THR GLY ILE ASP PRO VAL SER LEU ILE ALA          
SEQRES  15 F  201  PHE ASP LYS VAL VAL MET THR ALA ASP ALA VAL LYS GLN          
SEQRES  16 F  201  VAL GLU GLU MET LEU ALA                                      
SEQRES   1 G  179  MET ALA LYS LEU HIS ASP TYR TYR LYS ASP GLU VAL VAL          
SEQRES   2 G  179  LYS LYS LEU MET THR GLU PHE ASN TYR ASN SER VAL MET          
SEQRES   3 G  179  GLN VAL PRO ARG VAL GLU LYS ILE THR LEU ASN MET GLY          
SEQRES   4 G  179  VAL GLY GLU ALA ILE ALA ASP LYS LYS LEU LEU ASP ASN          
SEQRES   5 G  179  ALA ALA ALA ASP LEU ALA ALA ILE SER GLY GLN LYS PRO          
SEQRES   6 G  179  LEU ILE THR LYS ALA ARG LYS SER VAL ALA GLY PHE LYS          
SEQRES   7 G  179  ILE ARG GLN GLY TYR PRO ILE GLY CYS LYS VAL THR LEU          
SEQRES   8 G  179  ARG GLY GLU ARG MET TRP GLU PHE PHE GLU ARG LEU ILE          
SEQRES   9 G  179  THR ILE ALA VAL PRO ARG ILE ARG ASP PHE ARG GLY LEU          
SEQRES  10 G  179  SER ALA LYS SER PHE ASP GLY ARG GLY ASN TYR SER MET          
SEQRES  11 G  179  GLY VAL ARG GLU GLN ILE ILE PHE PRO GLU ILE ASP TYR          
SEQRES  12 G  179  ASP LYS VAL ASP ARG VAL ARG GLY LEU ASP ILE THR ILE          
SEQRES  13 G  179  THR THR THR ALA LYS SER ASP GLU GLU GLY ARG ALA LEU          
SEQRES  14 G  179  LEU ALA ALA PHE ASP PHE PRO PHE ARG LYS                      
SEQRES   1 H  177  MET SER ARG VAL ALA LYS ALA PRO VAL VAL VAL PRO ALA          
SEQRES   2 H  177  GLY VAL ASP VAL LYS ILE ASN GLY GLN VAL ILE THR ILE          
SEQRES   3 H  177  LYS GLY LYS ASN GLY GLU LEU THR ARG THR LEU ASN ASP          
SEQRES   4 H  177  ALA VAL GLU VAL LYS HIS ALA ASP ASN THR LEU THR PHE          
SEQRES   5 H  177  GLY PRO ARG ASP GLY TYR ALA ASP GLY TRP ALA GLN ALA          
SEQRES   6 H  177  GLY THR ALA ARG ALA LEU LEU ASN SER MET VAL ILE GLY          
SEQRES   7 H  177  VAL THR GLU GLY PHE THR LYS LYS LEU GLN LEU VAL GLY          
SEQRES   8 H  177  VAL GLY TYR ARG ALA ALA VAL LYS GLY ASN VAL ILE ASN          
SEQRES   9 H  177  LEU SER LEU GLY PHE SER HIS PRO VAL ASP HIS GLN LEU          
SEQRES  10 H  177  PRO ALA GLY ILE THR ALA GLU CYS PRO THR GLN THR GLU          
SEQRES  11 H  177  ILE VAL LEU LYS GLY ALA ASP LYS GLN VAL ILE GLY GLN          
SEQRES  12 H  177  VAL ALA ALA ASP LEU ARG ALA TYR ARG ARG PRO GLU PRO          
SEQRES  13 H  177  TYR LYS GLY LYS GLY VAL ARG TYR ALA ASP GLU VAL VAL          
SEQRES  14 H  177  ARG THR LYS GLU ALA LYS LYS LYS                              
SEQRES   1 I  149  MET GLN VAL ILE LEU LEU ASP LYS VAL ALA ASN LEU GLY          
SEQRES   2 I  149  SER LEU GLY ASP GLN VAL ASN VAL LYS ALA GLY TYR ALA          
SEQRES   3 I  149  ARG ASN PHE LEU VAL PRO GLN GLY LYS ALA VAL PRO ALA          
SEQRES   4 I  149  THR LYS LYS ASN ILE GLU PHE PHE GLU ALA ARG ARG ALA          
SEQRES   5 I  149  GLU LEU GLU ALA LYS LEU ALA GLU VAL LEU ALA ALA ALA          
SEQRES   6 I  149  ASN ALA ARG ALA GLU LYS ILE ASN ALA LEU GLU THR VAL          
SEQRES   7 I  149  THR ILE ALA SER LYS ALA GLY ASP GLU GLY LYS LEU PHE          
SEQRES   8 I  149  GLY SER ILE GLY THR ARG ASP ILE ALA ASP ALA VAL THR          
SEQRES   9 I  149  ALA ALA GLY VAL GLU VAL ALA LYS SER GLU VAL ARG LEU          
SEQRES  10 I  149  PRO ASN GLY VAL LEU ARG THR THR GLY GLU HIS GLU VAL          
SEQRES  11 I  149  SER PHE GLN VAL HIS SER GLU VAL PHE ALA LYS VAL ILE          
SEQRES  12 I  149  VAL ASN VAL VAL ALA GLU                                      
SEQRES   1 J  142  MET ALA LYS LYS VAL GLN ALA TYR VAL LYS LEU GLN VAL          
SEQRES   2 J  142  ALA ALA GLY MET ALA ASN PRO SER PRO PRO VAL GLY PRO          
SEQRES   3 J  142  ALA LEU GLY GLN GLN GLY VAL ASN ILE MET GLU PHE CYS          
SEQRES   4 J  142  LYS ALA PHE ASN ALA LYS THR ASP SER ILE GLU LYS GLY          
SEQRES   5 J  142  LEU PRO ILE PRO VAL VAL ILE THR VAL TYR ALA ASP ARG          
SEQRES   6 J  142  SER PHE THR PHE VAL THR LYS THR PRO PRO ALA ALA VAL          
SEQRES   7 J  142  LEU LEU LYS LYS ALA ALA GLY ILE LYS SER GLY SER GLY          
SEQRES   8 J  142  LYS PRO ASN LYS ASP LYS VAL GLY LYS ILE SER ARG ALA          
SEQRES   9 J  142  GLN LEU GLN GLU ILE ALA GLN THR LYS ALA ALA ASP MET          
SEQRES  10 J  142  THR GLY ALA ASP ILE GLU ALA MET THR ARG SER ILE GLU          
SEQRES  11 J  142  GLY THR ALA ARG SER MET GLY LEU VAL VAL GLU ASP              
SEQRES   1 K  142  MET LYS THR PHE THR ALA LYS PRO GLU THR VAL LYS ARG          
SEQRES   2 K  142  ASP TRP TYR VAL VAL ASP ALA THR GLY LYS THR LEU GLY          
SEQRES   3 K  142  ARG LEU ALA THR GLU LEU ALA ARG ARG LEU ARG GLY LYS          
SEQRES   4 K  142  HIS LYS ALA GLU TYR THR PRO HIS VAL ASP THR GLY ASP          
SEQRES   5 K  142  TYR ILE ILE VAL LEU ASN ALA ASP LYS VAL ALA VAL THR          
SEQRES   6 K  142  GLY ASN LYS ARG THR ASP LYS VAL TYR TYR HIS HIS THR          
SEQRES   7 K  142  GLY HIS ILE GLY GLY ILE LYS GLN ALA THR PHE GLU GLU          
SEQRES   8 K  142  MET ILE ALA ARG ARG PRO GLU ARG VAL ILE GLU ILE ALA          
SEQRES   9 K  142  VAL LYS GLY MET LEU PRO LYS GLY PRO LEU GLY ARG ALA          
SEQRES  10 K  142  MET PHE ARG LYS LEU LYS VAL TYR ALA GLY ASN GLU HIS          
SEQRES  11 K  142  ASN HIS ALA ALA GLN GLN PRO GLN VAL LEU ASP ILE              
SEQRES   1 L  123  MET ILE GLN GLU GLN THR MET LEU ASN VAL ALA ASP ASN          
SEQRES   2 L  123  SER GLY ALA ARG ARG VAL MET CYS ILE LYS VAL LEU GLY          
SEQRES   3 L  123  GLY SER HIS ARG ARG TYR ALA GLY VAL GLY ASP ILE ILE          
SEQRES   4 L  123  LYS ILE THR ILE LYS GLU ALA ILE PRO ARG GLY LYS VAL          
SEQRES   5 L  123  LYS LYS GLY ASP VAL LEU LYS ALA VAL VAL VAL ARG THR          
SEQRES   6 L  123  LYS LYS GLY VAL ARG ARG PRO ASP GLY SER VAL ILE ARG          
SEQRES   7 L  123  PHE ASP GLY ASN ALA CYS VAL LEU LEU ASN ASN ASN SER          
SEQRES   8 L  123  GLU GLN PRO ILE GLY THR ARG ILE PHE GLY PRO VAL THR          
SEQRES   9 L  123  ARG GLU LEU ARG SER GLU LYS PHE MET LYS ILE ILE SER          
SEQRES  10 L  123  LEU ALA PRO GLU VAL LEU                                      
SEQRES   1 M  144  MET ARG LEU ASN THR LEU SER PRO ALA GLU GLY SER LYS          
SEQRES   2 M  144  LYS ALA GLY LYS ARG LEU GLY ARG GLY ILE GLY SER GLY          
SEQRES   3 M  144  LEU GLY LYS THR GLY GLY ARG GLY HIS LYS GLY GLN LYS          
SEQRES   4 M  144  SER ARG SER GLY GLY GLY VAL ARG ARG GLY PHE GLU GLY          
SEQRES   5 M  144  GLY GLN MET PRO LEU TYR ARG ARG LEU PRO LYS PHE GLY          
SEQRES   6 M  144  PHE THR SER ARG LYS ALA ALA ILE THR ALA GLU ILE ARG          
SEQRES   7 M  144  LEU SER ASP LEU ALA LYS VAL GLU GLY GLY VAL VAL ASP          
SEQRES   8 M  144  LEU ASN THR LEU LYS ALA ALA ASN ILE ILE GLY ILE GLN          
SEQRES   9 M  144  ILE GLU PHE ALA LYS VAL ILE LEU ALA GLY GLU VAL THR          
SEQRES  10 M  144  THR PRO VAL THR VAL ARG GLY LEU ARG VAL THR LYS GLY          
SEQRES  11 M  144  ALA ARG ALA ALA ILE GLU ALA ALA GLY GLY LYS ILE GLU          
SEQRES  12 M  144  GLU                                                          
SEQRES   1 N  136  MET LEU GLN PRO LYS ARG THR LYS PHE ARG LYS MET HIS          
SEQRES   2 N  136  LYS GLY ARG ASN ARG GLY LEU ALA GLN GLY THR ASP VAL          
SEQRES   3 N  136  SER PHE GLY SER PHE GLY LEU LYS ALA VAL GLY ARG GLY          
SEQRES   4 N  136  ARG LEU THR ALA ARG GLN ILE GLU ALA ALA ARG ARG ALA          
SEQRES   5 N  136  MET THR ARG ALA VAL LYS ARG GLN GLY LYS ILE TRP ILE          
SEQRES   6 N  136  ARG VAL PHE PRO ASP LYS PRO ILE THR GLU LYS PRO LEU          
SEQRES   7 N  136  ALA VAL ARG MET GLY LYS GLY LYS GLY ASN VAL GLU TYR          
SEQRES   8 N  136  TRP VAL ALA LEU ILE GLN PRO GLY LYS VAL LEU TYR GLU          
SEQRES   9 N  136  MET ASP GLY VAL PRO GLU GLU LEU ALA ARG GLU ALA PHE          
SEQRES  10 N  136  LYS LEU ALA ALA ALA LYS LEU PRO ILE LYS THR THR PHE          
SEQRES  11 N  136  VAL THR LYS THR VAL MET                                      
SEQRES   1 O  127  MET ARG HIS ARG LYS SER GLY ARG GLN LEU ASN ARG ASN          
SEQRES   2 O  127  SER SER HIS ARG GLN ALA MET PHE ARG ASN MET ALA GLY          
SEQRES   3 O  127  SER LEU VAL ARG HIS GLU ILE ILE LYS THR THR LEU PRO          
SEQRES   4 O  127  LYS ALA LYS GLU LEU ARG ARG VAL VAL GLU PRO LEU ILE          
SEQRES   5 O  127  THR LEU ALA LYS THR ASP SER VAL ALA ASN ARG ARG LEU          
SEQRES   6 O  127  ALA PHE ALA ARG THR ARG ASP ASN GLU ILE VAL ALA LYS          
SEQRES   7 O  127  LEU PHE ASN GLU LEU GLY PRO ARG PHE ALA SER ARG ALA          
SEQRES   8 O  127  GLY GLY TYR THR ARG ILE LEU LYS CYS GLY PHE ARG ALA          
SEQRES   9 O  127  GLY ASP ASN ALA PRO MET ALA TYR ILE GLU LEU VAL ASP          
SEQRES  10 O  127  ARG SER GLU LYS ALA GLU ALA ALA ALA GLU                      
SEQRES   1 P  117  MET ASP LYS LYS SER ALA ARG ILE ARG ARG ALA THR ARG          
SEQRES   2 P  117  ALA ARG ARG LYS LEU GLN GLU LEU GLY ALA THR ARG LEU          
SEQRES   3 P  117  VAL VAL HIS ARG THR PRO ARG HIS ILE TYR ALA GLN VAL          
SEQRES   4 P  117  ILE ALA PRO ASN GLY SER GLU VAL LEU VAL ALA ALA SER          
SEQRES   5 P  117  THR VAL GLU LYS ALA ILE ALA GLU GLN LEU LYS TYR THR          
SEQRES   6 P  117  GLY ASN LYS ASP ALA ALA ALA ALA VAL GLY LYS ALA VAL          
SEQRES   7 P  117  ALA GLU ARG ALA LEU GLU LYS GLY ILE LYS ASP VAL SER          
SEQRES   8 P  117  PHE ASP ARG SER GLY PHE GLN TYR HIS GLY ARG VAL GLN          
SEQRES   9 P  117  ALA LEU ALA ASP ALA ALA ARG GLU ALA GLY LEU GLN PHE          
SEQRES   1 Q  115  MET SER ASN ILE ILE LYS GLN LEU GLU GLN GLU GLN MET          
SEQRES   2 Q  115  LYS GLN ASP VAL PRO SER PHE ARG PRO GLY ASP THR VAL          
SEQRES   3 Q  115  GLU VAL LYS VAL TRP VAL VAL GLU GLY SER LYS LYS ARG          
SEQRES   4 Q  115  LEU GLN ALA PHE GLU GLY VAL VAL ILE ALA ILE ARG ASN          
SEQRES   5 Q  115  ARG GLY LEU HIS SER ALA PHE THR VAL ARG LYS ILE SER          
SEQRES   6 Q  115  ASN GLY GLU GLY VAL GLU ARG VAL PHE GLN THR HIS SER          
SEQRES   7 Q  115  PRO VAL VAL ASP SER ILE SER VAL LYS ARG ARG GLY ALA          
SEQRES   8 Q  115  VAL ARG LYS ALA LYS LEU TYR TYR LEU ARG GLU ARG THR          
SEQRES   9 Q  115  GLY LYS ALA ALA ARG ILE LYS GLU ARG LEU ASN                  
SEQRES   1 R  118  MET ALA ARG VAL LYS ARG GLY VAL ILE ALA ARG ALA ARG          
SEQRES   2 R  118  HIS LYS LYS ILE LEU LYS GLN ALA LYS GLY TYR TYR GLY          
SEQRES   3 R  118  ALA ARG SER ARG VAL TYR ARG VAL ALA PHE GLN ALA VAL          
SEQRES   4 R  118  ILE LYS ALA GLY GLN TYR ALA TYR ARG ASP ARG ARG GLN          
SEQRES   5 R  118  ARG LYS ARG GLN PHE ARG GLN LEU TRP ILE ALA ARG ILE          
SEQRES   6 R  118  ASN ALA ALA ALA ARG GLN ASN GLY ILE SER TYR SER LYS          
SEQRES   7 R  118  PHE ILE ASN GLY LEU LYS LYS ALA SER VAL GLU ILE ASP          
SEQRES   8 R  118  ARG LYS ILE LEU ALA ASP ILE ALA VAL PHE ASP LYS VAL          
SEQRES   9 R  118  ALA PHE THR ALA LEU VAL GLU LYS ALA LYS ALA ALA LEU          
SEQRES  10 R  118  ALA                                                          
SEQRES   1 S  103  MET TYR ALA VAL PHE GLN SER GLY GLY LYS GLN HIS ARG          
SEQRES   2 S  103  VAL SER GLU GLY GLN THR VAL ARG LEU GLU LYS LEU ASP          
SEQRES   3 S  103  ILE ALA THR GLY GLU THR VAL GLU PHE ALA GLU VAL LEU          
SEQRES   4 S  103  MET ILE ALA ASN GLY GLU GLU VAL LYS ILE GLY VAL PRO          
SEQRES   5 S  103  PHE VAL ASP GLY GLY VAL ILE LYS ALA GLU VAL VAL ALA          
SEQRES   6 S  103  HIS GLY ARG GLY GLU LYS VAL LYS ILE VAL LYS PHE ARG          
SEQRES   7 S  103  ARG ARG LYS HIS TYR ARG LYS GLN GLN GLY HIS ARG GLN          
SEQRES   8 S  103  TRP PHE THR ASP VAL LYS ILE THR GLY ILE SER ALA              
SEQRES   1 T  110  MET GLU THR ILE ALA LYS HIS ARG HIS ALA ARG SER SER          
SEQRES   2 T  110  ALA GLN LYS VAL ARG LEU VAL ALA ASP LEU ILE ARG GLY          
SEQRES   3 T  110  LYS LYS VAL SER GLN ALA LEU ASP ILE LEU THR TYR THR          
SEQRES   4 T  110  ASN LYS LYS ALA ALA VAL LEU VAL LYS LYS VAL LEU GLU          
SEQRES   5 T  110  SER ALA ILE ALA ASN ALA GLU HIS ASN ASP GLY ALA ASP          
SEQRES   6 T  110  ILE ASP ASP LEU LYS VAL THR LYS ILE PHE VAL ASP GLU          
SEQRES   7 T  110  GLY PRO SER MET LYS ARG ILE MET PRO ARG ALA LYS GLY          
SEQRES   8 T  110  ARG ALA ASP ARG ILE LEU LYS ARG THR SER HIS ILE THR          
SEQRES   9 T  110  VAL VAL VAL SER ASP ARG                                      
SEQRES   1 U  100  MET ILE ARG GLU GLU ARG LEU LEU LYS VAL LEU ARG ALA          
SEQRES   2 U  100  PRO HIS VAL SER GLU LYS ALA SER THR ALA MET GLU LYS          
SEQRES   3 U  100  SER ASN THR ILE VAL LEU LYS VAL ALA LYS ASP ALA THR          
SEQRES   4 U  100  LYS ALA GLU ILE LYS ALA ALA VAL GLN LYS LEU PHE GLU          
SEQRES   5 U  100  VAL GLU VAL GLU VAL VAL ASN THR LEU VAL VAL LYS GLY          
SEQRES   6 U  100  LYS VAL LYS ARG HIS GLY GLN ARG ILE GLY ARG ARG SER          
SEQRES   7 U  100  ASP TRP LYS LYS ALA TYR VAL THR LEU LYS GLU GLY GLN          
SEQRES   8 U  100  ASN LEU ASP PHE VAL GLY GLY ALA GLU                          
SEQRES   1 V  104  MET ALA ALA LYS ILE ARG ARG ASP ASP GLU VAL ILE VAL          
SEQRES   2 V  104  LEU THR GLY LYS ASP LYS GLY LYS ARG GLY LYS VAL LYS          
SEQRES   3 V  104  ASN VAL LEU SER SER GLY LYS VAL ILE VAL GLU GLY ILE          
SEQRES   4 V  104  ASN LEU VAL LYS LYS HIS GLN LYS PRO VAL PRO ALA LEU          
SEQRES   5 V  104  ASN GLN PRO GLY GLY ILE VAL GLU LYS GLU ALA ALA ILE          
SEQRES   6 V  104  GLN VAL SER ASN VAL ALA ILE PHE ASN ALA ALA THR GLY          
SEQRES   7 V  104  LYS ALA ASP ARG VAL GLY PHE ARG PHE GLU ASP GLY LYS          
SEQRES   8 V  104  LYS VAL ARG PHE PHE LYS SER ASN SER GLU THR ILE LYS          
SEQRES   1 W   94  MET PHE THR ILE ASN ALA GLU VAL ARG LYS GLU GLN GLY          
SEQRES   2 W   94  LYS GLY ALA SER ARG ARG LEU ARG ALA ALA ASN LYS PHE          
SEQRES   3 W   94  PRO ALA ILE ILE TYR GLY GLY LYS GLU ALA PRO LEU ALA          
SEQRES   4 W   94  ILE GLU LEU ASP HIS ASP LYS VAL MET ASN MET GLN ALA          
SEQRES   5 W   94  LYS ALA GLU PHE TYR SER GLU VAL LEU THR ILE VAL VAL          
SEQRES   6 W   94  ASP GLY LYS GLU ILE LYS VAL LYS ALA GLN ASP VAL GLN          
SEQRES   7 W   94  ARG HIS PRO TYR LYS PRO LYS LEU GLN HIS ILE ASP PHE          
SEQRES   8 W   94  VAL ARG ALA                                                  
SEQRES   1 X   85  MET ALA HIS LYS LYS ALA GLY GLY SER THR ARG ASN GLY          
SEQRES   2 X   85  ARG ASP SER GLU ALA LYS ARG LEU GLY VAL LYS ARG PHE          
SEQRES   3 X   85  GLY GLY GLU SER VAL LEU ALA GLY SER ILE ILE VAL ARG          
SEQRES   4 X   85  GLN ARG GLY THR LYS PHE HIS ALA GLY ALA ASN VAL GLY          
SEQRES   5 X   85  CYS GLY ARG ASP HIS THR LEU PHE ALA LYS ALA ASP GLY          
SEQRES   6 X   85  LYS VAL LYS PHE GLU VAL LYS GLY PRO LYS ASN ARG LYS          
SEQRES   7 X   85  PHE ILE SER ILE GLU ALA GLU                                  
SEQRES   1 Y   78  MET SER ARG VAL CYS GLN VAL THR GLY LYS ARG PRO VAL          
SEQRES   2 Y   78  THR GLY ASN ASN ARG SER HIS ALA LEU ASN ALA THR LYS          
SEQRES   3 Y   78  ARG ARG PHE LEU PRO ASN LEU HIS SER HIS ARG PHE TRP          
SEQRES   4 Y   78  VAL GLU SER GLU LYS ARG PHE VAL THR LEU ARG VAL SER          
SEQRES   5 Y   78  ALA LYS GLY MET ARG VAL ILE ASP LYS LYS GLY ILE ASP          
SEQRES   6 Y   78  THR VAL LEU ALA GLU LEU ARG ALA ARG GLY GLU LYS TYR          
SEQRES   1 Z   63  MET LYS ALA LYS GLU LEU ARG GLU LYS SER VAL GLU GLU          
SEQRES   2 Z   63  LEU ASN THR GLU LEU LEU ASN LEU LEU ARG GLU GLN PHE          
SEQRES   3 Z   63  ASN LEU ARG MET GLN ALA ALA SER GLY GLN LEU GLN GLN          
SEQRES   4 Z   63  SER HIS LEU LEU LYS GLN VAL ARG ARG ASP VAL ALA ARG          
SEQRES   5 Z   63  VAL LYS THR LEU LEU ASN GLU LYS ALA GLY ALA                  
SEQRES   1 a   59  MET ALA LYS THR ILE LYS ILE THR GLN THR ARG SER ALA          
SEQRES   2 a   59  ILE GLY ARG LEU PRO LYS HIS LYS ALA THR LEU LEU GLY          
SEQRES   3 a   59  LEU GLY LEU ARG ARG ILE GLY HIS THR VAL GLU ARG GLU          
SEQRES   4 a   59  ASP THR PRO ALA ILE ARG GLY MET ILE ASN ALA VAL SER          
SEQRES   5 a   59  PHE MET VAL LYS VAL GLU GLU                                  
SEQRES   1 b   70  MET LYS LYS ASP ILE HIS PRO LYS TYR GLU GLU ILE THR          
SEQRES   2 b   70  ALA SER CYS SER CYS GLY ASN VAL MET LYS ILE ARG SER          
SEQRES   3 b   70  THR VAL GLY HIS ASP LEU ASN LEU ASP VAL CYS SER LYS          
SEQRES   4 b   70  CYS HIS PRO PHE PHE THR GLY LYS GLN ARG ASP VAL ALA          
SEQRES   5 b   70  THR GLY GLY ARG VAL ASP ARG PHE ASN LYS ARG PHE ASN          
SEQRES   6 b   70  ILE PRO GLY SER LYS                                          
SEQRES   1 c   57  MET ALA VAL GLN GLN ASN LYS PRO THR ARG SER LYS ARG          
SEQRES   2 c   57  GLY MET ARG ARG SER HIS ASP ALA LEU THR ALA VAL THR          
SEQRES   3 c   57  SER LEU SER VAL ASP LYS THR SER GLY GLU LYS HIS LEU          
SEQRES   4 c   57  ARG HIS HIS ILE THR ALA ASP GLY TYR TYR ARG GLY ARG          
SEQRES   5 c   57  LYS VAL ILE ALA LYS                                          
SEQRES   1 d   55  MET ALA LYS GLY ILE ARG GLU LYS ILE LYS LEU VAL SER          
SEQRES   2 d   55  SER ALA GLY THR GLY HIS PHE TYR THR THR THR LYS ASN          
SEQRES   3 d   55  LYS ARG THR LYS PRO GLU LYS LEU GLU LEU LYS LYS PHE          
SEQRES   4 d   55  ASP PRO VAL VAL ARG GLN HIS VAL ILE TYR LYS GLU ALA          
SEQRES   5 d   55  LYS ILE LYS                                                  
SEQRES   1 e   46  MET LYS ARG THR PHE GLN PRO SER VAL LEU LYS ARG ASN          
SEQRES   2 e   46  ARG SER HIS GLY PHE ARG ALA ARG MET ALA THR LYS ASN          
SEQRES   3 e   46  GLY ARG GLN VAL LEU ALA ARG ARG ARG ALA LYS GLY ARG          
SEQRES   4 e   46  ALA ARG LEU THR VAL SER LYS                                  
SEQRES   1 f   65  MET PRO LYS ILE LYS THR VAL ARG GLY ALA ALA LYS ARG          
SEQRES   2 f   65  PHE LYS LYS THR GLY LYS GLY GLY PHE LYS HIS LYS HIS          
SEQRES   3 f   65  ALA ASN LEU ARG HIS ILE LEU THR LYS LYS ALA THR LYS          
SEQRES   4 f   65  ARG LYS ARG HIS LEU ARG PRO LYS ALA MET VAL SER LYS          
SEQRES   5 f   65  GLY ASP LEU GLY LEU VAL ILE ALA CYS LEU PRO TYR ALA          
SEQRES   1 g   38  MET LYS VAL ARG ALA SER VAL LYS LYS LEU CYS ARG ASN          
SEQRES   2 g   38  CYS LYS ILE VAL LYS ARG ASP GLY VAL ILE ARG VAL ILE          
SEQRES   3 g   38  CYS SER ALA GLU PRO LYS HIS LYS GLN ARG GLN GLY              
MODRES 3IZU 1MG B  745    G  1N-METHYLGUANOSINE-5'-MONOPHOSPHATE                
MODRES 3IZU PSU B  746    U  PSEUDOURIDINE-5'-MONOPHOSPHATE                     
MODRES 3IZU 5MU B  747    U  5-METHYLURIDINE 5'-MONOPHOSPHATE                   
MODRES 3IZU PSU B  955    U  PSEUDOURIDINE-5'-MONOPHOSPHATE                     
MODRES 3IZU 6MZ B 1618    A  N6-METHYLADENOSINE-5'-MONOPHOSPHATE                
MODRES 3IZU 2MG B 1835    G  2N-METHYLGUANOSINE-5'-MONOPHOSPHATE                
MODRES 3IZU PSU B 1911    U  PSEUDOURIDINE-5'-MONOPHOSPHATE                     
MODRES 3IZU 3TD B 1915    U                                                     
MODRES 3IZU PSU B 1917    U  PSEUDOURIDINE-5'-MONOPHOSPHATE                     
MODRES 3IZU 5MU B 1939    U  5-METHYLURIDINE 5'-MONOPHOSPHATE                   
MODRES 3IZU 5MC B 1962    C  5-METHYLCYTIDINE-5'-MONOPHOSPHATE                  
MODRES 3IZU 6MZ B 2030    A  N6-METHYLADENOSINE-5'-MONOPHOSPHATE                
MODRES 3IZU 7MG B 2069    G                                                     
MODRES 3IZU OMG B 2251    G  O2'-METHYLGUANOSINE-5'-MONOPHOSPHATE               
MODRES 3IZU 2MG B 2445    G  2N-METHYLGUANOSINE-5'-MONOPHOSPHATE                
MODRES 3IZU H2U B 2449    U  5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE                
MODRES 3IZU PSU B 2457    U  PSEUDOURIDINE-5'-MONOPHOSPHATE                     
MODRES 3IZU OMC B 2498    C  O2'-METHYLYCYTIDINE-5'-MONOPHOSPHATE               
MODRES 3IZU 2MA B 2503    A  2-METHYLADENOSINE-5'-MONOPHOSPHATE                 
MODRES 3IZU PSU B 2504    U  PSEUDOURIDINE-5'-MONOPHOSPHATE                     
MODRES 3IZU OMU B 2552    U  O2'-METHYLURIDINE 5'-MONOPHOSPHATE                 
MODRES 3IZU  CH B 2575    C  N3-PROTONATED CYTIDINE-5'-MONOPHOSPHATE            
MODRES 3IZU PSU B 2580    U  PSEUDOURIDINE-5'-MONOPHOSPHATE                     
MODRES 3IZU PSU B 2605    U  PSEUDOURIDINE-5'-MONOPHOSPHATE                     
HET    1MG  B 745      24                                                       
HET    PSU  B 746      20                                                       
HET    5MU  B 747      21                                                       
HET    PSU  B 955      20                                                       
HET    6MZ  B1618      23                                                       
HET    2MG  B1835      24                                                       
HET    PSU  B1911      20                                                       
HET    3TD  B1915      21                                                       
HET    PSU  B1917      20                                                       
HET    5MU  B1939      21                                                       
HET    5MC  B1962      21                                                       
HET    6MZ  B2030      23                                                       
HET    7MG  B2069      24                                                       
HET    OMG  B2251      24                                                       
HET    2MG  B2445      24                                                       
HET    H2U  B2449      20                                                       
HET    PSU  B2457      20                                                       
HET    OMC  B2498      21                                                       
HET    2MA  B2503      23                                                       
HET    PSU  B2504      20                                                       
HET    OMU  B2552      21                                                       
HET     CH  B2575      20                                                       
HET    PSU  B2580      20                                                       
HET    PSU  B2605      20                                                       
HETNAM     1MG 1N-METHYLGUANOSINE-5'-MONOPHOSPHATE                              
HETNAM     PSU PSEUDOURIDINE-5'-MONOPHOSPHATE                                   
HETNAM     5MU 5-METHYLURIDINE 5'-MONOPHOSPHATE                                 
HETNAM     6MZ N6-METHYLADENOSINE-5'-MONOPHOSPHATE                              
HETNAM     2MG 2N-METHYLGUANOSINE-5'-MONOPHOSPHATE                              
HETNAM     3TD (1S)-1,4-ANHYDRO-1-(3-METHYL-2,4-DIOXO-1,2,3,4-                  
HETNAM   2 3TD  TETRAHYDROPYRIMIDIN-5-YL)-5-O-PHOSPHONO-D-RIBITOL               
HETNAM     5MC 5-METHYLCYTIDINE-5'-MONOPHOSPHATE                                
HETNAM     7MG 7N-METHYL-8-HYDROGUANOSINE-5'-MONOPHOSPHATE                      
HETNAM     OMG O2'-METHYLGUANOSINE-5'-MONOPHOSPHATE                             
HETNAM     H2U 5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE                              
HETNAM     OMC O2'-METHYLYCYTIDINE-5'-MONOPHOSPHATE                             
HETNAM     2MA 2-METHYLADENOSINE-5'-MONOPHOSPHATE                               
HETNAM     OMU O2'-METHYLURIDINE 5'-MONOPHOSPHATE                               
HETNAM      CH N3-PROTONATED CYTIDINE-5'-MONOPHOSPHATE                          
FORMUL   2  1MG    C11 H16 N5 O8 P                                              
FORMUL   2  PSU    8(C9 H13 N2 O9 P)                                            
FORMUL   2  5MU    2(C10 H15 N2 O9 P)                                           
FORMUL   2  6MZ    2(C11 H16 N5 O7 P)                                           
FORMUL   2  2MG    2(C11 H16 N5 O8 P)                                           
FORMUL   2  3TD    C10 H15 N2 O9 P                                              
FORMUL   2  5MC    C10 H16 N3 O8 P                                              
FORMUL   2  7MG    C11 H18 N5 O8 P                                              
FORMUL   2  OMG    C11 H16 N5 O8 P                                              
FORMUL   2  H2U    C9 H15 N2 O9 P                                               
FORMUL   2  OMC    C10 H16 N3 O8 P                                              
FORMUL   2  2MA    C11 H16 N5 O7 P                                              
FORMUL   2  OMU    C10 H15 N2 O9 P                                              
FORMUL   2   CH    C9 H15 N3 O8 P 1+                                            
HELIX    1   1 ASP C   22  ALA C   34  1                                  13    
HELIX    2   2 ASN C   83  ALA C   90  1                                   8    
HELIX    3   3 ASP C   99  ILE C  104  1                                   6    
HELIX    4   4 ALA C  120  GLY C  125  1                                   6    
HELIX    5   5 ASN C  148  LYS C  157  1                                  10    
HELIX    6   6 ASP C  181  LYS C  198  1                                  18    
HELIX    7   7 PHE D   29  PRO D   31  5                                   3    
HELIX    8   8 GLU D  198  ARG D  202  5                                   5    
HELIX    9   9 ALA D  207  TRP D  212  1                                   6    
HELIX   10  10 ARG D  220  MET D  224  5                                   5    
HELIX   11  11 GLY D  234  PHE D  239  5                                   6    
HELIX   12  12 THR D  262  LYS D  264  5                                   3    
HELIX   13  13 THR E   61  GLY E   72  1                                  12    
HELIX   14  14 SER E   97  PHE E  101  5                                   5    
HELIX   15  15 ASN F   24  ALA F   39  1                                  16    
HELIX   16  16 THR F   48  VAL F   52  5                                   5    
HELIX   17  17 ASN F   97  GLN F  115  1                                  19    
HELIX   18  18 LYS F  130  MET F  141  1                                  12    
HELIX   19  19 ASP F  176  ILE F  181  1                                   6    
HELIX   20  20 ASP F  191  VAL F  196  1                                   6    
HELIX   21  21 VAL F  196  ALA F  201  1                                   6    
HELIX   22  22 LYS G    2  GLU G   10  1                                   9    
HELIX   23  23 GLU G   10  ASN G   20  1                                  11    
HELIX   24  24 SER G   23  VAL G   27  5                                   5    
HELIX   25  25 LYS G   47  ILE G   59  1                                  13    
HELIX   26  26 GLY G   92  PHE G   98  1                                   7    
HELIX   27  27 PHE G   99  LEU G  102  5                                   4    
HELIX   28  28 ASP G  141  VAL G  145  5                                   5    
HELIX   29  29 GLU G  164  LEU G  168  5                                   5    
HELIX   30  30 GLN H   63  VAL H   78  1                                  16    
HELIX   31  31 GLN H  138  TYR H  150  1                                  13    
HELIX   32  32 GLU H  166  THR H  170  5                                   5    
HELIX   33  33 VAL I   31  GLY I   34  5                                   4    
HELIX   34  34 ILE I   44  GLU I   48  5                                   5    
HELIX   35  35 ARG I   50  ALA I   59  1                                  10    
HELIX   36  36 ILE I   99  THR I  104  1                                   6    
HELIX   37  37 VAL J   23  GLY J   28  1                                   6    
HELIX   38  38 GLN J   29  GLY J   31  5                                   3    
HELIX   39  39 ASN J   33  ASP J   46  1                                  14    
HELIX   40  40 PRO J   74  ALA J   83  1                                  10    
HELIX   41  41 SER J  101  ALA J  113  1                                  13    
HELIX   42  42 ALA J  114  MET J  116  5                                   3    
HELIX   43  43 ASP J  120  GLY J  136  1                                  17    
HELIX   44  44 LEU K   25  GLY K   38  1                                  14    
HELIX   45  45 ASN K   67  LYS K   72  1                                   6    
HELIX   46  46 PHE K   89  ILE K   93  1                                   5    
HELIX   47  47 ARG K   96  GLU K   98  5                                   3    
HELIX   48  48 ARG K   99  GLY K  107  1                                   9    
HELIX   49  49 GLY K  112  ARG K  120  1                                   9    
HELIX   50  50 SER L  109  LYS L  111  5                                   3    
HELIX   51  51 PHE L  112  SER L  117  1                                   6    
HELIX   52  52 PRO M   56  LEU M   61  1                                   6    
HELIX   53  53 LYS M   70  ALA M   72  5                                   3    
HELIX   54  54 LEU M   79  ALA M   83  1                                   5    
HELIX   55  55 LYS M   84  GLU M   86  5                                   3    
HELIX   56  56 THR M  128  ALA M  138  1                                  11    
HELIX   57  57 ALA N   43  VAL N   57  1                                  15    
HELIX   58  58 PRO N  109  LEU N  124  1                                  16    
HELIX   59  59 ASN O   13  ARG O   30  1                                  18    
HELIX   60  60 LEU O   38  LEU O   54  1                                  17    
HELIX   61  61 ALA O   55  THR O   57  5                                   3    
HELIX   62  62 SER O   59  ARG O   69  1                                  11    
HELIX   63  63 ASN O   73  LEU O   79  1                                   7    
HELIX   64  64 LEU O   83  ALA O   88  1                                   6    
HELIX   65  65 ASP P    2  GLU P   20  1                                  19    
HELIX   66  66 ALA P   57  GLN P   61  5                                   5    
HELIX   67  67 LYS P   68  GLU P   84  1                                  17    
HELIX   68  68 HIS P  100  ALA P  113  1                                  14    
HELIX   69  69 LEU Q    7  GLN Q   11  5                                   5    
HELIX   70  70 ARG Q   52  HIS Q   55  5                                   4    
HELIX   71  71 LEU Q   96  GLU Q  101  5                                   6    
HELIX   72  72 ILE R    8  LYS R   18  1                                  11    
HELIX   73  73 GLY R   25  VAL R   30  1                                   6    
HELIX   74  74 VAL R   30  PHE R   56  1                                  27    
HELIX   75  75 PHE R   56  ARG R   69  1                                  14    
HELIX   76  76 SER R   74  ALA R   85  1                                  12    
HELIX   77  77 SER R   86  GLU R   88  5                                   3    
HELIX   78  78 ARG R   91  ASP R  101  5                                  11    
HELIX   79  79 ALA R  104  ALA R  117  1                                  14    
HELIX   80  80 SER T   13  ARG T   25  1                                  13    
HELIX   81  81 LYS T   28  LEU T   33  1                                   6    
HELIX   82  82 LYS T   41  HIS T   60  1                                  20    
HELIX   83  83 ALA T   89  GLY T   91  5                                   3    
HELIX   84  84 THR U   39  LYS U   49  1                                  11    
HELIX   85  85 ASN U   92  GLY U   97  1                                   6    
HELIX   86  86 THR V   14  LYS V   18  5                                   5    
HELIX   87  87 PRO V   49  GLN V   53  5                                   5    
HELIX   88  88 GLY W   13  ALA W   23  1                                  11    
HELIX   89  89 HIS W   44  GLN W   51  1                                   8    
HELIX   90  90 ALA W   52  SER W   58  5                                   7    
HELIX   91  91 GLY X   72  ASN X   75  5                                   4    
HELIX   92  92 LYS Y   53  GLY Y   62  1                                  10    
HELIX   93  93 GLY Y   62  ARG Y   71  1                                  10    
HELIX   94  94 LEU Z    6  LYS Z    9  5                                   4    
HELIX   95  95 SER Z   10  GLU Z   17  1                                   8    
HELIX   96  96 ARG Z   23  LEU Z   28  1                                   6    
HELIX   97  97 SER Z   40  GLN Z   45  1                                   6    
HELIX   98  98 VAL Z   46  LEU Z   56  1                                  11    
HELIX   99  99 LEU a   16  GLY a   27  1                                  12    
HELIX  100 100 THR a   40  SER a   51  1                                  12    
HELIX  101 101 LYS b    8  THR b   13  1                                   6    
HELIX  102 102 SER c   10  ARG c   16  1                                   7    
HELIX  103 103 VAL e    9  GLY e   17  1                                   9    
HELIX  104 104 GLY e   17  ALA e   23  1                                   7    
HELIX  105 105 THR e   24  GLY e   38  1                                  15    
HELIX  106 106 ILE f   31  LYS f   35  5                                   5    
HELIX  107 107 ALA f   36  HIS f   42  1                                   7    
HELIX  108 108 ASP f   53  LEU f   61  1                                   9    
HELIX  109 109 GLU g   30  LYS g   34  5                                   5    
SHEET    1   A 5 GLN C  20  TYR C  21  0                                        
SHEET    2   A 5 GLY C 221  VAL C 224  1  O  ALA C 223   N  TYR C  21           
SHEET    3   A 5 ALA C 204  THR C 216 -1  N  ILE C 214   O  VAL C 222           
SHEET    4   A 5 SER C  41  ILE C  50 -1  N  ASN C  47   O  LYS C 211           
SHEET    5   A 5 ILE C 170  LYS C 177 -1  O  ILE C 171   N  VAL C  46           
SHEET    1   B 2 ARG C  60  VAL C  64  0                                        
SHEET    2   B 2 GLN C 160  ARG C 164 -1  O  VAL C 161   N  THR C  63           
SHEET    1   C 3 LEU C  94  VAL C  95  0                                        
SHEET    2   C 3 VAL C  75  PHE C  78  1  N  VAL C  77   O  LEU C  94           
SHEET    3   C 3 VAL C 113  ALA C 116  1  O  ILE C 115   N  ALA C  76           
SHEET    1   D 2 VAL D   2  LYS D   4  0                                        
SHEET    2   D 2 VAL D  16  VAL D  18 -1  O  LYS D  17   N  VAL D   3           
SHEET    1   E 2 LEU D  33  GLU D  34  0                                        
SHEET    2   E 2 TYR D  61  ARG D  62 -1  O  TYR D  61   N  GLU D  34           
SHEET    1   F 4 ARG D 100  LEU D 104  0                                        
SHEET    2   F 4 ASN D  89  TYR D  95 -1  N  VAL D  93   O  ARG D 101           
SHEET    3   F 4 ALA D  75  TYR D  82 -1  N  ARG D  79   O  LEU D  92           
SHEET    4   F 4 GLN D 114  ILE D 115 -1  O  ILE D 115   N  ALA D  75           
SHEET    1   G 4 GLN D 162  ASP D 167  0                                        
SHEET    2   G 4 TYR D 170  ARG D 174 -1  O  THR D 172   N  ALA D 165           
SHEET    3   G 4 MET D 180  GLU D 184 -1  O  VAL D 183   N  VAL D 171           
SHEET    4   G 4 ILE D 266  ARG D 268 -1  O  VAL D 267   N  MET D 180           
SHEET    1   H 7 LEU E   4  PHE E  15  0                                        
SHEET    2   H 7 SER E  21  VAL E  29 -1  O  VAL E  24   N  THR E  12           
SHEET    3   H 7 LEU E 186  LYS E 190 -1  O  LEU E 187   N  ILE E  27           
SHEET    4   H 7 THR E 171  ASP E 181 -1  N  ARG E 179   O  LEU E 188           
SHEET    5   H 7 LYS E 106  THR E 110 -1  N  VAL E 109   O  VAL E 172           
SHEET    6   H 7 ASP E 200  PRO E 205 -1  O  LYS E 204   N  ASP E 108           
SHEET    7   H 7 LEU E   4  PHE E  15 -1  N  GLY E   6   O  LEU E 201           
SHEET    1   I 3 ARG E  33  VAL E  37  0                                        
SHEET    2   I 3 ALA E  47  GLY E  53 -1  O  GLN E  49   N  GLN E  36           
SHEET    3   I 3 GLY E  76  ARG E  83 -1  O  ARG E  77   N  THR E  52           
SHEET    1   J 2 GLU F   2  LEU F   5  0                                        
SHEET    2   J 2 SER F  10  THR F  13 -1  O  LEU F  12   N  LEU F   3           
SHEET    1   K 4 LEU F 118  VAL F 120  0                                        
SHEET    2   K 4 VAL F 186  MET F 188  1  O  MET F 188   N  ILE F 119           
SHEET    3   K 4 VAL F 146  THR F 150  1  N  ILE F 149   O  VAL F 187           
SHEET    4   K 4 VAL F 167  ASP F 171  1  O  ASP F 168   N  ILE F 148           
SHEET    1   L 4 THR G  89  LEU G  90  0                                        
SHEET    2   L 4 VAL G  30  LEU G  35 -1  N  ILE G  33   O  LEU G  90           
SHEET    3   L 4 ILE G 153  THR G 157 -1  O  THR G 156   N  GLU G  31           
SHEET    4   L 4 TYR G 127  SER G 128 -1  N  TYR G 127   O  ILE G 155           
SHEET    1   M 3 ASP H  15  ILE H  18  0                                        
SHEET    2   M 3 VAL H  22  LYS H  26 -1  O  THR H  24   N  LYS H  17           
SHEET    3   M 3 THR H  33  LEU H  36 -1  O  THR H  35   N  ILE H  23           
SHEET    1   N 2 VAL H  40  GLU H  41  0                                        
SHEET    2   N 2 GLY H  52  PRO H  53 -1  O  GLY H  52   N  GLU H  41           
SHEET    1   O 3 PHE H  82  THR H  83  0                                        
SHEET    2   O 3 GLU H 129  GLY H 134 -1  O  GLY H 134   N  PHE H  82           
SHEET    3   O 3 ILE H 120  THR H 126 -1  N  THR H 121   O  LYS H 133           
SHEET    1   P 2 GLN H  87  VAL H  89  0                                        
SHEET    2   P 2 GLY H 160  ARG H 162 -1  O  ARG H 162   N  GLN H  87           
SHEET    1   Q 3 ARG H  94  LYS H  98  0                                        
SHEET    2   Q 3 VAL H 101  SER H 105 -1  O  VAL H 101   N  LYS H  98           
SHEET    3   Q 3 HIS H 114  GLN H 115 -1  O  HIS H 114   N  ILE H 102           
SHEET    1   R 2 ILE I   4  LEU I   5  0                                        
SHEET    2   R 2 ALA I  36  VAL I  37 -1  O  VAL I  37   N  ILE I   4           
SHEET    1   S 5 LEU I  90  GLY I  92  0                                        
SHEET    2   S 5 VAL I  78  ALA I  84 -1  N  LYS I  83   O  PHE I  91           
SHEET    3   S 5 PHE I 139  VAL I 147  1  O  VAL I 147   N  SER I  82           
SHEET    4   S 5 GLY I 126  GLN I 133 -1  N  PHE I 132   O  ALA I 140           
SHEET    5   S 5 VAL I 115  ARG I 116 -1  N  ARG I 116   O  SER I 131           
SHEET    1   T 3 VAL J   8  VAL J  12  0                                        
SHEET    2   T 3 ILE J  54  TYR J  61 -1  O  ILE J  54   N  VAL J  12           
SHEET    3   T 3 SER J  65  THR J  70 -1  O  SER J  65   N  TYR J  61           
SHEET    1   U 2 GLY J  98  ILE J 100  0                                        
SHEET    2   U 2 LEU J 137  VAL J 139  1  O  VAL J 138   N  GLY J  98           
SHEET    1   V 4 LEU K 122  LYS K 123  0                                        
SHEET    2   V 4 TYR K  53  VAL K  56  1  N  VAL K  56   O  LYS K 123           
SHEET    3   V 4 TRP K  15  VAL K  18  1  N  TYR K  16   O  ILE K  55           
SHEET    4   V 4 GLN K 138  VAL K 139  1  O  GLN K 138   N  VAL K  17           
SHEET    1   W 2 VAL K  73  HIS K  76  0                                        
SHEET    2   W 2 LYS K  85  THR K  88 -1  O  LYS K  85   N  HIS K  76           
SHEET    1   X 6 MET L   7  VAL L  10  0                                        
SHEET    2   X 6 ARG L  18  VAL L  24 -1  O  VAL L  19   N  LEU L   8           
SHEET    3   X 6 ILE L  38  ILE L  43 -1  O  LYS L  40   N  LYS L  23           
SHEET    4   X 6 ASP L  56  ARG L  64 -1  O  LEU L  58   N  ILE L  41           
SHEET    5   X 6 ALA L  83  LEU L  87 -1  O  VAL L  85   N  VAL L  61           
SHEET    6   X 6 MET L   7  VAL L  10  1  N  ASN L   9   O  CYS L  84           
SHEET    1   Y 6 ILE L  77  PHE L  79  0                                        
SHEET    2   Y 6 VAL Q  69  GLN Q  74 -1  O  GLU Q  70   N  ARG L  78           
SHEET    3   Y 6 ALA Q  57  ARG Q  61 -1  N  VAL Q  60   O  ARG Q  71           
SHEET    4   Y 6 LEU Q  39  ALA Q  48 -1  N  ILE Q  47   O  THR Q  59           
SHEET    5   Y 6 THR Q  24  TRP Q  30 -1  N  VAL Q  29   O  GLN Q  40           
SHEET    6   Y 6 VAL Q  80  ARG Q  87 -1  O  SER Q  82   N  LYS Q  28           
SHEET    1   Z 3 THR M  74  ARG M  78  0                                        
SHEET    2   Z 3 PHE M 107  ILE M 111  1  O  ILE M 111   N  ILE M  77           
SHEET    3   Z 3 ARG M 126  VAL M 127  1  O  ARG M 126   N  VAL M 110           
SHEET    1  AA 3 VAL M  89  VAL M  90  0                                        
SHEET    2  AA 3 THR M 121  VAL M 122  1  O  THR M 121   N  VAL M  90           
SHEET    3  AA 3 LYS M 141  ILE M 142  1  O  LYS M 141   N  VAL M 122           
SHEET    1  AB 4 ILE N  63  ILE N  65  0                                        
SHEET    2  AB 4 VAL N 101  MET N 105 -1  O  GLU N 104   N  TRP N  64           
SHEET    3  AB 4 PHE N  31  LYS N  34 -1  N  LEU N  33   O  LEU N 102           
SHEET    4  AB 4 THR N 129  THR N 132 -1  O  THR N 129   N  LYS N  34           
SHEET    1  AC 3 GLY N  39  THR N  42  0                                        
SHEET    2  AC 3 ASN N  88  ILE N  96 -1  O  ALA N  94   N  LEU N  41           
SHEET    3  AC 3 LYS N  71  GLU N  75 -1  N  ILE N  73   O  GLU N  90           
SHEET    1  AD 3 ILE O  33  THR O  37  0                                        
SHEET    2  AD 3 MET O 110  LEU O 115 -1  O  ALA O 111   N  THR O  36           
SHEET    3  AD 3 THR O  95  GLY O 101 -1  N  ARG O  96   O  GLU O 114           
SHEET    1  AE 4 VAL P  47  SER P  52  0                                        
SHEET    2  AE 4 ILE P  35  ILE P  40 -1  N  VAL P  39   O  LEU P  48           
SHEET    3  AE 4 ARG P  25  ARG P  30 -1  N  ARG P  25   O  ILE P  40           
SHEET    4  AE 4 SER P  91  PHE P  92  1  O  SER P  91   N  LEU P  26           
SHEET    1  AF 2 GLY Q  89  ALA Q  90  0                                        
SHEET    2  AF 2 LYS Q 110  GLU Q 111 -1  O  LYS Q 110   N  ALA Q  90           
SHEET    1  AG 3 LYS S  10  SER S  15  0                                        
SHEET    2  AG 3 TYR S   2  SER S   7 -1  N  PHE S   5   O  HIS S  12           
SHEET    3  AG 3 VAL S  38  ALA S  42 -1  O  ALA S  42   N  TYR S   2           
SHEET    1  AH 4 THR S  19  GLU S  23  0                                        
SHEET    2  AH 4 TRP S  92  ILE S  98 -1  O  THR S  94   N  LEU S  22           
SHEET    3  AH 4 ILE S  59  ARG S  68 -1  N  GLY S  67   O  PHE S  93           
SHEET    4  AH 4 THR S  32  PHE S  35 -1  N  VAL S  33   O  ALA S  61           
SHEET    1  AI 2 VAL S  72  ARG S  78  0                                        
SHEET    2  AI 2 TYR S  83  HIS S  89 -1  O  GLN S  87   N  ILE S  74           
SHEET    1  AJ 3 GLU T   2  ALA T  10  0                                        
SHEET    2  AJ 3 SER T 101  SER T 108 -1  O  VAL T 107   N  THR T   3           
SHEET    3  AJ 3 LYS T  70  GLU T  78 -1  N  ASP T  77   O  HIS T 102           
SHEET    1  AK 2 MET T  82  PRO T  87  0                                        
SHEET    2  AK 2 ALA T  93  LYS T  98 -1  O  ASP T  94   N  MET T  86           
SHEET    1  AL 4 ALA U  13  PRO U  14  0                                        
SHEET    2  AL 4 THR U  29  LYS U  33 -1  O  LYS U  33   N  ALA U  13           
SHEET    3  AL 4 TRP U  80  GLU U  89 -1  O  VAL U  85   N  ILE U  30           
SHEET    4  AL 4 GLU U  54  VAL U  63 -1  N  GLU U  56   O  THR U  86           
SHEET    1  AM 2 VAL U  67  LYS U  68  0                                        
SHEET    2  AM 2 GLY U  75  ARG U  76 -1  O  GLY U  75   N  LYS U  68           
SHEET    1  AN 5 ILE V  64  GLN V  65  0                                        
SHEET    2  AN 5 LYS V  32  VAL V  35 -1  N  VAL V  33   O  ILE V  64           
SHEET    3  AN 5 ARG V  21  LEU V  28 -1  N  ASN V  26   O  ILE V  34           
SHEET    4  AN 5 GLU V   9  VAL V  12 -1  N  VAL V  10   O  GLY V  22           
SHEET    5  AN 5 VAL V  69  ILE V  71 -1  O  ALA V  70   N  ILE V  11           
SHEET    1  AO 2 LEU V  40  GLN V  45  0                                        
SHEET    2  AO 2 GLY V  56  GLU V  61 -1  O  VAL V  58   N  LYS V  43           
SHEET    1  AP 7 THR W   3  VAL W   8  0                                        
SHEET    2  AP 7 LEU W  38  ASP W  43 -1  O  GLU W  41   N  GLU W   7           
SHEET    3  AP 7 LYS W  25  TYR W  31 -1  N  ILE W  30   O  LEU W  38           
SHEET    4  AP 7 LEU W  86  ARG W  93  1  O  ARG W  93   N  TYR W  31           
SHEET    5  AP 7 LYS W  71  ARG W  79 -1  N  GLN W  78   O  HIS W  88           
SHEET    6  AP 7 LEU W  61  VAL W  64 -1  N  LEU W  61   O  VAL W  72           
SHEET    7  AP 7 THR W   3  VAL W   8  1  N  ILE W   4   O  THR W  62           
SHEET    1  AQ 3 LYS X  43  ALA X  46  0                                        
SHEET    2  AQ 3 LYS X  77  GLU X  82  1  O  ILE X  79   N  PHE X  44           
SHEET    3  AQ 3 LYS X  65  VAL X  70 -1  N  LYS X  67   O  SER X  80           
SHEET    1  AR 2 ASN Y  15  ASN Y  16  0                                        
SHEET    2  AR 2 THR Y  24  LYS Y  25 -1  O  THR Y  24   N  ASN Y  16           
SHEET    1  AS 2 LEU Y  32  VAL Y  39  0                                        
SHEET    2  AS 2 ARG Y  44  SER Y  51 -1  O  VAL Y  46   N  PHE Y  37           
SHEET    1  AT 3 VAL a  35  GLU a  38  0                                        
SHEET    2  AT 3 THR a   3  THR a   7 -1  N  ILE a   6   O  VAL a  35           
SHEET    3  AT 3 LYS a  55  GLU a  57 -1  O  GLU a  57   N  LYS a   5           
SHEET    1  AU 2 SER c  28  VAL c  29  0                                        
SHEET    2  AU 2 LYS c  36  HIS c  37 -1  O  HIS c  37   N  SER c  28           
SHEET    1  AV 3 PHE d  19  THR d  22  0                                        
SHEET    2  AV 3 ILE d   8  SER d  12 -1  N  LEU d  10   O  TYR d  20           
SHEET    3  AV 3 TYR d  48  LYS d  49 -1  O  LYS d  49   N  VAL d  11           
SHEET    1  AW 2 LYS d  37  ASP d  39  0                                        
SHEET    2  AW 2 GLN d  44  VAL d  46 -1  O  VAL d  46   N  LYS d  37           
SHEET    1  AX 3 LYS f  14  LYS f  15  0                                        
SHEET    2  AX 3 PHE f  21  HIS f  23 -1  O  LYS f  22   N  LYS f  14           
SHEET    3  AX 3 ALA f  47  MET f  48 -1  O  ALA f  47   N  HIS f  23           
SHEET    1  AY 2 CYS g  14  ARG g  19  0                                        
SHEET    2  AY 2 VAL g  22  CYS g  27 -1  O  ILE g  26   N  LYS g  15           
LINK         O3'   U B 744                 P   1MG B 745     1555   1555  1.62  
LINK         O3' 1MG B 745                 P   PSU B 746     1555   1555  1.61  
LINK         O3' PSU B 746                 P   5MU B 747     1555   1555  1.63  
LINK         O3' 5MU B 747                 P     G B 748     1555   1555  1.60  
LINK         O3'   G B 954                 P   PSU B 955     1555   1555  1.60  
LINK         O3' PSU B 955                 P     G B 956     1555   1555  1.62  
LINK         O3'   C B1617                 P   6MZ B1618     1555   1555  1.61  
LINK         O3'   U B1834                 P   2MG B1835     1555   1555  1.61  
LINK         O3' 2MG B1835                 P     C B1836     1555   1555  1.60  
LINK         O3'   G B1910                 P   PSU B1911     1555   1555  1.62  
LINK         O3' PSU B1911                 P     A B1912     1555   1555  1.62  
LINK         O3'   A B1916                 P   PSU B1917     1555   1555  1.62  
LINK         O3' PSU B1917                 P     A B1918     1555   1555  1.62  
LINK         O3'   A B1938                 P   5MU B1939     1555   1555  1.62  
LINK         O3' 5MU B1939                 P     U B1940     1555   1555  1.59  
LINK         O3'   C B1961                 P   5MC B1962     1555   1555  1.61  
LINK         O3' 5MC B1962                 P     U B1963     1555   1555  1.59  
LINK         O3'   G B2029                 P   6MZ B2030     1555   1555  1.62  
LINK         O3'   U B2068                 P   7MG B2069     1555   1555  1.62  
LINK         O3' 7MG B2069                 P     A B2070     1555   1555  1.61  
LINK         O3'   G B2250                 P   OMG B2251     1555   1555  1.62  
LINK         O3' OMG B2251                 P     G B2252     1555   1555  1.62  
LINK         O3'   G B2444                 P   2MG B2445     1555   1555  1.63  
LINK         O3' 2MG B2445                 P     G B2446     1555   1555  1.61  
LINK         O3'   A B2448                 P   H2U B2449     1555   1555  1.63  
LINK         O3' H2U B2449                 P     A B2450     1555   1555  1.61  
LINK         O3'   C B2456                 P   PSU B2457     1555   1555  1.61  
LINK         O3' PSU B2457                 P     G B2458     1555   1555  1.61  
LINK         O3'   A B2497                 P   OMC B2498     1555   1555  1.61  
LINK         O3' OMC B2498                 P     C B2499     1555   1555  1.62  
LINK         O3'   G B2502                 P   2MA B2503     1555   1555  1.61  
LINK         O3' 2MA B2503                 P   PSU B2504     1555   1555  1.62  
LINK         O3' PSU B2504                 P     G B2505     1555   1555  1.63  
LINK         O3'   C B2551                 P   OMU B2552     1555   1555  1.59  
LINK         O3' OMU B2552                 P     G B2553     1555   1555  1.61  
LINK         O3'   G B2574                 P    CH B2575     1555   1555  1.61  
LINK         O3'  CH B2575                 P     G B2576     1555   1555  1.62  
LINK         O3'   C B2579                 P   PSU B2580     1555   1555  1.61  
LINK         O3' PSU B2580                 P     G B2581     1555   1555  1.61  
LINK         O3'   U B2604                 P   PSU B2605     1555   1555  1.62  
LINK         O3' PSU B2605                 P     C B2606     1555   1555  1.62  
LINK         O3'   C B1914                 P   3TD B1915     1555   1555  1.62  
LINK         O3' 3TD B1915                 P     A B1916     1555   1555  1.62  
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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