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Database: PDB
Entry: 2WWQ
LinkDB: 2WWQ
Original site: 2WWQ 
HEADER    RIBOSOME                                26-OCT-09   2WWQ              
TITLE     E.COLI 70S RIBOSOME STALLED DURING TRANSLATION OF TNAC                
TITLE    2 LEADER PEPTIDE. THIS FILE CONTAINS THE 50S, THE P-SITE               
TITLE    3 TRNA AND THE TNAC LEADER PEPTIDE (PART 2 OF 2).                      
SPLIT      2WWL 2WWQ                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 23S RIBOSOMAL RNA;                                         
COMPND   3 CHAIN: B;                                                            
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: 5S RIBOSOMAL RNA;                                          
COMPND   6 CHAIN: A;                                                            
COMPND   7 MOL_ID: 3;                                                           
COMPND   8 MOLECULE: 50S RIBOSOMAL PROTEIN L1;                                  
COMPND   9 CHAIN: 5;                                                            
COMPND  10 MOL_ID: 4;                                                           
COMPND  11 MOLECULE: 50S RIBOSOMAL PROTEIN L2;                                  
COMPND  12 CHAIN: C;                                                            
COMPND  13 MOL_ID: 5;                                                           
COMPND  14 MOLECULE: 50S RIBOSOMAL PROTEIN L3;                                  
COMPND  15 CHAIN: D;                                                            
COMPND  16 MOL_ID: 6;                                                           
COMPND  17 MOLECULE: 50S RIBOSOMAL PROTEIN L4;                                  
COMPND  18 CHAIN: E;                                                            
COMPND  19 MOL_ID: 7;                                                           
COMPND  20 MOLECULE: 50S RIBOSOMAL PROTEIN L5;                                  
COMPND  21 CHAIN: F;                                                            
COMPND  22 MOL_ID: 8;                                                           
COMPND  23 MOLECULE: 50S RIBOSOMAL PROTEIN L6;                                  
COMPND  24 CHAIN: G;                                                            
COMPND  25 MOL_ID: 9;                                                           
COMPND  26 MOLECULE: 50S RIBOSOMAL PROTEIN L9;                                  
COMPND  27 CHAIN: H;                                                            
COMPND  28 MOL_ID: 10;                                                          
COMPND  29 MOLECULE: 50S RIBOSOMAL PROTEIN L11;                                 
COMPND  30 CHAIN: I;                                                            
COMPND  31 MOL_ID: 11;                                                          
COMPND  32 MOLECULE: 50S RIBOSOMAL PROTEIN L13;                                 
COMPND  33 CHAIN: J;                                                            
COMPND  34 MOL_ID: 12;                                                          
COMPND  35 MOLECULE: 50S RIBOSOMAL PROTEIN L14;                                 
COMPND  36 CHAIN: K;                                                            
COMPND  37 MOL_ID: 13;                                                          
COMPND  38 MOLECULE: 50S RIBOSOMAL PROTEIN L15;                                 
COMPND  39 CHAIN: L;                                                            
COMPND  40 FRAGMENT: RESIDUES 2-144;                                            
COMPND  41 MOL_ID: 14;                                                          
COMPND  42 MOLECULE: 50S RIBOSOMAL PROTEIN L16;                                 
COMPND  43 CHAIN: M;                                                            
COMPND  44 MOL_ID: 15;                                                          
COMPND  45 MOLECULE: 50S RIBOSOMAL PROTEIN L17;                                 
COMPND  46 CHAIN: N;                                                            
COMPND  47 MOL_ID: 16;                                                          
COMPND  48 MOLECULE: 50S RIBOSOMAL PROTEIN L18;                                 
COMPND  49 CHAIN: O;                                                            
COMPND  50 FRAGMENT: RESIDUES 2-117;                                            
COMPND  51 MOL_ID: 17;                                                          
COMPND  52 MOLECULE: 50S RIBOSOMAL PROTEIN L19;                                 
COMPND  53 CHAIN: P;                                                            
COMPND  54 MOL_ID: 18;                                                          
COMPND  55 MOLECULE: 50S RIBOSOMAL PROTEIN L20;                                 
COMPND  56 CHAIN: Q;                                                            
COMPND  57 MOL_ID: 19;                                                          
COMPND  58 MOLECULE: 50S RIBOSOMAL PROTEIN L21;                                 
COMPND  59 CHAIN: R;                                                            
COMPND  60 MOL_ID: 20;                                                          
COMPND  61 MOLECULE: 50S RIBOSOMAL PROTEIN L22;                                 
COMPND  62 CHAIN: S;                                                            
COMPND  63 MOL_ID: 21;                                                          
COMPND  64 MOLECULE: 50S RIBOSOMAL PROTEIN L23;                                 
COMPND  65 CHAIN: T;                                                            
COMPND  66 MOL_ID: 22;                                                          
COMPND  67 MOLECULE: 50S RIBOSOMAL PROTEIN L24;                                 
COMPND  68 CHAIN: U;                                                            
COMPND  69 MOL_ID: 23;                                                          
COMPND  70 MOLECULE: 50S RIBOSOMAL PROTEIN L25;                                 
COMPND  71 CHAIN: W;                                                            
COMPND  72 MOL_ID: 24;                                                          
COMPND  73 MOLECULE: 50S RIBOSOMAL PROTEIN L27;                                 
COMPND  74 CHAIN: Y;                                                            
COMPND  75 FRAGMENT: RESIDUES 7-85;                                             
COMPND  76 MOL_ID: 25;                                                          
COMPND  77 MOLECULE: 50S RIBOSOMAL PROTEIN L28;                                 
COMPND  78 CHAIN: 0;                                                            
COMPND  79 MOL_ID: 26;                                                          
COMPND  80 MOLECULE: 50S RIBOSOMAL PROTEIN L29;                                 
COMPND  81 CHAIN: 1;                                                            
COMPND  82 MOL_ID: 27;                                                          
COMPND  83 MOLECULE: 50S RIBOSOMAL PROTEIN L30;                                 
COMPND  84 CHAIN: 2;                                                            
COMPND  85 MOL_ID: 28;                                                          
COMPND  86 MOLECULE: 50S RIBOSOMAL PROTEIN L32;                                 
COMPND  87 CHAIN: 3;                                                            
COMPND  88 MOL_ID: 29;                                                          
COMPND  89 MOLECULE: 50S RIBOSOMAL PROTEIN L33;                                 
COMPND  90 CHAIN: 4;                                                            
COMPND  91 MOL_ID: 30;                                                          
COMPND  92 MOLECULE: 50S RIBOSOMAL PROTEIN L34;                                 
COMPND  93 CHAIN: 6;                                                            
COMPND  94 MOL_ID: 31;                                                          
COMPND  95 MOLECULE: 50S RIBOSOMAL PROTEIN L35;                                 
COMPND  96 CHAIN: 7;                                                            
COMPND  97 MOL_ID: 32;                                                          
COMPND  98 MOLECULE: 50S RIBOSOMAL PROTEIN L36;                                 
COMPND  99 CHAIN: 8;                                                            
COMPND 100 MOL_ID: 33;                                                          
COMPND 101 MOLECULE: MRNA;                                                      
COMPND 102 CHAIN: X;                                                            
COMPND 103 MOL_ID: 34;                                                          
COMPND 104 MOLECULE: P-SITE TRNA 2;                                             
COMPND 105 CHAIN: V;                                                            
COMPND 106 MOL_ID: 35;                                                          
COMPND 107 MOLECULE: NASCENT TNAC LEADER PEPTIDE 5;                             
COMPND 108 CHAIN: Z                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   6 ORGANISM_TAXID: 562;                                                 
SOURCE   7 MOL_ID: 3;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   9 ORGANISM_TAXID: 562;                                                 
SOURCE  10 MOL_ID: 4;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  12 ORGANISM_TAXID: 562;                                                 
SOURCE  13 MOL_ID: 5;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  15 ORGANISM_TAXID: 562;                                                 
SOURCE  16 MOL_ID: 6;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  18 ORGANISM_TAXID: 562;                                                 
SOURCE  19 MOL_ID: 7;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  21 ORGANISM_TAXID: 562;                                                 
SOURCE  22 MOL_ID: 8;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  24 ORGANISM_TAXID: 562;                                                 
SOURCE  25 MOL_ID: 9;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  27 ORGANISM_TAXID: 562;                                                 
SOURCE  28 MOL_ID: 10;                                                          
SOURCE  29 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  30 ORGANISM_TAXID: 562;                                                 
SOURCE  31 MOL_ID: 11;                                                          
SOURCE  32 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  33 ORGANISM_TAXID: 562;                                                 
SOURCE  34 MOL_ID: 12;                                                          
SOURCE  35 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  36 ORGANISM_TAXID: 562;                                                 
SOURCE  37 MOL_ID: 13;                                                          
SOURCE  38 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  39 ORGANISM_TAXID: 562;                                                 
SOURCE  40 MOL_ID: 14;                                                          
SOURCE  41 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  42 ORGANISM_TAXID: 562;                                                 
SOURCE  43 MOL_ID: 15;                                                          
SOURCE  44 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  45 ORGANISM_TAXID: 562;                                                 
SOURCE  46 MOL_ID: 16;                                                          
SOURCE  47 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  48 ORGANISM_TAXID: 562;                                                 
SOURCE  49 MOL_ID: 17;                                                          
SOURCE  50 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  51 ORGANISM_TAXID: 562;                                                 
SOURCE  52 MOL_ID: 18;                                                          
SOURCE  53 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  54 ORGANISM_TAXID: 562;                                                 
SOURCE  55 MOL_ID: 19;                                                          
SOURCE  56 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  57 ORGANISM_TAXID: 562;                                                 
SOURCE  58 MOL_ID: 20;                                                          
SOURCE  59 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  60 ORGANISM_TAXID: 562;                                                 
SOURCE  61 MOL_ID: 21;                                                          
SOURCE  62 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  63 ORGANISM_TAXID: 562;                                                 
SOURCE  64 MOL_ID: 22;                                                          
SOURCE  65 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  66 ORGANISM_TAXID: 562;                                                 
SOURCE  67 MOL_ID: 23;                                                          
SOURCE  68 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  69 ORGANISM_TAXID: 562;                                                 
SOURCE  70 MOL_ID: 24;                                                          
SOURCE  71 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  72 ORGANISM_TAXID: 562;                                                 
SOURCE  73 MOL_ID: 25;                                                          
SOURCE  74 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  75 ORGANISM_TAXID: 562;                                                 
SOURCE  76 MOL_ID: 26;                                                          
SOURCE  77 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  78 ORGANISM_TAXID: 562;                                                 
SOURCE  79 MOL_ID: 27;                                                          
SOURCE  80 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  81 ORGANISM_TAXID: 562;                                                 
SOURCE  82 MOL_ID: 28;                                                          
SOURCE  83 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  84 ORGANISM_TAXID: 562;                                                 
SOURCE  85 MOL_ID: 29;                                                          
SOURCE  86 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  87 ORGANISM_TAXID: 562;                                                 
SOURCE  88 MOL_ID: 30;                                                          
SOURCE  89 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  90 ORGANISM_TAXID: 562;                                                 
SOURCE  91 MOL_ID: 31;                                                          
SOURCE  92 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  93 ORGANISM_TAXID: 562;                                                 
SOURCE  94 MOL_ID: 32;                                                          
SOURCE  95 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  96 ORGANISM_TAXID: 562;                                                 
SOURCE  97 MOL_ID: 33;                                                          
SOURCE  98 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  99 ORGANISM_TAXID: 562;                                                 
SOURCE 100 MOL_ID: 34;                                                          
SOURCE 101 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE 102 ORGANISM_TAXID: 562;                                                 
SOURCE 103 MOL_ID: 35;                                                          
SOURCE 104 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE 105 ORGANISM_TAXID: 562                                                  
KEYWDS    RIBOSOMAL PROTEIN, RIBONUCLEOPROTEIN, NUCLEOTIDE-BINDING,             
KEYWDS   2 PROTEIN BIOSYNTHESIS, TRANSLATION, ZINC-FINGER, TNAC, 70S            
KEYWDS   3 RIBOSOME, STALLING, RIBOSOME                                         
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    B.SEIDELT,C.A.INNIS,D.N.WILSON,M.GARTMANN,J.ARMACHE,E.VILLA,          
AUTHOR   2 L.G.TRABUCO,T.BECKER,T.MIELKE,K.SCHULTEN,T.A.STEITZ,                 
AUTHOR   3 R.BECKMANN                                                           
REVDAT   1   14-APR-10 2WWQ    0                                                
JRNL        AUTH   B.SEIDELT,C.A.INNIS,D.N.WILSON,M.GARTMANN,                   
JRNL        AUTH 2 J.ARMACHE,E.VILLA,L.G.TRABUCO,T.BECKER,T.MIELKE,             
JRNL        AUTH 3 K.SCHULTEN,T.A.STEITZ,R.BECKMANN                             
JRNL        TITL   STRUCTURAL INSIGHT INTO NASCENT POLYPEPTIDE CHAIN-           
JRNL        TITL 2 MEDIATED TRANSLATIONAL STALLING.                             
JRNL        REF    SCIENCE                       V. 326  1412 2009              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   19933110                                                     
JRNL        DOI    10.1126/SCIENCE.1177662                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    5.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : SPIDER                                    
REMARK   3   RECONSTRUCTION SCHEMA  : PROJECTION MATCHING                       
REMARK   3                                                                      
REMARK   3  EM MAP-MODEL FITTING AND REFINEMENT                                 
REMARK   3   PDB ENTRY                    : 3FIH,3FIK                           
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : FLEXIBLE FITTING                    
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3  FITTING PROCEDURE : 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)  : 5.8                            
REMARK   3   NUMBER OF PARTICLES               : 263000                         
REMARK   3   CTF CORRECTION METHOD             : DEFOCUS GROUP VOLUMES          
REMARK   3                                                                      
REMARK   3  EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                   
REMARK   3                                                                      
REMARK   3  OTHER DETAILS: NULL                                                 
REMARK   4                                                                      
REMARK   4 2WWQ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 26-OCT-09.                  
REMARK 100 THE PDBE ID CODE IS EBI-41520.                                       
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : VITREOUS ICE                      
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : NULL                              
REMARK 245   NAME OF SAMPLE                 : TNAC STALLED 70S RIBOSOME         
REMARK 245                                    WITH P-SITE TRNA.                 
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : HOLEY CARBON                      
REMARK 245   SAMPLE VITRIFICATION DETAILS   : VITRIFICATION 1 --                
REMARK 245                                    CRYOGEN ETHANE                    
REMARK 245   SAMPLE BUFFER                  : 50MM TRIS-HCL PH 8.0,             
REMARK 245                                    10MM MG-ACETATE, 50MM KCL,        
REMARK 245                                    10MM NH4CL, 2MM EGTA,             
REMARK 245                                    2MM L-TRYPTOPHAN AND 10MM         
REMARK 245                                    DDT                               
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      : 128                            
REMARK 245   TEMPERATURE (KELVIN)              : 95                             
REMARK 245   MICROSCOPE MODEL                  : FEI TECNAI F30                 
REMARK 245   DETECTOR TYPE                     : KODAK SO163                    
REMARK 245   MINIMUM DEFOCUS (NM)              : 1000                           
REMARK 245   MAXIMUM DEFOCUS (NM)              : 3000                           
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : 2.26                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 20                             
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 39000                          
REMARK 245   CALIBRATED MAGNIFICATION          : 38900                          
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 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 QUATERNARY STRUCTURE FOR THIS ENTRY: 35MERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J, K,      
REMARK 350                    AND CHAINS: L, M, N, O, P, Q, R, S, T, U, V,      
REMARK 350                    AND CHAINS: W, X, Y, Z, 1, 2, 3, 4, 5, 6, 7       
REMARK 350                    AND CHAINS: 8, 0                                  
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       C A     3                                                      
REMARK 465       G A     6                                                      
REMARK 465     VAL G     8                                                      
REMARK 465     ALA U     1                                                      
REMARK 465     ARG U     5                                                      
REMARK 465     ASP U     7                                                      
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     GLU K 121    O                                                   
REMARK 470     5MU V  54    C5M                                                 
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   N2     G V    35     C2     C X    18              2.08            
REMARK 500   O3'    A V    76     C    ALA Z    24              1.32            
REMARK 500   O3'    A V    76     O    ALA Z    24              1.20            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG 0  10   NE    ARG 0  10   CZ      0.081                       
REMARK 500    ARG 0  71   NE    ARG 0  71   CZ      0.091                       
REMARK 500    GLU 1  12   CB    GLU 1  12   CG      0.120                       
REMARK 500    ARG 1  47   CZ    ARG 1  47   NH2     0.095                       
REMARK 500    ARG 2  30   CZ    ARG 2  30   NH1     0.085                       
REMARK 500    ARG 3  16   NE    ARG 3  16   CZ      0.081                       
REMARK 500    TYR 3  47   CG    TYR 3  47   CD2     0.079                       
REMARK 500    ARG 3  49   NE    ARG 3  49   CZ      0.086                       
REMARK 500    PHE 4  19   CG    PHE 4  19   CD1     0.099                       
REMARK 500    TYR 5  21   CG    TYR 5  21   CD2     0.089                       
REMARK 500    GLY 5  49   N     GLY 5  49   CA      0.090                       
REMARK 500    ARG 5  74   NE    ARG 5  74   CZ      0.084                       
REMARK 500    GLY 5 159   CA    GLY 5 159   C      -0.114                       
REMARK 500    ARG 6  12   CD    ARG 6  12   NE      0.120                       
REMARK 500    ARG 6  12   NE    ARG 6  12   CZ      0.079                       
REMARK 500    ARG 6  28   CD    ARG 6  28   NE      0.117                       
REMARK 500    ARG 7  12   CZ    ARG 7  12   NH1     0.088                       
REMARK 500    ARG 7  39   CZ    ARG 7  39   NH1     0.084                       
REMARK 500    ARG 7  39   NE    ARG 7  39   CZ      0.102                       
REMARK 500    ARG 8  24   CD    ARG 8  24   NE      0.108                       
REMARK 500    CYS 8  27   CB    CYS 8  27   SG      0.129                       
REMARK 500      G A   2   C2'     G A   2   C1'    -0.096                       
REMARK 500      G A   2   N7      G A   2   C5     -0.037                       
REMARK 500      C A   4   C2      C A   4   N3      0.076                       
REMARK 500      C A   4   C4'     C A   4   C3'     0.078                       
REMARK 500      C A   4   C5      C A   4   C6     -0.052                       
REMARK 500      C A   4   N1      C A   4   C6     -0.042                       
REMARK 500      C A   4   N3      C A   4   C4      0.054                       
REMARK 500      U A   5   C2      U A   5   N3      0.066                       
REMARK 500      U A   5   N3      U A   5   C4      0.074                       
REMARK 500      U A   5   P       U A   5   O5'    -0.061                       
REMARK 500      G A   7   C2      G A   7   N3      0.054                       
REMARK 500      G A   7   C5'     G A   7   C4'    -0.048                       
REMARK 500      C A   8   C2'     C A   8   C1'    -0.052                       
REMARK 500      C A   8   N3      C A   8   C4      0.050                       
REMARK 500      G A   9   N1      G A   9   C2      0.053                       
REMARK 500      G A   9   N9      G A   9   C4     -0.050                       
REMARK 500      G A  10   N1      G A  10   C2      0.055                       
REMARK 500      G A  10   N7      G A  10   C5     -0.070                       
REMARK 500      G A  10   N9      G A  10   C8      0.058                       
REMARK 500      C A  11   C2      C A  11   N3     -0.050                       
REMARK 500      C A  11   N1      C A  11   C6      0.070                       
REMARK 500      C A  11   N3      C A  11   C4      0.055                       
REMARK 500      C A  12   C2'     C A  12   C1'    -0.058                       
REMARK 500      G A  13   C2      G A  13   N2      0.072                       
REMARK 500      G A  13   C8      G A  13   N7     -0.070                       
REMARK 500      G A  13   N9      G A  13   C4     -0.049                       
REMARK 500      C A  12   O3'     G A  13   P      -0.126                       
REMARK 500      A A  15   C5      A A  15   C6     -0.062                       
REMARK 500      A A  15   N7      A A  15   C5     -0.052                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS    6650 BOND DEVIATIONS.                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG 0  10   NE  -  CZ  -  NH2 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG 0  17   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG 0  26   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG 0  26   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    PHE 0  45   CB  -  CG  -  CD1 ANGL. DEV. =   7.5 DEGREES          
REMARK 500    PHE 0  45   CB  -  CG  -  CD2 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    ARG 0  49   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ARG 0  49   NE  -  CZ  -  NH2 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ARG 0  56   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ASP 0  59   CB  -  CG  -  OD2 ANGL. DEV. =   8.3 DEGREES          
REMARK 500    ASP 0  64   O   -  C   -  N   ANGL. DEV. =  10.4 DEGREES          
REMARK 500    ARG 0  73   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    ARG 0  73   NE  -  CZ  -  NH2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG 1   7   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG 1   7   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    PHE 1  26   CB  -  CG  -  CD1 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    ARG 1  29   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG 1  47   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ASP 1  49   CB  -  CG  -  OD1 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ARG 1  52   NE  -  CZ  -  NH2 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    THR 2   9   CA  -  CB  -  CG2 ANGL. DEV. = -10.0 DEGREES          
REMARK 500    ARG 2  30   NE  -  CZ  -  NH2 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG 2  44   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    PHE 2  52   CB  -  CG  -  CD1 ANGL. DEV. =   5.1 DEGREES          
REMARK 500    PHE 2  52   CB  -  CG  -  CD2 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    ARG 3  12   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.8 DEGREES          
REMARK 500    SER 3  28   N   -  CA  -  CB  ANGL. DEV. =  11.7 DEGREES          
REMARK 500    ARG 3  39   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    THR 3  43   CA  -  CB  -  CG2 ANGL. DEV. =  -9.8 DEGREES          
REMARK 500    TYR 3  48   CG  -  CD1 -  CE1 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ARG 3  49   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG 3  49   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    ARG 3  51   N   -  CA  -  CB  ANGL. DEV. =  14.5 DEGREES          
REMARK 500    ARG 3  51   NE  -  CZ  -  NH2 ANGL. DEV. =   8.0 DEGREES          
REMARK 500    ARG 4   5   N   -  CA  -  CB  ANGL. DEV. =  15.2 DEGREES          
REMARK 500    ARG 4   5   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    TYR 4  20   CB  -  CG  -  CD1 ANGL. DEV. =  -8.3 DEGREES          
REMARK 500    TYR 4  20   CB  -  CG  -  CD2 ANGL. DEV. =   4.9 DEGREES          
REMARK 500    PHE 4  38   CB  -  CG  -  CD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG 4  43   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG 5   7   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    ARG 5   7   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    MET 5   8   CG  -  SD  -  CE  ANGL. DEV. = -10.7 DEGREES          
REMARK 500    ARG 5   9   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    TYR 5  21   CB  -  CG  -  CD1 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    PHE 5  38   CB  -  CG  -  CD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP 5  43   CB  -  CG  -  OD1 ANGL. DEV. =   8.5 DEGREES          
REMARK 500    ASP 5  43   CB  -  CG  -  OD2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ASP 5  51   CB  -  CG  -  OD1 ANGL. DEV. =   8.7 DEGREES          
REMARK 500    ARG 5  53   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS   12521 ANGLE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG 0   2       51.11   -100.77                                   
REMARK 500    THR 0   7      -14.91   -153.15                                   
REMARK 500    ARG 0  17      106.95     60.21                                   
REMARK 500    HIS 0  19       14.06    -67.35                                   
REMARK 500    ALA 0  20       20.15   -150.90                                   
REMARK 500    LEU 0  21       44.20     77.00                                   
REMARK 500    THR 0  24      125.87   -173.98                                   
REMARK 500    ARG 0  26      -11.17   -155.71                                   
REMARK 500    ARG 0  27      123.84     76.12                                   
REMARK 500    LEU 0  32      123.47     68.41                                   
REMARK 500    GLU 0  40       -3.04     80.11                                   
REMARK 500    GLU 0  42      -21.64   -152.13                                   
REMARK 500    THR 0  65      -36.37   -159.27                                   
REMARK 500    LEU 0  70      -53.78     69.87                                   
REMARK 500    LYS 1   2      -95.32    -69.03                                   
REMARK 500    ARG 1  23       42.16     73.61                                   
REMARK 500    GLU 1  24       -9.03   -159.94                                   
REMARK 500    LEU 1  37      127.64     56.88                                   
REMARK 500    GLN 1  38       65.33   -100.09                                   
REMARK 500    GLN 1  39       74.43   -108.22                                   
REMARK 500    VAL 1  46      -60.63     70.62                                   
REMARK 500    ARG 1  48       41.30    -72.84                                   
REMARK 500    ASP 1  49      -44.26   -149.05                                   
REMARK 500    LEU 1  57      -50.92     74.03                                   
REMARK 500    GLN 2   8      -69.07   -103.84                                   
REMARK 500    ARG 2  10     -136.56   -149.70                                   
REMARK 500    LYS 2  18       36.21    -84.87                                   
REMARK 500    HIS 2  19      -58.70   -132.40                                   
REMARK 500    ARG 2  29        3.20   -160.47                                   
REMARK 500    GLN 3   3      170.55    -55.01                                   
REMARK 500    ASN 3   5      156.60     62.85                                   
REMARK 500    ALA 3  20      164.77    168.36                                   
REMARK 500    HIS 3  41     -161.00   -160.57                                   
REMARK 500    ALA 3  44       13.77     91.50                                   
REMARK 500    ASP 3  45       16.47   -148.07                                   
REMARK 500    TYR 3  48      -26.53   -142.82                                   
REMARK 500    ARG 3  49       27.67   -168.55                                   
REMARK 500    ARG 3  51      104.81     76.81                                   
REMARK 500    ALA 3  55       12.94   -151.10                                   
REMARK 500    LYS 4  24      148.38   -170.10                                   
REMARK 500    THR 4  28       13.59   -148.10                                   
REMARK 500    LYS 4  29       78.04   -169.64                                   
REMARK 500    LEU 4  33      140.98     69.55                                   
REMARK 500    LYS 4  37     -162.29    179.00                                   
REMARK 500    ARG 4  43       46.57     39.55                                   
REMARK 500    LYS 4  49     -169.76   -100.60                                   
REMARK 500    GLU 4  50      159.76     74.23                                   
REMARK 500    LEU 5   4       78.47   -115.32                                   
REMARK 500    ARG 5  53     -117.49    -98.01                                   
REMARK 500    LYS 5  54      -64.68   -127.27                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     555 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 0   52     LYS 0   53                  145.27                    
REMARK 500 SER 4   13     ALA 4   14                  137.16                    
REMARK 500 LYS 4   37     PHE 4   38                 -148.64                    
REMARK 500 THR 5  144     VAL 5  145                  145.52                    
REMARK 500 ARG 6   39     ALA 6   40                 -149.00                    
REMARK 500 GLU D   89     PHE D   90                 -147.40                    
REMARK 500 THR D  151     PRO D  152                  140.23                    
REMARK 500 LYS E   57     LYS E   58                 -147.58                    
REMARK 500 ARG E   88     PRO E   89                  149.21                    
REMARK 500 GLU F   18     PHE F   19                 -139.54                    
REMARK 500 ASP F  173     PHE F  174                  148.67                    
REMARK 500 THR G   83     LYS G   84                 -145.81                    
REMARK 500 VAL H   31     PRO H   32                   37.33                    
REMARK 500 GLY J  112     PRO J  113                 -145.64                    
REMARK 500 ARG K   70     ARG K   71                  148.16                    
REMARK 500 ARG K   71     PRO K   72                  -51.23                    
REMARK 500 ASN K   88     ASN K   89                 -148.10                    
REMARK 500 GLY M   37     ARG M   38                 -148.51                    
REMARK 500 THR N   95     ARG N   96                  148.21                    
REMARK 500 ASN P   51     ARG P   52                 -138.41                    
REMARK 500 VAL P   60     ARG P   61                  136.70                    
REMARK 500 GLY Q    6     VAL Q    7                  149.24                    
REMARK 500 PHE Y   68     GLU Y   69                  138.93                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG 0  36         0.09    SIDE CHAIN                              
REMARK 500    ARG 0  49         0.10    SIDE CHAIN                              
REMARK 500    ARG 0  73         0.13    SIDE CHAIN                              
REMARK 500    PHE 1  26         0.09    SIDE CHAIN                              
REMARK 500    ARG 3  12         0.09    SIDE CHAIN                              
REMARK 500    ARG 3  51         0.09    SIDE CHAIN                              
REMARK 500    TYR 4  48         0.07    SIDE CHAIN                              
REMARK 500    ARG 5   9         0.08    SIDE CHAIN                              
REMARK 500    ARG 5  60         0.08    SIDE CHAIN                              
REMARK 500    ARG 5  71         0.09    SIDE CHAIN                              
REMARK 500    ARG 5 164         0.12    SIDE CHAIN                              
REMARK 500    TYR 5 208         0.15    SIDE CHAIN                              
REMARK 500    ARG 6  12         0.08    SIDE CHAIN                              
REMARK 500    ARG 6  28         0.10    SIDE CHAIN                              
REMARK 500    HIS 7  25         0.07    SIDE CHAIN                              
REMARK 500      G A   2         0.10    SIDE CHAIN                              
REMARK 500      C A   4         0.13    SIDE CHAIN                              
REMARK 500      U A   5         0.10    SIDE CHAIN                              
REMARK 500      G A   7         0.07    SIDE CHAIN                              
REMARK 500      G A  10         0.06    SIDE CHAIN                              
REMARK 500      C A  12         0.08    SIDE CHAIN                              
REMARK 500      G A  16         0.09    SIDE CHAIN                              
REMARK 500      C A  17         0.10    SIDE CHAIN                              
REMARK 500      G A  18         0.07    SIDE CHAIN                              
REMARK 500      G A  21         0.09    SIDE CHAIN                              
REMARK 500      G A  24         0.13    SIDE CHAIN                              
REMARK 500      C A  26         0.09    SIDE CHAIN                              
REMARK 500      C A  27         0.08    SIDE CHAIN                              
REMARK 500      C A  31         0.07    SIDE CHAIN                              
REMARK 500      C A  37         0.10    SIDE CHAIN                              
REMARK 500      U A  40         0.08    SIDE CHAIN                              
REMARK 500      G A  41         0.09    SIDE CHAIN                              
REMARK 500      G A  44         0.12    SIDE CHAIN                              
REMARK 500      A A  45         0.10    SIDE CHAIN                              
REMARK 500      C A  47         0.05    SIDE CHAIN                              
REMARK 500      C A  49         0.10    SIDE CHAIN                              
REMARK 500      G A  51         0.08    SIDE CHAIN                              
REMARK 500      G A  54         0.17    SIDE CHAIN                              
REMARK 500      A A  58         0.06    SIDE CHAIN                              
REMARK 500      A A  59         0.10    SIDE CHAIN                              
REMARK 500      G A  61         0.07    SIDE CHAIN                              
REMARK 500      G A  64         0.06    SIDE CHAIN                              
REMARK 500      A A  66         0.08    SIDE CHAIN                              
REMARK 500      C A  68         0.10    SIDE CHAIN                              
REMARK 500      C A  70         0.12    SIDE CHAIN                              
REMARK 500      C A  71         0.08    SIDE CHAIN                              
REMARK 500      G A  72         0.12    SIDE CHAIN                              
REMARK 500      G A  75         0.09    SIDE CHAIN                              
REMARK 500      A A  78         0.07    SIDE CHAIN                              
REMARK 500      G A  79         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS    1488 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    SER Y  34         11.36                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LEU 0  32        23.8      L          L   OUTSIDE RANGE           
REMARK 500    SER 1  10        23.1      L          L   OUTSIDE RANGE           
REMARK 500    ARG 1  23        25.0      L          L   OUTSIDE RANGE           
REMARK 500    VAL 1  46        24.9      L          L   OUTSIDE RANGE           
REMARK 500    LEU 1  57        24.0      L          L   OUTSIDE RANGE           
REMARK 500    THR 2   9        22.1      L          L   OUTSIDE RANGE           
REMARK 500    ASP 2  39        24.6      L          L   OUTSIDE RANGE           
REMARK 500    ALA 3  44        23.5      L          L   OUTSIDE RANGE           
REMARK 500    ARG 3  51        19.9      L          L   OUTSIDE RANGE           
REMARK 500    GLU 4  50        24.2      L          L   OUTSIDE RANGE           
REMARK 500    THR 5 144        24.7      L          L   OUTSIDE RANGE           
REMARK 500    VAL 5 178        22.9      L          L   OUTSIDE RANGE           
REMARK 500    GLU 5 187        23.2      L          L   OUTSIDE RANGE           
REMARK 500    LYS 5 210        23.8      L          L   OUTSIDE RANGE           
REMARK 500      A B1088       -45.3      D          D   OUTSIDE RANGE           
REMARK 500    ALA C 154        24.9      L          L   OUTSIDE RANGE           
REMARK 500    THR D  91        24.3      L          L   OUTSIDE RANGE           
REMARK 500    VAL D 107        24.7      L          L   OUTSIDE RANGE           
REMARK 500    ILE E 148        17.0      L          L   OUTSIDE RANGE           
REMARK 500    LEU F  48        23.5      L          L   OUTSIDE RANGE           
REMARK 500    ALA F  58        24.6      L          L   OUTSIDE RANGE           
REMARK 500    ARG F  79        23.7      L          L   OUTSIDE RANGE           
REMARK 500    ILE G 140        23.1      L          L   OUTSIDE RANGE           
REMARK 500    LEU H  15        24.3      L          L   OUTSIDE RANGE           
REMARK 500    THR H  96        24.1      L          L   OUTSIDE RANGE           
REMARK 500    VAL J 105        21.1      L          L   OUTSIDE RANGE           
REMARK 500    LYS L  29        22.3      L          L   OUTSIDE RANGE           
REMARK 500    THR L  30        24.2      L          L   OUTSIDE RANGE           
REMARK 500    LYS L  36        24.0      L          L   OUTSIDE RANGE           
REMARK 500    GLU L  86        24.8      L          L   OUTSIDE RANGE           
REMARK 500    THR L 117        24.0      L          L   OUTSIDE RANGE           
REMARK 500    VAL M  57        24.4      L          L   OUTSIDE RANGE           
REMARK 500    ASP O   2        23.5      L          L   OUTSIDE RANGE           
REMARK 500    GLU O  55        24.5      L          L   OUTSIDE RANGE           
REMARK 500    LEU O 106        24.8      L          L   OUTSIDE RANGE           
REMARK 500    THR P  59        21.8      L          L   OUTSIDE RANGE           
REMARK 500    THR P 103        23.9      L          L   OUTSIDE RANGE           
REMARK 500    ILE Q  73        22.1      L          L   OUTSIDE RANGE           
REMARK 500    ARG Q  91        23.6      L          L   OUTSIDE RANGE           
REMARK 500    GLU R  16        22.2      L          L   OUTSIDE RANGE           
REMARK 500    PHE R  53        24.3      L          L   OUTSIDE RANGE           
REMARK 500    HIS S   9        24.2      L          L   OUTSIDE RANGE           
REMARK 500    VAL S  45        23.5      L          L   OUTSIDE RANGE           
REMARK 500    ASN S  61        21.9      L          L   OUTSIDE RANGE           
REMARK 500    THR S  72        24.4      L          L   OUTSIDE RANGE           
REMARK 500    LYS T  19        24.1      L          L   OUTSIDE RANGE           
REMARK 500    THR T  29        24.2      L          L   OUTSIDE RANGE           
REMARK 500    THR T  86        24.6      L          L   OUTSIDE RANGE           
REMARK 500    SER W  17        20.5      L          L   OUTSIDE RANGE           
REMARK 500    ASP W  45        23.3      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      51 CHIRALITY DEVIATIONS.                         
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "WA" IN EACH CHAIN ON SHEET RECORDS          
REMARK 700 BELOW IS ACTUALLY AN  6-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 ARE IDENTICAL.                                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1DFU   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF E.COLI RIBOSOMAL                               
REMARK 900  PROTEIN L25 COMPLEXEDWITH A 5S RRNA FRAGMENT                        
REMARK 900   AT 1.8 A RESOLUTION                                                
REMARK 900 RELATED ID: 2J28   RELATED DB: PDB                                   
REMARK 900  MODEL OF E. COLI SRP BOUND TO 70S RNCS                              
REMARK 900 RELATED ID: 2VHM   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF PDF BINDING HELIX IN COMPLEX                           
REMARK 900  WITH THE RIBOSOME                                                   
REMARK 900 RELATED ID: 2VRH   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE E. COLI TRIGGER FACTOR                             
REMARK 900  BOUND TO A TRANSLATING RIBOSOME                                     
REMARK 900 RELATED ID: 1B75   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF RIBOSOMAL PROTEIN L25                         
REMARK 900  FROMESCHERICHIA COLI                                                
REMARK 900 RELATED ID: 487D   RELATED DB: PDB                                   
REMARK 900  SEVEN RIBOSOMAL PROTEINS FITTED TO A CRYO-                          
REMARK 900  ELECTRONMICROSCOPIC MAP OF THE LARGE 50S                            
REMARK 900  SUBUNIT AT 7.5 ANGSTROMSRESOLUTION                                  
REMARK 900 RELATED ID: 2AW4   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE BACTERIAL RIBOSOME                         
REMARK 900  FROMESCHERICHIA COLI AT 3.5 A RESOLUTION.                           
REMARK 900  THIS FILE CONTAINSTHE 50S SUBUNIT OF ONE                            
REMARK 900  70S RIBOSOME. THE ENTIRE CRYSTALSTRUCTURE                           
REMARK 900  CONTAINS TWO 70S RIBOSOMES AND IS DESCRIBED                         
REMARK 900   INREMARK 400.                                                      
REMARK 900 RELATED ID: 1P86   RELATED DB: PDB                                   
REMARK 900  REAL SPACE REFINED COORDINATES OF THE 50S                           
REMARK 900  SUBUNIT FITTEDINTO THE LOW RESOLUTION CRYO-                         
REMARK 900  EM MAP OF THE INITIATION-LIKESTATE OF E.                            
REMARK 900  COLI 70S RIBOSOME                                                   
REMARK 900 RELATED ID: 1P85   RELATED DB: PDB                                   
REMARK 900  REAL SPACE REFINED COORDINATES OF THE 50S                           
REMARK 900  SUBUNIT FITTEDINTO THE LOW RESOLUTION CRYO-                         
REMARK 900  EM MAP OF THE EF-G.GTP STATEOF E. COLI                              
REMARK 900   70S RIBOSOME                                                       
REMARK 900 RELATED ID: 1D6K   RELATED DB: PDB                                   
REMARK 900  NMR SOLUTION STRUCTURE OF THE 5S RRNA E-                            
REMARK 900  LOOP/L25 COMPLEX                                                    
REMARK 900 RELATED ID: 2VHN   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF PDF BINDING HELIX IN COMPLEX                           
REMARK 900  WITH THE RIBOSOME                                                   
REMARK 900 RELATED ID: 2AWB   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE BACTERIAL RIBOSOME                         
REMARK 900  FROMESCHERICHIA COLI AT 3.5 A RESOLUTION.                           
REMARK 900  THIS FILE CONTAINSTHE 50S SUBUNIT OF THE                            
REMARK 900  SECOND 70S RIBOSOME. THE ENTIRECRYSTAL                              
REMARK 900  STRUCTURE CONTAINS TWO 70S RIBOSOMES AND                            
REMARK 900  IS DESCRIBED IN REMARK 400.                                         
REMARK 900 RELATED ID: 2WWL   RELATED DB: PDB                                   
REMARK 900  E.COLI 70S RIBOSOME STALLED DURING                                  
REMARK 900  TRANSLATION OF TNAC LEADER PEPTIDE                                  
REMARK 900 RELATED ID: EMD-1657   RELATED DB: EMDB                              
REMARK 900  STRUCTURAL INSIGHT INTO NASCENT POLYPEPTIDE                         
REMARK 900  CHAIN-MEDIATED TRANSLATIONAL STALLING                               
DBREF  2WWQ 0    1    77  UNP    P0A7M2   RL28_ECOLI       2     78             
DBREF  2WWQ 1    1    63  UNP    P0A7M6   RL29_ECOLI       1     63             
DBREF  2WWQ 2    1    58  UNP    P0AG51   RL30_ECOLI       2     59             
DBREF  2WWQ 3    1    56  UNP    P0A7N4   RL32_ECOLI       2     57             
DBREF  2WWQ 4    3    52  UNP    P0A7N9   RL33_ECOLI       4     53             
DBREF  2WWQ 5    1   234  UNP    P0A7L0   RL1_ECOLI        1    234             
DBREF  2WWQ 6    1    46  UNP    P0A7P5   RL34_ECOLI       1     46             
DBREF  2WWQ 7    1    64  UNP    P0A7Q1   RL35_ECOLI       2     65             
DBREF  2WWQ 8    1    38  UNP    P0A7Q6   RL36_ECOLI       1     38             
DBREF1 2WWQ A    2   118  GB                   CP001396                         
DBREF2 2WWQ A    238859724                       228756      228872             
DBREF1 2WWQ B    1  2903  GB                   CP001396                         
DBREF2 2WWQ B    238859724                      2613011     2610109             
DBREF  2WWQ C    1   271  UNP    P60422   RL2_ECOLI        2    272             
DBREF  2WWQ D    1   209  UNP    P60438   RL3_ECOLI        1    209             
DBREF  2WWQ E    1   201  UNP    P60723   RL4_ECOLI        1    201             
DBREF  2WWQ F    1   178  UNP    P62399   RL5_ECOLI        2    179             
DBREF  2WWQ G    1   176  UNP    P0AG55   RL6_ECOLI        2    177             
DBREF  2WWQ H    1   149  UNP    P0A7R1   RL9_ECOLI        1    149             
DBREF  2WWQ I    1   141  UNP    P0A7J7   RL11_ECOLI       2    142             
DBREF  2WWQ J    1   142  UNP    P0AA10   RL13_ECOLI       1    142             
DBREF  2WWQ K    1   121  UNP    P0ADY3   RL14_ECOLI       2    122             
DBREF  2WWQ L    2   144  UNP    P02413   RL15_ECOLI       2    144             
DBREF  2WWQ M    1   136  UNP    P0ADY7   RL16_ECOLI       1    136             
DBREF  2WWQ N    1   120  UNP    P0AG44   RL17_ECOLI       1    120             
DBREF  2WWQ O    2   117  UNP    P0C018   RL18_ECOLI       2    117             
DBREF  2WWQ P    1   114  UNP    P0A7K6   RL19_ECOLI       2    115             
DBREF  2WWQ Q    1   117  UNP    P0A7L3   RL20_ECOLI       2    118             
DBREF  2WWQ R    1   103  UNP    P0AG48   RL21_ECOLI       1    103             
DBREF  2WWQ S    1   110  UNP    P61175   RL22_ECOLI       1    110             
DBREF  2WWQ T    1    93  UNP    P0ADZ0   RL23_ECOLI       1     93             
DBREF  2WWQ U    1   102  UNP    P60624   RL24_ECOLI       2    103             
DBREF1 2WWQ V    1    76  GB                   CP001396                         
DBREF2 2WWQ V    238859724                      2170038     2170114             
DBREF  2WWQ W    1    94  UNP    P68919   RL25_ECOLI       1     94             
DBREF  2WWQ X   12    22  PDB    2WWQ     2WWQ            12     22             
DBREF  2WWQ Y    6    84  UNP    P0A7L8   RL27_ECOLI       7     85             
DBREF  2WWQ Z    5    24  PDB    2WWQ     2WWQ             5     24             
SEQRES   1 0   77  SER ARG VAL CYS GLN VAL THR GLY LYS ARG PRO VAL THR          
SEQRES   2 0   77  GLY ASN ASN ARG SER HIS ALA LEU ASN ALA THR LYS ARG          
SEQRES   3 0   77  ARG PHE LEU PRO ASN LEU HIS SER HIS ARG PHE TRP VAL          
SEQRES   4 0   77  GLU SER GLU LYS ARG PHE VAL THR LEU ARG VAL SER ALA          
SEQRES   5 0   77  LYS GLY MET ARG VAL ILE ASP LYS LYS GLY ILE ASP THR          
SEQRES   6 0   77  VAL LEU ALA GLU LEU ARG ALA ARG GLY GLU LYS TYR              
SEQRES   1 1   63  MET LYS ALA LYS GLU LEU ARG GLU LYS SER VAL GLU GLU          
SEQRES   2 1   63  LEU ASN THR GLU LEU LEU ASN LEU LEU ARG GLU GLN PHE          
SEQRES   3 1   63  ASN LEU ARG MET GLN ALA ALA SER GLY GLN LEU GLN GLN          
SEQRES   4 1   63  SER HIS LEU LEU LYS GLN VAL ARG ARG ASP VAL ALA ARG          
SEQRES   5 1   63  VAL LYS THR LEU LEU ASN GLU LYS ALA GLY ALA                  
SEQRES   1 2   58  ALA LYS THR ILE LYS ILE THR GLN THR ARG SER ALA ILE          
SEQRES   2 2   58  GLY ARG LEU PRO LYS HIS LYS ALA THR LEU LEU GLY LEU          
SEQRES   3 2   58  GLY LEU ARG ARG ILE GLY HIS THR VAL GLU ARG GLU ASP          
SEQRES   4 2   58  THR PRO ALA ILE ARG GLY MET ILE ASN ALA VAL SER PHE          
SEQRES   5 2   58  MET VAL LYS VAL GLU GLU                                      
SEQRES   1 3   56  ALA VAL GLN GLN ASN LYS PRO THR ARG SER LYS ARG GLY          
SEQRES   2 3   56  MET ARG ARG SER HIS ASP ALA LEU THR ALA VAL THR SER          
SEQRES   3 3   56  LEU SER VAL ASP LYS THR SER GLY GLU LYS HIS LEU ARG          
SEQRES   4 3   56  HIS HIS ILE THR ALA ASP GLY TYR TYR ARG GLY ARG LYS          
SEQRES   5 3   56  VAL ILE ALA LYS                                              
SEQRES   1 4   50  GLY ILE ARG GLU LYS ILE LYS LEU VAL SER SER ALA GLY          
SEQRES   2 4   50  THR GLY HIS PHE TYR THR THR THR LYS ASN LYS ARG THR          
SEQRES   3 4   50  LYS PRO GLU LYS LEU GLU LEU LYS LYS PHE ASP PRO VAL          
SEQRES   4 4   50  VAL ARG GLN HIS VAL ILE TYR LYS GLU ALA LYS                  
SEQRES   1 5  234  MET ALA LYS LEU THR LYS ARG MET ARG VAL ILE ARG GLU          
SEQRES   2 5  234  LYS VAL ASP ALA THR LYS GLN TYR ASP ILE ASN GLU ALA          
SEQRES   3 5  234  ILE ALA LEU LEU LYS GLU LEU ALA THR ALA LYS PHE VAL          
SEQRES   4 5  234  GLU SER VAL ASP VAL ALA VAL ASN LEU GLY ILE ASP ALA          
SEQRES   5 5  234  ARG LYS SER ASP GLN ASN VAL ARG GLY ALA THR VAL LEU          
SEQRES   6 5  234  PRO HIS GLY THR GLY ARG SER VAL ARG VAL ALA VAL PHE          
SEQRES   7 5  234  THR GLN GLY ALA ASN ALA GLU ALA ALA LYS ALA ALA GLY          
SEQRES   8 5  234  ALA GLU LEU VAL GLY MET GLU ASP LEU ALA ASP GLN ILE          
SEQRES   9 5  234  LYS LYS GLY GLU MET ASN PHE ASP VAL VAL ILE ALA SER          
SEQRES  10 5  234  PRO ASP ALA MET ARG VAL VAL GLY GLN LEU GLY GLN VAL          
SEQRES  11 5  234  LEU GLY PRO ARG GLY LEU MET PRO ASN PRO LYS VAL GLY          
SEQRES  12 5  234  THR VAL THR PRO ASN VAL ALA GLU ALA VAL LYS ASN ALA          
SEQRES  13 5  234  LYS ALA GLY GLN VAL ARG TYR ARG ASN ASP LYS ASN GLY          
SEQRES  14 5  234  ILE ILE HIS THR THR ILE GLY LYS VAL ASP PHE ASP ALA          
SEQRES  15 5  234  ASP LYS LEU LYS GLU ASN LEU GLU ALA LEU LEU VAL ALA          
SEQRES  16 5  234  LEU LYS LYS ALA LYS PRO THR GLN ALA LYS GLY VAL TYR          
SEQRES  17 5  234  ILE LYS LYS VAL SER ILE SER THR THR MET GLY ALA GLY          
SEQRES  18 5  234  VAL ALA VAL ASP GLN ALA GLY LEU SER ALA SER VAL ASN          
SEQRES   1 6   46  MET LYS ARG THR PHE GLN PRO SER VAL LEU LYS ARG ASN          
SEQRES   2 6   46  ARG SER HIS GLY PHE ARG ALA ARG MET ALA THR LYS ASN          
SEQRES   3 6   46  GLY ARG GLN VAL LEU ALA ARG ARG ARG ALA LYS GLY ARG          
SEQRES   4 6   46  ALA ARG LEU THR VAL SER LYS                                  
SEQRES   1 7   64  PRO LYS ILE LYS THR VAL ARG GLY ALA ALA LYS ARG PHE          
SEQRES   2 7   64  LYS LYS THR GLY LYS GLY GLY PHE LYS HIS LYS HIS ALA          
SEQRES   3 7   64  ASN LEU ARG HIS ILE LEU THR LYS LYS ALA THR LYS ARG          
SEQRES   4 7   64  LYS ARG HIS LEU ARG PRO LYS ALA MET VAL SER LYS GLY          
SEQRES   5 7   64  ASP LEU GLY LEU VAL ILE ALA CYS LEU PRO TYR ALA              
SEQRES   1 8   38  MET LYS VAL ARG ALA SER VAL LYS LYS LEU CYS ARG ASN          
SEQRES   2 8   38  CYS LYS ILE VAL LYS ARG ASP GLY VAL ILE ARG VAL ILE          
SEQRES   3 8   38  CYS SER ALA GLU PRO LYS HIS LYS GLN ARG GLN GLY              
SEQRES   1 A  117    G   C   C   U   G   G   C   G   G   C   C   G   U          
SEQRES   2 A  117    A   G   C   G   C   G   G   U   G   G   U   C   C          
SEQRES   3 A  117    C   A   C   C   U   G   A   C   C   C   C   A   U          
SEQRES   4 A  117    G   C   C   G   A   A   C   U   C   A   G   A   A          
SEQRES   5 A  117    G   U   G   A   A   A   C   G   C   C   G   U   A          
SEQRES   6 A  117    G   C   G   C   C   G   A   U   G   G   U   A   G          
SEQRES   7 A  117    U   G   U   G   G   G   G   U   C   U   C   C   C          
SEQRES   8 A  117    C   A   U   G   C   G   A   G   A   G   U   A   G          
SEQRES   9 A  117    G   G   A   A   C   U   G   C   C   A   G   G   C          
SEQRES   1 B 2903    G   G   U   U   A   A   G   C   G   A   C   U   A          
SEQRES   2 B 2903    A   G   C   G   U   A   C   A   C   G   G   U   G          
SEQRES   3 B 2903    G   A   U   G   C   C   C   U   G   G   C   A   G          
SEQRES   4 B 2903    U   C   A   G   A   G   G   C   G   A   U   G   A          
SEQRES   5 B 2903    A   G   G   A   C   G   U   G   C   U   A   A   U          
SEQRES   6 B 2903    C   U   G   C   G   A   U   A   A   G   C   G   U          
SEQRES   7 B 2903    C   G   G   U   A   A   G   G   U   G   A   U   A          
SEQRES   8 B 2903    U   G   A   A   C   C   G   U   U   A   U   A   A          
SEQRES   9 B 2903    C   C   G   G   C   G   A   U   U   U   C   C   G          
SEQRES  10 B 2903    A   A   U   G   G   G   G   A   A   A   C   C   C          
SEQRES  11 B 2903    A   G   U   G   U   G   U   U   U   C   G   A   C          
SEQRES  12 B 2903    A   C   A   C   U   A   U   C   A   U   U   A   A          
SEQRES  13 B 2903    C   U   G   A   A   U   C   C   A   U   A   G   G          
SEQRES  14 B 2903    U   U   A   A   U   G   A   G   G   C   G   A   A          
SEQRES  15 B 2903    C   C   G   G   G   G   G   A   A   C   U   G   A          
SEQRES  16 B 2903    A   A   C   A   U   C   U   A   A   G   U   A   C          
SEQRES  17 B 2903    C   C   C   G   A   G   G   A   A   A   A   G   A          
SEQRES  18 B 2903    A   A   U   C   A   A   C   C   G   A   G   A   U          
SEQRES  19 B 2903    U   C   C   C   C   C   A   G   U   A   G   C   G          
SEQRES  20 B 2903    G   C   G   A   G   C   G   A   A   C   G   G   G          
SEQRES  21 B 2903    G   A   G   C   A   G   C   C   C   A   G   A   G          
SEQRES  22 B 2903    C   C   U   G   A   A   U   C   A   G   U   G   U          
SEQRES  23 B 2903    G   U   G   U   G   U   U   A   G   U   G   G   A          
SEQRES  24 B 2903    A   G   C   G   U   C   U   G   G   A   A   A   G          
SEQRES  25 B 2903    G   C   G   C   G   C   G   A   U   A   C   A   G          
SEQRES  26 B 2903    G   G   U   G   A   C   A   G   C   C   C   C   G          
SEQRES  27 B 2903    U   A   C   A   C   A   A   A   A   A   U   G   C          
SEQRES  28 B 2903    A   C   A   U   G   C   U   G   U   G   A   G   C          
SEQRES  29 B 2903    U   C   G   A   U   G   A   G   U   A   G   G   G          
SEQRES  30 B 2903    C   G   G   G   A   C   A   C   G   U   G   G   U          
SEQRES  31 B 2903    A   U   C   C   U   G   U   C   U   G   A   A   U          
SEQRES  32 B 2903    A   U   G   G   G   G   G   G   A   C   C   A   U          
SEQRES  33 B 2903    C   C   U   C   C   A   A   G   G   C   U   A   A          
SEQRES  34 B 2903    A   U   A   C   U   C   C   U   G   A   C   U   G          
SEQRES  35 B 2903    A   C   C   G   A   U   A   G   U   G   A   A   C          
SEQRES  36 B 2903    C   A   G   U   A   C   C   G   U   G   A   G   G          
SEQRES  37 B 2903    G   A   A   A   G   G   C   G   A   A   A   A   G          
SEQRES  38 B 2903    A   A   C   C   C   C   G   G   C   G   A   G   G          
SEQRES  39 B 2903    G   G   A   G   U   G   A   A   A   A   A   G   A          
SEQRES  40 B 2903    A   C   C   U   G   A   A   A   C   C   G   U   G          
SEQRES  41 B 2903    U   A   C   G   U   A   C   A   A   G   C   A   G          
SEQRES  42 B 2903    U   G   G   G   A   G   C   A   C   G   C   U   U          
SEQRES  43 B 2903    A   G   G   C   G   U   G   U   G   A   C   U   G          
SEQRES  44 B 2903    C   G   U   A   C   C   U   U   U   U   G   U   A          
SEQRES  45 B 2903    U   A   A   U   G   G   G   U   C   A   G   C   G          
SEQRES  46 B 2903    A   C   U   U   A   U   A   U   U   C   U   G   U          
SEQRES  47 B 2903    A   G   C   A   A   G   G   U   U   A   A   C   C          
SEQRES  48 B 2903    G   A   A   U   A   G   G   G   G   A   G   C   C          
SEQRES  49 B 2903    G   A   A   G   G   G   A   A   A   C   C   G   A          
SEQRES  50 B 2903    G   U   C   U   U   A   A   C   U   G   G   G   C          
SEQRES  51 B 2903    G   U   U   A   A   G   U   U   G   C   A   G   G          
SEQRES  52 B 2903    G   U   A   U   A   G   A   C   C   C   G   A   A          
SEQRES  53 B 2903    A   C   C   C   G   G   U   G   A   U   C   U   A          
SEQRES  54 B 2903    G   C   C   A   U   G   G   G   C   A   G   G   U          
SEQRES  55 B 2903    U   G   A   A   G   G   U   U   G   G   G   U   A          
SEQRES  56 B 2903    A   C   A   C   U   A   A   C   U   G   G   A   G          
SEQRES  57 B 2903    G   A   C   C   G   A   A   C   C   G   A   C   U          
SEQRES  58 B 2903    A   A   U   G   U   U   G   A   A   A   A   A   U          
SEQRES  59 B 2903    U   A   G   C   G   G   A   U   G   A   C   U   U          
SEQRES  60 B 2903    G   U   G   G   C   U   G   G   G   G   G   U   G          
SEQRES  61 B 2903    A   A   A   G   G   C   C   A   A   U   C   A   A          
SEQRES  62 B 2903    A   C   C   G   G   G   A   G   A   U   A   G   C          
SEQRES  63 B 2903    U   G   G   U   U   C   U   C   C   C   C   G   A          
SEQRES  64 B 2903    A   A   G   C   U   A   U   U   U   A   G   G   U          
SEQRES  65 B 2903    A   G   C   G   C   C   U   C   G   U   G   A   A          
SEQRES  66 B 2903    U   U   C   A   U   C   U   C   C   G   G   G   G          
SEQRES  67 B 2903    G   U   A   G   A   G   C   A   C   U   G   U   U          
SEQRES  68 B 2903    U   C   G   G   C   A   A   G   G   G   G   G   U          
SEQRES  69 B 2903    C   A   U   C   C   C   G   A   C   U   U   A   C          
SEQRES  70 B 2903    C   A   A   C   C   C   G   A   U   G   C   A   A          
SEQRES  71 B 2903    A   C   U   G   C   G   A   A   U   A   C   C   G          
SEQRES  72 B 2903    G   A   G   A   A   U   G   U   U   A   U   C   A          
SEQRES  73 B 2903    C   G   G   G   A   G   A   C   A   C   A   C   G          
SEQRES  74 B 2903    G   C   G   G   G   U   G   C   U   A   A   C   G          
SEQRES  75 B 2903    U   C   C   G   U   C   G   U   G   A   A   G   A          
SEQRES  76 B 2903    G   G   G   A   A   A   C   A   A   C   C   C   A          
SEQRES  77 B 2903    G   A   C   C   G   C   C   A   G   C   U   A   A          
SEQRES  78 B 2903    G   G   U   C   C   C   A   A   A   G   U   C   A          
SEQRES  79 B 2903    U   G   G   U   U   A   A   G   U   G   G   G   A          
SEQRES  80 B 2903    A   A   C   G   A   U   G   U   G   G   G   A   A          
SEQRES  81 B 2903    G   G   C   C   C   A   G   A   C   A   G   C   C          
SEQRES  82 B 2903    A   G   G   A   U   G   U   U   G   G   C   U   U          
SEQRES  83 B 2903    A   G   A   A   G   C   A   G   C   C   A   U   C          
SEQRES  84 B 2903    A   U   U   U   A   A   A   G   A   A   A   G   C          
SEQRES  85 B 2903    G   U   A   A   U   A   G   C   U   C   A   C   U          
SEQRES  86 B 2903    G   G   U   C   G   A   G   U   C   G   G   C   C          
SEQRES  87 B 2903    U   G   C   G   C   G   G   A   A   G   A   U   G          
SEQRES  88 B 2903    U   A   A   C   G   G   G   G   C   U   A   A   A          
SEQRES  89 B 2903    C   C   A   U   G   C   A   C   C   G   A   A   G          
SEQRES  90 B 2903    C   U   G   C   G   G   C   A   G   C   G   A   C          
SEQRES  91 B 2903    G   C   U   U   A   U   G   C   G   U   U   G   U          
SEQRES  92 B 2903    U   G   G   G   U   A   G   G   G   G   A   G   C          
SEQRES  93 B 2903    G   U   U   C   U   G   U   A   A   G   C   C   U          
SEQRES  94 B 2903    G   C   G   A   A   G   G   U   G   U   G   C   U          
SEQRES  95 B 2903    G   U   G   A   G   G   C   A   U   G   C   U   G          
SEQRES  96 B 2903    G   A   G   G   U   A   U   C   A   G   A   A   G          
SEQRES  97 B 2903    U   G   C   G   A   A   U   G   C   U   G   A   C          
SEQRES  98 B 2903    A   U   A   A   G   U   A   A   C   G   A   U   A          
SEQRES  99 B 2903    A   A   G   C   G   G   G   U   G   A   A   A   A          
SEQRES 100 B 2903    G   C   C   C   G   C   U   C   G   C   C   G   G          
SEQRES 101 B 2903    A   A   G   A   C   C   A   A   G   G   G   U   U          
SEQRES 102 B 2903    C   C   U   G   U   C   C   A   A   C   G   U   U          
SEQRES 103 B 2903    A   A   U   C   G   G   G   G   C   A   G   G   G          
SEQRES 104 B 2903    U   G   A   G   U   C   G   A   C   C   C   C   U          
SEQRES 105 B 2903    A   A   G   G   C   G   A   G   G   C   C   G   A          
SEQRES 106 B 2903    A   A   G   G   C   G   U   A   G   U   C   G   A          
SEQRES 107 B 2903    U   G   G   G   A   A   A   C   A   G   G   U   U          
SEQRES 108 B 2903    A   A   U   A   U   U   C   C   U   G   U   A   C          
SEQRES 109 B 2903    U   U   G   G   U   G   U   U   A   C   U   G   C          
SEQRES 110 B 2903    G   A   A   G   G   G   G   G   G   A   C   G   G          
SEQRES 111 B 2903    A   G   A   A   G   G   C   U   A   U   G   U   U          
SEQRES 112 B 2903    G   G   C   C   G   G   G   C   G   A   C   G   G          
SEQRES 113 B 2903    U   U   G   U   C   C   C   G   G   U   U   U   A          
SEQRES 114 B 2903    A   G   C   G   U   G   U   A   G   G   C   U   G          
SEQRES 115 B 2903    G   U   U   U   U   C   C   A   G   G   C   A   A          
SEQRES 116 B 2903    A   U   C   C   G   G   A   A   A   A   U   C   A          
SEQRES 117 B 2903    A   G   G   C   U   G   A   G   G   C   G   U   G          
SEQRES 118 B 2903    A   U   G   A   C   G   A   G   G   C   A   C   U          
SEQRES 119 B 2903    A   C   G   G   U   G   C   U   G   A   A   G   C          
SEQRES 120 B 2903    A   A   C   A   A   A   U   G   C   C   C   U   G          
SEQRES 121 B 2903    C   U   U   C   C   A   G   G   A   A   A   A   G          
SEQRES 122 B 2903    C   C   U   C   U   A   A   G   C   A   U   C   A          
SEQRES 123 B 2903    G   G   U   A   A   C   A   U   C   A   A   A   U          
SEQRES 124 B 2903    C   G   U   A   C   C   C   C   A   A   A   C   C          
SEQRES 125 B 2903    G   A   C   A   C   A   G   G   U   G   G   U   C          
SEQRES 126 B 2903    A   G   G   U   A   G   A   G   A   A   U   A   C          
SEQRES 127 B 2903    C   A   A   G   G   C   G   C   U   U   G   A   G          
SEQRES 128 B 2903    A   G   A   A   C   U   C   G   G   G   U   G   A          
SEQRES 129 B 2903    A   G   G   A   A   C   U   A   G   G   C   A   A          
SEQRES 130 B 2903    A   A   U   G   G   U   G   C   C   G   U   A   A          
SEQRES 131 B 2903    C   U   U   C   G   G   G   A   G   A   A   G   G          
SEQRES 132 B 2903    C   A   C   G   C   U   G   A   U   A   U   G   U          
SEQRES 133 B 2903    A   G   G   U   G   A   G   G   U   C   C   C   U          
SEQRES 134 B 2903    C   G   C   G   G   A   U   G   G   A   G   C   U          
SEQRES 135 B 2903    G   A   A   A   U   C   A   G   U   C   G   A   A          
SEQRES 136 B 2903    G   A   U   A   C   C   A   G   C   U   G   G   C          
SEQRES 137 B 2903    U   G   C   A   A   C   U   G   U   U   U   A   U          
SEQRES 138 B 2903    U   A   A   A   A   A   C   A   C   A   G   C   A          
SEQRES 139 B 2903    C   U   G   U   G   C   A   A   A   C   A   C   G          
SEQRES 140 B 2903    A   A   A   G   U   G   G   A   C   G   U   A   U          
SEQRES 141 B 2903    A   C   G   G   U   G   U   G   A   C   G   C   C          
SEQRES 142 B 2903    U   G   C   C   C   G   G   U   G   C   C   G   G          
SEQRES 143 B 2903    A   A   G   G   U   U   A   A   U   U   G   A   U          
SEQRES 144 B 2903    G   G   G   G   U   U   A   G   C   G   C   A   A          
SEQRES 145 B 2903    G   C   G   A   A   G   C   U   C   U   U   G   A          
SEQRES 146 B 2903    U   C   G   A   A   G   C   C   C   C   G   G   U          
SEQRES 147 B 2903    A   A   A   C   G   G   C   G   G   C   C   G   U          
SEQRES 148 B 2903    A   A   C   U   A   U   A   A   C   G   G   U   C          
SEQRES 149 B 2903    C   U   A   A   G   G   U   A   G   C   G   A   A          
SEQRES 150 B 2903    A   U   U   C   C   U   U   G   U   C   G   G   G          
SEQRES 151 B 2903    U   A   A   G   U   U   C   C   G   A   C   C   U          
SEQRES 152 B 2903    G   C   A   C   G   A   A   U   G   G   C   G   U          
SEQRES 153 B 2903    A   A   U   G   A   U   G   G   C   C   A   G   G          
SEQRES 154 B 2903    C   U   G   U   C   U   C   C   A   C   C   C   G          
SEQRES 155 B 2903    A   G   A   C   U   C   A   G   U   G   A   A   A          
SEQRES 156 B 2903    U   U   G   A   A   C   U   C   G   C   U   G   U          
SEQRES 157 B 2903    G   A   A   G   A   U   G   C   A   G   U   G   U          
SEQRES 158 B 2903    A   C   C   C   G   C   G   G   C   A   A   G   A          
SEQRES 159 B 2903    C   G   G   A   A   A   G   A   C   C   C   C   G          
SEQRES 160 B 2903    U   G   A   A   C   C   U   U   U   A   C   U   A          
SEQRES 161 B 2903    U   A   G   C   U   U   G   A   C   A   C   U   G          
SEQRES 162 B 2903    A   A   C   A   U   U   G   A   G   C   C   U   U          
SEQRES 163 B 2903    G   A   U   G   U   G   U   A   G   G   A   U   A          
SEQRES 164 B 2903    G   G   U   G   G   G   A   G   G   C   U   U   U          
SEQRES 165 B 2903    G   A   A   G   U   G   U   G   G   A   C   G   C          
SEQRES 166 B 2903    C   A   G   U   C   U   G   C   A   U   G   G   A          
SEQRES 167 B 2903    G   C   C   G   A   C   C   U   U   G   A   A   A          
SEQRES 168 B 2903    U   A   C   C   A   C   C   C   U   U   U   A   A          
SEQRES 169 B 2903    U   G   U   U   U   G   A   U   G   U   U   C   U          
SEQRES 170 B 2903    A   A   C   G   U   U   G   A   C   C   C   G   U          
SEQRES 171 B 2903    A   A   U   C   C   G   G   G   U   U   G   C   G          
SEQRES 172 B 2903    G   A   C   A   G   U   G   U   C   U   G   G   U          
SEQRES 173 B 2903    G   G   G   U   A   G   U   U   U   G   A   C   U          
SEQRES 174 B 2903    G   G   G   G   C   G   G   U   C   U   C   C   U          
SEQRES 175 B 2903    C   C   U   A   A   A   G   A   G   U   A   A   C          
SEQRES 176 B 2903    G   G   A   G   G   A   G   C   A   C   G   A   A          
SEQRES 177 B 2903    G   G   U   U   G   G   C   U   A   A   U   C   C          
SEQRES 178 B 2903    U   G   G   U   C   G   G   A   C   A   U   C   A          
SEQRES 179 B 2903    G   G   A   G   G   U   U   A   G   U   G   C   A          
SEQRES 180 B 2903    A   U   G   G   C   A   U   A   A   G   C   C   A          
SEQRES 181 B 2903    G   C   U   U   G   A   C   U   G   C   G   A   G          
SEQRES 182 B 2903    C   G   U   G   A   C   G   G   C   G   C   G   A          
SEQRES 183 B 2903    G   C   A   G   G   U   G   C   G   A   A   A   G          
SEQRES 184 B 2903    C   A   G   G   U   C   A   U   A   G   U   G   A          
SEQRES 185 B 2903    U   C   C   G   G   U   G   G   U   U   C   U   G          
SEQRES 186 B 2903    A   A   U   G   G   A   A   G   G   G   C   C   A          
SEQRES 187 B 2903    U   C   G   C   U   C   A   A   C   G   G   A   U          
SEQRES 188 B 2903    A   A   A   A   G   G   U   A   C   U   C   C   G          
SEQRES 189 B 2903    G   G   G   A   U   A   A   C   A   G   G   C   U          
SEQRES 190 B 2903    G   A   U   A   C   C   G   C   C   C   A   A   G          
SEQRES 191 B 2903    A   G   U   U   C   A   U   A   U   C   G   A   C          
SEQRES 192 B 2903    G   G   C   G   G   U   G   U   U   U   G   G   C          
SEQRES 193 B 2903    A   C   C   U   C   G   A   U   G   U   C   G   G          
SEQRES 194 B 2903    C   U   C   A   U   C   A   C   A   U   C   C   U          
SEQRES 195 B 2903    G   G   G   G   C   U   G   A   A   G   U   A   G          
SEQRES 196 B 2903    G   U   C   C   C   A   A   G   G   G   U   A   U          
SEQRES 197 B 2903    G   G   C   U   G   U   U   C   G   C   C   A   U          
SEQRES 198 B 2903    U   U   A   A   A   G   U   G   G   U   A   C   G          
SEQRES 199 B 2903    C   G   A   G   C   U   G   G   G   U   U   U   A          
SEQRES 200 B 2903    G   A   A   C   G   U   C   G   U   G   A   G   A          
SEQRES 201 B 2903    C   A   G   U   U   C   G   G   U   C   C   C   U          
SEQRES 202 B 2903    A   U   C   U   G   C   C   G   U   G   G   G   C          
SEQRES 203 B 2903    G   C   U   G   G   A   G   A   A   C   U   G   A          
SEQRES 204 B 2903    G   G   G   G   G   G   C   U   G   C   U   C   C          
SEQRES 205 B 2903    U   A   G   U   A   C   G   A   G   A   G   G   A          
SEQRES 206 B 2903    C   C   G   G   A   G   U   G   G   A   C   G   C          
SEQRES 207 B 2903    A   U   C   A   C   U   G   G   U   G   U   U   C          
SEQRES 208 B 2903    G   G   G   U   U   G   U   C   A   U   G   C   C          
SEQRES 209 B 2903    A   A   U   G   G   C   A   C   U   G   C   C   C          
SEQRES 210 B 2903    G   G   U   A   G   C   U   A   A   A   U   G   C          
SEQRES 211 B 2903    G   G   A   A   G   A   G   A   U   A   A   G   U          
SEQRES 212 B 2903    G   C   U   G   A   A   A   G   C   A   U   C   U          
SEQRES 213 B 2903    A   A   G   C   A   C   G   A   A   A   C   U   U          
SEQRES 214 B 2903    G   C   C   C   C   G   A   G   A   U   G   A   G          
SEQRES 215 B 2903    U   U   C   U   C   C   C   U   G   A   C   C   C          
SEQRES 216 B 2903    U   U   U   A   A   G   G   G   U   C   C   U   G          
SEQRES 217 B 2903    A   A   G   G   A   A   C   G   U   U   G   A   A          
SEQRES 218 B 2903    G   A   C   G   A   C   G   A   C   G   U   U   G          
SEQRES 219 B 2903    A   U   A   G   G   C   C   G   G   G   U   G   U          
SEQRES 220 B 2903    G   U   A   A   G   C   G   C   A   G   C   G   A          
SEQRES 221 B 2903    U   G   C   G   U   U   G   A   G   C   U   A   A          
SEQRES 222 B 2903    C   C   G   G   U   A   C   U   A   A   U   G   A          
SEQRES 223 B 2903    A   C   C   G   U   G   A   G   G   C   U   U   A          
SEQRES 224 B 2903    A   C   C   U                                              
SEQRES   1 C  271  ALA VAL VAL LYS CYS LYS PRO THR SER PRO GLY ARG ARG          
SEQRES   2 C  271  HIS VAL VAL LYS VAL VAL ASN PRO GLU LEU HIS LYS GLY          
SEQRES   3 C  271  LYS PRO PHE ALA PRO LEU LEU GLU LYS ASN SER LYS SER          
SEQRES   4 C  271  GLY GLY ARG ASN ASN ASN GLY ARG ILE THR THR ARG HIS          
SEQRES   5 C  271  ILE GLY GLY GLY HIS LYS GLN ALA TYR ARG ILE VAL ASP          
SEQRES   6 C  271  PHE LYS ARG ASN LYS ASP GLY ILE PRO ALA VAL VAL GLU          
SEQRES   7 C  271  ARG LEU GLU TYR ASP PRO ASN ARG SER ALA ASN ILE ALA          
SEQRES   8 C  271  LEU VAL LEU TYR LYS ASP GLY GLU ARG ARG TYR ILE LEU          
SEQRES   9 C  271  ALA PRO LYS GLY LEU LYS ALA GLY ASP GLN ILE GLN SER          
SEQRES  10 C  271  GLY VAL ASP ALA ALA ILE LYS PRO GLY ASN THR LEU PRO          
SEQRES  11 C  271  MET ARG ASN ILE PRO VAL GLY SER THR VAL HIS ASN VAL          
SEQRES  12 C  271  GLU MET LYS PRO GLY LYS GLY GLY GLN LEU ALA ARG SER          
SEQRES  13 C  271  ALA GLY THR TYR VAL GLN ILE VAL ALA ARG ASP GLY ALA          
SEQRES  14 C  271  TYR VAL THR LEU ARG LEU ARG SER GLY GLU MET ARG LYS          
SEQRES  15 C  271  VAL GLU ALA ASP CYS ARG ALA THR LEU GLY GLU VAL GLY          
SEQRES  16 C  271  ASN ALA GLU HIS MET LEU ARG VAL LEU GLY LYS ALA GLY          
SEQRES  17 C  271  ALA ALA ARG TRP ARG GLY VAL ARG PRO THR VAL ARG GLY          
SEQRES  18 C  271  THR ALA MET ASN PRO VAL ASP HIS PRO HIS GLY GLY GLY          
SEQRES  19 C  271  GLU GLY ARG ASN PHE GLY LYS HIS PRO VAL THR PRO TRP          
SEQRES  20 C  271  GLY VAL GLN THR LYS GLY LYS LYS THR ARG SER ASN LYS          
SEQRES  21 C  271  ARG THR ASP LYS PHE ILE VAL ARG ARG ARG SER                  
SEQRES   1 D  209  MET ILE GLY LEU VAL GLY LYS LYS VAL GLY MET THR ARG          
SEQRES   2 D  209  ILE PHE THR GLU ASP GLY VAL SER ILE PRO VAL THR VAL          
SEQRES   3 D  209  ILE GLU VAL GLU ALA ASN ARG VAL THR GLN VAL LYS ASP          
SEQRES   4 D  209  LEU ALA ASN ASP GLY TYR ARG ALA ILE GLN VAL THR THR          
SEQRES   5 D  209  GLY ALA LYS LYS ALA ASN ARG VAL THR LYS PRO GLU ALA          
SEQRES   6 D  209  GLY HIS PHE ALA LYS ALA GLY VAL GLU ALA GLY ARG GLY          
SEQRES   7 D  209  LEU TRP GLU PHE ARG LEU ALA GLU GLY GLU GLU PHE THR          
SEQRES   8 D  209  VAL GLY GLN SER ILE SER VAL GLU LEU PHE ALA ASP VAL          
SEQRES   9 D  209  LYS LYS VAL ASP VAL THR GLY THR SER LYS GLY LYS GLY          
SEQRES  10 D  209  PHE ALA GLY THR VAL LYS ARG TRP ASN PHE ARG THR GLN          
SEQRES  11 D  209  ASP ALA THR HIS GLY ASN SER LEU SER HIS ARG VAL PRO          
SEQRES  12 D  209  GLY SER ILE GLY GLN ASN GLN THR PRO GLY LYS VAL PHE          
SEQRES  13 D  209  LYS GLY LYS LYS MET ALA GLY GLN MET GLY ASN GLU ARG          
SEQRES  14 D  209  VAL THR VAL GLN SER LEU ASP VAL VAL ARG VAL ASP ALA          
SEQRES  15 D  209  GLU ARG ASN LEU LEU LEU VAL LYS GLY ALA VAL PRO GLY          
SEQRES  16 D  209  ALA THR GLY SER ASP LEU ILE VAL LYS PRO ALA VAL LYS          
SEQRES  17 D  209  ALA                                                          
SEQRES   1 E  201  MET GLU LEU VAL LEU LYS ASP ALA GLN SER ALA LEU THR          
SEQRES   2 E  201  VAL SER GLU THR THR PHE GLY ARG ASP PHE ASN GLU ALA          
SEQRES   3 E  201  LEU VAL HIS GLN VAL VAL VAL ALA TYR ALA ALA GLY ALA          
SEQRES   4 E  201  ARG GLN GLY THR ARG ALA GLN LYS THR ARG ALA GLU VAL          
SEQRES   5 E  201  THR GLY SER GLY LYS LYS PRO TRP ARG GLN LYS GLY THR          
SEQRES   6 E  201  GLY ARG ALA ARG SER GLY SER ILE LYS SER PRO ILE TRP          
SEQRES   7 E  201  ARG SER GLY GLY VAL THR PHE ALA ALA ARG PRO GLN ASP          
SEQRES   8 E  201  HIS SER GLN LYS VAL ASN LYS LYS MET TYR ARG GLY ALA          
SEQRES   9 E  201  LEU LYS SER ILE LEU SER GLU LEU VAL ARG GLN ASP ARG          
SEQRES  10 E  201  LEU ILE VAL VAL GLU LYS PHE SER VAL GLU ALA PRO LYS          
SEQRES  11 E  201  THR LYS LEU LEU ALA GLN LYS LEU LYS ASP MET ALA LEU          
SEQRES  12 E  201  GLU ASP VAL LEU ILE ILE THR GLY GLU LEU ASP GLU ASN          
SEQRES  13 E  201  LEU PHE LEU ALA ALA ARG ASN LEU HIS LYS VAL ASP VAL          
SEQRES  14 E  201  ARG ASP ALA THR GLY ILE ASP PRO VAL SER LEU ILE ALA          
SEQRES  15 E  201  PHE ASP LYS VAL VAL MET THR ALA ASP ALA VAL LYS GLN          
SEQRES  16 E  201  VAL GLU GLU MET LEU ALA                                      
SEQRES   1 F  178  ALA LYS LEU HIS ASP TYR TYR LYS ASP GLU VAL VAL LYS          
SEQRES   2 F  178  LYS LEU MET THR GLU PHE ASN TYR ASN SER VAL MET GLN          
SEQRES   3 F  178  VAL PRO ARG VAL GLU LYS ILE THR LEU ASN MET GLY VAL          
SEQRES   4 F  178  GLY GLU ALA ILE ALA ASP LYS LYS LEU LEU ASP ASN ALA          
SEQRES   5 F  178  ALA ALA ASP LEU ALA ALA ILE SER GLY GLN LYS PRO LEU          
SEQRES   6 F  178  ILE THR LYS ALA ARG LYS SER VAL ALA GLY PHE LYS ILE          
SEQRES   7 F  178  ARG GLN GLY TYR PRO ILE GLY CYS LYS VAL THR LEU ARG          
SEQRES   8 F  178  GLY GLU ARG MET TRP GLU PHE PHE GLU ARG LEU ILE THR          
SEQRES   9 F  178  ILE ALA VAL PRO ARG ILE ARG ASP PHE ARG GLY LEU SER          
SEQRES  10 F  178  ALA LYS SER PHE ASP GLY ARG GLY ASN TYR SER MET GLY          
SEQRES  11 F  178  VAL ARG GLU GLN ILE ILE PHE PRO GLU ILE ASP TYR ASP          
SEQRES  12 F  178  LYS VAL ASP ARG VAL ARG GLY LEU ASP ILE THR ILE THR          
SEQRES  13 F  178  THR THR ALA LYS SER ASP GLU GLU GLY ARG ALA LEU LEU          
SEQRES  14 F  178  ALA ALA PHE ASP PHE PRO PHE ARG LYS                          
SEQRES   1 G  176  SER ARG VAL ALA LYS ALA PRO VAL VAL VAL PRO ALA GLY          
SEQRES   2 G  176  VAL ASP VAL LYS ILE ASN GLY GLN VAL ILE THR ILE LYS          
SEQRES   3 G  176  GLY LYS ASN GLY GLU LEU THR ARG THR LEU ASN ASP ALA          
SEQRES   4 G  176  VAL GLU VAL LYS HIS ALA ASP ASN THR LEU THR PHE GLY          
SEQRES   5 G  176  PRO ARG ASP GLY TYR ALA ASP GLY TRP ALA GLN ALA GLY          
SEQRES   6 G  176  THR ALA ARG ALA LEU LEU ASN SER MET VAL ILE GLY VAL          
SEQRES   7 G  176  THR GLU GLY PHE THR LYS LYS LEU GLN LEU VAL GLY VAL          
SEQRES   8 G  176  GLY TYR ARG ALA ALA VAL LYS GLY ASN VAL ILE ASN LEU          
SEQRES   9 G  176  SER LEU GLY PHE SER HIS PRO VAL ASP HIS GLN LEU PRO          
SEQRES  10 G  176  ALA GLY ILE THR ALA GLU CYS PRO THR GLN THR GLU ILE          
SEQRES  11 G  176  VAL LEU LYS GLY ALA ASP LYS GLN VAL ILE GLY GLN VAL          
SEQRES  12 G  176  ALA ALA ASP LEU ARG ALA TYR ARG ARG PRO GLU PRO TYR          
SEQRES  13 G  176  LYS GLY LYS GLY VAL ARG TYR ALA ASP GLU VAL VAL ARG          
SEQRES  14 G  176  THR LYS GLU ALA LYS LYS LYS                                  
SEQRES   1 H  149  MET GLN VAL ILE LEU LEU ASP LYS VAL ALA ASN LEU GLY          
SEQRES   2 H  149  SER LEU GLY ASP GLN VAL ASN VAL LYS ALA GLY TYR ALA          
SEQRES   3 H  149  ARG ASN PHE LEU VAL PRO GLN GLY LYS ALA VAL PRO ALA          
SEQRES   4 H  149  THR LYS LYS ASN ILE GLU PHE PHE GLU ALA ARG ARG ALA          
SEQRES   5 H  149  GLU LEU GLU ALA LYS LEU ALA GLU VAL LEU ALA ALA ALA          
SEQRES   6 H  149  ASN ALA ARG ALA GLU LYS ILE ASN ALA LEU GLU THR VAL          
SEQRES   7 H  149  THR ILE ALA SER LYS ALA GLY ASP GLU GLY LYS LEU PHE          
SEQRES   8 H  149  GLY SER ILE GLY THR ARG ASP ILE ALA ASP ALA VAL THR          
SEQRES   9 H  149  ALA ALA GLY VAL GLU VAL ALA LYS SER GLU VAL ARG LEU          
SEQRES  10 H  149  PRO ASN GLY VAL LEU ARG THR THR GLY GLU HIS GLU VAL          
SEQRES  11 H  149  SER PHE GLN VAL HIS SER GLU VAL PHE ALA LYS VAL ILE          
SEQRES  12 H  149  VAL ASN VAL VAL ALA GLU                                      
SEQRES   1 I  141  ALA LYS LYS VAL GLN ALA TYR VAL LYS LEU GLN VAL ALA          
SEQRES   2 I  141  ALA GLY MET ALA ASN PRO SER PRO PRO VAL GLY PRO ALA          
SEQRES   3 I  141  LEU GLY GLN GLN GLY VAL ASN ILE MET GLU PHE CYS LYS          
SEQRES   4 I  141  ALA PHE ASN ALA LYS THR ASP SER ILE GLU LYS GLY LEU          
SEQRES   5 I  141  PRO ILE PRO VAL VAL ILE THR VAL TYR ALA ASP ARG SER          
SEQRES   6 I  141  PHE THR PHE VAL THR LYS THR PRO PRO ALA ALA VAL LEU          
SEQRES   7 I  141  LEU LYS LYS ALA ALA GLY ILE LYS SER GLY SER GLY LYS          
SEQRES   8 I  141  PRO ASN LYS ASP LYS VAL GLY LYS ILE SER ARG ALA GLN          
SEQRES   9 I  141  LEU GLN GLU ILE ALA GLN THR LYS ALA ALA ASP MET THR          
SEQRES  10 I  141  GLY ALA ASP ILE GLU ALA MET THR ARG SER ILE GLU GLY          
SEQRES  11 I  141  THR ALA ARG SER MET GLY LEU VAL VAL GLU ASP                  
SEQRES   1 J  142  MET LYS THR PHE THR ALA LYS PRO GLU THR VAL LYS ARG          
SEQRES   2 J  142  ASP TRP TYR VAL VAL ASP ALA THR GLY LYS THR LEU GLY          
SEQRES   3 J  142  ARG LEU ALA THR GLU LEU ALA ARG ARG LEU ARG GLY LYS          
SEQRES   4 J  142  HIS LYS ALA GLU TYR THR PRO HIS VAL ASP THR GLY ASP          
SEQRES   5 J  142  TYR ILE ILE VAL LEU ASN ALA ASP LYS VAL ALA VAL THR          
SEQRES   6 J  142  GLY ASN LYS ARG THR ASP LYS VAL TYR TYR HIS HIS THR          
SEQRES   7 J  142  GLY HIS ILE GLY GLY ILE LYS GLN ALA THR PHE GLU GLU          
SEQRES   8 J  142  MET ILE ALA ARG ARG PRO GLU ARG VAL ILE GLU ILE ALA          
SEQRES   9 J  142  VAL LYS GLY MET LEU PRO LYS GLY PRO LEU GLY ARG ALA          
SEQRES  10 J  142  MET PHE ARG LYS LEU LYS VAL TYR ALA GLY ASN GLU HIS          
SEQRES  11 J  142  ASN HIS ALA ALA GLN GLN PRO GLN VAL LEU ASP ILE              
SEQRES   1 K  121  MET ILE GLN GLU GLN THR MET LEU ASN VAL ALA ASP ASN          
SEQRES   2 K  121  SER GLY ALA ARG ARG VAL MET CYS ILE LYS VAL LEU GLY          
SEQRES   3 K  121  GLY SER HIS ARG ARG TYR ALA GLY VAL GLY ASP ILE ILE          
SEQRES   4 K  121  LYS ILE THR ILE LYS GLU ALA ILE PRO ARG GLY LYS VAL          
SEQRES   5 K  121  LYS LYS GLY ASP VAL LEU LYS ALA VAL VAL VAL ARG THR          
SEQRES   6 K  121  LYS LYS GLY VAL ARG ARG PRO ASP GLY SER VAL ILE ARG          
SEQRES   7 K  121  PHE ASP GLY ASN ALA CYS VAL LEU LEU ASN ASN ASN SER          
SEQRES   8 K  121  GLU GLN PRO ILE GLY THR ARG ILE PHE GLY PRO VAL THR          
SEQRES   9 K  121  ARG GLU LEU ARG SER GLU LYS PHE MET LYS ILE ILE SER          
SEQRES  10 K  121  LEU ALA PRO GLU                                              
SEQRES   1 L  143  ARG LEU ASN THR LEU SER PRO ALA GLU GLY SER LYS LYS          
SEQRES   2 L  143  ALA GLY LYS ARG LEU GLY ARG GLY ILE GLY SER GLY LEU          
SEQRES   3 L  143  GLY LYS THR GLY GLY ARG GLY HIS LYS GLY GLN LYS SER          
SEQRES   4 L  143  ARG SER GLY GLY GLY VAL ARG ARG GLY PHE GLU GLY GLY          
SEQRES   5 L  143  GLN MET PRO LEU TYR ARG ARG LEU PRO LYS PHE GLY PHE          
SEQRES   6 L  143  THR SER ARG LYS ALA ALA ILE THR ALA GLU ILE ARG LEU          
SEQRES   7 L  143  SER ASP LEU ALA LYS VAL GLU GLY GLY VAL VAL ASP LEU          
SEQRES   8 L  143  ASN THR LEU LYS ALA ALA ASN ILE ILE GLY ILE GLN ILE          
SEQRES   9 L  143  GLU PHE ALA LYS VAL ILE LEU ALA GLY GLU VAL THR THR          
SEQRES  10 L  143  PRO VAL THR VAL ARG GLY LEU ARG VAL THR LYS GLY ALA          
SEQRES  11 L  143  ARG ALA ALA ILE GLU ALA ALA GLY GLY LYS ILE GLU GLU          
SEQRES   1 M  136  MET LEU GLN PRO LYS ARG THR LYS PHE ARG LYS MET HIS          
SEQRES   2 M  136  LYS GLY ARG ASN ARG GLY LEU ALA GLN GLY THR ASP VAL          
SEQRES   3 M  136  SER PHE GLY SER PHE GLY LEU LYS ALA VAL GLY ARG GLY          
SEQRES   4 M  136  ARG LEU THR ALA ARG GLN ILE GLU ALA ALA ARG ARG ALA          
SEQRES   5 M  136  MET THR ARG ALA VAL LYS ARG GLN GLY LYS ILE TRP ILE          
SEQRES   6 M  136  ARG VAL PHE PRO ASP LYS PRO ILE THR GLU LYS PRO LEU          
SEQRES   7 M  136  ALA VAL ARG MET GLY LYS GLY LYS GLY ASN VAL GLU TYR          
SEQRES   8 M  136  TRP VAL ALA LEU ILE GLN PRO GLY LYS VAL LEU TYR GLU          
SEQRES   9 M  136  MET ASP GLY VAL PRO GLU GLU LEU ALA ARG GLU ALA PHE          
SEQRES  10 M  136  LYS LEU ALA ALA ALA LYS LEU PRO ILE LYS THR THR PHE          
SEQRES  11 M  136  VAL THR LYS THR VAL MET                                      
SEQRES   1 N  120  MET ARG HIS ARG LYS SER GLY ARG GLN LEU ASN ARG ASN          
SEQRES   2 N  120  SER SER HIS ARG GLN ALA MET PHE ARG ASN MET ALA GLY          
SEQRES   3 N  120  SER LEU VAL ARG HIS GLU ILE ILE LYS THR THR LEU PRO          
SEQRES   4 N  120  LYS ALA LYS GLU LEU ARG ARG VAL VAL GLU PRO LEU ILE          
SEQRES   5 N  120  THR LEU ALA LYS THR ASP SER VAL ALA ASN ARG ARG LEU          
SEQRES   6 N  120  ALA PHE ALA ARG THR ARG ASP ASN GLU ILE VAL ALA LYS          
SEQRES   7 N  120  LEU PHE ASN GLU LEU GLY PRO ARG PHE ALA SER ARG ALA          
SEQRES   8 N  120  GLY GLY TYR THR ARG ILE LEU LYS CYS GLY PHE ARG ALA          
SEQRES   9 N  120  GLY ASP ASN ALA PRO MET ALA TYR ILE GLU LEU VAL ASP          
SEQRES  10 N  120  ARG SER GLU                                                  
SEQRES   1 O  116  ASP LYS LYS SER ALA ARG ILE ARG ARG ALA THR ARG ALA          
SEQRES   2 O  116  ARG ARG LYS LEU GLN GLU LEU GLY ALA THR ARG LEU VAL          
SEQRES   3 O  116  VAL HIS ARG THR PRO ARG HIS ILE TYR ALA GLN VAL ILE          
SEQRES   4 O  116  ALA PRO ASN GLY SER GLU VAL LEU VAL ALA ALA SER THR          
SEQRES   5 O  116  VAL GLU LYS ALA ILE ALA GLU GLN LEU LYS TYR THR GLY          
SEQRES   6 O  116  ASN LYS ASP ALA ALA ALA ALA VAL GLY LYS ALA VAL ALA          
SEQRES   7 O  116  GLU ARG ALA LEU GLU LYS GLY ILE LYS ASP VAL SER PHE          
SEQRES   8 O  116  ASP ARG SER GLY PHE GLN TYR HIS GLY ARG VAL GLN ALA          
SEQRES   9 O  116  LEU ALA ASP ALA ALA ARG GLU ALA GLY LEU GLN PHE              
SEQRES   1 P  114  SER ASN ILE ILE LYS GLN LEU GLU GLN GLU GLN MET LYS          
SEQRES   2 P  114  GLN ASP VAL PRO SER PHE ARG PRO GLY ASP THR VAL GLU          
SEQRES   3 P  114  VAL LYS VAL TRP VAL VAL GLU GLY SER LYS LYS ARG LEU          
SEQRES   4 P  114  GLN ALA PHE GLU GLY VAL VAL ILE ALA ILE ARG ASN ARG          
SEQRES   5 P  114  GLY LEU HIS SER ALA PHE THR VAL ARG LYS ILE SER ASN          
SEQRES   6 P  114  GLY GLU GLY VAL GLU ARG VAL PHE GLN THR HIS SER PRO          
SEQRES   7 P  114  VAL VAL ASP SER ILE SER VAL LYS ARG ARG GLY ALA VAL          
SEQRES   8 P  114  ARG LYS ALA LYS LEU TYR TYR LEU ARG GLU ARG THR GLY          
SEQRES   9 P  114  LYS ALA ALA ARG ILE LYS GLU ARG LEU ASN                      
SEQRES   1 Q  117  ALA ARG VAL LYS ARG GLY VAL ILE ALA ARG ALA ARG HIS          
SEQRES   2 Q  117  LYS LYS ILE LEU LYS GLN ALA LYS GLY TYR TYR GLY ALA          
SEQRES   3 Q  117  ARG SER ARG VAL TYR ARG VAL ALA PHE GLN ALA VAL ILE          
SEQRES   4 Q  117  LYS ALA GLY GLN TYR ALA TYR ARG ASP ARG ARG GLN ARG          
SEQRES   5 Q  117  LYS ARG GLN PHE ARG GLN LEU TRP ILE ALA ARG ILE ASN          
SEQRES   6 Q  117  ALA ALA ALA ARG GLN ASN GLY ILE SER TYR SER LYS PHE          
SEQRES   7 Q  117  ILE ASN GLY LEU LYS LYS ALA SER VAL GLU ILE ASP ARG          
SEQRES   8 Q  117  LYS ILE LEU ALA ASP ILE ALA VAL PHE ASP LYS VAL ALA          
SEQRES   9 Q  117  PHE THR ALA LEU VAL GLU LYS ALA LYS ALA ALA LEU ALA          
SEQRES   1 R  103  MET TYR ALA VAL PHE GLN SER GLY GLY LYS GLN HIS ARG          
SEQRES   2 R  103  VAL SER GLU GLY GLN THR VAL ARG LEU GLU LYS LEU ASP          
SEQRES   3 R  103  ILE ALA THR GLY GLU THR VAL GLU PHE ALA GLU VAL LEU          
SEQRES   4 R  103  MET ILE ALA ASN GLY GLU GLU VAL LYS ILE GLY VAL PRO          
SEQRES   5 R  103  PHE VAL ASP GLY GLY VAL ILE LYS ALA GLU VAL VAL ALA          
SEQRES   6 R  103  HIS GLY ARG GLY GLU LYS VAL LYS ILE VAL LYS PHE ARG          
SEQRES   7 R  103  ARG ARG LYS HIS TYR ARG LYS GLN GLN GLY HIS ARG GLN          
SEQRES   8 R  103  TRP PHE THR ASP VAL LYS ILE THR GLY ILE SER ALA              
SEQRES   1 S  110  MET GLU THR ILE ALA LYS HIS ARG HIS ALA ARG SER SER          
SEQRES   2 S  110  ALA GLN LYS VAL ARG LEU VAL ALA ASP LEU ILE ARG GLY          
SEQRES   3 S  110  LYS LYS VAL SER GLN ALA LEU ASP ILE LEU THR TYR THR          
SEQRES   4 S  110  ASN LYS LYS ALA ALA VAL LEU VAL LYS LYS VAL LEU GLU          
SEQRES   5 S  110  SER ALA ILE ALA ASN ALA GLU HIS ASN ASP GLY ALA ASP          
SEQRES   6 S  110  ILE ASP ASP LEU LYS VAL THR LYS ILE PHE VAL ASP GLU          
SEQRES   7 S  110  GLY PRO SER MET LYS ARG ILE MET PRO ARG ALA LYS GLY          
SEQRES   8 S  110  ARG ALA ASP ARG ILE LEU LYS ARG THR SER HIS ILE THR          
SEQRES   9 S  110  VAL VAL VAL SER ASP ARG                                      
SEQRES   1 T   93  MET ILE ARG GLU GLU ARG LEU LEU LYS VAL LEU ARG ALA          
SEQRES   2 T   93  PRO HIS VAL SER GLU LYS ALA SER THR ALA MET GLU LYS          
SEQRES   3 T   93  SER ASN THR ILE VAL LEU LYS VAL ALA LYS ASP ALA THR          
SEQRES   4 T   93  LYS ALA GLU ILE LYS ALA ALA VAL GLN LYS LEU PHE GLU          
SEQRES   5 T   93  VAL GLU VAL GLU VAL VAL ASN THR LEU VAL VAL LYS GLY          
SEQRES   6 T   93  LYS VAL LYS ARG HIS GLY GLN ARG ILE GLY ARG ARG SER          
SEQRES   7 T   93  ASP TRP LYS LYS ALA TYR VAL THR LEU LYS GLU GLY GLN          
SEQRES   8 T   93  ASN LEU                                                      
SEQRES   1 U  102  ALA ALA LYS ILE ARG ARG ASP ASP GLU VAL ILE VAL LEU          
SEQRES   2 U  102  THR GLY LYS ASP LYS GLY LYS ARG GLY LYS VAL LYS ASN          
SEQRES   3 U  102  VAL LEU SER SER GLY LYS VAL ILE VAL GLU GLY ILE ASN          
SEQRES   4 U  102  LEU VAL LYS LYS HIS GLN LYS PRO VAL PRO ALA LEU ASN          
SEQRES   5 U  102  GLN PRO GLY GLY ILE VAL GLU LYS GLU ALA ALA ILE GLN          
SEQRES   6 U  102  VAL SER ASN VAL ALA ILE PHE ASN ALA ALA THR GLY LYS          
SEQRES   7 U  102  ALA ASP ARG VAL GLY PHE ARG PHE GLU ASP GLY LYS LYS          
SEQRES   8 U  102  VAL ARG PHE PHE LYS SER ASN SER GLU THR ILE                  
SEQRES   1 V   77    C   G   G   C   A   C   G   U   A   G   C   G   C          
SEQRES   2 V   77    A   G   C   C   U   G   G   U   A   G   C   G   C          
SEQRES   3 V   77    A   C   C   G   U   C   A   U   G   G   G   G   U          
SEQRES   4 V   77    G   U   C   G   G   G   G   G   U   C   G   G   A          
SEQRES   5 V   77    G   G 5MU   U   C   A   A   A   U   C   C   U   C          
SEQRES   6 V   77    U   C   G   U   G   C   C   G   A   C   C   A              
SEQRES   1 W   94  MET PHE THR ILE ASN ALA GLU VAL ARG LYS GLU GLN GLY          
SEQRES   2 W   94  LYS GLY ALA SER ARG ARG LEU ARG ALA ALA ASN LYS PHE          
SEQRES   3 W   94  PRO ALA ILE ILE TYR GLY GLY LYS GLU ALA PRO LEU ALA          
SEQRES   4 W   94  ILE GLU LEU ASP HIS ASP LYS VAL MET ASN MET GLN ALA          
SEQRES   5 W   94  LYS ALA GLU PHE TYR SER GLU VAL LEU THR ILE VAL VAL          
SEQRES   6 W   94  ASP GLY LYS GLU ILE LYS VAL LYS ALA GLN ASP VAL GLN          
SEQRES   7 W   94  ARG HIS PRO TYR LYS PRO LYS LEU GLN HIS ILE ASP PHE          
SEQRES   8 W   94  VAL ARG ALA                                                  
SEQRES   1 X   11    A   A   A   A   C   C   C   A   G   U   A                  
SEQRES   1 Y   79  GLY GLY SER THR ARG ASN GLY ARG ASP SER GLU ALA LYS          
SEQRES   2 Y   79  ARG LEU GLY VAL LYS ARG PHE GLY GLY GLU SER VAL LEU          
SEQRES   3 Y   79  ALA GLY SER ILE ILE VAL ARG GLN ARG GLY THR LYS PHE          
SEQRES   4 Y   79  HIS ALA GLY ALA ASN VAL GLY CYS GLY ARG ASP HIS THR          
SEQRES   5 Y   79  LEU PHE ALA LYS ALA ASP GLY LYS VAL LYS PHE GLU VAL          
SEQRES   6 Y   79  LYS GLY PRO LYS ASN ARG LYS PHE ILE SER ILE GLU ALA          
SEQRES   7 Y   79  GLU                                                          
SEQRES   1 Z   20  ALA ALA ALA ALA ALA ALA ALA ALA ALA ALA ALA ALA ALA          
SEQRES   2 Z   20  ALA ALA ALA ALA ALA ALA ALA                                  
MODRES 2WWQ 5MU V   54    U  5-METHYLURIDINE 5'-MONOPHOSPHATE                   
HET    5MU  V  54      20                                                       
HETNAM     5MU 5-METHYLURIDINE 5'-MONOPHOSPHATE                                 
FORMUL  31  5MU    C10 H15 N2 O9 P                                              
HELIX    1   1 LYS 0   53  GLY 0   62  1                                  10    
HELIX    2   2 GLY 0   62  LEU 0   67  1                                   6    
HELIX    3   3 MET 1    1  ARG 1    7  1                                   7    
HELIX    4   4 LYS 1    9  LEU 1   22  1                                  14    
HELIX    5   5 GLN 1   25  ALA 1   33  1                                   9    
HELIX    6   6 GLN 1   39  LEU 1   42  5                                   4    
HELIX    7   7 LEU 1   43  LEU 1   56  1                                  14    
HELIX    8   8 HIS 2   19  LEU 2   26  1                                   8    
HELIX    9   9 ALA 2   42  VAL 2   50  1                                   9    
HELIX   10  10 SER 2   51  VAL 2   54  5                                   4    
HELIX   11  11 THR 3    8  MET 3   14  1                                   7    
HELIX   12  12 ARG 3   15  ASP 3   19  5                                   5    
HELIX   13  13 THR 5    5  GLU 5   13  1                                   9    
HELIX   14  14 ASP 5   22  LEU 5   33  1                                  12    
HELIX   15  15 ASN 5   83  GLY 5   91  1                                   9    
HELIX   16  16 MET 5   97  GLY 5  107  1                                  11    
HELIX   17  17 SER 5  117  VAL 5  124  1                                   8    
HELIX   18  18 VAL 5  149  GLY 5  159  1                                  11    
HELIX   19  19 ASP 5  181  ALA 5  199  1                                  19    
HELIX   20  20 SER 6    8  ARG 6   14  1                                   7    
HELIX   21  21 LYS 6   25  LYS 6   37  1                                  13    
HELIX   22  22 GLY 7    8  ARG 7   12  5                                   5    
HELIX   23  23 ALA 7   36  HIS 7   42  1                                   7    
HELIX   24  24 ASP 7   53  VAL 7   57  5                                   5    
HELIX   25  25 GLU 8   30  HIS 8   33  5                                   4    
HELIX   26  26 PHE C   29  LEU C   33  5                                   5    
HELIX   27  27 LYS C  206  TRP C  212  1                                   7    
HELIX   28  28 ARG C  220  MET C  224  5                                   5    
HELIX   29  29 ASN C  225  HIS C  229  5                                   5    
HELIX   30  30 ARG C  261  LYS C  264  5                                   4    
HELIX   31  31 LYS D   62  LYS D   70  1                                   9    
HELIX   32  32 SER D   97  ASP D  103  5                                   7    
HELIX   33  33 ASN E   24  GLY E   38  1                                  15    
HELIX   34  34 ASN E   97  ILE E  108  1                                  12    
HELIX   35  35 ILE E  108  VAL E  113  1                                   6    
HELIX   36  36 LYS E  132  ASP E  140  1                                   9    
HELIX   37  37 ASP E  154  ARG E  162  1                                   9    
HELIX   38  38 ASP E  176  ALA E  182  1                                   7    
HELIX   39  39 THR E  189  LEU E  200  1                                  12    
HELIX   40  40 ALA F    1  ASP F    9  1                                   9    
HELIX   41  41 ASP F    9  PHE F   19  1                                  11    
HELIX   42  42 LYS F   47  SER F   60  1                                  14    
HELIX   43  43 ARG F   91  PHE F   99  1                                   9    
HELIX   44  44 SER F  161  ALA F  170  1                                  10    
HELIX   45  45 SER G    1  ALA G    6  5                                   6    
HELIX   46  46 TRP G   61  VAL G   78  1                                  18    
HELIX   47  47 ASP G  136  ALA G  149  1                                  14    
HELIX   48  48 LYS H   42  LEU H   58  1                                  17    
HELIX   49  49 ALA H   63  ALA H   74  1                                  12    
HELIX   50  50 GLY H   95  ILE H   99  5                                   5    
HELIX   51  51 GLY I   24  GLN I   29  1                                   6    
HELIX   52  52 ASN I   33  ASP I   46  1                                  14    
HELIX   53  53 PRO I   74  GLY I   84  1                                  11    
HELIX   54  54 SER I  101  ALA I  113  1                                  13    
HELIX   55  55 ASP I  120  MET I  135  1                                  16    
HELIX   56  56 LEU J   28  ARG J   37  1                                  10    
HELIX   57  57 THR J   88  ARG J   95  1                                   8    
HELIX   58  58 GLU J   98  GLY J  107  1                                  10    
HELIX   59  59 GLY J  112  LYS J  121  1                                  10    
HELIX   60  60 HIS J  132  GLN J  136  5                                   5    
HELIX   61  61 THR K  104  ARG K  108  5                                   5    
HELIX   62  62 LYS K  114  LEU K  118  5                                   5    
HELIX   63  63 PRO L   56  ARG L   60  5                                   5    
HELIX   64  64 SER L   80  LEU L   82  5                                   3    
HELIX   65  65 ALA M   43  LYS M   58  1                                  16    
HELIX   66  66 PRO M  109  ALA M  121  1                                  13    
HELIX   67  67 ASN N   13  GLU N   32  1                                  20    
HELIX   68  68 LEU N   38  LYS N   56  1                                  19    
HELIX   69  69 VAL N   60  LEU N   65  1                                   6    
HELIX   70  70 ALA N   66  ALA N   68  5                                   3    
HELIX   71  71 GLU N   74  GLU N   82  1                                   9    
HELIX   72  72 ASP O    2  ARG O   10  1                                   9    
HELIX   73  73 ARG O   13  GLY O   22  1                                  10    
HELIX   74  74 GLU O   55  GLU O   60  1                                   6    
HELIX   75  75 ALA O   73  LEU O   83  1                                  11    
HELIX   76  76 ASN P    2  GLU P   10  1                                   9    
HELIX   77  77 TYR P   97  THR P  103  1                                   7    
HELIX   78  78 ILE Q    8  GLN Q   19  1                                  12    
HELIX   79  79 GLY Q   25  VAL Q   30  1                                   6    
HELIX   80  80 TYR Q   31  ALA Q   34  5                                   4    
HELIX   81  81 PHE Q   35  ASN Q   71  1                                  37    
HELIX   82  82 SER Q   74  SER Q   86  1                                  13    
HELIX   83  83 ASP Q  101  ALA Q  117  1                                  17    
HELIX   84  84 SER S   13  ARG S   25  1                                  13    
HELIX   85  85 ILE S   35  THR S   39  5                                   5    
HELIX   86  86 ALA S   43  HIS S   60  1                                  18    
HELIX   87  87 GLU T    4  LEU T    8  5                                   5    
HELIX   88  88 THR T   22  SER T   27  1                                   6    
HELIX   89  89 LYS T   40  LEU T   50  1                                  11    
HELIX   90  90 GLY W   13  ALA W   22  1                                  10    
HELIX   91  91 ASP W   43  LYS W   53  1                                  11    
HELIX   92  92 ALA W   54  SER W   58  5                                   5    
SHEET    1  0A 2 HIS 0  33  TRP 0  38  0                                        
SHEET    2  0A 2 PHE 0  45  VAL 0  50 -1  O  VAL 0  46   N  PHE 0  37           
SHEET    1  2A 2 THR 2   3  ILE 2   6  0                                        
SHEET    2  2A 2 VAL 2  35  GLU 2  38 -1  O  VAL 2  35   N  ILE 2   6           
SHEET    1  3A 2 LEU 3  27  SER 3  28  0                                        
SHEET    2  3A 2 HIS 3  37  LEU 3  38 -1  O  HIS 3  37   N  SER 3  28           
SHEET    1  4A 4 PHE 4  19  LYS 4  24  0                                        
SHEET    2  4A 4 GLU 4   6  SER 4  12 -1  O  GLU 4   6   N  LYS 4  24           
SHEET    3  4A 4 GLN 4  44  LYS 4  49 -1  O  LYS 4  49   N  VAL 4  11           
SHEET    4  4A 4 LEU 4  35  ASP 4  39 -1  O  LEU 4  35   N  TYR 4  48           
SHEET    1  5A 5 GLN 5  20  TYR 5  21  0                                        
SHEET    2  5A 5 GLY 5 221  VAL 5 224  1  O  ALA 5 223   N  TYR 5  21           
SHEET    3  5A 5 ILE 5 209  THR 5 216 -1  O  VAL 5 212   N  VAL 5 224           
SHEET    4  5A 5 SER 5  41  LEU 5  48 -1  O  ASP 5  43   N  SER 5 215           
SHEET    5  5A 5 ILE 5 170  LYS 5 177 -1  O  ILE 5 171   N  VAL 5  46           
SHEET    1  5B 2 GLY 5  61  VAL 5  64  0                                        
SHEET    2  5B 2 GLN 5 160  TYR 5 163 -1  O  VAL 5 161   N  THR 5  63           
SHEET    1  5C 3 LEU 5  94  VAL 5  95  0                                        
SHEET    2  5C 3 VAL 5  75  PHE 5  78  1  N  VAL 5  77   O  LEU 5  94           
SHEET    3  5C 3 VAL 5 113  ALA 5 116  1  O  VAL 5 113   N  ALA 5  76           
SHEET    1  7A 2 LYS 7  22  HIS 7  23  0                                        
SHEET    2  7A 2 ALA 7  47  MET 7  48 -1  O  ALA 7  47   N  HIS 7  23           
SHEET    1  8A 2 LYS 8   2  VAL 8   3  0                                        
SHEET    2  8A 2 GLN 8  35  GLN 8  37  1  N  ARG 8  36   O  LYS 8   2           
SHEET    1  8B 2 VAL 8  17  LYS 8  18  0                                        
SHEET    2  8B 2 ILE 8  23  ARG 8  24 -1  O  ARG 8  24   N  VAL 8  17           
SHEET    1  CA 2 VAL C   3  LYS C   4  0                                        
SHEET    2  CA 2 VAL C  16  LYS C  17 -1  O  LYS C  17   N  VAL C   3           
SHEET    1  CB 3 ALA C  75  VAL C  77  0                                        
SHEET    2  CB 3 ALA C  91  TYR C  95 -1  O  LEU C  94   N  VAL C  76           
SHEET    3  CB 3 ARG C 100  ILE C 103 -1  O  ARG C 101   N  VAL C  93           
SHEET    1  CC 8 GLN C 116  SER C 117  0                                        
SHEET    2  CC 8 ASN C 127  PRO C 130  1  N  THR C 128   O  GLN C 116           
SHEET    3  CC 8 ARG C 188  LEU C 191 -1  O  ALA C 189   N  LEU C 129           
SHEET    4  CC 8 THR C 139  HIS C 141 -1  O  HIS C 141   N  THR C 190           
SHEET    5  CC 8 VAL C 161  ALA C 165 -1  O  VAL C 161   N  VAL C 140           
SHEET    6  CC 8 VAL C 171  LEU C 175 -1  O  THR C 172   N  ALA C 165           
SHEET    7  CC 8 GLU C 179  VAL C 183 -1  O  GLU C 179   N  LEU C 175           
SHEET    8  CC 8 ILE C 266  ARG C 268 -1  N  VAL C 267   O  MET C 180           
SHEET    1  DA 5 VAL D 177  ASP D 181  0                                        
SHEET    2  DA 5 LEU D 186  VAL D 189 -1  O  LEU D 186   N  ASP D 181           
SHEET    3  DA 5 SER D  21  GLU D  28 -1  O  THR D  25   N  VAL D 189           
SHEET    4  DA 5 GLY D   6  PHE D  15 -1  O  LYS D   7   N  GLU D  28           
SHEET    5  DA 5 ASP D 200  LEU D 201 -1  O  LEU D 201   N  GLY D   6           
SHEET    1  DB 3 VAL D  34  VAL D  37  0                                        
SHEET    2  DB 3 ALA D  47  VAL D  50 -1  O  GLN D  49   N  THR D  35           
SHEET    3  DB 3 PHE D  82  ARG D  83 -1  O  PHE D  82   N  ILE D  48           
SHEET    1  DC 2 GLY D 111  THR D 112  0                                        
SHEET    2  DC 2 ARG D 169  VAL D 170 -1  O  VAL D 170   N  GLY D 111           
SHEET    1  EA 2 LEU E 118  VAL E 120  0                                        
SHEET    2  EA 2 VAL E 186  MET E 188  1  O  VAL E 186   N  ILE E 119           
SHEET    1  FA 5 LEU F  65  LYS F  68  0                                        
SHEET    2  FA 5 PRO F  83  THR F  89 -1  N  ILE F  84   O  THR F  67           
SHEET    3  FA 5 THR F  34  MET F  37 -1  O  LEU F  35   N  VAL F  88           
SHEET    4  FA 5 ASP F 152  THR F 154 -1  O  ASP F 152   N  ASN F  36           
SHEET    5  FA 5 SER F 128  GLY F 130 -1  O  MET F 129   N  ILE F 153           
SHEET    1  GA 2 ASP G  15  ILE G  18  0                                        
SHEET    2  GA 2 ILE G  23  LYS G  26 -1  O  THR G  24   N  LYS G  17           
SHEET    1  HA 3 GLN H  18  ASN H  20  0                                        
SHEET    2  HA 3 GLN H   2  LEU H   5 -1  O  VAL H   3   N  VAL H  19           
SHEET    3  HA 3 ALA H  36  ALA H  39 -1  O  VAL H  37   N  ILE H   4           
SHEET    1  HB 2 GLN H 133  HIS H 135  0                                        
SHEET    2  HB 2 VAL H 138  PHE H 139 -1  O  VAL H 138   N  VAL H 134           
SHEET    1  IA 3 VAL I   8  VAL I  12  0                                        
SHEET    2  IA 3 ILE I  54  VAL I  60 -1  O  ILE I  54   N  VAL I  12           
SHEET    3  IA 3 PHE I  66  THR I  70 -1  O  THR I  67   N  THR I  59           
SHEET    1  IB 2 GLY I  98  LYS I  99  0                                        
SHEET    2  IB 2 LEU I 137  VAL I 138  1  N  VAL I 138   O  GLY I  98           
SHEET    1  JA 2 TYR J  16  VAL J  17  0                                        
SHEET    2  JA 2 GLN J 138  VAL J 139  1  O  GLN J 138   N  VAL J  17           
SHEET    1  JB 2 ILE J  54  ILE J  55  0                                        
SHEET    2  JB 2 LEU J 122  LYS J 123  1  N  LYS J 123   O  ILE J  54           
SHEET    1  KA 5 ASN K   9  VAL K  10  0                                        
SHEET    2  KA 5 ALA K  83  LEU K  87  1  N  CYS K  84   O  ASN K   9           
SHEET    3  KA 5 VAL K  57  VAL K  62 -1  O  LYS K  59   N  LEU K  87           
SHEET    4  KA 5 ILE K  38  ILE K  43 -1  O  ILE K  39   N  ALA K  60           
SHEET    5  KA 5 VAL K  19  LYS K  23 -1  O  MET K  20   N  THR K  42           
SHEET    1  KB 3 VAL K  69  ARG K  71  0                                        
SHEET    2  KB 3 SER K  75  PHE K  79 -1  O  SER K  75   N  ARG K  71           
SHEET    3  KB 3 VAL P  69  ARG P  71 -1  O  GLU P  70   N  ARG K  78           
SHEET    1  LA 3 THR L  74  ARG L  78  0                                        
SHEET    2  LA 3 PHE L 107  ILE L 111  1  O  PHE L 107   N  ALA L  75           
SHEET    3  LA 3 ARG L 126  VAL L 127  1  O  ARG L 126   N  VAL L 110           
SHEET    1  MA 4 ILE M  63  ILE M  65  0                                        
SHEET    2  MA 4 TYR M 103  MET M 105 -1  O  GLU M 104   N  TRP M  64           
SHEET    3  MA 4 PHE M  31  VAL M  36 -1  O  PHE M  31   N  MET M 105           
SHEET    4  MA 4 LYS M 127  VAL M 131 -1  O  LYS M 127   N  VAL M  36           
SHEET    1  MB 2 GLY M  39  LEU M  41  0                                        
SHEET    2  MB 2 ALA M  94  ILE M  96 -1  O  ALA M  94   N  LEU M  41           
SHEET    1  MC 2 THR M  74  GLU M  75  0                                        
SHEET    2  MC 2 ASN M  88  VAL M  89 -1  O  ASN M  88   N  GLU M  75           
SHEET    1  NA 3 ILE N  33  THR N  37  0                                        
SHEET    2  NA 3 MET N 110  GLU N 114 -1  O  ALA N 111   N  THR N  36           
SHEET    3  NA 3 LYS N  99  GLY N 101 -1  N  CYS N 100   O  MET N 110           
SHEET    1  OA 4 VAL O  47  SER O  52  0                                        
SHEET    2  OA 4 ILE O  35  ILE O  40 -1  O  ALA O  37   N  ALA O  51           
SHEET    3  OA 4 THR O  24  ARG O  30 -1  O  ARG O  25   N  ILE O  40           
SHEET    4  OA 4 VAL O  90  ASP O  93  1  O  SER O  91   N  LEU O  26           
SHEET    1  PA 3 LEU P  39  PHE P  42  0                                        
SHEET    2  PA 3 GLU P  26  TRP P  30 -1  N  VAL P  27   O  PHE P  42           
SHEET    3  PA 3 SER P  82  SER P  84 -1  O  SER P  82   N  LYS P  28           
SHEET    1  PB 2 GLY P  89  ALA P  90  0                                        
SHEET    2  PB 2 LYS P 110  GLU P 111 -1  O  LYS P 110   N  ALA P  90           
SHEET    1  RA 2 PHE R   5  GLN R   6  0                                        
SHEET    2  RA 2 GLN R  11  HIS R  12 -1  O  HIS R  12   N  PHE R   5           
SHEET    1  RB 3 VAL R  20  GLU R  23  0                                        
SHEET    2  RB 3 TRP R  92  VAL R  96 -1  O  THR R  94   N  LEU R  22           
SHEET    3  RB 3 GLY R  67  ARG R  68 -1  O  GLY R  67   N  PHE R  93           
SHEET    1  RC 2 VAL R  72  ARG R  78  0                                        
SHEET    2  RC 2 TYR R  83  HIS R  89 -1  O  TYR R  83   N  ARG R  78           
SHEET    1  SA 3 LYS S   6  ARG S  11  0                                        
SHEET    2  SA 3 THR S 100  ASP S 109 -1  O  SER S 101   N  ALA S  10           
SHEET    3  SA 3 LEU S  69  GLU S  78 -1  N  LYS S  70   O  SER S 108           
SHEET    1  SB 2 MET S  82  PRO S  87  0                                        
SHEET    2  SB 2 ALA S  93  LYS S  98 -1  O  ASP S  94   N  MET S  86           
SHEET    1  TA 3 VAL T  31  LYS T  33  0                                        
SHEET    2  TA 3 TRP T  80  TYR T  84 -1  O  ALA T  83   N  LEU T  32           
SHEET    3  TA 3 ASN T  59  VAL T  63 -1  O  ASN T  59   N  TYR T  84           
SHEET    1  UA 4 GLU U   9  VAL U  10  0                                        
SHEET    2  UA 4 GLY U  22  LEU U  28 -1  O  GLY U  22   N  VAL U  10           
SHEET    3  UA 4 LYS U  32  VAL U  35 -1  O  LYS U  32   N  LEU U  28           
SHEET    4  UA 4 ILE U  64  GLN U  65 -1  O  ILE U  64   N  VAL U  33           
SHEET    1  UB 2 LEU U  40  VAL U  41  0                                        
SHEET    2  UB 2 LYS U  60  GLU U  61 -1  O  LYS U  60   N  VAL U  41           
SHEET    1  UC 2 GLY U  83  GLU U  87  0                                        
SHEET    2  UC 2 LYS U  91  PHE U  94 -1  O  VAL U  92   N  PHE U  86           
SHEET    1  WA 7 ASN W   5  VAL W   8  0                                        
SHEET    2  WA 7 LEU W  61  VAL W  65  1  O  VAL W  64   N  ALA W   6           
SHEET    3  WA 7 LYS W  68  ALA W  74 -1  O  LYS W  68   N  VAL W  65           
SHEET    4  WA 7 ASP W  90  VAL W  92 -1  O  VAL W  92   N  LYS W  73           
SHEET    5  WA 7 PHE W  26  TYR W  31  1  O  ILE W  29   N  PHE W  91           
SHEET    6  WA 7 LEU W  38  LEU W  42 -1  O  LEU W  38   N  ILE W  30           
SHEET    7  WA 7 ASN W   5  VAL W   8 -1  O  GLU W   7   N  GLU W  41           
SHEET    1  YA 3 HIS Y  45  ALA Y  46  0                                        
SHEET    2  YA 3 ILE Y  79  GLU Y  82  1  O  ILE Y  79   N  ALA Y  46           
SHEET    3  YA 3 LYS Y  65  VAL Y  66 -1  O  LYS Y  65   N  GLU Y  82           
LINK         O3'   G V  53                 P   5MU V  54     1555   1555  1.59  
LINK         O3' 5MU V  54                 P     U V  55     1555   1555  1.58  
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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