GenomeNet

Database: PDB
Entry: 3IZW
LinkDB: 3IZW
Original site: 3IZW 
HEADER    RIBOSOME                                07-JAN-11   3IZW              
TITLE     STRUCTURAL INSIGHTS INTO COGNATE VS. NEAR-COGNATE DISCRIMINATION      
TITLE    2 DURING DECODING.THIS ENTRY CONTAINS THE SMALL SUBUNIT OF A RIBOSOME  
TITLE    3 PROGRAMMED WITH A COGNATE CODON, A/T-SITE TRNA, P-SITE TRNA, MRNA AND
TITLE    4 EF-TU                                                                
SPLIT      3IZU 3IZW                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 16S RIBOSOMAL RNA;                                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: A/T-SITE TRNA PHE;                                         
COMPND   6 CHAIN: B, E;                                                         
COMPND   7 MOL_ID: 3;                                                           
COMPND   8 MOLECULE: ELONGATION FACTOR TU 2;                                    
COMPND   9 CHAIN: C;                                                            
COMPND  10 MOL_ID: 4;                                                           
COMPND  11 MOLECULE: MRNA;                                                      
COMPND  12 CHAIN: D;                                                            
COMPND  13 MOL_ID: 5;                                                           
COMPND  14 MOLECULE: 30S RIBOSOMAL PROTEIN S2;                                  
COMPND  15 CHAIN: F;                                                            
COMPND  16 MOL_ID: 6;                                                           
COMPND  17 MOLECULE: 30S RIBOSOMAL PROTEIN S3;                                  
COMPND  18 CHAIN: G;                                                            
COMPND  19 MOL_ID: 7;                                                           
COMPND  20 MOLECULE: 30S RIBOSOMAL PROTEIN S4;                                  
COMPND  21 CHAIN: H;                                                            
COMPND  22 MOL_ID: 8;                                                           
COMPND  23 MOLECULE: 30S RIBOSOMAL PROTEIN S5;                                  
COMPND  24 CHAIN: I;                                                            
COMPND  25 MOL_ID: 9;                                                           
COMPND  26 MOLECULE: 30S RIBOSOMAL PROTEIN S6;                                  
COMPND  27 CHAIN: J;                                                            
COMPND  28 MOL_ID: 10;                                                          
COMPND  29 MOLECULE: 30S RIBOSOMAL PROTEIN S7;                                  
COMPND  30 CHAIN: K;                                                            
COMPND  31 MOL_ID: 11;                                                          
COMPND  32 MOLECULE: 30S RIBOSOMAL PROTEIN S8;                                  
COMPND  33 CHAIN: L;                                                            
COMPND  34 MOL_ID: 12;                                                          
COMPND  35 MOLECULE: 30S RIBOSOMAL PROTEIN S9;                                  
COMPND  36 CHAIN: M;                                                            
COMPND  37 MOL_ID: 13;                                                          
COMPND  38 MOLECULE: 30S RIBOSOMAL PROTEIN S10;                                 
COMPND  39 CHAIN: N;                                                            
COMPND  40 MOL_ID: 14;                                                          
COMPND  41 MOLECULE: 30S RIBOSOMAL PROTEIN S11;                                 
COMPND  42 CHAIN: O;                                                            
COMPND  43 MOL_ID: 15;                                                          
COMPND  44 MOLECULE: 30S RIBOSOMAL PROTEIN S12;                                 
COMPND  45 CHAIN: P;                                                            
COMPND  46 MOL_ID: 16;                                                          
COMPND  47 MOLECULE: 30S RIBOSOMAL PROTEIN S13;                                 
COMPND  48 CHAIN: Q;                                                            
COMPND  49 MOL_ID: 17;                                                          
COMPND  50 MOLECULE: 30S RIBOSOMAL PROTEIN S14;                                 
COMPND  51 CHAIN: R;                                                            
COMPND  52 MOL_ID: 18;                                                          
COMPND  53 MOLECULE: 30S RIBOSOMAL PROTEIN S15;                                 
COMPND  54 CHAIN: S;                                                            
COMPND  55 MOL_ID: 19;                                                          
COMPND  56 MOLECULE: 30S RIBOSOMAL PROTEIN S16;                                 
COMPND  57 CHAIN: T;                                                            
COMPND  58 MOL_ID: 20;                                                          
COMPND  59 MOLECULE: 30S RIBOSOMAL PROTEIN S17;                                 
COMPND  60 CHAIN: U;                                                            
COMPND  61 MOL_ID: 21;                                                          
COMPND  62 MOLECULE: 30S RIBOSOMAL PROTEIN S18;                                 
COMPND  63 CHAIN: V;                                                            
COMPND  64 MOL_ID: 22;                                                          
COMPND  65 MOLECULE: 30S RIBOSOMAL PROTEIN S19;                                 
COMPND  66 CHAIN: W;                                                            
COMPND  67 MOL_ID: 23;                                                          
COMPND  68 MOLECULE: 30S RIBOSOMAL PROTEIN S20;                                 
COMPND  69 CHAIN: X;                                                            
COMPND  70 MOL_ID: 24;                                                          
COMPND  71 MOLECULE: 30S RIBOSOMAL PROTEIN S21;                                 
COMPND  72 CHAIN: Y                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI DH1;                           
SOURCE   3 ORGANISM_TAXID: 536056;                                              
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI DH1;                           
SOURCE   6 ORGANISM_TAXID: 536056;                                              
SOURCE   7 MOL_ID: 3;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE   9 ORGANISM_TAXID: 83333;                                               
SOURCE  10 STRAIN: K12;                                                         
SOURCE  11 MOL_ID: 4;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  13 ORGANISM_TAXID: 562;                                                 
SOURCE  14 MOL_ID: 5;                                                           
SOURCE  15 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE  16 ORGANISM_TAXID: 83333;                                               
SOURCE  17 STRAIN: K12;                                                         
SOURCE  18 MOL_ID: 6;                                                           
SOURCE  19 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE  20 ORGANISM_TAXID: 83333;                                               
SOURCE  21 STRAIN: K12;                                                         
SOURCE  22 MOL_ID: 7;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE  24 ORGANISM_TAXID: 83333;                                               
SOURCE  25 STRAIN: K12;                                                         
SOURCE  26 MOL_ID: 8;                                                           
SOURCE  27 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE  28 ORGANISM_TAXID: 83333;                                               
SOURCE  29 STRAIN: K12;                                                         
SOURCE  30 MOL_ID: 9;                                                           
SOURCE  31 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE  32 ORGANISM_TAXID: 83333;                                               
SOURCE  33 STRAIN: K12;                                                         
SOURCE  34 MOL_ID: 10;                                                          
SOURCE  35 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE  36 ORGANISM_TAXID: 83333;                                               
SOURCE  37 STRAIN: K12;                                                         
SOURCE  38 MOL_ID: 11;                                                          
SOURCE  39 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE  40 ORGANISM_TAXID: 83333;                                               
SOURCE  41 STRAIN: K12;                                                         
SOURCE  42 MOL_ID: 12;                                                          
SOURCE  43 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE  44 ORGANISM_TAXID: 83333;                                               
SOURCE  45 STRAIN: K12;                                                         
SOURCE  46 MOL_ID: 13;                                                          
SOURCE  47 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE  48 ORGANISM_TAXID: 83333;                                               
SOURCE  49 STRAIN: K12;                                                         
SOURCE  50 MOL_ID: 14;                                                          
SOURCE  51 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE  52 ORGANISM_TAXID: 83333;                                               
SOURCE  53 STRAIN: K12;                                                         
SOURCE  54 MOL_ID: 15;                                                          
SOURCE  55 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE  56 ORGANISM_TAXID: 83333;                                               
SOURCE  57 STRAIN: K12;                                                         
SOURCE  58 MOL_ID: 16;                                                          
SOURCE  59 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE  60 ORGANISM_TAXID: 83333;                                               
SOURCE  61 STRAIN: K12;                                                         
SOURCE  62 MOL_ID: 17;                                                          
SOURCE  63 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE  64 ORGANISM_TAXID: 83333;                                               
SOURCE  65 STRAIN: K12;                                                         
SOURCE  66 MOL_ID: 18;                                                          
SOURCE  67 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI O157:H7;                       
SOURCE  68 ORGANISM_TAXID: 83334;                                               
SOURCE  69 MOL_ID: 19;                                                          
SOURCE  70 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE  71 ORGANISM_TAXID: 83333;                                               
SOURCE  72 STRAIN: K12;                                                         
SOURCE  73 MOL_ID: 20;                                                          
SOURCE  74 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE  75 ORGANISM_TAXID: 83333;                                               
SOURCE  76 STRAIN: K12;                                                         
SOURCE  77 MOL_ID: 21;                                                          
SOURCE  78 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE  79 ORGANISM_TAXID: 83333;                                               
SOURCE  80 STRAIN: K12;                                                         
SOURCE  81 MOL_ID: 22;                                                          
SOURCE  82 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE  83 ORGANISM_TAXID: 83333;                                               
SOURCE  84 STRAIN: K12;                                                         
SOURCE  85 MOL_ID: 23;                                                          
SOURCE  86 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE  87 ORGANISM_TAXID: 83333;                                               
SOURCE  88 STRAIN: K12;                                                         
SOURCE  89 MOL_ID: 24;                                                          
SOURCE  90 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE  91 ORGANISM_TAXID: 83333;                                               
SOURCE  92 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 3IZW    1       DBREF  HET    HETATM HETNAM              
REVDAT   4 2                   1       LINK   MODRES REMARK SEQRES              
REVDAT   3   14-DEC-11 3IZW    1       HET    HETATM HETNAM SEQRES              
REVDAT   3 2                   1       VERSN                                    
REVDAT   2   04-MAY-11 3IZW    1       JRNL                                     
REVDAT   1   23-MAR-11 3IZW    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                    : 2I2U                                
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 3IZW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-JAN-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB160074.                                      
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: 25-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                   
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 F     0                                                      
REMARK 465     MET G     0                                                      
REMARK 465     MET H     0                                                      
REMARK 465     MET I     0                                                      
REMARK 465     MET K     0                                                      
REMARK 465     MET L     0                                                      
REMARK 465     MET M     0                                                      
REMARK 465     MET O     0                                                      
REMARK 465     MET P     0                                                      
REMARK 465     MET Q     0                                                      
REMARK 465     MET R     0                                                      
REMARK 465     MET S     0                                                      
REMARK 465     MET U     0                                                      
REMARK 465     MET V     0                                                      
REMARK 465     MET W     0                                                      
REMARK 465     MET X     0                                                      
REMARK 465     MET Y     0                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     3AU B  47    OP1                                                 
REMARK 470     3AU E  47    OP1                                                 
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500      A A   1   O4' -  C1' -  N9  ANGL. DEV. =   6.0 DEGREES          
REMARK 500      A A   2   C5' -  C4' -  C3' ANGL. DEV. = -10.3 DEGREES          
REMARK 500      A A   2   C5' -  C4' -  O4' ANGL. DEV. =   6.9 DEGREES          
REMARK 500      U A   4   C5' -  C4' -  C3' ANGL. DEV. =  -9.4 DEGREES          
REMARK 500      U A   4   C5' -  C4' -  O4' ANGL. DEV. =   6.0 DEGREES          
REMARK 500      G A   6   C5' -  C4' -  C3' ANGL. DEV. =  -9.5 DEGREES          
REMARK 500      G A   9   N3  -  C4  -  C5  ANGL. DEV. =  -3.0 DEGREES          
REMARK 500      G A  11   C5' -  C4' -  O4' ANGL. DEV. =   5.4 DEGREES          
REMARK 500      U A  13   O4' -  C1' -  N1  ANGL. DEV. =   4.5 DEGREES          
REMARK 500      C A  18   O4' -  C1' -  N1  ANGL. DEV. =   4.3 DEGREES          
REMARK 500      A A  19   O4' -  C1' -  N9  ANGL. DEV. =   4.6 DEGREES          
REMARK 500      C A  23   O4' -  C1' -  N1  ANGL. DEV. =   4.4 DEGREES          
REMARK 500      U A  24   O4' -  C1' -  N1  ANGL. DEV. =   5.5 DEGREES          
REMARK 500      C A  25   O4' -  C1' -  N1  ANGL. DEV. =   6.2 DEGREES          
REMARK 500      U A  29   O4' -  C1' -  N1  ANGL. DEV. =   7.3 DEGREES          
REMARK 500      G A  31   O4' -  C1' -  N9  ANGL. DEV. =   6.1 DEGREES          
REMARK 500      G A  39   O4' -  C1' -  N9  ANGL. DEV. =   5.1 DEGREES          
REMARK 500      C A  40   O4' -  C1' -  N1  ANGL. DEV. =   4.2 DEGREES          
REMARK 500      A A  44   O4' -  C1' -  N9  ANGL. DEV. =   4.5 DEGREES          
REMARK 500      G A  46   O4' -  C1' -  N9  ANGL. DEV. =   4.3 DEGREES          
REMARK 500      C A  48   O4' -  C1' -  N1  ANGL. DEV. =   4.5 DEGREES          
REMARK 500      A A  51   O4' -  C1' -  N9  ANGL. DEV. =   5.0 DEGREES          
REMARK 500      C A  52   C5' -  C4' -  O4' ANGL. DEV. =   7.3 DEGREES          
REMARK 500      C A  52   C1' -  O4' -  C4' ANGL. DEV. =  -5.5 DEGREES          
REMARK 500      C A  52   O4' -  C1' -  N1  ANGL. DEV. =   5.7 DEGREES          
REMARK 500      G A  57   N3  -  C4  -  C5  ANGL. DEV. =  -3.0 DEGREES          
REMARK 500      G A  57   C8  -  N9  -  C4  ANGL. DEV. =  -2.6 DEGREES          
REMARK 500      C A  58   O4' -  C1' -  N1  ANGL. DEV. =   4.9 DEGREES          
REMARK 500      A A  59   C5' -  C4' -  O4' ANGL. DEV. =   7.6 DEGREES          
REMARK 500      G A  61   O5' -  C5' -  C4' ANGL. DEV. =  -5.3 DEGREES          
REMARK 500      A A  60   C3' -  O3' -  P   ANGL. DEV. =   8.1 DEGREES          
REMARK 500      A A  65   O4' -  C1' -  N9  ANGL. DEV. =   6.0 DEGREES          
REMARK 500      G A  68   N9  -  C1' -  C2' ANGL. DEV. =  -6.9 DEGREES          
REMARK 500      G A  68   O4' -  C1' -  N9  ANGL. DEV. =   4.6 DEGREES          
REMARK 500      G A  69   O4' -  C1' -  N9  ANGL. DEV. =   6.7 DEGREES          
REMARK 500      U A  70   O4' -  C1' -  N1  ANGL. DEV. =   4.8 DEGREES          
REMARK 500      A A  72   C5' -  C4' -  O4' ANGL. DEV. =   7.4 DEGREES          
REMARK 500      C A  73   O4' -  C1' -  N1  ANGL. DEV. =   6.0 DEGREES          
REMARK 500      A A  74   O4' -  C1' -  N9  ANGL. DEV. =   4.5 DEGREES          
REMARK 500      A A  78   O4' -  C1' -  N9  ANGL. DEV. =   6.3 DEGREES          
REMARK 500      A A  81   O4' -  C1' -  N9  ANGL. DEV. =   4.5 DEGREES          
REMARK 500      C A  83   O4' -  C1' -  N1  ANGL. DEV. =   5.9 DEGREES          
REMARK 500      U A  85   O4' -  C1' -  N1  ANGL. DEV. =   6.2 DEGREES          
REMARK 500      U A  88   O4' -  C1' -  N1  ANGL. DEV. =   5.2 DEGREES          
REMARK 500      C A  90   O4' -  C1' -  N1  ANGL. DEV. =   6.8 DEGREES          
REMARK 500      U A  91   C5' -  C4' -  O4' ANGL. DEV. =   7.2 DEGREES          
REMARK 500      U A  92   O4' -  C1' -  N1  ANGL. DEV. =   5.2 DEGREES          
REMARK 500      U A  96   O4' -  C1' -  N1  ANGL. DEV. =   5.9 DEGREES          
REMARK 500      G A  97   C8  -  N9  -  C4  ANGL. DEV. =  -2.6 DEGREES          
REMARK 500      A A  98   O4' -  C1' -  N9  ANGL. DEV. =   4.4 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     834 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    LYS C   9      163.47     50.99                                   
REMARK 500    ASP C  21      -15.26     56.08                                   
REMARK 500    ARG C  58      -46.41   -140.43                                   
REMARK 500    ILE C  60       13.73    -57.67                                   
REMARK 500    THR C  61      -50.22     60.21                                   
REMARK 500    SER C  65       87.41    -66.69                                   
REMARK 500    VAL C 125      -30.50   -139.44                                   
REMARK 500    PRO C 128       33.01    -74.68                                   
REMARK 500    ILE C 188      -39.84   -138.96                                   
REMARK 500    SER C 197      -11.31   -147.88                                   
REMARK 500    ALA C 205       56.50    -95.19                                   
REMARK 500    ARG C 333     -118.89     49.50                                   
REMARK 500    LYS C 390      154.87    178.97                                   
REMARK 500    MET F   8       -8.11    -59.45                                   
REMARK 500    HIS F  14     -172.40     58.12                                   
REMARK 500    THR F  19       71.70     45.88                                   
REMARK 500    ASN F  41       86.14     37.01                                   
REMARK 500    ASN F  92       -9.28   -151.81                                   
REMARK 500    GLN F 121      -36.00   -130.18                                   
REMARK 500    LYS F 130      -23.01   -141.33                                   
REMARK 500    LYS F 131      -16.39   -141.40                                   
REMARK 500    GLU F 132      -29.03    -38.48                                   
REMARK 500    THR F 188       -2.36     60.98                                   
REMARK 500    VAL G  14        9.90     54.30                                   
REMARK 500    ALA G  23       38.86   -151.38                                   
REMARK 500    THR G  25       19.49     46.61                                   
REMARK 500    LYS G  26      -14.14   -154.78                                   
REMARK 500    LYS G 107       70.93     45.51                                   
REMARK 500    PRO G 223      151.80    -45.74                                   
REMARK 500    LEU H  18        1.87     44.50                                   
REMARK 500    ILE H  27       25.71     38.41                                   
REMARK 500    LYS H  30       53.24     39.42                                   
REMARK 500    HIS H 119       39.83    -90.74                                   
REMARK 500    ASN H 139       17.20     58.39                                   
REMARK 500    SER H 188       22.87    -74.48                                   
REMARK 500    ASP H 189      -39.67   -136.35                                   
REMARK 500    ILE I   3        9.96    -68.71                                   
REMARK 500    GLN I   6      -31.32    -39.64                                   
REMARK 500    GLU I   9      -12.72   -152.58                                   
REMARK 500    THR I  23       63.99     66.76                                   
REMARK 500    ASN I  42      -41.22   -135.37                                   
REMARK 500    ASN I  77       95.41    -46.44                                   
REMARK 500    PHE I  94      -41.24   -152.09                                   
REMARK 500    HIS I 120      -23.04   -158.49                                   
REMARK 500    ILE I 140      -22.46   -140.66                                   
REMARK 500    VAL I 152      -26.84   -146.53                                   
REMARK 500    GLU I 162      -15.33    -45.36                                   
REMARK 500    ASP J  13       -9.85    -59.82                                   
REMARK 500    THR J  92       88.21     51.75                                   
REMARK 500    GLU J 125       48.35    -92.06                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     149 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 ALA G  221     GLN G  222                  143.30                    
REMARK 500 MET I  146     ASN I  147                 -139.05                    
REMARK 500 ALA I  154     LYS I  155                  145.62                    
REMARK 500 SER J   87     MET J   88                  146.91                    
REMARK 500 VAL K    5     ILE K    6                  141.93                    
REMARK 500 LEU O   81     GLU O   82                  138.14                    
REMARK 500 LYS Y    4     VAL Y    5                 -147.64                    
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      A A   3         0.11    SIDE CHAIN                              
REMARK 500      U A   4         0.07    SIDE CHAIN                              
REMARK 500      U A   5         0.07    SIDE CHAIN                              
REMARK 500      A A   7         0.09    SIDE CHAIN                              
REMARK 500      A A   8         0.16    SIDE CHAIN                              
REMARK 500      G A  11         0.06    SIDE CHAIN                              
REMARK 500      G A  15         0.08    SIDE CHAIN                              
REMARK 500      A A  16         0.08    SIDE CHAIN                              
REMARK 500      G A  22         0.07    SIDE CHAIN                              
REMARK 500      C A  25         0.06    SIDE CHAIN                              
REMARK 500      G A  27         0.08    SIDE CHAIN                              
REMARK 500      U A  29         0.08    SIDE CHAIN                              
REMARK 500      G A  31         0.09    SIDE CHAIN                              
REMARK 500      A A  33         0.05    SIDE CHAIN                              
REMARK 500      C A  34         0.07    SIDE CHAIN                              
REMARK 500      G A  39         0.08    SIDE CHAIN                              
REMARK 500      C A  43         0.09    SIDE CHAIN                              
REMARK 500      A A  50         0.07    SIDE CHAIN                              
REMARK 500      G A  61         0.08    SIDE CHAIN                              
REMARK 500      U A  62         0.11    SIDE CHAIN                              
REMARK 500      G A  64         0.10    SIDE CHAIN                              
REMARK 500      A A  66         0.07    SIDE CHAIN                              
REMARK 500      G A  69         0.07    SIDE CHAIN                              
REMARK 500      A A  71         0.06    SIDE CHAIN                              
REMARK 500      C A  73         0.08    SIDE CHAIN                              
REMARK 500      G A  76         0.08    SIDE CHAIN                              
REMARK 500      G A  82         0.05    SIDE CHAIN                              
REMARK 500      U A  84         0.10    SIDE CHAIN                              
REMARK 500      U A  85         0.09    SIDE CHAIN                              
REMARK 500      U A  88         0.07    SIDE CHAIN                              
REMARK 500      U A  89         0.12    SIDE CHAIN                              
REMARK 500      U A  91         0.07    SIDE CHAIN                              
REMARK 500      U A  92         0.07    SIDE CHAIN                              
REMARK 500      G A  94         0.07    SIDE CHAIN                              
REMARK 500      C A  99         0.12    SIDE CHAIN                              
REMARK 500      G A 100         0.07    SIDE CHAIN                              
REMARK 500      G A 104         0.07    SIDE CHAIN                              
REMARK 500      G A 113         0.08    SIDE CHAIN                              
REMARK 500      A A 116         0.06    SIDE CHAIN                              
REMARK 500      G A 128         0.09    SIDE CHAIN                              
REMARK 500      G A 134         0.07    SIDE CHAIN                              
REMARK 500      U A 137         0.07    SIDE CHAIN                              
REMARK 500      G A 138         0.05    SIDE CHAIN                              
REMARK 500      G A 142         0.07    SIDE CHAIN                              
REMARK 500      A A 143         0.10    SIDE CHAIN                              
REMARK 500      A A 149         0.08    SIDE CHAIN                              
REMARK 500      U A 150         0.12    SIDE CHAIN                              
REMARK 500      A A 152         0.07    SIDE CHAIN                              
REMARK 500      C A 153         0.09    SIDE CHAIN                              
REMARK 500      G A 159         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     513 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    PRO G 223        -11.08                                           
REMARK 500    MET I 146         17.42                                           
REMARK 500    PRO K 172        -13.85                                           
REMARK 500    ALA P  16        -10.57                                           
REMARK 500    ARG R  60        -11.34                                           
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 3IZW A    1  1542  GB                   AP012030.1                       
DBREF2 3IZW A     AP012030                      4145764     4147305             
DBREF1 3IZW B    1    76  GB                   AP012030.1                       
DBREF2 3IZW B     AP012030                      3088273     3088348             
DBREF  3IZW C    1   393  UNP    P0CE48   EFTU2_ECOLI      2    394             
DBREF  3IZW D   24    47  PDB    3IZW     3IZW             1     24             
DBREF1 3IZW E    1    76  GB                   AP012030.1                       
DBREF2 3IZW E     AP012030                      3088273     3088348             
DBREF  3IZW F    0   240  UNP    P0A7V0   RS2_ECOLI        1    241             
DBREF  3IZW G    0   232  UNP    P0A7V3   RS3_ECOLI        1    233             
DBREF  3IZW H    0   205  UNP    P0A7V8   RS4_ECOLI        1    206             
DBREF  3IZW I    0   166  UNP    P0A7W1   RS5_ECOLI        1    167             
DBREF  3IZW J    1   135  UNP    P02358   RS6_ECOLI        1    135             
DBREF  3IZW K    0   178  UNP    P02359   RS7_ECOLI        1    179             
DBREF  3IZW L    0   129  UNP    P0A7W7   RS8_ECOLI        1    130             
DBREF  3IZW M    0   129  UNP    P0A7X3   RS9_ECOLI        1    130             
DBREF  3IZW N    1   103  UNP    P0A7R5   RS10_ECOLI       1    103             
DBREF  3IZW O    0   128  UNP    P0A7R9   RS11_ECOLI       1    129             
DBREF  3IZW P    0   123  UNP    P0A7S3   RS12_ECOLI       1    124             
DBREF  3IZW Q    0   117  UNP    P0A7S9   RS13_ECOLI       1    118             
DBREF  3IZW R    0   100  UNP    P0AG59   RS14_ECOLI       1    101             
DBREF  3IZW S    0    88  UNP    Q8X9M2   RS15_ECO57       1     89             
DBREF  3IZW T    1    82  UNP    P0A7T3   RS16_ECOLI       1     82             
DBREF  3IZW U    0    83  UNP    P0AG63   RS17_ECOLI       1     84             
DBREF  3IZW V    0    74  UNP    P0A7T7   RS18_ECOLI       1     75             
DBREF  3IZW W    0    91  UNP    P0A7U3   RS19_ECOLI       1     92             
DBREF  3IZW X    0    86  UNP    P0A7U7   RS20_ECOLI       1     87             
DBREF  3IZW Y    0    70  UNP    P68679   RS21_ECOLI       1     71             
SEQRES   1 A 1542    A   A   A   U   U   G   A   A   G   A   G   U   U          
SEQRES   2 A 1542    U   G   A   U   C   A   U   G   G   C   U   C   A          
SEQRES   3 A 1542    G   A   U   U   G   A   A   C   G   C   U   G   G          
SEQRES   4 A 1542    C   G   G   C   A   G   G   C   C   U   A   A   C          
SEQRES   5 A 1542    A   C   A   U   G   C   A   A   G   U   C   G   A          
SEQRES   6 A 1542    A   C   G   G   U   A   A   C   A   G   G   A   A          
SEQRES   7 A 1542    G   A   A   G   C   U   U   G   C   U   U   C   U          
SEQRES   8 A 1542    U   U   G   C   U   G   A   C   G   A   G   U   G          
SEQRES   9 A 1542    G   C   G   G   A   C   G   G   G   U   G   A   G          
SEQRES  10 A 1542    U   A   A   U   G   U   C   U   G   G   G   A   A          
SEQRES  11 A 1542    A   C   U   G   C   C   U   G   A   U   G   G   A          
SEQRES  12 A 1542    G   G   G   G   G   A   U   A   A   C   U   A   C          
SEQRES  13 A 1542    U   G   G   A   A   A   C   G   G   U   A   G   C          
SEQRES  14 A 1542    U   A   A   U   A   C   C   G   C   A   U   A   A          
SEQRES  15 A 1542    C   G   U   C   G   C   A   A   G   A   C   C   A          
SEQRES  16 A 1542    A   A   G   A   G   G   G   G   G   A   C   C   U          
SEQRES  17 A 1542    U   C   G   G   G   C   C   U   C   U   U   G   C          
SEQRES  18 A 1542    C   A   U   C   G   G   A   U   G   U   G   C   C          
SEQRES  19 A 1542    C   A   G   A   U   G   G   G   A   U   U   A   G          
SEQRES  20 A 1542    C   U   A   G   U   A   G   G   U   G   G   G   G          
SEQRES  21 A 1542    U   A   A   C   G   G   C   U   C   A   C   C   U          
SEQRES  22 A 1542    A   G   G   C   G   A   C   G   A   U   C   C   C          
SEQRES  23 A 1542    U   A   G   C   U   G   G   U   C   U   G   A   G          
SEQRES  24 A 1542    A   G   G   A   U   G   A   C   C   A   G   C   C          
SEQRES  25 A 1542    A   C   A   C   U   G   G   A   A   C   U   G   A          
SEQRES  26 A 1542    G   A   C   A   C   G   G   U   C   C   A   G   A          
SEQRES  27 A 1542    C   U   C   C   U   A   C   G   G   G   A   G   G          
SEQRES  28 A 1542    C   A   G   C   A   G   U   G   G   G   G   A   A          
SEQRES  29 A 1542    U   A   U   U   G   C   A   C   A   A   U   G   G          
SEQRES  30 A 1542    G   C   G   C   A   A   G   C   C   U   G   A   U          
SEQRES  31 A 1542    G   C   A   G   C   C   A   U   G   C   C   G   C          
SEQRES  32 A 1542    G   U   G   U   A   U   G   A   A   G   A   A   G          
SEQRES  33 A 1542    G   C   C   U   U   C   G   G   G   U   U   G   U          
SEQRES  34 A 1542    A   A   A   G   U   A   C   U   U   U   C   A   G          
SEQRES  35 A 1542    C   G   G   G   G   A   G   G   A   A   G   G   G          
SEQRES  36 A 1542    A   G   U   A   A   A   G   U   U   A   A   U   A          
SEQRES  37 A 1542    C   C   U   U   U   G   C   U   C   A   U   U   G          
SEQRES  38 A 1542    A   C   G   U   U   A   C   C   C   G   C   A   G          
SEQRES  39 A 1542    A   A   G   A   A   G   C   A   C   C   G   G   C          
SEQRES  40 A 1542    U   A   A   C   U   C   C   G PSU   G   C   C   A          
SEQRES  41 A 1542    G   C   A   G   C   C 7MG   C   G   G   U   A   A          
SEQRES  42 A 1542    U   A   C   G   G   A   G   G   G   U   G   C   A          
SEQRES  43 A 1542    A   G   C   G   U   U   A   A   U   C   G   G   A          
SEQRES  44 A 1542    A   U   U   A   C   U   G   G   G   C   G   U   A          
SEQRES  45 A 1542    A   A   G   C   G   C   A   C   G   C   A   G   G          
SEQRES  46 A 1542    C   G   G   U   U   U   G   U   U   A   A   G   U          
SEQRES  47 A 1542    C   A   G   A   U   G   U   G   A   A   A   U   C          
SEQRES  48 A 1542    C   C   C   G   G   G   C   U   C   A   A   C   C          
SEQRES  49 A 1542    U   G   G   G   A   A   C   U   G   C   A   U   C          
SEQRES  50 A 1542    U   G   A   U   A   C   U   G   G   C   A   A   G          
SEQRES  51 A 1542    C   U   U   G   A   G   U   C   U   C   G   U   A          
SEQRES  52 A 1542    G   A   G   G   G   G   G   G   U   A   G   A   A          
SEQRES  53 A 1542    U   U   C   C   A   G   G   U   G   U   A   G   C          
SEQRES  54 A 1542    G   G   U   G   A   A   A   U   G   C   G   U   A          
SEQRES  55 A 1542    G   A   G   A   U   C   U   G   G   A   G   G   A          
SEQRES  56 A 1542    A   U   A   C   C   G   G   U   G   G   C   G   A          
SEQRES  57 A 1542    A   G   G   C   G   G   C   C   C   C   C   U   G          
SEQRES  58 A 1542    G   A   C   G   A   A   G   A   C   U   G   A   C          
SEQRES  59 A 1542    G   C   U   C   A   G   G   U   G   C   G   A   A          
SEQRES  60 A 1542    A   G   C   G   U   G   G   G   G   A   G   C   A          
SEQRES  61 A 1542    A   A   C   A   G   G   A   U   U   A   G   A   U          
SEQRES  62 A 1542    A   C   C   C   U   G   G   U   A   G   U   C   C          
SEQRES  63 A 1542    A   C   G   C   C   G   U   A   A   A   C   G   A          
SEQRES  64 A 1542    U   G   U   C   G   A   C   U   U   G   G   A   G          
SEQRES  65 A 1542    G   U   U   G   U   G   C   C   C   U   U   G   A          
SEQRES  66 A 1542    G   G   C   G   U   G   G   C   U   U   C   C   G          
SEQRES  67 A 1542    G   A   G   C   U   A   A   C   G   C   G   U   U          
SEQRES  68 A 1542    A   A   G   U   C   G   A   C   C   G   C   C   U          
SEQRES  69 A 1542    G   G   G   G   A   G   U   A   C   G   G   C   C          
SEQRES  70 A 1542    G   C   A   A   G   G   U   U   A   A   A   A   C          
SEQRES  71 A 1542    U   C   A   A   A   U   G   A   A   U   U   G   A          
SEQRES  72 A 1542    C   G   G   G   G   G   C   C   C   G   C   A   C          
SEQRES  73 A 1542    A   A   G   C   G   G   U   G   G   A   G   C   A          
SEQRES  74 A 1542    U   G   U   G   G   U   U   U   A   A   U   U   C          
SEQRES  75 A 1542    G   A   U 2MG 5MC   A   A   C   G   C   G   A   A          
SEQRES  76 A 1542    G   A   A   C   C   U   U   A   C   C   U   G   G          
SEQRES  77 A 1542    U   C   U   U   G   A   C   A   U   C   C   A   C          
SEQRES  78 A 1542    G   G   A   A   G   U   U   U   U   C   A   G   A          
SEQRES  79 A 1542    G   A   U   G   A   G   A   A   U   G   U   G   C          
SEQRES  80 A 1542    C   U   U   C   G   G   G   A   A   C   C   G   U          
SEQRES  81 A 1542    G   A   G   A   C   A   G   G   U   G   C   U   G          
SEQRES  82 A 1542    C   A   U   G   G   C   U   G   U   C   G   U   C          
SEQRES  83 A 1542    A   G   C   U   C   G   U   G   U   U   G   U   G          
SEQRES  84 A 1542    A   A   A   U   G   U   U   G   G   G   U   U   A          
SEQRES  85 A 1542    A   G   U   C   C   C   G   C   A   A   C   G   A          
SEQRES  86 A 1542    G   C   G   C   A   A   C   C   C   U   U   A   U          
SEQRES  87 A 1542    C   C   U   U   U   G   U   U   G   C   C   A   G          
SEQRES  88 A 1542    C   G   G   U   C   C   G   G   C   C   G   G   G          
SEQRES  89 A 1542    A   A   C   U   C   A   A   A   G   G   A   G   A          
SEQRES  90 A 1542    C   U   G   C   C   A   G   U   G   A   U   A   A          
SEQRES  91 A 1542    A   C   U   G   G   A   G   G   A   A   G   G   U          
SEQRES  92 A 1542    G   G   G   G   A   U   G   A   C   G   U   C   A          
SEQRES  93 A 1542    A   G   U   C   A   U   C   A   U   G 2MG   C   C          
SEQRES  94 A 1542    C   U   U   A   C   G   A   C   C   A   G   G   G          
SEQRES  95 A 1542    C   U   A   C   A   C   A   C   G   U   G   C   U          
SEQRES  96 A 1542    A   C   A   A   U   G   G   C   G   C   A   U   A          
SEQRES  97 A 1542    C   A   A   A   G   A   G   A   A   G   C   G   A          
SEQRES  98 A 1542    C   C   U   C   G   C   G   A   G   A   G   C   A          
SEQRES  99 A 1542    A   G   C   G   G   A   C   C   U   C   A   U   A          
SEQRES 100 A 1542    A   A   G   U   G   C   G   U   C   G   U   A   G          
SEQRES 101 A 1542    U   C   C   G   G   A   U   U   G   G   A   G   U          
SEQRES 102 A 1542    C   U   G   C   A   A   C   U   C   G   A   C   U          
SEQRES 103 A 1542    C   C   A   U   G   A   A   G   U   C   G   G   A          
SEQRES 104 A 1542    A   U   C   G   C   U   A   G   U   A   A   U   C          
SEQRES 105 A 1542    G   U   G   G   A   U   C   A   G   A   A   U   G          
SEQRES 106 A 1542    C   C   A   C   G   G   U   G   A   A   U   A   C          
SEQRES 107 A 1542    G   U   U   C   C   C   G   G   G   C   C   U   U          
SEQRES 108 A 1542    G   U   A   C   A   C   A   C   C   G 4OC   C   C          
SEQRES 109 A 1542    G   U 5MC   A   C   A   C   C   A   U   G   G   G          
SEQRES 110 A 1542    A   G   U   G   G   G   U   U   G   C   A   A   A          
SEQRES 111 A 1542    A   G   A   A   G   U   A   G   G   U   A   G   C          
SEQRES 112 A 1542    U   U   A   A   C   C   U   U   C   G   G   G   A          
SEQRES 113 A 1542    G   G   G   C   G   C   U   U   A   C   C   A   C          
SEQRES 114 A 1542    U   U   U   G   U   G   A   U   U   C   A   U   G          
SEQRES 115 A 1542    A   C   U   G   G   G   G   U   G   A   A   G   U          
SEQRES 116 A 1542    C   G UR3   A   A   C   A   A   G   G   U   A   A          
SEQRES 117 A 1542    C   C   G   U   A   G   G 2MG   G MA6 MA6   C   C          
SEQRES 118 A 1542    U   G   C   G   G   U   U   G   G   A   U   C   A          
SEQRES 119 A 1542    C   C   U   C   C   U   U   A                              
SEQRES   1 B   76    G   C   C   C   G   G   A 4SU   A   G   C   U   C          
SEQRES   2 B   76    A   G H2U   C   G   G H2U   A   G   A   G   C   A          
SEQRES   3 B   76    G   G   G   G   A PSU   U   G   A   A MIA   A PSU          
SEQRES   4 B   76    C   C   C   C   G   U 7MG 3AU   C   C   U   U   G          
SEQRES   5 B   76    G 5MU PSU   C   G   A   U   U   C   C   G   A   G          
SEQRES   6 B   76    U   C   C   G   G   G   C   A   C   C   A                  
SEQRES   1 C  393  SER LYS GLU LYS PHE GLU ARG THR LYS PRO HIS VAL ASN          
SEQRES   2 C  393  VAL GLY THR ILE GLY HIS VAL ASP HIS GLY LYS THR THR          
SEQRES   3 C  393  LEU THR ALA ALA ILE THR THR VAL LEU ALA LYS THR TYR          
SEQRES   4 C  393  GLY GLY ALA ALA ARG ALA PHE ASP GLN ILE ASP ASN ALA          
SEQRES   5 C  393  PRO GLU GLU LYS ALA ARG GLY ILE THR ILE ASN THR SER          
SEQRES   6 C  393  HIS VAL GLU TYR ASP THR PRO THR ARG HIS TYR ALA HIS          
SEQRES   7 C  393  VAL ASP CYS PRO GLY HIS ALA ASP TYR VAL LYS ASN MET          
SEQRES   8 C  393  ILE THR GLY ALA ALA GLN MET ASP GLY ALA ILE LEU VAL          
SEQRES   9 C  393  VAL ALA ALA THR ASP GLY PRO MET PRO GLN THR ARG GLU          
SEQRES  10 C  393  HIS ILE LEU LEU GLY ARG GLN VAL GLY VAL PRO TYR ILE          
SEQRES  11 C  393  ILE VAL PHE LEU ASN LYS CYS ASP MET VAL ASP ASP GLU          
SEQRES  12 C  393  GLU LEU LEU GLU LEU VAL GLU MET GLU VAL ARG GLU LEU          
SEQRES  13 C  393  LEU SER GLN TYR ASP PHE PRO GLY ASP ASP THR PRO ILE          
SEQRES  14 C  393  VAL ARG GLY SER ALA LEU LYS ALA LEU GLU GLY ASP ALA          
SEQRES  15 C  393  GLU TRP GLU ALA LYS ILE LEU GLU LEU ALA GLY PHE LEU          
SEQRES  16 C  393  ASP SER TYR ILE PRO GLU PRO GLU ARG ALA ILE ASP LYS          
SEQRES  17 C  393  PRO PHE LEU LEU PRO ILE GLU ASP VAL PHE SER ILE SER          
SEQRES  18 C  393  GLY ARG GLY THR VAL VAL THR GLY ARG VAL GLU ARG GLY          
SEQRES  19 C  393  ILE ILE LYS VAL GLY GLU GLU VAL GLU ILE VAL GLY ILE          
SEQRES  20 C  393  LYS GLU THR GLN LYS SER THR CYS THR GLY VAL GLU MET          
SEQRES  21 C  393  PHE ARG LYS LEU LEU ASP GLU GLY ARG ALA GLY GLU ASN          
SEQRES  22 C  393  VAL GLY VAL LEU LEU ARG GLY ILE LYS ARG GLU GLU ILE          
SEQRES  23 C  393  GLU ARG GLY GLN VAL LEU ALA LYS PRO GLY THR ILE LYS          
SEQRES  24 C  393  PRO HIS THR LYS PHE GLU SER GLU VAL TYR ILE LEU SER          
SEQRES  25 C  393  LYS ASP GLU GLY GLY ARG HIS THR PRO PHE PHE LYS GLY          
SEQRES  26 C  393  TYR ARG PRO GLN PHE TYR PHE ARG THR THR ASP VAL THR          
SEQRES  27 C  393  GLY THR ILE GLU LEU PRO GLU GLY VAL GLU MET VAL MET          
SEQRES  28 C  393  PRO GLY ASP ASN ILE LYS MET VAL VAL THR LEU ILE HIS          
SEQRES  29 C  393  PRO ILE ALA MET ASP ASP GLY LEU ARG PHE ALA ILE ARG          
SEQRES  30 C  393  GLU GLY GLY ARG THR VAL GLY ALA GLY VAL VAL ALA LYS          
SEQRES  31 C  393  VAL LEU SER                                                  
SEQRES   1 D   24    A   U   U   A   U   G   U   U   U   U   U   U   U          
SEQRES   2 D   24    U   U   U   G   A   U   U   U   G   C   C                  
SEQRES   1 E   76    G   C   C   C   G   G   A 4SU   A   G   C   U   C          
SEQRES   2 E   76    A   G H2U   C   G   G H2U   A   G   A   G   C   A          
SEQRES   3 E   76    G   G   G   G   A PSU   U   G   A   A MIA   A PSU          
SEQRES   4 E   76    C   C   C   C   G   U 7MG 3AU   C   C   U   U   G          
SEQRES   5 E   76    G 5MU PSU   C   G   A   U   U   C   C   G   A   G          
SEQRES   6 E   76    U   C   C   G   G   G   C   A   C   C   A                  
SEQRES   1 F  241  MET ALA THR VAL SER MET ARG ASP MET LEU LYS ALA GLY          
SEQRES   2 F  241  VAL HIS PHE GLY HIS GLN THR ARG TYR TRP ASN PRO LYS          
SEQRES   3 F  241  MET LYS PRO PHE ILE PHE GLY ALA ARG ASN LYS VAL HIS          
SEQRES   4 F  241  ILE ILE ASN LEU GLU LYS THR VAL PRO MET PHE ASN GLU          
SEQRES   5 F  241  ALA LEU ALA GLU LEU ASN LYS ILE ALA SER ARG LYS GLY          
SEQRES   6 F  241  LYS ILE LEU PHE VAL GLY THR LYS ARG ALA ALA SER GLU          
SEQRES   7 F  241  ALA VAL LYS ASP ALA ALA LEU SER CYS ASP GLN PHE PHE          
SEQRES   8 F  241  VAL ASN HIS ARG TRP LEU GLY GLY MET LEU THR ASN TRP          
SEQRES   9 F  241  LYS THR VAL ARG GLN SER ILE LYS ARG LEU LYS ASP LEU          
SEQRES  10 F  241  GLU THR GLN SER GLN ASP GLY THR PHE ASP LYS LEU THR          
SEQRES  11 F  241  LYS LYS GLU ALA LEU MET ARG THR ARG GLU LEU GLU LYS          
SEQRES  12 F  241  LEU GLU ASN SER LEU GLY GLY ILE LYS ASP MET GLY GLY          
SEQRES  13 F  241  LEU PRO ASP ALA LEU PHE VAL ILE ASP ALA ASP HIS GLU          
SEQRES  14 F  241  HIS ILE ALA ILE LYS GLU ALA ASN ASN LEU GLY ILE PRO          
SEQRES  15 F  241  VAL PHE ALA ILE VAL ASP THR ASN SER ASP PRO ASP GLY          
SEQRES  16 F  241  VAL ASP PHE VAL ILE PRO GLY ASN ASP ASP ALA ILE ARG          
SEQRES  17 F  241  ALA VAL THR LEU TYR LEU GLY ALA VAL ALA ALA THR VAL          
SEQRES  18 F  241  ARG GLU GLY ARG SER GLN ASP LEU ALA SER GLN ALA GLU          
SEQRES  19 F  241  GLU SER PHE VAL GLU ALA GLU                                  
SEQRES   1 G  233  MET GLY GLN LYS VAL HIS PRO ASN GLY ILE ARG LEU GLY          
SEQRES   2 G  233  ILE VAL LYS PRO TRP ASN SER THR TRP PHE ALA ASN THR          
SEQRES   3 G  233  LYS GLU PHE ALA ASP ASN LEU ASP SER ASP PHE LYS VAL          
SEQRES   4 G  233  ARG GLN TYR LEU THR LYS GLU LEU ALA LYS ALA SER VAL          
SEQRES   5 G  233  SER ARG ILE VAL ILE GLU ARG PRO ALA LYS SER ILE ARG          
SEQRES   6 G  233  VAL THR ILE HIS THR ALA ARG PRO GLY ILE VAL ILE GLY          
SEQRES   7 G  233  LYS LYS GLY GLU ASP VAL GLU LYS LEU ARG LYS VAL VAL          
SEQRES   8 G  233  ALA ASP ILE ALA GLY VAL PRO ALA GLN ILE ASN ILE ALA          
SEQRES   9 G  233  GLU VAL ARG LYS PRO GLU LEU ASP ALA LYS LEU VAL ALA          
SEQRES  10 G  233  ASP SER ILE THR SER GLN LEU GLU ARG ARG VAL MET PHE          
SEQRES  11 G  233  ARG ARG ALA MET LYS ARG ALA VAL GLN ASN ALA MET ARG          
SEQRES  12 G  233  LEU GLY ALA LYS GLY ILE LYS VAL GLU VAL SER GLY ARG          
SEQRES  13 G  233  LEU GLY GLY ALA GLU ILE ALA ARG THR GLU TRP TYR ARG          
SEQRES  14 G  233  GLU GLY ARG VAL PRO LEU HIS THR LEU ARG ALA ASP ILE          
SEQRES  15 G  233  ASP TYR ASN THR SER GLU ALA HIS THR THR TYR GLY VAL          
SEQRES  16 G  233  ILE GLY VAL LYS VAL TRP ILE PHE LYS GLY GLU ILE LEU          
SEQRES  17 G  233  GLY GLY MET ALA ALA VAL GLU GLN PRO GLU LYS PRO ALA          
SEQRES  18 G  233  ALA GLN PRO LYS LYS GLN GLN ARG LYS GLY ARG LYS              
SEQRES   1 H  206  MET ALA ARG TYR LEU GLY PRO LYS LEU LYS LEU SER ARG          
SEQRES   2 H  206  ARG GLU GLY THR ASP LEU PHE LEU LYS SER GLY VAL ARG          
SEQRES   3 H  206  ALA ILE ASP THR LYS CYS LYS ILE GLU GLN ALA PRO GLY          
SEQRES   4 H  206  GLN HIS GLY ALA ARG LYS PRO ARG LEU SER ASP TYR GLY          
SEQRES   5 H  206  VAL GLN LEU ARG GLU LYS GLN LYS VAL ARG ARG ILE TYR          
SEQRES   6 H  206  GLY VAL LEU GLU ARG GLN PHE ARG ASN TYR TYR LYS GLU          
SEQRES   7 H  206  ALA ALA ARG LEU LYS GLY ASN THR GLY GLU ASN LEU LEU          
SEQRES   8 H  206  ALA LEU LEU GLU GLY ARG LEU ASP ASN VAL VAL TYR ARG          
SEQRES   9 H  206  MET GLY PHE GLY ALA THR ARG ALA GLU ALA ARG GLN LEU          
SEQRES  10 H  206  VAL SER HIS LYS ALA ILE MET VAL ASN GLY ARG VAL VAL          
SEQRES  11 H  206  ASN ILE ALA SER TYR GLN VAL SER PRO ASN ASP VAL VAL          
SEQRES  12 H  206  SER ILE ARG GLU LYS ALA LYS LYS GLN SER ARG VAL LYS          
SEQRES  13 H  206  ALA ALA LEU GLU LEU ALA GLU GLN ARG GLU LYS PRO THR          
SEQRES  14 H  206  TRP LEU GLU VAL ASP ALA GLY LYS MET GLU GLY THR PHE          
SEQRES  15 H  206  LYS ARG LYS PRO GLU ARG SER ASP LEU SER ALA ASP ILE          
SEQRES  16 H  206  ASN GLU HIS LEU ILE VAL GLU LEU TYR SER LYS                  
SEQRES   1 I  167  MET ALA HIS ILE GLU LYS GLN ALA GLY GLU LEU GLN GLU          
SEQRES   2 I  167  LYS LEU ILE ALA VAL ASN ARG VAL SER LYS THR VAL LYS          
SEQRES   3 I  167  GLY GLY ARG ILE PHE SER PHE THR ALA LEU THR VAL VAL          
SEQRES   4 I  167  GLY ASP GLY ASN GLY ARG VAL GLY PHE GLY TYR GLY LYS          
SEQRES   5 I  167  ALA ARG GLU VAL PRO ALA ALA ILE GLN LYS ALA MET GLU          
SEQRES   6 I  167  LYS ALA ARG ARG ASN MET ILE ASN VAL ALA LEU ASN ASN          
SEQRES   7 I  167  GLY THR LEU GLN HIS PRO VAL LYS GLY VAL HIS THR GLY          
SEQRES   8 I  167  SER ARG VAL PHE MET GLN PRO ALA SER GLU GLY THR GLY          
SEQRES   9 I  167  ILE ILE ALA GLY GLY ALA MET ARG ALA VAL LEU GLU VAL          
SEQRES  10 I  167  ALA GLY VAL HIS ASN VAL LEU ALA LYS ALA TYR GLY SER          
SEQRES  11 I  167  THR ASN PRO ILE ASN VAL VAL ARG ALA THR ILE ASP GLY          
SEQRES  12 I  167  LEU GLU ASN MET ASN SER PRO GLU MET VAL ALA ALA LYS          
SEQRES  13 I  167  ARG GLY LYS SER VAL GLU GLU ILE LEU GLY LYS                  
SEQRES   1 J  135  MET ARG HIS TYR GLU ILE VAL PHE MET VAL HIS PRO ASP          
SEQRES   2 J  135  GLN SER GLU GLN VAL PRO GLY MET ILE GLU ARG TYR THR          
SEQRES   3 J  135  ALA ALA ILE THR GLY ALA GLU GLY LYS ILE HIS ARG LEU          
SEQRES   4 J  135  GLU ASP TRP GLY ARG ARG GLN LEU ALA TYR PRO ILE ASN          
SEQRES   5 J  135  LYS LEU HIS LYS ALA HIS TYR VAL LEU MET ASN VAL GLU          
SEQRES   6 J  135  ALA PRO GLN GLU VAL ILE ASP GLU LEU GLU THR THR PHE          
SEQRES   7 J  135  ARG PHE ASN ASP ALA VAL ILE ARG SER MET VAL MET ARG          
SEQRES   8 J  135  THR LYS HIS ALA VAL THR GLU ALA SER PRO MET VAL LYS          
SEQRES   9 J  135  ALA LYS ASP GLU ARG ARG GLU ARG ARG ASP ASP PHE ALA          
SEQRES  10 J  135  ASN GLU THR ALA ASP ASP ALA GLU ALA GLY ASP SER GLU          
SEQRES  11 J  135  GLU GLU GLU GLU GLU                                          
SEQRES   1 K  179  MET PRO ARG ARG ARG VAL ILE GLY GLN ARG LYS ILE LEU          
SEQRES   2 K  179  PRO ASP PRO LYS PHE GLY SER GLU LEU LEU ALA LYS PHE          
SEQRES   3 K  179  VAL ASN ILE LEU MET VAL ASP GLY LYS LYS SER THR ALA          
SEQRES   4 K  179  GLU SER ILE VAL TYR SER ALA LEU GLU THR LEU ALA GLN          
SEQRES   5 K  179  ARG SER GLY LYS SER GLU LEU GLU ALA PHE GLU VAL ALA          
SEQRES   6 K  179  LEU GLU ASN VAL ARG PRO THR VAL GLU VAL LYS SER ARG          
SEQRES   7 K  179  ARG VAL GLY GLY SER THR TYR GLN VAL PRO VAL GLU VAL          
SEQRES   8 K  179  ARG PRO VAL ARG ARG ASN ALA LEU ALA MET ARG TRP ILE          
SEQRES   9 K  179  VAL GLU ALA ALA ARG LYS ARG GLY ASP LYS SER MET ALA          
SEQRES  10 K  179  LEU ARG LEU ALA ASN GLU LEU SER ASP ALA ALA GLU ASN          
SEQRES  11 K  179  LYS GLY THR ALA VAL LYS LYS ARG GLU ASP VAL HIS ARG          
SEQRES  12 K  179  MET ALA GLU ALA ASN LYS ALA PHE ALA HIS TYR ARG TRP          
SEQRES  13 K  179  LEU SER LEU ARG SER PHE SER HIS GLN ALA GLY ALA SER          
SEQRES  14 K  179  SER LYS GLN PRO ALA LEU GLY TYR LEU ASN                      
SEQRES   1 L  130  MET SER MET GLN ASP PRO ILE ALA ASP MET LEU THR ARG          
SEQRES   2 L  130  ILE ARG ASN GLY GLN ALA ALA ASN LYS ALA ALA VAL THR          
SEQRES   3 L  130  MET PRO SER SER LYS LEU LYS VAL ALA ILE ALA ASN VAL          
SEQRES   4 L  130  LEU LYS GLU GLU GLY PHE ILE GLU ASP PHE LYS VAL GLU          
SEQRES   5 L  130  GLY ASP THR LYS PRO GLU LEU GLU LEU THR LEU LYS TYR          
SEQRES   6 L  130  PHE GLN GLY LYS ALA VAL VAL GLU SER ILE GLN ARG VAL          
SEQRES   7 L  130  SER ARG PRO GLY LEU ARG ILE TYR LYS ARG LYS ASP GLU          
SEQRES   8 L  130  LEU PRO LYS VAL MET ALA GLY LEU GLY ILE ALA VAL VAL          
SEQRES   9 L  130  SER THR SER LYS GLY VAL MET THR ASP ARG ALA ALA ARG          
SEQRES  10 L  130  GLN ALA GLY LEU GLY GLY GLU ILE ILE CYS TYR VAL ALA          
SEQRES   1 M  130  MET ALA GLU ASN GLN TYR TYR GLY THR GLY ARG ARG LYS          
SEQRES   2 M  130  SER SER ALA ALA ARG VAL PHE ILE LYS PRO GLY ASN GLY          
SEQRES   3 M  130  LYS ILE VAL ILE ASN GLN ARG SER LEU GLU GLN TYR PHE          
SEQRES   4 M  130  GLY ARG GLU THR ALA ARG MET VAL VAL ARG GLN PRO LEU          
SEQRES   5 M  130  GLU LEU VAL ASP MET VAL GLU LYS LEU ASP LEU TYR ILE          
SEQRES   6 M  130  THR VAL LYS GLY GLY GLY ILE SER GLY GLN ALA GLY ALA          
SEQRES   7 M  130  ILE ARG HIS GLY ILE THR ARG ALA LEU MET GLU TYR ASP          
SEQRES   8 M  130  GLU SER LEU ARG SER GLU LEU ARG LYS ALA GLY PHE VAL          
SEQRES   9 M  130  THR ARG ASP ALA ARG GLN VAL GLU ARG LYS LYS VAL GLY          
SEQRES  10 M  130  LEU ARG LYS ALA ARG ARG ARG PRO GLN PHE SER LYS ARG          
SEQRES   1 N  103  MET GLN ASN GLN ARG ILE ARG ILE ARG LEU LYS ALA PHE          
SEQRES   2 N  103  ASP HIS ARG LEU ILE ASP GLN ALA THR ALA GLU ILE VAL          
SEQRES   3 N  103  GLU THR ALA LYS ARG THR GLY ALA GLN VAL ARG GLY PRO          
SEQRES   4 N  103  ILE PRO LEU PRO THR ARG LYS GLU ARG PHE THR VAL LEU          
SEQRES   5 N  103  ILE SER PRO HIS VAL ASN LYS ASP ALA ARG ASP GLN TYR          
SEQRES   6 N  103  GLU ILE ARG THR HIS LEU ARG LEU VAL ASP ILE VAL GLU          
SEQRES   7 N  103  PRO THR GLU LYS THR VAL ASP ALA LEU MET ARG LEU ASP          
SEQRES   8 N  103  LEU ALA ALA GLY VAL ASP VAL GLN ILE SER LEU GLY              
SEQRES   1 O  129  MET ALA LYS ALA PRO ILE ARG ALA ARG LYS ARG VAL ARG          
SEQRES   2 O  129  LYS GLN VAL SER ASP GLY VAL ALA HIS ILE HIS ALA SER          
SEQRES   3 O  129  PHE ASN ASN THR ILE VAL THR ILE THR ASP ARG GLN GLY          
SEQRES   4 O  129  ASN ALA LEU GLY TRP ALA THR ALA GLY GLY SER GLY PHE          
SEQRES   5 O  129  ARG GLY SER ARG LYS SER THR PRO PHE ALA ALA GLN VAL          
SEQRES   6 O  129  ALA ALA GLU ARG CYS ALA ASP ALA VAL LYS GLU TYR GLY          
SEQRES   7 O  129  ILE LYS ASN LEU GLU VAL MET VAL LYS GLY PRO GLY PRO          
SEQRES   8 O  129  GLY ARG GLU SER THR ILE ARG ALA LEU ASN ALA ALA GLY          
SEQRES   9 O  129  PHE ARG ILE THR ASN ILE THR ASP VAL THR PRO ILE PRO          
SEQRES  10 O  129  HIS ASN GLY CYS ARG PRO PRO LYS LYS ARG ARG VAL              
SEQRES   1 P  124  MET ALA THR VAL ASN GLN LEU VAL ARG LYS PRO ARG ALA          
SEQRES   2 P  124  ARG LYS VAL ALA LYS SER ASN VAL PRO ALA LEU GLU ALA          
SEQRES   3 P  124  CYS PRO GLN LYS ARG GLY VAL CYS THR ARG VAL TYR THR          
SEQRES   4 P  124  THR THR PRO LYS LYS PRO ASN SER ALA LEU ARG LYS VAL          
SEQRES   5 P  124  CYS ARG VAL ARG LEU THR ASN GLY PHE GLU VAL THR SER          
SEQRES   6 P  124  TYR ILE GLY GLY GLU GLY HIS ASN LEU GLN GLU HIS SER          
SEQRES   7 P  124  VAL ILE LEU ILE ARG GLY GLY ARG VAL LYS ASP LEU PRO          
SEQRES   8 P  124  GLY VAL ARG TYR HIS THR VAL ARG GLY ALA LEU ASP CYS          
SEQRES   9 P  124  SER GLY VAL LYS ASP ARG LYS GLN ALA ARG SER LYS TYR          
SEQRES  10 P  124  GLY VAL LYS ARG PRO LYS ALA                                  
SEQRES   1 Q  118  MET ALA ARG ILE ALA GLY ILE ASN ILE PRO ASP HIS LYS          
SEQRES   2 Q  118  HIS ALA VAL ILE ALA LEU THR SER ILE TYR GLY VAL GLY          
SEQRES   3 Q  118  LYS THR ARG SER LYS ALA ILE LEU ALA ALA ALA GLY ILE          
SEQRES   4 Q  118  ALA GLU ASP VAL LYS ILE SER GLU LEU SER GLU GLY GLN          
SEQRES   5 Q  118  ILE ASP THR LEU ARG ASP GLU VAL ALA LYS PHE VAL VAL          
SEQRES   6 Q  118  GLU GLY ASP LEU ARG ARG GLU ILE SER MET SER ILE LYS          
SEQRES   7 Q  118  ARG LEU MET ASP LEU GLY CYS TYR ARG GLY LEU ARG HIS          
SEQRES   8 Q  118  ARG ARG GLY LEU PRO VAL ARG GLY GLN ARG THR LYS THR          
SEQRES   9 Q  118  ASN ALA ARG THR ARG LYS GLY PRO ARG LYS PRO ILE LYS          
SEQRES  10 Q  118  LYS                                                          
SEQRES   1 R  101  MET ALA LYS GLN SER MET LYS ALA ARG GLU VAL LYS ARG          
SEQRES   2 R  101  VAL ALA LEU ALA ASP LYS TYR PHE ALA LYS ARG ALA GLU          
SEQRES   3 R  101  LEU LYS ALA ILE ILE SER ASP VAL ASN ALA SER ASP GLU          
SEQRES   4 R  101  ASP ARG TRP ASN ALA VAL LEU LYS LEU GLN THR LEU PRO          
SEQRES   5 R  101  ARG ASP SER SER PRO SER ARG GLN ARG ASN ARG CYS ARG          
SEQRES   6 R  101  GLN THR GLY ARG PRO HIS GLY PHE LEU ARG LYS PHE GLY          
SEQRES   7 R  101  LEU SER ARG ILE LYS VAL ARG GLU ALA ALA MET ARG GLY          
SEQRES   8 R  101  GLU ILE PRO GLY LEU LYS LYS ALA SER TRP                      
SEQRES   1 S   89  MET SER LEU SER THR GLU ALA THR ALA LYS ILE VAL SER          
SEQRES   2 S   89  GLU PHE GLY ARG ASP ALA ASN ASP THR GLY SER THR GLU          
SEQRES   3 S   89  VAL GLN VAL ALA LEU LEU THR ALA GLN ILE ASN HIS LEU          
SEQRES   4 S   89  GLN GLY HIS PHE ALA GLU HIS LYS LYS ASP HIS HIS SER          
SEQRES   5 S   89  ARG ARG GLY LEU LEU ARG MET VAL SER GLN ARG ARG LYS          
SEQRES   6 S   89  LEU LEU ASP TYR LEU LYS ARG LYS ASP VAL ALA ARG TYR          
SEQRES   7 S   89  THR ARG LEU ILE GLU ARG LEU GLY LEU ARG ARG                  
SEQRES   1 T   82  MET VAL THR ILE ARG LEU ALA ARG HIS GLY ALA LYS LYS          
SEQRES   2 T   82  ARG PRO PHE TYR GLN VAL VAL VAL ALA ASP SER ARG ASN          
SEQRES   3 T   82  ALA ARG ASN GLY ARG PHE ILE GLU ARG VAL GLY PHE PHE          
SEQRES   4 T   82  ASN PRO ILE ALA SER GLU LYS GLU GLU GLY THR ARG LEU          
SEQRES   5 T   82  ASP LEU ASP ARG ILE ALA HIS TRP VAL GLY GLN GLY ALA          
SEQRES   6 T   82  THR ILE SER ASP ARG VAL ALA ALA LEU ILE LYS GLU VAL          
SEQRES   7 T   82  ASN LYS ALA ALA                                              
SEQRES   1 U   84  MET THR ASP LYS ILE ARG THR LEU GLN GLY ARG VAL VAL          
SEQRES   2 U   84  SER ASP LYS MET GLU LYS SER ILE VAL VAL ALA ILE GLU          
SEQRES   3 U   84  ARG PHE VAL LYS HIS PRO ILE TYR GLY LYS PHE ILE LYS          
SEQRES   4 U   84  ARG THR THR LYS LEU HIS VAL HIS ASP GLU ASN ASN GLU          
SEQRES   5 U   84  CYS GLY ILE GLY ASP VAL VAL GLU ILE ARG GLU CYS ARG          
SEQRES   6 U   84  PRO LEU SER LYS THR LYS SER TRP THR LEU VAL ARG VAL          
SEQRES   7 U   84  VAL GLU LYS ALA VAL LEU                                      
SEQRES   1 V   75  MET ALA ARG TYR PHE ARG ARG ARG LYS PHE CYS ARG PHE          
SEQRES   2 V   75  THR ALA GLU GLY VAL GLN GLU ILE ASP TYR LYS ASP ILE          
SEQRES   3 V   75  ALA THR LEU LYS ASN TYR ILE THR GLU SER GLY LYS ILE          
SEQRES   4 V   75  VAL PRO SER ARG ILE THR GLY THR ARG ALA LYS TYR GLN          
SEQRES   5 V   75  ARG GLN LEU ALA ARG ALA ILE LYS ARG ALA ARG TYR LEU          
SEQRES   6 V   75  SER LEU LEU PRO TYR THR ASP ARG HIS GLN                      
SEQRES   1 W   92  MET PRO ARG SER LEU LYS LYS GLY PRO PHE ILE ASP LEU          
SEQRES   2 W   92  HIS LEU LEU LYS LYS VAL GLU LYS ALA VAL GLU SER GLY          
SEQRES   3 W   92  ASP LYS LYS PRO LEU ARG THR TRP SER ARG ARG SER THR          
SEQRES   4 W   92  ILE PHE PRO ASN MET ILE GLY LEU THR ILE ALA VAL HIS          
SEQRES   5 W   92  ASN GLY ARG GLN HIS VAL PRO VAL PHE VAL THR ASP GLU          
SEQRES   6 W   92  MET VAL GLY HIS LYS LEU GLY GLU PHE ALA PRO THR ARG          
SEQRES   7 W   92  THR TYR ARG GLY HIS ALA ALA ASP LYS LYS ALA LYS LYS          
SEQRES   8 W   92  LYS                                                          
SEQRES   1 X   87  MET ALA ASN ILE LYS SER ALA LYS LYS ARG ALA ILE GLN          
SEQRES   2 X   87  SER GLU LYS ALA ARG LYS HIS ASN ALA SER ARG ARG SER          
SEQRES   3 X   87  MET MET ARG THR PHE ILE LYS LYS VAL TYR ALA ALA ILE          
SEQRES   4 X   87  GLU ALA GLY ASP LYS ALA ALA ALA GLN LYS ALA PHE ASN          
SEQRES   5 X   87  GLU MET GLN PRO ILE VAL ASP ARG GLN ALA ALA LYS GLY          
SEQRES   6 X   87  LEU ILE HIS LYS ASN LYS ALA ALA ARG HIS LYS ALA ASN          
SEQRES   7 X   87  LEU THR ALA GLN ILE ASN LYS LEU ALA                          
SEQRES   1 Y   71  MET PRO VAL ILE LYS VAL ARG GLU ASN GLU PRO PHE ASP          
SEQRES   2 Y   71  VAL ALA LEU ARG ARG PHE LYS ARG SER CYS GLU LYS ALA          
SEQRES   3 Y   71  GLY VAL LEU ALA GLU VAL ARG ARG ARG GLU PHE TYR GLU          
SEQRES   4 Y   71  LYS PRO THR THR GLU ARG LYS ARG ALA LYS ALA SER ALA          
SEQRES   5 Y   71  VAL LYS ARG HIS ALA LYS LYS LEU ALA ARG GLU ASN ALA          
SEQRES   6 Y   71  ARG ARG THR ARG LEU TYR                                      
MODRES 3IZW PSU A  516    U  PSEUDOURIDINE-5'-MONOPHOSPHATE                     
MODRES 3IZW 7MG A  527    G                                                     
MODRES 3IZW 2MG A  966    G  2N-METHYLGUANOSINE-5'-MONOPHOSPHATE                
MODRES 3IZW 5MC A  967    C  5-METHYLCYTIDINE-5'-MONOPHOSPHATE                  
MODRES 3IZW 2MG A 1207    G  2N-METHYLGUANOSINE-5'-MONOPHOSPHATE                
MODRES 3IZW 4OC A 1402    C  4N,O2'-METHYLCYTIDINE-5'-MONOPHOSPHATE             
MODRES 3IZW 5MC A 1407    C  5-METHYLCYTIDINE-5'-MONOPHOSPHATE                  
MODRES 3IZW UR3 A 1498    U  3-METHYLURIDINE-5'-MONOPHOSHATE                    
MODRES 3IZW 2MG A 1516    G  2N-METHYLGUANOSINE-5'-MONOPHOSPHATE                
MODRES 3IZW MA6 A 1518    A  6N-DIMETHYLADENOSINE-5'-MONOPHOSHATE               
MODRES 3IZW MA6 A 1519    A  6N-DIMETHYLADENOSINE-5'-MONOPHOSHATE               
MODRES 3IZW 4SU B    8    U  4-THIOURIDINE-5'-MONOPHOSPHATE                     
MODRES 3IZW H2U B   16    U  5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE                
MODRES 3IZW H2U B   20    U  5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE                
MODRES 3IZW PSU B   32    U  PSEUDOURIDINE-5'-MONOPHOSPHATE                     
MODRES 3IZW MIA B   37    A                                                     
MODRES 3IZW PSU B   39    U  PSEUDOURIDINE-5'-MONOPHOSPHATE                     
MODRES 3IZW 7MG B   46    G                                                     
MODRES 3IZW 3AU B   47    U                                                     
MODRES 3IZW 5MU B   54    U  5-METHYLURIDINE 5'-MONOPHOSPHATE                   
MODRES 3IZW PSU B   55    U  PSEUDOURIDINE-5'-MONOPHOSPHATE                     
MODRES 3IZW 4SU E    8    U  4-THIOURIDINE-5'-MONOPHOSPHATE                     
MODRES 3IZW H2U E   16    U  5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE                
MODRES 3IZW H2U E   20    U  5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE                
MODRES 3IZW PSU E   32    U  PSEUDOURIDINE-5'-MONOPHOSPHATE                     
MODRES 3IZW MIA E   37    A                                                     
MODRES 3IZW PSU E   39    U  PSEUDOURIDINE-5'-MONOPHOSPHATE                     
MODRES 3IZW 7MG E   46    G                                                     
MODRES 3IZW 3AU E   47    U                                                     
MODRES 3IZW 5MU E   54    U  5-METHYLURIDINE 5'-MONOPHOSPHATE                   
MODRES 3IZW PSU E   55    U  PSEUDOURIDINE-5'-MONOPHOSPHATE                     
HET    PSU  A 516      20                                                       
HET    7MG  A 527      24                                                       
HET    2MG  A 966      24                                                       
HET    5MC  A 967      21                                                       
HET    2MG  A1207      24                                                       
HET    4OC  A1402      22                                                       
HET    5MC  A1407      21                                                       
HET    UR3  A1498      21                                                       
HET    2MG  A1516      24                                                       
HET    MA6  A1518      24                                                       
HET    MA6  A1519      24                                                       
HET    4SU  B   8      20                                                       
HET    H2U  B  16      20                                                       
HET    H2U  B  20      20                                                       
HET    PSU  B  32      20                                                       
HET    MIA  B  37      29                                                       
HET    PSU  B  39      20                                                       
HET    7MG  B  46      24                                                       
HET    3AU  B  47      27                                                       
HET    5MU  B  54      21                                                       
HET    PSU  B  55      20                                                       
HET    4SU  E   8      20                                                       
HET    H2U  E  16      20                                                       
HET    H2U  E  20      20                                                       
HET    PSU  E  32      20                                                       
HET    MIA  E  37      29                                                       
HET    PSU  E  39      20                                                       
HET    7MG  E  46      24                                                       
HET    3AU  E  47      27                                                       
HET    5MU  E  54      21                                                       
HET    PSU  E  55      20                                                       
HETNAM     PSU PSEUDOURIDINE-5'-MONOPHOSPHATE                                   
HETNAM     7MG 7N-METHYL-8-HYDROGUANOSINE-5'-MONOPHOSPHATE                      
HETNAM     2MG 2N-METHYLGUANOSINE-5'-MONOPHOSPHATE                              
HETNAM     5MC 5-METHYLCYTIDINE-5'-MONOPHOSPHATE                                
HETNAM     4OC 4N,O2'-METHYLCYTIDINE-5'-MONOPHOSPHATE                           
HETNAM     UR3 3-METHYLURIDINE-5'-MONOPHOSHATE                                  
HETNAM     MA6 6N-DIMETHYLADENOSINE-5'-MONOPHOSHATE                             
HETNAM     4SU 4-THIOURIDINE-5'-MONOPHOSPHATE                                   
HETNAM     H2U 5,6-DIHYDROURIDINE-5'-MONOPHOSPHATE                              
HETNAM     MIA 2-METHYLTHIO-N6-ISOPENTENYL-ADENOSINE-5'-MONOPHOSPHATE           
HETNAM     3AU 3-[(3S)-3-AMINO-3-CARBOXYPROPYL]URIDINE 5'-(DIHYDROGEN           
HETNAM   2 3AU  PHOSPHATE)                                                      
HETNAM     5MU 5-METHYLURIDINE 5'-MONOPHOSPHATE                                 
HETSYN     3AU NONE                                                             
FORMUL   1  PSU    7(C9 H13 N2 O9 P)                                            
FORMUL   1  7MG    3(C11 H18 N5 O8 P)                                           
FORMUL   1  2MG    3(C11 H16 N5 O8 P)                                           
FORMUL   1  5MC    2(C10 H16 N3 O8 P)                                           
FORMUL   1  4OC    C11 H18 N3 O8 P                                              
FORMUL   1  UR3    C10 H15 N2 O9 P                                              
FORMUL   1  MA6    2(C12 H18 N5 O7 P)                                           
FORMUL   2  4SU    2(C9 H13 N2 O8 P S)                                          
FORMUL   2  H2U    4(C9 H15 N2 O9 P)                                            
FORMUL   2  MIA    2(C16 H26 N5 O7 P S)                                         
FORMUL   2  3AU    2(C13 H20 N3 O11 P)                                          
FORMUL   2  5MU    2(C10 H15 N2 O9 P)                                           
HELIX    1   1 THR C   25  TYR C   39  1                                  15    
HELIX    2   2 ALA C   45  ASP C   50  1                                   6    
HELIX    3   3 ALA C   52  ALA C   57  1                                   6    
HELIX    4   4 VAL C   88  MET C   98  1                                  11    
HELIX    5   5 MET C  112  ILE C  119  1                                   8    
HELIX    6   6 LEU C  120  VAL C  125  1                                   6    
HELIX    7   7 LYS C  136  VAL C  140  5                                   5    
HELIX    8   8 ASP C  142  TYR C  160  1                                  19    
HELIX    9   9 SER C  173  GLY C  180  1                                   8    
HELIX   10  10 TRP C  184  ILE C  188  5                                   5    
HELIX   11  11 LEU C  189  ILE C  199  1                                  11    
HELIX   12  12 SER C  312  GLY C  316  5                                   5    
HELIX   13  13 ALA F    1  GLY F   12  5                                  12    
HELIX   14  14 ASN F   23  LYS F   27  5                                   5    
HELIX   15  15 ASN F   41  LYS F   44  5                                   4    
HELIX   16  16 THR F   45  LEU F   56  1                                  12    
HELIX   17  17 ASN F   57  ALA F   60  5                                   4    
HELIX   18  18 GLU F   77  ALA F   82  1                                   6    
HELIX   19  19 ASN F  102  GLN F  119  1                                  18    
HELIX   20  20 ASP F  122  LYS F  127  5                                   6    
HELIX   21  21 LYS F  131  LEU F  147  1                                  17    
HELIX   22  22 GLY F  148  LYS F  151  5                                   4    
HELIX   23  23 GLU F  168  GLY F  179  1                                  12    
HELIX   24  24 ILE F  206  ALA F  232  1                                  27    
HELIX   25  25 SER F  235  ALA F  239  5                                   5    
HELIX   26  26 GLU G   27  ALA G   47  1                                  21    
HELIX   27  27 GLY G   77  GLU G   81  5                                   5    
HELIX   28  28 VAL G   83  ALA G   94  1                                  12    
HELIX   29  29 ASP G  111  ARG G  125  1                                  15    
HELIX   30  30 PHE G  129  LEU G  143  1                                  15    
HELIX   31  31 THR G  176  ALA G  179  5                                   4    
HELIX   32  32 LYS H    7  GLU H   14  1                                   8    
HELIX   33  33 ARG H   25  THR H   29  5                                   5    
HELIX   34  34 SER H   48  TYR H   64  1                                  17    
HELIX   35  35 LEU H   67  LEU H   81  1                                  15    
HELIX   36  36 ASN H   84  ARG H   96  1                                  13    
HELIX   37  37 ARG H   96  MET H  104  1                                   9    
HELIX   38  38 THR H  109  HIS H  119  1                                  11    
HELIX   39  39 GLN H  151  LEU H  158  1                                   8    
HELIX   40  40 HIS H  197  LEU H  202  1                                   6    
HELIX   41  41 TYR H  203  LYS H  205  5                                   3    
HELIX   42  42 GLU I    4  GLY I    8  5                                   5    
HELIX   43  43 GLU I   54  ARG I   67  1                                  14    
HELIX   44  44 GLY I  107  VAL I  116  1                                  10    
HELIX   45  45 ASN I  131  VAL I  136  1                                   6    
HELIX   46  46 SER I  148  ALA I  153  1                                   6    
HELIX   47  47 PRO J   12  SER J   15  5                                   4    
HELIX   48  48 VAL J   18  GLY J   31  1                                  14    
HELIX   49  49 PRO J   67  ASN J   81  1                                  15    
HELIX   50  50 MET J  102  ARG J  113  1                                  12    
HELIX   51  51 GLU J  119  ALA J  124  1                                   6    
HELIX   52  52 SER K   19  MET K   30  1                                  12    
HELIX   53  53 LYS K   34  ALA K   50  1                                  17    
HELIX   54  54 SER K   56  ARG K   69  1                                  14    
HELIX   55  55 ARG K   91  VAL K  104  1                                  14    
HELIX   56  56 SER K  114  GLU K  128  1                                  15    
HELIX   57  57 GLY K  131  HIS K  141  1                                  11    
HELIX   58  58 SER K  160  ALA K  165  5                                   6    
HELIX   59  59 ASP L    8  ALA L   19  1                                  12    
HELIX   60  60 SER L   29  GLU L   42  1                                  14    
HELIX   61  61 ASP L  112  ALA L  118  1                                   7    
HELIX   62  62 LEU M   34  PHE M   38  1                                   5    
HELIX   63  63 THR M   42  VAL M   47  1                                   6    
HELIX   64  64 ARG M   48  VAL M   54  1                                   7    
HELIX   65  65 GLY M   70  ASP M   90  1                                  21    
HELIX   66  66 LEU M   93  GLY M  101  1                                   9    
HELIX   67  67 ARG N   16  ALA N   21  1                                   6    
HELIX   68  68 THR N   22  GLU N   27  1                                   6    
HELIX   69  69 THR N   28  THR N   32  5                                   5    
HELIX   70  70 LYS N   82  LEU N   87  1                                   6    
HELIX   71  71 THR O   58  LYS O   74  1                                  17    
HELIX   72  72 GLU O   93  ALA O  101  1                                   9    
HELIX   73  73 THR P    2  VAL P    7  1                                   6    
HELIX   74  74 HIS Q   13  ILE Q   21  5                                   9    
HELIX   75  75 THR Q   27  ALA Q   36  1                                  10    
HELIX   76  76 LYS Q   43  LEU Q   47  5                                   5    
HELIX   77  77 SER Q   48  VAL Q   59  1                                  12    
HELIX   78  78 GLU Q   65  GLY Q   83  1                                  19    
HELIX   79  79 CYS Q   84  ARG Q   92  1                                   9    
HELIX   80  80 ALA Q  105  GLY Q  110  1                                   6    
HELIX   81  81 LYS R    2  TYR R   19  1                                  18    
HELIX   82  82 VAL R   44  GLN R   48  5                                   5    
HELIX   83  83 ARG R   80  ARG R   89  1                                  10    
HELIX   84  84 SER S    3  PHE S   14  1                                  12    
HELIX   85  85 SER S   23  ALA S   43  1                                  21    
HELIX   86  86 ASP S   48  ASP S   73  1                                  26    
HELIX   87  87 ASP S   73  GLY S   85  1                                  13    
HELIX   88  88 ASP T   53  GLN T   63  1                                  11    
HELIX   89  89 SER T   68  ILE T   75  1                                   8    
HELIX   90  90 ASP V   24  LYS V   29  1                                   6    
HELIX   91  91 ASN V   30  ILE V   32  5                                   3    
HELIX   92  92 PRO V   40  GLY V   45  1                                   6    
HELIX   93  93 ARG V   47  LEU V   64  1                                  18    
HELIX   94  94 LEU W   14  LYS W   20  1                                   7    
HELIX   95  95 PHE W   40  ILE W   44  5                                   5    
HELIX   96  96 LYS W   69  ALA W   74  5                                   6    
HELIX   97  97 LYS X    8  SER X   25  1                                  18    
HELIX   98  98 SER X   25  PHE X   30  1                                   6    
HELIX   99  99 ILE X   31  ALA X   40  1                                  10    
HELIX  100 100 ASP X   42  ASP X   58  1                                  17    
HELIX  101 101 ASP X   58  LYS X   63  1                                   6    
HELIX  102 102 LYS X   70  ASN X   83  1                                  14    
HELIX  103 103 ALA Y   25  GLU Y   30  5                                   6    
HELIX  104 104 GLU Y   38  ALA Y   51  1                                  14    
HELIX  105 105 ALA Y   51  THR Y   67  1                                  17    
SHEET    1   A 6 LYS C   4  PHE C   5  0                                        
SHEET    2   A 6 LYS C 263  LEU C 265  1  O  LEU C 264   N  PHE C   5           
SHEET    3   A 6 GLN C 251  MET C 260 -1  N  MET C 260   O  LYS C 263           
SHEET    4   A 6 GLU C 241  GLY C 246 -1  N  VAL C 242   O  SER C 253           
SHEET    5   A 6 GLN C 290  ALA C 293 -1  O  ALA C 293   N  GLU C 243           
SHEET    6   A 6 LEU C 211  PRO C 213 -1  N  LEU C 212   O  LEU C 292           
SHEET    1   B 6 LYS C   4  PHE C   5  0                                        
SHEET    2   B 6 LYS C 263  LEU C 265  1  O  LEU C 264   N  PHE C   5           
SHEET    3   B 6 GLN C 251  MET C 260 -1  N  MET C 260   O  LYS C 263           
SHEET    4   B 6 ASN C 273  LEU C 278 -1  O  GLY C 275   N  GLU C 259           
SHEET    5   B 6 GLY C 224  ARG C 230 -1  N  VAL C 227   O  VAL C 276           
SHEET    6   B 6 ASP C 216  ILE C 220 -1  N  ASP C 216   O  THR C 228           
SHEET    1   C 6 VAL C  67  ASP C  70  0                                        
SHEET    2   C 6 HIS C  75  VAL C  79 -1  O  TYR C  76   N  TYR C  69           
SHEET    3   C 6 HIS C  11  ILE C  17  1  N  VAL C  14   O  ALA C  77           
SHEET    4   C 6 ALA C 101  ALA C 106  1  O  VAL C 104   N  ILE C  17           
SHEET    5   C 6 ILE C 130  ASN C 135  1  O  ASN C 135   N  VAL C 105           
SHEET    6   C 6 ILE C 169  ARG C 171  1  O  VAL C 170   N  LEU C 134           
SHEET    1   D 2 ILE C 235  ILE C 236  0                                        
SHEET    2   D 2 GLY C 268  ARG C 269 -1  O  GLY C 268   N  ILE C 236           
SHEET    1   E 7 PRO C 300  ILE C 310  0                                        
SHEET    2   E 7 ASN C 355  ALA C 367 -1  O  LEU C 362   N  THR C 302           
SHEET    3   E 7 THR C 335  GLU C 342 -1  N  THR C 340   O  THR C 361           
SHEET    4   E 7 GLN C 329  PHE C 332 -1  N  PHE C 332   O  THR C 335           
SHEET    5   E 7 ARG C 373  ARG C 377 -1  O  ARG C 377   N  GLN C 329           
SHEET    6   E 7 THR C 382  LEU C 392 -1  O  GLY C 384   N  ILE C 376           
SHEET    7   E 7 PRO C 300  ILE C 310 -1  N  TYR C 309   O  ALA C 385           
SHEET    1   F 2 PHE C 322  PHE C 323  0                                        
SHEET    2   F 2 MET C 349  VAL C 350 -1  O  VAL C 350   N  PHE C 322           
SHEET    1   G 2 GLY F  32  ARG F  34  0                                        
SHEET    2   G 2 VAL F  37  ILE F  39 -1  O  VAL F  37   N  ARG F  34           
SHEET    1   H 5 GLN F  88  VAL F  91  0                                        
SHEET    2   H 5 ILE F  66  VAL F  69  1  N  PHE F  68   O  PHE F  89           
SHEET    3   H 5 ALA F 159  VAL F 162  1  O  PHE F 161   N  LEU F  67           
SHEET    4   H 5 VAL F 182  ILE F 185  1  O  PHE F 183   N  LEU F 160           
SHEET    5   H 5 PHE F 197  ILE F 199  1  O  PHE F 197   N  VAL F 182           
SHEET    1   I 4 SER G  19  THR G  20  0                                        
SHEET    2   I 4 ILE G  54  GLU G  57  1  O  ILE G  56   N  THR G  20           
SHEET    3   I 4 ILE G  63  ILE G  67 -1  O  ARG G  64   N  GLU G  57           
SHEET    4   I 4 ALA G  98  ILE G 102  1  O  GLN G  99   N  ILE G  63           
SHEET    1   J 4 GLU G 165  GLY G 170  0                                        
SHEET    2   J 4 GLY G 147  VAL G 152 -1  N  VAL G 150   O  TYR G 167           
SHEET    3   J 4 GLY G 193  PHE G 202 -1  O  TRP G 200   N  LYS G 149           
SHEET    4   J 4 ILE G 181  THR G 190 -1  N  SER G 186   O  VAL G 197           
SHEET    1   K 4 ARG H 127  VAL H 129  0                                        
SHEET    2   K 4 ILE H 122  VAL H 124 -1  N  ILE H 122   O  VAL H 129           
SHEET    3   K 4 ASP H 140  ILE H 144 -1  O  SER H 143   N  MET H 123           
SHEET    4   K 4 GLU H 178  PHE H 181 -1  O  GLY H 179   N  VAL H 142           
SHEET    1   L 4 GLN I  11  VAL I  20  0                                        
SHEET    2   L 4 SER I  31  GLY I  39 -1  O  GLY I  39   N  GLN I  11           
SHEET    3   L 4 ARG I  44  ALA I  52 -1  O  GLY I  50   N  ALA I  34           
SHEET    4   L 4 ILE I  71  ASN I  72 -1  O  ILE I  71   N  VAL I  45           
SHEET    1   M 2 LEU I  75  ASN I  76  0                                        
SHEET    2   M 2 THR I  79  LEU I  80 -1  O  THR I  79   N  ASN I  76           
SHEET    1   N 2 GLN I  96  PRO I  97  0                                        
SHEET    2   N 2 VAL I 122  LEU I 123 -1  O  LEU I 123   N  GLN I  96           
SHEET    1   O 4 LYS J  35  ILE J  51  0                                        
SHEET    2   O 4 LEU J  54  ALA J  66 -1  O  ALA J  57   N  ARG J  45           
SHEET    3   O 4 ARG J   2  VAL J  10 -1  N  VAL J  10   O  HIS J  58           
SHEET    4   O 4 VAL J  84  ARG J  91 -1  O  MET J  88   N  VAL J   7           
SHEET    1   P 2 VAL K  72  LYS K  75  0                                        
SHEET    2   P 2 VAL K  86  GLU K  89 -1  O  VAL K  88   N  GLU K  73           
SHEET    1   Q 3 ALA L  23  PRO L  27  0                                        
SHEET    2   Q 3 GLU L  57  THR L  61 -1  O  LEU L  58   N  MET L  26           
SHEET    3   Q 3 ASP L  47  GLU L  51 -1  N  GLU L  51   O  GLU L  57           
SHEET    1   R 3 GLN L  75  ARG L  76  0                                        
SHEET    2   R 3 GLY L 122  TYR L 127 -1  O  TYR L 127   N  GLN L  75           
SHEET    3   R 3 TYR L  85  LYS L  86 -1  N  LYS L  86   O  GLY L 122           
SHEET    1   S 4 GLN L  75  ARG L  76  0                                        
SHEET    2   S 4 GLY L 122  TYR L 127 -1  O  TYR L 127   N  GLN L  75           
SHEET    3   S 4 ALA L 101  THR L 105 -1  N  SER L 104   O  GLU L 123           
SHEET    4   S 4 GLY L 108  THR L 111 -1  O  MET L 110   N  VAL L 103           
SHEET    1   T 3 TYR M   5  TYR M   6  0                                        
SHEET    2   T 3 SER M  14  PRO M  22 -1  O  ILE M  20   N  TYR M   5           
SHEET    3   T 3 GLY M   9  ARG M  11 -1  N  GLY M   9   O  ALA M  16           
SHEET    1   U 5 TYR M   5  TYR M   6  0                                        
SHEET    2   U 5 SER M  14  PRO M  22 -1  O  ILE M  20   N  TYR M   5           
SHEET    3   U 5 LEU M  60  LYS M  67 -1  O  TYR M  63   N  PHE M  19           
SHEET    4   U 5 ILE M  27  ILE M  29  1  N  VAL M  28   O  ILE M  64           
SHEET    5   U 5 ARG M  32  SER M  33 -1  O  ARG M  32   N  ILE M  29           
SHEET    1   V 4 ARG N  45  VAL N  51  0                                        
SHEET    2   V 4 ASP N  63  ARG N  72 -1  O  ASP N  63   N  VAL N  51           
SHEET    3   V 4 ARG N   7  ALA N  12 -1  N  LEU N  10   O  ARG N  72           
SHEET    4   V 4 VAL N  96  SER N 101 -1  O  SER N 101   N  ARG N   7           
SHEET    1   W 3 ARG N  45  VAL N  51  0                                        
SHEET    2   W 3 ASP N  63  ARG N  72 -1  O  ASP N  63   N  VAL N  51           
SHEET    3   W 3 LYS R  96  LYS R  97 -1  O  LYS R  96   N  GLU N  66           
SHEET    1   X 5 ALA O  40  THR O  45  0                                        
SHEET    2   X 5 THR O  29  THR O  34 -1  N  VAL O  31   O  ALA O  44           
SHEET    3   X 5 SER O  16  ALA O  24 -1  N  HIS O  21   O  THR O  32           
SHEET    4   X 5 ILE O  78  LYS O  86  1  O  ASN O  80   N  SER O  16           
SHEET    5   X 5 ILE O 109  ASP O 111  1  O  THR O 110   N  VAL O  83           
SHEET    1   Y 6 GLN P  28  THR P  39  0                                        
SHEET    2   Y 6 ARG P  49  LEU P  56 -1  O  ARG P  55   N  VAL P  32           
SHEET    3   Y 6 GLU P  61  TYR P  65 -1  O  VAL P  62   N  VAL P  54           
SHEET    4   Y 6 TYR P  94  THR P  96  1  O  THR P  96   N  TYR P  65           
SHEET    5   Y 6 VAL P  78  GLY P  83 -1  N  ARG P  82   O  HIS P  95           
SHEET    6   Y 6 GLN P  28  THR P  39 -1  N  GLY P  31   O  ILE P  79           
SHEET    1   Z 2 PHE R  72  LEU R  73  0                                        
SHEET    2   Z 2 LEU R  78  SER R  79 -1  O  LEU R  78   N  LEU R  73           
SHEET    1  AA 5 ARG T  51  LEU T  52  0                                        
SHEET    2  AA 5 GLU T  34  PHE T  39 -1  N  PHE T  38   O  ARG T  51           
SHEET    3  AA 5 ARG T  14  ALA T  22 -1  N  TYR T  17   O  PHE T  39           
SHEET    4  AA 5 THR T   3  ALA T  11 -1  N  HIS T   9   O  PHE T  16           
SHEET    5  AA 5 THR T  66  ILE T  67  1  O  THR T  66   N  ILE T   4           
SHEET    1  AB 6 THR U   6  SER U  13  0                                        
SHEET    2  AB 6 SER U  19  LYS U  29 -1  O  ALA U  23   N  ARG U  10           
SHEET    3  AB 6 PHE U  36  HIS U  46 -1  O  ILE U  37   N  VAL U  28           
SHEET    4  AB 6 LYS U  70  GLU U  79  1  O  TRP U  72   N  HIS U  46           
SHEET    5  AB 6 VAL U  57  SER U  67 -1  N  GLU U  59   O  VAL U  75           
SHEET    6  AB 6 THR U   6  SER U  13 -1  N  LEU U   7   O  ILE U  60           
SHEET    1  AC 3 LEU W  30  THR W  32  0                                        
SHEET    2  AC 3 THR W  47  HIS W  51  1  O  ALA W  49   N  THR W  32           
SHEET    3  AC 3 HIS W  56  PHE W  60 -1  O  VAL W  57   N  VAL W  50           
LINK         O3'   G A 515                 P   PSU A 516     1555   1555  1.62  
LINK         O3' PSU A 516                 P     G A 517     1555   1555  1.61  
LINK         O3'   C A 526                 P   7MG A 527     1555   1555  1.60  
LINK         O3' 7MG A 527                 P     C A 528     1555   1555  1.62  
LINK         O3'   U A 965                 P   2MG A 966     1555   1555  1.61  
LINK         O3' 2MG A 966                 P   5MC A 967     1555   1555  1.62  
LINK         O3' 5MC A 967                 P     A A 968     1555   1555  1.61  
LINK         O3'   G A1206                 P   2MG A1207     1555   1555  1.61  
LINK         O3' 2MG A1207                 P     C A1208     1555   1555  1.60  
LINK         O3'   U A1406                 P   5MC A1407     1555   1555  1.62  
LINK         O3' 5MC A1407                 P     A A1408     1555   1555  1.60  
LINK         O3'   G A1515                 P   2MG A1516     1555   1555  1.62  
LINK         O3' 2MG A1516                 P     G A1517     1555   1555  1.61  
LINK         O3'   G A1517                 P   MA6 A1518     1555   1555  1.61  
LINK         O3' MA6 A1518                 P   MA6 A1519     1555   1555  1.61  
LINK         O3' MA6 A1519                 P     C A1520     1555   1555  1.62  
LINK         O3'   A B   7                 P   4SU B   8     1555   1555  1.60  
LINK         O3' 4SU B   8                 P     A B   9     1555   1555  1.61  
LINK         O3'   G B  15                 P   H2U B  16     1555   1555  1.61  
LINK         O3' H2U B  16                 P     C B  17     1555   1555  1.62  
LINK         O3'   G B  19                 P   H2U B  20     1555   1555  1.62  
LINK         O3' H2U B  20                 P     A B  21     1555   1555  1.62  
LINK         O3'   A B  31                 P   PSU B  32     1555   1555  1.61  
LINK         O3' PSU B  32                 P     U B  33     1555   1555  1.61  
LINK         O3'   A B  36                 P   MIA B  37     1555   1555  1.62  
LINK         O3' MIA B  37                 P     A B  38     1555   1555  1.62  
LINK         O3'   A B  38                 P   PSU B  39     1555   1555  1.62  
LINK         O3' PSU B  39                 P     C B  40     1555   1555  1.61  
LINK         O3'   U B  45                 P   7MG B  46     1555   1555  1.62  
LINK         O3'   G B  53                 P   5MU B  54     1555   1555  1.62  
LINK         O3' 5MU B  54                 P   PSU B  55     1555   1555  1.61  
LINK         O3' PSU B  55                 P     C B  56     1555   1555  1.62  
LINK         O3'   A E   7                 P   4SU E   8     1555   1555  1.59  
LINK         O3' 4SU E   8                 P     A E   9     1555   1555  1.62  
LINK         O3'   G E  15                 P   H2U E  16     1555   1555  1.63  
LINK         O3' H2U E  16                 P     C E  17     1555   1555  1.61  
LINK         O3'   G E  19                 P   H2U E  20     1555   1555  1.62  
LINK         O3' H2U E  20                 P     A E  21     1555   1555  1.61  
LINK         O3'   A E  31                 P   PSU E  32     1555   1555  1.61  
LINK         O3' PSU E  32                 P     U E  33     1555   1555  1.61  
LINK         O3'   A E  36                 P   MIA E  37     1555   1555  1.61  
LINK         O3' MIA E  37                 P     A E  38     1555   1555  1.62  
LINK         O3'   A E  38                 P   PSU E  39     1555   1555  1.61  
LINK         O3' PSU E  39                 P     C E  40     1555   1555  1.61  
LINK         O3'   U E  45                 P   7MG E  46     1555   1555  1.61  
LINK         O3'   G E  53                 P   5MU E  54     1555   1555  1.61  
LINK         O3' 5MU E  54                 P   PSU E  55     1555   1555  1.61  
LINK         O3' PSU E  55                 P     C E  56     1555   1555  1.62  
LINK         O3'   G A1497                 P   UR3 A1498     1555   1555  1.63  
LINK         O3' UR3 A1498                 P     A A1499     1555   1555  1.62  
LINK         O3'   G A1401                 P   4OC A1402     1555   1555  1.61  
LINK         O3' 4OC A1402                 P     C A1403     1555   1555  1.61  
CISPEP   1 ILE C  199    PRO C  200          0       -12.28                     
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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