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Database: PDB
Entry: 3J3V
LinkDB: 3J3V
Original site: 3J3V 
HEADER    RIBOSOME                                28-APR-13   3J3V              
TITLE     ATOMIC MODEL OF THE IMMATURE 50S SUBUNIT FROM BACILLUS SUBTILIS (STATE
TITLE    2 I-A)                                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 50S RIBOSOMAL PROTEIN L32;                                 
COMPND   3 CHAIN: 0;                                                            
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: 50S RIBOSOMAL PROTEIN L34;                                 
COMPND   6 CHAIN: 2;                                                            
COMPND   7 MOL_ID: 3;                                                           
COMPND   8 MOLECULE: 50S RIBOSOMAL PROTEIN L1;                                  
COMPND   9 CHAIN: 5;                                                            
COMPND  10 SYNONYM: BL1;                                                        
COMPND  11 MOL_ID: 4;                                                           
COMPND  12 MOLECULE: 50S RIBOSOMAL PROTEIN L11;                                 
COMPND  13 CHAIN: 6;                                                            
COMPND  14 SYNONYM: BL11;                                                       
COMPND  15 MOL_ID: 5;                                                           
COMPND  16 MOLECULE: RIBOSOME RNA 23S;                                          
COMPND  17 CHAIN: A;                                                            
COMPND  18 MOL_ID: 6;                                                           
COMPND  19 MOLECULE: RIBOSOME RNA 5S;                                           
COMPND  20 CHAIN: B;                                                            
COMPND  21 MOL_ID: 7;                                                           
COMPND  22 MOLECULE: 50S RIBOSOMAL PROTEIN L2;                                  
COMPND  23 CHAIN: C;                                                            
COMPND  24 SYNONYM: BL2;                                                        
COMPND  25 MOL_ID: 8;                                                           
COMPND  26 MOLECULE: 50S RIBOSOMAL PROTEIN L3;                                  
COMPND  27 CHAIN: D;                                                            
COMPND  28 SYNONYM: BL3;                                                        
COMPND  29 MOL_ID: 9;                                                           
COMPND  30 MOLECULE: 50S RIBOSOMAL PROTEIN L4;                                  
COMPND  31 CHAIN: E;                                                            
COMPND  32 MOL_ID: 10;                                                          
COMPND  33 MOLECULE: 50S RIBOSOMAL PROTEIN L5;                                  
COMPND  34 CHAIN: F;                                                            
COMPND  35 SYNONYM: BL6;                                                        
COMPND  36 MOL_ID: 11;                                                          
COMPND  37 MOLECULE: 50S RIBOSOMAL PROTEIN L6;                                  
COMPND  38 CHAIN: G;                                                            
COMPND  39 SYNONYM: BL10;                                                       
COMPND  40 MOL_ID: 12;                                                          
COMPND  41 MOLECULE: 50S RIBOSOMAL PROTEIN L13;                                 
COMPND  42 CHAIN: J;                                                            
COMPND  43 MOL_ID: 13;                                                          
COMPND  44 MOLECULE: 50S RIBOSOMAL PROTEIN L14;                                 
COMPND  45 CHAIN: K;                                                            
COMPND  46 MOL_ID: 14;                                                          
COMPND  47 MOLECULE: 50S RIBOSOMAL PROTEIN L15;                                 
COMPND  48 CHAIN: L;                                                            
COMPND  49 MOL_ID: 15;                                                          
COMPND  50 MOLECULE: 50S RIBOSOMAL PROTEIN L17;                                 
COMPND  51 CHAIN: N;                                                            
COMPND  52 SYNONYM: BL15, BL21;                                                 
COMPND  53 MOL_ID: 16;                                                          
COMPND  54 MOLECULE: 50S RIBOSOMAL PROTEIN L18;                                 
COMPND  55 CHAIN: O;                                                            
COMPND  56 SYNONYM: BL16;                                                       
COMPND  57 MOL_ID: 17;                                                          
COMPND  58 MOLECULE: 50S RIBOSOMAL PROTEIN L19;                                 
COMPND  59 CHAIN: P;                                                            
COMPND  60 MOL_ID: 18;                                                          
COMPND  61 MOLECULE: 50S RIBOSOMAL PROTEIN L20;                                 
COMPND  62 CHAIN: Q;                                                            
COMPND  63 MOL_ID: 19;                                                          
COMPND  64 MOLECULE: 50S RIBOSOMAL PROTEIN L21;                                 
COMPND  65 CHAIN: R;                                                            
COMPND  66 SYNONYM: BL20;                                                       
COMPND  67 MOL_ID: 20;                                                          
COMPND  68 MOLECULE: 50S RIBOSOMAL PROTEIN L22;                                 
COMPND  69 CHAIN: S;                                                            
COMPND  70 MOL_ID: 21;                                                          
COMPND  71 MOLECULE: 50S RIBOSOMAL PROTEIN L23;                                 
COMPND  72 CHAIN: T;                                                            
COMPND  73 MOL_ID: 22;                                                          
COMPND  74 MOLECULE: 50S RIBOSOMAL PROTEIN L24;                                 
COMPND  75 CHAIN: U;                                                            
COMPND  76 SYNONYM: 12 KDA DNA-BINDING PROTEIN, BL23, HPB12;                    
COMPND  77 MOL_ID: 23;                                                          
COMPND  78 MOLECULE: 50S RIBOSOMAL PROTEIN L29;                                 
COMPND  79 CHAIN: X;                                                            
COMPND  80 MOL_ID: 24;                                                          
COMPND  81 MOLECULE: 50S RIBOSOMAL PROTEIN L30;                                 
COMPND  82 CHAIN: Y;                                                            
COMPND  83 SYNONYM: BL27                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 224308;                                              
SOURCE   4 STRAIN: 168;                                                         
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   7 ORGANISM_TAXID: 224308;                                              
SOURCE   8 STRAIN: 168;                                                         
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE  11 ORGANISM_TAXID: 224308;                                              
SOURCE  12 STRAIN: 168;                                                         
SOURCE  13 MOL_ID: 4;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE  15 ORGANISM_TAXID: 224308;                                              
SOURCE  16 STRAIN: 168;                                                         
SOURCE  17 MOL_ID: 5;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE  19 ORGANISM_TAXID: 224308;                                              
SOURCE  20 STRAIN: 168;                                                         
SOURCE  21 MOL_ID: 6;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE  23 ORGANISM_TAXID: 224308;                                              
SOURCE  24 STRAIN: 168;                                                         
SOURCE  25 MOL_ID: 7;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE  27 ORGANISM_TAXID: 224308;                                              
SOURCE  28 STRAIN: 168;                                                         
SOURCE  29 MOL_ID: 8;                                                           
SOURCE  30 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE  31 ORGANISM_TAXID: 224308;                                              
SOURCE  32 STRAIN: 168;                                                         
SOURCE  33 MOL_ID: 9;                                                           
SOURCE  34 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE  35 ORGANISM_TAXID: 224308;                                              
SOURCE  36 STRAIN: 168;                                                         
SOURCE  37 MOL_ID: 10;                                                          
SOURCE  38 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE  39 ORGANISM_TAXID: 224308;                                              
SOURCE  40 STRAIN: 168;                                                         
SOURCE  41 MOL_ID: 11;                                                          
SOURCE  42 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE  43 ORGANISM_TAXID: 224308;                                              
SOURCE  44 STRAIN: 168;                                                         
SOURCE  45 MOL_ID: 12;                                                          
SOURCE  46 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE  47 ORGANISM_TAXID: 224308;                                              
SOURCE  48 STRAIN: 168;                                                         
SOURCE  49 MOL_ID: 13;                                                          
SOURCE  50 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE  51 ORGANISM_TAXID: 224308;                                              
SOURCE  52 STRAIN: 168;                                                         
SOURCE  53 MOL_ID: 14;                                                          
SOURCE  54 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE  55 ORGANISM_TAXID: 224308;                                              
SOURCE  56 STRAIN: 168;                                                         
SOURCE  57 MOL_ID: 15;                                                          
SOURCE  58 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE  59 ORGANISM_TAXID: 224308;                                              
SOURCE  60 STRAIN: 168;                                                         
SOURCE  61 MOL_ID: 16;                                                          
SOURCE  62 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE  63 ORGANISM_TAXID: 224308;                                              
SOURCE  64 STRAIN: 168;                                                         
SOURCE  65 MOL_ID: 17;                                                          
SOURCE  66 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE  67 ORGANISM_TAXID: 224308;                                              
SOURCE  68 STRAIN: 168;                                                         
SOURCE  69 MOL_ID: 18;                                                          
SOURCE  70 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE  71 ORGANISM_TAXID: 224308;                                              
SOURCE  72 STRAIN: 168;                                                         
SOURCE  73 MOL_ID: 19;                                                          
SOURCE  74 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE  75 ORGANISM_TAXID: 224308;                                              
SOURCE  76 STRAIN: 168;                                                         
SOURCE  77 MOL_ID: 20;                                                          
SOURCE  78 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE  79 ORGANISM_TAXID: 224308;                                              
SOURCE  80 STRAIN: 168;                                                         
SOURCE  81 MOL_ID: 21;                                                          
SOURCE  82 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE  83 ORGANISM_TAXID: 224308;                                              
SOURCE  84 STRAIN: 168;                                                         
SOURCE  85 MOL_ID: 22;                                                          
SOURCE  86 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE  87 ORGANISM_TAXID: 224308;                                              
SOURCE  88 STRAIN: 168;                                                         
SOURCE  89 MOL_ID: 23;                                                          
SOURCE  90 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE  91 ORGANISM_TAXID: 224308;                                              
SOURCE  92 STRAIN: 168;                                                         
SOURCE  93 MOL_ID: 24;                                                          
SOURCE  94 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE  95 ORGANISM_TAXID: 224308;                                              
SOURCE  96 STRAIN: 168                                                          
KEYWDS    RIBOSOME BIOGENESIS, RIBOSOME ASSEMBLY, RNA FOLDING, YLQF, RIBOSOME   
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    N.LI,Q.GUO,Y.ZHANG,Y.YUAN,C.MA,J.LEI,N.GAO                            
REVDAT   3   18-DEC-19 3J3V    1       REMARK                                   
REVDAT   2   28-AUG-13 3J3V    1       JRNL                                     
REVDAT   1   12-JUN-13 3J3V    0                                                
JRNL        AUTH   N.LI,Y.CHEN,Q.GUO,Y.ZHANG,Y.YUAN,C.MA,H.DENG,J.LEI,N.GAO     
JRNL        TITL   CRYO-EM STRUCTURES OF THE LATE-STAGE ASSEMBLY INTERMEDIATES  
JRNL        TITL 2 OF THE BACTERIAL 50S RIBOSOMAL SUBUNIT                       
JRNL        REF    NUCLEIC ACIDS RES.            V.  41  7073 2013              
JRNL        REFN                   ISSN 0305-1048                               
JRNL        PMID   23700310                                                     
JRNL        DOI    10.1093/NAR/GKT423                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.   13.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : MDFF, MODELLER, MODERNA, S2S, RELION      
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 2J01                                
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : FLEXIBLE FIT                        
REMARK   3   REFINEMENT TARGET            : CROSS-CORRELATION                   
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : METHOD--FLEXIBLE FITTING REFINEMENT PROTOCOL-    
REMARK   3  -ATOM MODELS OF THE 23S AND 5S RRNAS WERE BUILT USING THE           
REMARK   3  SOFTWARE S2S AND MODERNA, WITH THE CRYSTAL STRUCTURES OF THE 50S    
REMARK   3  SUBUNITS FROM E. COLI (PDB ID- 2AW4) AND THERMUS THERMOPHILUS       
REMARK   3  (PDB ID- 2J01) AS TEMPLATE. MODELS OF RIBOSOMAL PROTEINS, L1, L3,   
REMARK   3  L4, L6, L10, L13, L14, L15, L17, L19, L20, L21, L22, L23, L24,      
REMARK   3  L27, L29, L30, L31, L32, L33, L34, L35 AND L36 WERE DOWNLOADED      
REMARK   3  FROM THE SWISS-MODEL REPOSITORY. THE OTHERS, INCLUDING L2, L5,      
REMARK   3  L11, L16, L18 AND L28 WERE MODELED USING MODELLER WITH CRYSTAL      
REMARK   3  STRUCTURES OF E. COLI AND T. THERMOPHILUS 50S SUBUNITS AS           
REMARK   3  TEMPLATES.THE COMBINED ATOMIC MODEL OF THE B. SUBTILIS 50S          
REMARK   3  SUBUNIT WAS DOCKED INTO A HIGH RESOLUTION MATURE 50S DENSITY MAP    
REMARK   3  AND OPTIMIZED USING MDFF. THIS OPTIMIZED MODEL WAS DOCKED INTO      
REMARK   3  THE EM DENSITY USING CHIMERA AND FLEXIBLE FITTED INTO THE           
REMARK   3  DENSITY USING MDFF. DETAILS--REF- SCHUWIRTH, B.S., BOROVINSKAYA,    
REMARK   3  M.A., HAU, C.W., ZHANG, W., VILA-SANJURJO, A., HOLTON, J.M. AND     
REMARK   3  CATE, J.H. (2005) STRUCTURES OF THE BACTERIAL RIBOSOME AT 3.5 A     
REMARK   3  RESOLUTION. SCIENCE, 310, 827-834. SELMER, M., DUNHAM, C.M.,        
REMARK   3  MURPHY, F.V.T., WEIXLBAUMER, A., PETRY, S., KELLEY, A.C., WEIR,     
REMARK   3  J.R. AND RAMAKRISHNAN, V. (2006) STRUCTURE OF THE 70S RIBOSOME      
REMARK   3  COMPLEXED WITH MRNA AND TRNA. SCIENCE, 313, 1935-1942. JOSSINET,    
REMARK   3  F. AND WESTHOF, E. (2005) SEQUENCE TO STRUCTURE (S2S)- DISPLAY,     
REMARK   3  MANIPULATE AND INTERCONNECT RNA DATA FROM SEQUENCE TO STRUCTURE.    
REMARK   3  BIOINFORMATICS, 21, 3320-3321. ROTHER, M., ROTHER, K., PUTON, T.    
REMARK   3  AND BUJNICKI, J.M. (2011) MODERNA- A TOOL FOR COMPARATIVE           
REMARK   3  MODELING OF RNA 3D STRUCTURE. NUCLEIC ACIDS RESEARCH, 39, 4007-     
REMARK   3  4022. KIEFER, F., ARNOLD, K., KUNZLI, M., BORDOLI, L. AND           
REMARK   3  SCHWEDE, T. (2009) THE SWISS-MODEL REPOSITORY AND ASSOCIATED        
REMARK   3  RESOURCES. NUCLEIC ACIDS RESEARCH, 37, D387-392. ESWAR, N., WEBB,   
REMARK   3  B., MARTI-RENOM, M.A., MADHUSUDHAN, M.S., ERAMIAN, D., SHEN,        
REMARK   3  M.Y., PIEPER, U. AND SALI, A. (2006) COMPARATIVE PROTEIN            
REMARK   3  STRUCTURE MODELING USING MODELLER. CURRENT PROTOCOLS IN             
REMARK   3  BIOINFORMATICS / EDITORAL BOARD, ANDREAS D. BAXEVANIS ... [ET       
REMARK   3  AL.], CHAPTER 5, UNIT 5 6. TRABUCO, L.G., VILLA, E., MITRA, K.,     
REMARK   3  FRANK, J. AND SCHULTEN, K. (2008) FLEXIBLE FITTING OF ATOMIC        
REMARK   3  STRUCTURES INTO ELECTRON MICROSCOPY MAPS USING MOLECULAR            
REMARK   3  DYNAMICS. STRUCTURE, 16, 673-683. PETTERSEN, E.F., GODDARD, T.D.,   
REMARK   3  HUANG, C.C., COUCH, G.S., GREENBLATT, D.M., MENG, E.C. AND          
REMARK   3  FERRIN, T.E. (2004) UCSF CHIMERA--A VISUALIZATION SYSTEM FOR        
REMARK   3  EXPLORATORY RESEARCH AND ANALYSIS. JOURNAL OF COMPUTATIONAL         
REMARK   3  CHEMISTRY, 25, 1605-1612.                                           
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)  : 13.30                          
REMARK   3   NUMBER OF PARTICLES               : 21020                          
REMARK   3   CTF CORRECTION METHOD             : NULL                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: (SINGLE PARTICLE DETAILS: THIS IS ONE OF THE          
REMARK   3  CLASSIFIED GROUPS WITH THE SOFTWARE RELION) (SINGLE PARTICLE--      
REMARK   3  APPLIED SYMMETRY: C1)                                               
REMARK   4                                                                      
REMARK   4 3J3V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ.                               
REMARK 100 THE DEPOSITION ID IS D_1000160217.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : VITREOUS ICE (CRYO EM)            
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : IMMATURE 50S SUBUNIT FROM YLQF    
REMARK 245                                    -DEFICIENT BACILLUS SUBTILIS      
REMARK 245                                    STRAIN                            
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : 100MM NH4CL, 20MM TRIS-HCL,       
REMARK 245                                    10MM MGOAC2, 1MM TCEP.            
REMARK 245   PH                             : 7.50                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : 06-DEC-11                      
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : FEI EAGLE (4K X 4K)            
REMARK 245   MINIMUM DEFOCUS (NM)              : 1000.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 4000.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : 0.00                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : 0.00                           
REMARK 245   NOMINAL CS                        : 2.70                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 20.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 59000                          
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
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 AUTHOR DETERMINED BIOLOGICAL UNIT: 24-MERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 0, 2, 5, 6, A, B, C, D, E, F,         
REMARK 350                    AND CHAINS: G, J, K, L, N, O, P, Q, R,            
REMARK 350                    AND CHAINS: S, T, U, X, Y                         
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET 0     1                                                      
REMARK 465     LYS 0    57                                                      
REMARK 465     SER 0    58                                                      
REMARK 465     ASN 0    59                                                      
REMARK 465     MET 5     1                                                      
REMARK 465     ILE 5    59                                                      
REMARK 465     ARG 5    60                                                      
REMARK 465     GLY 5    61                                                      
REMARK 465     ALA 5    62                                                      
REMARK 465     VAL 5    63                                                      
REMARK 465     VAL 5    64                                                      
REMARK 465     LEU 5    65                                                      
REMARK 465     PRO 5    66                                                      
REMARK 465     ASN 5    67                                                      
REMARK 465     GLY 5    68                                                      
REMARK 465     THR 5    69                                                      
REMARK 465     GLY 5    70                                                      
REMARK 465     LYS 5    71                                                      
REMARK 465     THR 5    72                                                      
REMARK 465     GLN 5    73                                                      
REMARK 465     ARG 5    74                                                      
REMARK 465     VAL 5    75                                                      
REMARK 465     LEU 5    76                                                      
REMARK 465     VAL 5    77                                                      
REMARK 465     PHE 5    78                                                      
REMARK 465     ALA 5    79                                                      
REMARK 465     LYS 5    80                                                      
REMARK 465     GLY 5    81                                                      
REMARK 465     GLU 5    82                                                      
REMARK 465     LYS 5    83                                                      
REMARK 465     ALA 5    84                                                      
REMARK 465     LYS 5    85                                                      
REMARK 465     GLU 5    86                                                      
REMARK 465     ALA 5    87                                                      
REMARK 465     GLU 5    88                                                      
REMARK 465     ALA 5    89                                                      
REMARK 465     ALA 5    90                                                      
REMARK 465     GLY 5    91                                                      
REMARK 465     ALA 5    92                                                      
REMARK 465     ASP 5    93                                                      
REMARK 465     PHE 5    94                                                      
REMARK 465     VAL 5    95                                                      
REMARK 465     GLY 5    96                                                      
REMARK 465     ASP 5    97                                                      
REMARK 465     THR 5    98                                                      
REMARK 465     ASP 5    99                                                      
REMARK 465     TYR 5   100                                                      
REMARK 465     ILE 5   101                                                      
REMARK 465     ASN 5   102                                                      
REMARK 465     LYS 5   103                                                      
REMARK 465     ILE 5   104                                                      
REMARK 465     GLN 5   105                                                      
REMARK 465     GLN 5   106                                                      
REMARK 465     GLY 5   107                                                      
REMARK 465     TRP 5   108                                                      
REMARK 465     PHE 5   109                                                      
REMARK 465     ASP 5   110                                                      
REMARK 465     PHE 5   111                                                      
REMARK 465     ASP 5   112                                                      
REMARK 465     VAL 5   113                                                      
REMARK 465     ILE 5   114                                                      
REMARK 465     VAL 5   115                                                      
REMARK 465     ALA 5   116                                                      
REMARK 465     THR 5   117                                                      
REMARK 465     PRO 5   118                                                      
REMARK 465     ASP 5   119                                                      
REMARK 465     MET 5   120                                                      
REMARK 465     MET 5   121                                                      
REMARK 465     GLY 5   122                                                      
REMARK 465     GLU 5   123                                                      
REMARK 465     VAL 5   124                                                      
REMARK 465     GLY 5   125                                                      
REMARK 465     LYS 5   126                                                      
REMARK 465     ILE 5   127                                                      
REMARK 465     GLY 5   128                                                      
REMARK 465     ARG 5   129                                                      
REMARK 465     VAL 5   130                                                      
REMARK 465     LEU 5   131                                                      
REMARK 465     GLY 5   132                                                      
REMARK 465     PRO 5   133                                                      
REMARK 465     LYS 5   134                                                      
REMARK 465     GLY 5   135                                                      
REMARK 465     LEU 5   136                                                      
REMARK 465     MET 5   137                                                      
REMARK 465     PRO 5   138                                                      
REMARK 465     ASN 5   139                                                      
REMARK 465     PRO 5   140                                                      
REMARK 465     LYS 5   141                                                      
REMARK 465     THR 5   142                                                      
REMARK 465     GLY 5   143                                                      
REMARK 465     THR 5   144                                                      
REMARK 465     VAL 5   145                                                      
REMARK 465     THR 5   146                                                      
REMARK 465     PHE 5   147                                                      
REMARK 465     GLU 5   148                                                      
REMARK 465     VAL 5   149                                                      
REMARK 465     GLU 5   150                                                      
REMARK 465     LYS 5   151                                                      
REMARK 465     ALA 5   152                                                      
REMARK 465     ILE 5   153                                                      
REMARK 465     GLY 5   154                                                      
REMARK 465     GLU 5   155                                                      
REMARK 465     ILE 5   156                                                      
REMARK 465     LYS 5   157                                                      
REMARK 465     ALA 5   158                                                      
REMARK 465     GLY 5   159                                                      
REMARK 465     LYS 5   160                                                      
REMARK 465     VAL 5   161                                                      
REMARK 465     GLU 5   162                                                      
REMARK 465     TYR 5   163                                                      
REMARK 465     ARG 5   164                                                      
REMARK 465     VAL 5   165                                                      
REMARK 465     PHE 5   229                                                      
REMARK 465     ASN 5   230                                                      
REMARK 465     VAL 5   231                                                      
REMARK 465     LYS 5   232                                                      
REMARK 465       G A  1878                                                      
REMARK 465       G A  1879                                                      
REMARK 465       U A  1880                                                      
REMARK 465       U A  1881                                                      
REMARK 465       A A  1882                                                      
REMARK 465       A A  1883                                                      
REMARK 465       G A  1884                                                      
REMARK 465       A A  1885                                                      
REMARK 465       G A  1886                                                      
REMARK 465       G A  1887                                                      
REMARK 465       A A  1888                                                      
REMARK 465       G A  1889                                                      
REMARK 465       C A  1890                                                      
REMARK 465       G A  1891                                                      
REMARK 465       C A  1892                                                      
REMARK 465       U A  1893                                                      
REMARK 465       U A  1894                                                      
REMARK 465       A A  1895                                                      
REMARK 465       G A  1896                                                      
REMARK 465       C A  1897                                                      
REMARK 465       G A  1898                                                      
REMARK 465       U A  1899                                                      
REMARK 465       A A  1900                                                      
REMARK 465       A A  1901                                                      
REMARK 465       G A  1902                                                      
REMARK 465       C A  1903                                                      
REMARK 465       G A  1904                                                      
REMARK 465       A A  1905                                                      
REMARK 465       A A  1906                                                      
REMARK 465       G A  1907                                                      
REMARK 465       G A  1908                                                      
REMARK 465       U A  1909                                                      
REMARK 465       G A  1910                                                      
REMARK 465       C A  1911                                                      
REMARK 465       G A  1912                                                      
REMARK 465       A A  1913                                                      
REMARK 465       A A  1914                                                      
REMARK 465       U A  1915                                                      
REMARK 465       U A  1916                                                      
REMARK 465       G A  1917                                                      
REMARK 465       A A  1918                                                      
REMARK 465       A A  1919                                                      
REMARK 465       G A  1920                                                      
REMARK 465     MET D     1                                                      
REMARK 465     THR D     2                                                      
REMARK 465     LYS D   209                                                      
REMARK 465     MET E     1                                                      
REMARK 465     MET G     1                                                      
REMARK 465     SER G     2                                                      
REMARK 465     ARG G     3                                                      
REMARK 465     VAL G     4                                                      
REMARK 465     GLY G     5                                                      
REMARK 465     LYS G     6                                                      
REMARK 465     LYS G     7                                                      
REMARK 465     LEU G     8                                                      
REMARK 465     ARG G   172                                                      
REMARK 465     LYS G   173                                                      
REMARK 465     GLU G   174                                                      
REMARK 465     GLY G   175                                                      
REMARK 465     LYS G   176                                                      
REMARK 465     SER G   177                                                      
REMARK 465     ALA G   178                                                      
REMARK 465     LYS G   179                                                      
REMARK 465     ARG J   144                                                      
REMARK 465     GLY J   145                                                      
REMARK 465     MET P     1                                                      
REMARK 465     GLN P     2                                                      
REMARK 465     ARG P   115                                                      
REMARK 465     MET Q     1                                                      
REMARK 465     LYS Q   119                                                      
REMARK 465     GLY S   113                                                      
REMARK 465     ILE X    62                                                      
REMARK 465     ALA X    63                                                      
REMARK 465     ALA X    64                                                      
REMARK 465     ASN X    65                                                      
REMARK 465     LYS X    66                                                      
REMARK 465     MET Y     1                                                      
REMARK 465     ALA Y     2                                                      
REMARK 465     GLN Y    59                                                      
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       C A1921    P    OP1  OP2                                       
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      U A 163   C2      U A 163   N3      0.042                       
REMARK 500      A A 225   C5      A A 225   N7     -0.039                       
REMARK 500      A A 353   C5      A A 353   N7     -0.045                       
REMARK 500      A A 374   C5      A A 374   N7     -0.037                       
REMARK 500      A A 518   C5      A A 518   N7     -0.040                       
REMARK 500      G A 535   C2'     G A 535   C1'    -0.049                       
REMARK 500      C A 586   C2'     C A 586   C1'    -0.054                       
REMARK 500      G A 629   C2'     G A 629   C1'    -0.075                       
REMARK 500      A A 630   C5      A A 630   N7     -0.039                       
REMARK 500      A A 752   C5      A A 752   N7     -0.039                       
REMARK 500      A A 758   C5      A A 758   N7     -0.036                       
REMARK 500      A A 765   C5      A A 765   N7     -0.038                       
REMARK 500      A A1253   C5      A A1253   N7     -0.045                       
REMARK 500      C A1449   P       C A1449   O5'    -0.071                       
REMARK 500      A A1485   C5      A A1485   N7     -0.036                       
REMARK 500      G A1497   C2'     G A1497   C1'    -0.049                       
REMARK 500      G A1525   P       G A1525   O5'    -0.063                       
REMARK 500      G A1628   C2'     G A1628   C1'    -0.062                       
REMARK 500      A A1722   C2'     A A1722   C1'    -0.049                       
REMARK 500      A A1831   C5      A A1831   N7     -0.038                       
REMARK 500      A A1839   C5      A A1839   N7     -0.039                       
REMARK 500      A A2176   C5      A A2176   N7     -0.037                       
REMARK 500      A A2216   C2'     A A2216   C1'    -0.049                       
REMARK 500      A A2254   C5      A A2254   N7     -0.039                       
REMARK 500      A A2297   C5      A A2297   N7     -0.041                       
REMARK 500      A A2505   C2'     A A2505   C1'    -0.057                       
REMARK 500      A A2627   C5      A A2627   N7     -0.037                       
REMARK 500      G A2829   C2'     G A2829   C1'    -0.049                       
REMARK 500      A B  71   C5      A B  71   N7     -0.040                       
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      G A   1   N1  -  C6  -  O6  ANGL. DEV. =   5.3 DEGREES          
REMARK 500      G A   1   C5  -  C6  -  O6  ANGL. DEV. =  -4.3 DEGREES          
REMARK 500      G A   2   O4' -  C1' -  N9  ANGL. DEV. =   4.4 DEGREES          
REMARK 500      G A   2   N1  -  C6  -  O6  ANGL. DEV. =   5.3 DEGREES          
REMARK 500      G A   2   C5  -  C6  -  O6  ANGL. DEV. =  -4.1 DEGREES          
REMARK 500      U A   3   O4' -  C1' -  N1  ANGL. DEV. =   6.7 DEGREES          
REMARK 500      U A   4   O4' -  C1' -  N1  ANGL. DEV. =   4.8 DEGREES          
REMARK 500      A A   5   C4  -  C5  -  C6  ANGL. DEV. =   3.2 DEGREES          
REMARK 500      A A   5   N1  -  C6  -  N6  ANGL. DEV. =   7.0 DEGREES          
REMARK 500      A A   6   N1  -  C6  -  N6  ANGL. DEV. =   7.0 DEGREES          
REMARK 500      G A   7   O4' -  C1' -  N9  ANGL. DEV. =   4.7 DEGREES          
REMARK 500      G A   7   N1  -  C6  -  O6  ANGL. DEV. =   5.5 DEGREES          
REMARK 500      G A   7   C5  -  C6  -  O6  ANGL. DEV. =  -4.5 DEGREES          
REMARK 500      U A   8   O4' -  C1' -  N1  ANGL. DEV. =   5.8 DEGREES          
REMARK 500      U A   9   O4' -  C1' -  N1  ANGL. DEV. =   5.3 DEGREES          
REMARK 500      U A   9   C3' -  O3' -  P   ANGL. DEV. =   8.4 DEGREES          
REMARK 500      A A  10   C5' -  C4' -  O4' ANGL. DEV. =   5.4 DEGREES          
REMARK 500      A A  10   O4' -  C1' -  N9  ANGL. DEV. =   4.3 DEGREES          
REMARK 500      A A  10   C4  -  C5  -  C6  ANGL. DEV. =   3.1 DEGREES          
REMARK 500      A A  10   N1  -  C6  -  N6  ANGL. DEV. =   7.2 DEGREES          
REMARK 500      G A  11   O4' -  C1' -  N9  ANGL. DEV. =   4.2 DEGREES          
REMARK 500      G A  11   N1  -  C6  -  O6  ANGL. DEV. =   5.5 DEGREES          
REMARK 500      G A  11   C5  -  C6  -  O6  ANGL. DEV. =  -4.3 DEGREES          
REMARK 500      A A  12   C4  -  C5  -  C6  ANGL. DEV. =   3.3 DEGREES          
REMARK 500      A A  12   N1  -  C6  -  N6  ANGL. DEV. =   6.5 DEGREES          
REMARK 500      A A  13   N1  -  C6  -  N6  ANGL. DEV. =   5.0 DEGREES          
REMARK 500      A A  14   O4' -  C1' -  N9  ANGL. DEV. =   5.4 DEGREES          
REMARK 500      A A  14   C5  -  C6  -  N1  ANGL. DEV. =  -3.1 DEGREES          
REMARK 500      A A  14   N1  -  C6  -  N6  ANGL. DEV. =   8.2 DEGREES          
REMARK 500      A A  14   C5  -  C6  -  N6  ANGL. DEV. =  -5.2 DEGREES          
REMARK 500      G A  15   O4' -  C1' -  N9  ANGL. DEV. =   4.8 DEGREES          
REMARK 500      G A  15   N1  -  C6  -  O6  ANGL. DEV. =   7.3 DEGREES          
REMARK 500      G A  15   C5  -  C6  -  O6  ANGL. DEV. =  -6.2 DEGREES          
REMARK 500      G A  16   O4' -  C1' -  N9  ANGL. DEV. =   5.4 DEGREES          
REMARK 500      G A  16   N1  -  C6  -  O6  ANGL. DEV. =   6.3 DEGREES          
REMARK 500      G A  16   C5  -  C6  -  O6  ANGL. DEV. =  -4.6 DEGREES          
REMARK 500      G A  17   O4' -  C1' -  N9  ANGL. DEV. =   4.5 DEGREES          
REMARK 500      G A  17   N1  -  C6  -  O6  ANGL. DEV. =   6.1 DEGREES          
REMARK 500      G A  17   C5  -  C6  -  O6  ANGL. DEV. =  -5.0 DEGREES          
REMARK 500      C A  18   O4' -  C1' -  N1  ANGL. DEV. =   5.7 DEGREES          
REMARK 500      C A  18   N3  -  C4  -  N4  ANGL. DEV. =   4.4 DEGREES          
REMARK 500      G A  19   O4' -  C1' -  N9  ANGL. DEV. =   5.8 DEGREES          
REMARK 500      G A  19   N1  -  C6  -  O6  ANGL. DEV. =   6.0 DEGREES          
REMARK 500      G A  19   C5  -  C6  -  O6  ANGL. DEV. =  -4.5 DEGREES          
REMARK 500      C A  20   O4' -  C1' -  N1  ANGL. DEV. =   5.5 DEGREES          
REMARK 500      C A  20   N3  -  C4  -  N4  ANGL. DEV. =   4.3 DEGREES          
REMARK 500      A A  21   N1  -  C6  -  N6  ANGL. DEV. =   7.6 DEGREES          
REMARK 500      A A  21   C5  -  C6  -  N6  ANGL. DEV. =  -4.8 DEGREES          
REMARK 500      C A  22   O4' -  C1' -  N1  ANGL. DEV. =   6.0 DEGREES          
REMARK 500      C A  22   N3  -  C4  -  N4  ANGL. DEV. =   4.4 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS    6204 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  17        0.53    -65.92                                   
REMARK 500    PHE 0  20       47.23     71.47                                   
REMARK 500    LEU 0  22     -161.89     62.13                                   
REMARK 500    CYS 0  33        0.02   -160.88                                   
REMARK 500    VAL 0  42      135.86    -36.95                                   
REMARK 500    CYS 0  43     -128.36    -84.11                                   
REMARK 500    LYS 0  44       -0.20   -161.28                                   
REMARK 500    ALA 0  45        4.22   -162.63                                   
REMARK 500    CYS 0  46      -25.23   -145.46                                   
REMARK 500    TYR 0  49       75.32   -178.68                                   
REMARK 500    GLN 2   6      111.21    177.75                                   
REMARK 500    ARG 2  39     -146.22   -142.29                                   
REMARK 500    LEU 2  42      -48.02   -171.16                                   
REMARK 500    LYS 5   4     -175.29     51.23                                   
REMARK 500    ASP 5  16      108.23     83.53                                   
REMARK 500    THR 5  35       -4.55   -150.22                                   
REMARK 500    ALA 5  40      115.10     78.74                                   
REMARK 500    THR 5  41      110.96      2.69                                   
REMARK 500    ALA 5  45       18.11   -147.32                                   
REMARK 500    PRO 5  52     -165.70   -115.49                                   
REMARK 500    LYS 5 167        8.83   -162.58                                   
REMARK 500    ALA 5 168       -8.87   -158.94                                   
REMARK 500    HIS 5 172     -147.97   -123.77                                   
REMARK 500    SER 5 179       -1.91   -162.65                                   
REMARK 500    GLU 5 181      -98.10    -88.24                                   
REMARK 500    ALA 5 199      122.07    165.12                                   
REMARK 500    TYR 5 208      -99.80     64.71                                   
REMARK 500    VAL 5 209      127.65    165.93                                   
REMARK 500    VAL 5 212      110.43    177.17                                   
REMARK 500    LYS 6   3     -143.17   -110.91                                   
REMARK 500    LYS 6   7       21.68     80.44                                   
REMARK 500    ALA 6  18        9.29   -154.18                                   
REMARK 500    ASN 6  19      -60.78   -158.34                                   
REMARK 500    ALA 6  27       -3.99   -164.03                                   
REMARK 500    LEU 6  28       14.81   -158.58                                   
REMARK 500    GLN 6  30       -7.79   -162.24                                   
REMARK 500    ALA 6  50       14.66   -155.75                                   
REMARK 500    LEU 6  52      -61.36    -90.70                                   
REMARK 500    SER 6  65       57.78   -105.36                                   
REMARK 500    SER 6  87      130.39    177.77                                   
REMARK 500    SER 6  89        3.89   -161.03                                   
REMARK 500    ASN 6  93       87.27    111.93                                   
REMARK 500    VAL 6  97       -9.21   -149.06                                   
REMARK 500    LEU 6 116     -146.59    -83.32                                   
REMARK 500    ALA 6 119        8.38   -163.40                                   
REMARK 500    GLU 6 140       55.49   -155.29                                   
REMARK 500    THR C   9        0.71   -155.49                                   
REMARK 500    ARG C  14       25.00   -149.75                                   
REMARK 500    PHE C  21       55.60   -141.30                                   
REMARK 500    THR C  25     -146.21     51.02                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     381 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASP D  150     PRO D  151                 -144.64                    
REMARK 500 ALA E   14     GLY E   15                   33.42                    
REMARK 500 MET L   55     PRO L   56                  139.96                    
REMARK 500 ILE L   69     ASN L   70                 -134.64                    
REMARK 500 LEU P   17     PRO P   18                 -145.82                    
REMARK 500 GLY T   61     LYS T   62                 -131.18                    
REMARK 500 LYS T   62     SER T   63                  117.83                    
REMARK 500 SER T   87     LYS T   88                 -126.46                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500      U A   3         0.07    SIDE CHAIN                              
REMARK 500      A A  14         0.10    SIDE CHAIN                              
REMARK 500      G A  15         0.13    SIDE CHAIN                              
REMARK 500      G A  27         0.10    SIDE CHAIN                              
REMARK 500      A A  28         0.08    SIDE CHAIN                              
REMARK 500      C A  31         0.09    SIDE CHAIN                              
REMARK 500      U A  33         0.09    SIDE CHAIN                              
REMARK 500      U A  34         0.10    SIDE CHAIN                              
REMARK 500      G A  36         0.06    SIDE CHAIN                              
REMARK 500      C A  37         0.09    SIDE CHAIN                              
REMARK 500      U A  40         0.08    SIDE CHAIN                              
REMARK 500      G A  42         0.07    SIDE CHAIN                              
REMARK 500      G A  59         0.09    SIDE CHAIN                              
REMARK 500      G A  63         0.08    SIDE CHAIN                              
REMARK 500      A A  65         0.14    SIDE CHAIN                              
REMARK 500      A A  67         0.12    SIDE CHAIN                              
REMARK 500      A A  73         0.08    SIDE CHAIN                              
REMARK 500      U A  74         0.16    SIDE CHAIN                              
REMARK 500      G A  81         0.07    SIDE CHAIN                              
REMARK 500      G A  83         0.10    SIDE CHAIN                              
REMARK 500      G A  88         0.10    SIDE CHAIN                              
REMARK 500      U A  89         0.23    SIDE CHAIN                              
REMARK 500      G A 106         0.07    SIDE CHAIN                              
REMARK 500      U A 113         0.16    SIDE CHAIN                              
REMARK 500      G A 116         0.08    SIDE CHAIN                              
REMARK 500      A A 118         0.15    SIDE CHAIN                              
REMARK 500      C A 132         0.09    SIDE CHAIN                              
REMARK 500      G A 143         0.07    SIDE CHAIN                              
REMARK 500      A A 144         0.08    SIDE CHAIN                              
REMARK 500      G A 145         0.07    SIDE CHAIN                              
REMARK 500      U A 151         0.07    SIDE CHAIN                              
REMARK 500      C A 153         0.11    SIDE CHAIN                              
REMARK 500      U A 163         0.11    SIDE CHAIN                              
REMARK 500      A A 178         0.09    SIDE CHAIN                              
REMARK 500      U A 209         0.09    SIDE CHAIN                              
REMARK 500      A A 210         0.05    SIDE CHAIN                              
REMARK 500      C A 213         0.09    SIDE CHAIN                              
REMARK 500      G A 215         0.07    SIDE CHAIN                              
REMARK 500      A A 229         0.08    SIDE CHAIN                              
REMARK 500      A A 230         0.10    SIDE CHAIN                              
REMARK 500      G A 235         0.08    SIDE CHAIN                              
REMARK 500      C A 241         0.10    SIDE CHAIN                              
REMARK 500      G A 243         0.06    SIDE CHAIN                              
REMARK 500      U A 246         0.08    SIDE CHAIN                              
REMARK 500      G A 257         0.07    SIDE CHAIN                              
REMARK 500      G A 269         0.10    SIDE CHAIN                              
REMARK 500      A A 275         0.06    SIDE CHAIN                              
REMARK 500      C A 288         0.07    SIDE CHAIN                              
REMARK 500      U A 290         0.13    SIDE CHAIN                              
REMARK 500      G A 296         0.08    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     466 PLANE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-5642   RELATED DB: EMDB                              
REMARK 900 IMMATURE 50S SUBUNIT FROM BACILLUS SUBTILIS (STATE I-A)              
REMARK 900 RELATED ID: 3J3W   RELATED DB: PDB                                   
DBREF  3J3V 0    1    59  UNP    O34687   RL32_BACSU       1     59             
DBREF  3J3V 2    1    44  UNP    P05647   RL34_BACSU       1     44             
DBREF  3J3V 5    1   232  UNP    Q06797   RL1_BACSU        1    232             
DBREF  3J3V 6    1   141  UNP    Q06796   RL11_BACSU       1    141             
DBREF1 3J3V A    1  2927  GB                   AL009126                         
DBREF2 3J3V A     AL009126.3                      32177       35103             
DBREF1 3J3V B    1   119  GB                   AL009126                         
DBREF2 3J3V B     AL009126.3                      14692       14810             
DBREF  3J3V C    1   277  UNP    P42919   RL2_BACSU        1    277             
DBREF  3J3V D    1   209  UNP    P42920   RL3_BACSU        1    209             
DBREF  3J3V E    1   207  UNP    P42921   RL4_BACSU        1    207             
DBREF  3J3V F    1   179  UNP    P12877   RL5_BACSU        1    179             
DBREF  3J3V G    1   179  UNP    P46898   RL6_BACSU        1    179             
DBREF  3J3V J    1   145  UNP    P70974   RL13_BACSU       1    145             
DBREF  3J3V K    1   122  UNP    P12875   RL14_BACSU       1    122             
DBREF  3J3V L    1   146  UNP    P19946   RL15_BACSU       1    146             
DBREF  3J3V N    1   120  UNP    P20277   RL17_BACSU       1    120             
DBREF  3J3V O    1   120  UNP    P46899   RL18_BACSU       1    120             
DBREF  3J3V P    1   115  UNP    O31742   RL19_BACSU       1    115             
DBREF  3J3V Q    1   119  UNP    P55873   RL20_BACSU       1    119             
DBREF  3J3V R    1   102  UNP    P26908   RL21_BACSU       1    102             
DBREF  3J3V S    1   113  UNP    P42060   RL22_BACSU       1    113             
DBREF  3J3V T    1    95  UNP    P42924   RL23_BACSU       1     95             
DBREF  3J3V U    1   103  UNP    P0CI78   RL24_BACSU       1    103             
DBREF  3J3V X    1    66  UNP    P12873   RL29_BACSU       1     66             
DBREF  3J3V Y    1    59  UNP    P19947   RL30_BACSU       1     59             
SEQRES   1 0   59  MET ALA VAL PRO PHE ARG ARG THR SER LYS MET LYS LYS          
SEQRES   2 0   59  ARG LEU ARG ARG THR HIS PHE LYS LEU ASN VAL PRO GLY          
SEQRES   3 0   59  MET THR GLU CYS PRO SER CYS GLY GLU MET LYS LEU SER          
SEQRES   4 0   59  HIS ARG VAL CYS LYS ALA CYS GLY SER TYR ASN GLY LYS          
SEQRES   5 0   59  ASP ILE ASN VAL LYS SER ASN                                  
SEQRES   1 2   44  MET LYS ARG THR PHE GLN PRO ASN ASN ARG LYS ARG SER          
SEQRES   2 2   44  LYS VAL HIS GLY PHE ARG SER ARG MET SER SER LYS ASN          
SEQRES   3 2   44  GLY ARG LEU VAL LEU ALA ARG ARG ARG ARG LYS GLY ARG          
SEQRES   4 2   44  LYS VAL LEU SER ALA                                          
SEQRES   1 5  232  MET ALA LYS LYS GLY LYS LYS TYR VAL GLU ALA ALA LYS          
SEQRES   2 5  232  LEU VAL ASP ARG SER LYS ALA TYR ASP VAL SER GLU ALA          
SEQRES   3 5  232  VAL ALA LEU VAL LYS LYS THR ASN THR ALA LYS PHE ASP          
SEQRES   4 5  232  ALA THR VAL GLU VAL ALA PHE ARG LEU GLY VAL ASP PRO          
SEQRES   5 5  232  ARG LYS ASN ASP GLN GLN ILE ARG GLY ALA VAL VAL LEU          
SEQRES   6 5  232  PRO ASN GLY THR GLY LYS THR GLN ARG VAL LEU VAL PHE          
SEQRES   7 5  232  ALA LYS GLY GLU LYS ALA LYS GLU ALA GLU ALA ALA GLY          
SEQRES   8 5  232  ALA ASP PHE VAL GLY ASP THR ASP TYR ILE ASN LYS ILE          
SEQRES   9 5  232  GLN GLN GLY TRP PHE ASP PHE ASP VAL ILE VAL ALA THR          
SEQRES  10 5  232  PRO ASP MET MET GLY GLU VAL GLY LYS ILE GLY ARG VAL          
SEQRES  11 5  232  LEU GLY PRO LYS GLY LEU MET PRO ASN PRO LYS THR GLY          
SEQRES  12 5  232  THR VAL THR PHE GLU VAL GLU LYS ALA ILE GLY GLU ILE          
SEQRES  13 5  232  LYS ALA GLY LYS VAL GLU TYR ARG VAL ASP LYS ALA GLY          
SEQRES  14 5  232  ASN ILE HIS VAL PRO ILE GLY LYS VAL SER PHE GLU ASP          
SEQRES  15 5  232  GLU LYS LEU VAL GLU ASN PHE THR THR MET TYR ASP THR          
SEQRES  16 5  232  ILE LEU LYS ALA LYS PRO ALA ALA ALA LYS GLY VAL TYR          
SEQRES  17 5  232  VAL LYS ASN VAL ALA VAL THR SER THR MET GLY PRO GLY          
SEQRES  18 5  232  VAL LYS VAL ASP SER SER THR PHE ASN VAL LYS                  
SEQRES   1 6  141  MET ALA LYS LYS VAL VAL LYS VAL VAL LYS LEU GLN ILE          
SEQRES   2 6  141  PRO ALA GLY LYS ALA ASN PRO ALA PRO PRO VAL GLY PRO          
SEQRES   3 6  141  ALA LEU GLY GLN ALA GLY VAL ASN ILE MET GLY PHE CYS          
SEQRES   4 6  141  LYS GLU PHE ASN ALA ARG THR ALA ASP GLN ALA GLY LEU          
SEQRES   5 6  141  ILE ILE PRO VAL GLU ILE SER VAL TYR GLU ASP ARG SER          
SEQRES   6 6  141  PHE THR PHE ILE THR LYS THR PRO PRO ALA ALA VAL LEU          
SEQRES   7 6  141  LEU LYS LYS ALA ALA GLY ILE GLU SER GLY SER GLY GLU          
SEQRES   8 6  141  PRO ASN ARG ASN LYS VAL ALA THR VAL LYS ARG ASP LYS          
SEQRES   9 6  141  VAL ARG GLU ILE ALA GLU THR LYS MET PRO ASP LEU ASN          
SEQRES  10 6  141  ALA ALA ASP VAL GLU ALA ALA MET ARG MET VAL GLU GLY          
SEQRES  11 6  141  THR ALA ARG SER MET GLY ILE VAL ILE GLU ASP                  
SEQRES   1 A 2927    G   G   U   U   A   A   G   U   U   A   G   A   A          
SEQRES   2 A 2927    A   G   G   G   C   G   C   A   C   G   G   U   G          
SEQRES   3 A 2927    G   A   U   G   C   C   U   U   G   G   C   A   C          
SEQRES   4 A 2927    U   A   G   G   A   G   C   C   G   A   U   G   A          
SEQRES   5 A 2927    A   G   G   A   C   G   G   G   A   C   G   A   A          
SEQRES   6 A 2927    C   A   C   C   G   A   U   A   U   G   C   U   U          
SEQRES   7 A 2927    C   G   G   G   G   A   G   C   U   G   U   A   A          
SEQRES   8 A 2927    G   C   A   A   G   C   U   U   U   G   A   U   C          
SEQRES   9 A 2927    C   G   G   A   G   A   U   U   U   C   C   G   A          
SEQRES  10 A 2927    A   U   G   G   G   G   A   A   A   C   C   C   A          
SEQRES  11 A 2927    C   C   A   C   U   C   G   U   A   A   U   G   G          
SEQRES  12 A 2927    A   G   U   G   G   U   A   U   C   C   A   U   A          
SEQRES  13 A 2927    U   C   U   G   A   A   U   U   C   A   U   A   G          
SEQRES  14 A 2927    G   A   U   A   U   G   A   G   A   A   G   G   C          
SEQRES  15 A 2927    A   G   A   C   C   C   G   G   G   G   A   A   C          
SEQRES  16 A 2927    U   G   A   A   A   C   A   U   C   U   A   A   G          
SEQRES  17 A 2927    U   A   C   C   C   G   G   A   G   G   A   A   G          
SEQRES  18 A 2927    A   G   A   A   A   G   C   A   A   A   U   G   C          
SEQRES  19 A 2927    G   A   U   U   C   C   C   U   G   A   G   U   A          
SEQRES  20 A 2927    G   C   G   G   C   G   A   G   C   G   A   A   A          
SEQRES  21 A 2927    C   G   G   G   A   U   U   A   G   C   C   C   A          
SEQRES  22 A 2927    A   A   C   C   A   A   G   A   G   G   C   U   U          
SEQRES  23 A 2927    G   C   C   U   C   U   U   G   G   G   G   U   U          
SEQRES  24 A 2927    G   U   A   G   G   A   C   A   C   U   C   U   G          
SEQRES  25 A 2927    U   A   C   G   G   A   G   U   U   A   C   A   A          
SEQRES  26 A 2927    A   G   G   A   A   C   G   A   G   G   U   A   G          
SEQRES  27 A 2927    A   U   G   A   A   G   A   G   G   U   C   U   G          
SEQRES  28 A 2927    G   A   A   A   G   G   C   C   C   G   C   C   A          
SEQRES  29 A 2927    U   A   G   G   A   G   G   U   A   A   C   A   G          
SEQRES  30 A 2927    C   C   C   U   G   U   A   G   U   C   A   A   A          
SEQRES  31 A 2927    A   C   U   U   C   G   U   U   C   U   C   U   C          
SEQRES  32 A 2927    C   U   G   A   G   U   G   G   A   U   C   C   U          
SEQRES  33 A 2927    G   A   G   U   A   C   G   G   C   G   G   A   A          
SEQRES  34 A 2927    C   A   C   G   U   G   A   A   A   U   U   C   C          
SEQRES  35 A 2927    G   U   C   G   G   A   A   U   C   C   G   G   G          
SEQRES  36 A 2927    A   G   G   A   C   C   A   U   C   U   C   C   C          
SEQRES  37 A 2927    A   A   G   G   C   U   A   A   A   U   A   C   U          
SEQRES  38 A 2927    C   C   C   U   A   G   U   G   A   C   C   G   A          
SEQRES  39 A 2927    U   A   G   U   G   A   A   C   C   A   G   U   A          
SEQRES  40 A 2927    C   C   G   U   G   A   G   G   G   A   A   A   G          
SEQRES  41 A 2927    G   U   G   A   A   A   A   G   C   A   C   C   C          
SEQRES  42 A 2927    C   G   G   A   A   G   G   G   G   A   G   U   G          
SEQRES  43 A 2927    A   A   A   G   A   G   A   U   C   C   U   G   A          
SEQRES  44 A 2927    A   A   C   C   G   U   G   U   G   C   C   U   A          
SEQRES  45 A 2927    C   A   A   G   U   A   G   U   C   A   G   A   G          
SEQRES  46 A 2927    C   C   C   G   U   U   A   A   C   G   G   G   U          
SEQRES  47 A 2927    G   A   U   G   G   C   G   U   G   C   C   U   U          
SEQRES  48 A 2927    U   U   G   U   A   G   A   A   U   G   A   A   C          
SEQRES  49 A 2927    C   G   G   C   G   A   G   U   U   A   C   G   A          
SEQRES  50 A 2927    U   C   C   C   G   U   G   C   A   A   G   G   U          
SEQRES  51 A 2927    U   A   A   G   C   A   G   A   A   G   A   U   G          
SEQRES  52 A 2927    C   G   G   A   G   C   C   G   C   A   G   C   G          
SEQRES  53 A 2927    A   A   A   G   C   G   A   G   U   C   U   G   A          
SEQRES  54 A 2927    A   U   A   G   G   G   C   G   C   A   U   G   A          
SEQRES  55 A 2927    G   U   A   C   G   U   G   G   U   C   G   U   A          
SEQRES  56 A 2927    G   A   C   C   C   G   A   A   A   C   C   A   G          
SEQRES  57 A 2927    G   U   G   A   U   C   U   A   C   C   C   A   U          
SEQRES  58 A 2927    G   U   C   C   A   G   G   G   U   G   A   A   G          
SEQRES  59 A 2927    U   U   C   A   G   G   U   A   A   C   A   C   U          
SEQRES  60 A 2927    G   A   A   U   G   G   A   G   G   C   C   C   G          
SEQRES  61 A 2927    A   A   C   C   C   A   C   G   C   A   C   G   U          
SEQRES  62 A 2927    U   G   A   A   A   A   G   U   G   C   G   G   G          
SEQRES  63 A 2927    G   A   U   G   A   G   G   U   G   U   G   G   G          
SEQRES  64 A 2927    U   A   G   G   G   G   U   G   A   A   A   U   G          
SEQRES  65 A 2927    C   C   A   A   U   C   G   A   A   C   C   U   G          
SEQRES  66 A 2927    G   A   G   A   U   A   G   C   U   G   G   U   U          
SEQRES  67 A 2927    C   U   C   U   C   C   G   A   A   A   U   A   G          
SEQRES  68 A 2927    C   U   U   U   A   G   G   G   C   U   A   G   C          
SEQRES  69 A 2927    C   U   C   A   A   G   G   U   A   A   G   A   G          
SEQRES  70 A 2927    U   C   U   U   G   G   A   G   G   U   A   G   A          
SEQRES  71 A 2927    G   C   A   C   U   G   A   U   U   G   G   A   C          
SEQRES  72 A 2927    U   A   G   G   G   G   C   C   C   C   U   A   C          
SEQRES  73 A 2927    C   G   G   G   U   U   A   C   C   G   A   A   U          
SEQRES  74 A 2927    U   C   A   G   U   C   A   A   A   C   U   C   C          
SEQRES  75 A 2927    G   A   A   U   G   C   C   A   A   U   G   A   C          
SEQRES  76 A 2927    U   U   A   U   C   C   U   U   G   G   G   A   G          
SEQRES  77 A 2927    U   C   A   G   A   C   U   G   C   G   A   G   U          
SEQRES  78 A 2927    G   A   U   A   A   G   A   U   C   C   G   U   A          
SEQRES  79 A 2927    G   U   C   G   A   A   A   G   G   G   A   A   A          
SEQRES  80 A 2927    C   A   G   C   C   C   A   G   A   C   C   G   C          
SEQRES  81 A 2927    C   A   G   C   U   A   A   G   G   U   C   C   C          
SEQRES  82 A 2927    A   A   A   G   U   A   U   A   C   G   U   U   A          
SEQRES  83 A 2927    A   G   U   G   G   A   A   A   A   G   G   A   U          
SEQRES  84 A 2927    G   U   G   G   A   G   U   U   G   C   U   U   A          
SEQRES  85 A 2927    G   A   C   A   A   C   C   A   G   G   A   U   G          
SEQRES  86 A 2927    U   U   G   G   C   U   U   A   G   A   A   G   C          
SEQRES  87 A 2927    A   G   C   C   A   C   C   A   U   U   U   A   A          
SEQRES  88 A 2927    A   G   A   G   U   G   C   G   U   A   A   U   A          
SEQRES  89 A 2927    G   C   U   C   A   C   U   G   G   U   C   G   A          
SEQRES  90 A 2927    G   U   G   A   C   U   C   U   G   C   G   C   C          
SEQRES  91 A 2927    G   A   A   A   A   U   G   U   A   C   C   G   G          
SEQRES  92 A 2927    G   G   C   U   A   A   A   C   G   U   A   U   C          
SEQRES  93 A 2927    A   C   C   G   A   A   G   C   U   G   C   G   G          
SEQRES  94 A 2927    A   C   U   G   U   U   C   U   U   C   G   A   A          
SEQRES  95 A 2927    C   A   G   U   G   G   U   A   G   G   A   G   A          
SEQRES  96 A 2927    G   C   G   U   U   C   U   A   A   G   G   G   C          
SEQRES  97 A 2927    U   G   U   G   A   A   G   C   C   A   G   A   C          
SEQRES  98 A 2927    C   G   G   A   A   G   G   A   C   U   G   G   U          
SEQRES  99 A 2927    G   G   A   G   C   G   C   U   U   A   G   A   A          
SEQRES 100 A 2927    G   U   G   A   G   A   A   U   G   C   C   G   G          
SEQRES 101 A 2927    U   A   U   G   A   G   U   A   G   C   G   A   A          
SEQRES 102 A 2927    A   G   A   G   G   G   G   U   G   A   G   A   A          
SEQRES 103 A 2927    U   C   C   C   C   U   C   C   A   C   C   G   A          
SEQRES 104 A 2927    A   U   G   C   C   U   A   A   G   G   U   U   U          
SEQRES 105 A 2927    C   C   U   G   A   G   G   A   A   G   G   C   U          
SEQRES 106 A 2927    C   G   U   C   C   G   C   U   C   A   G   G   G          
SEQRES 107 A 2927    U   U   A   G   U   C   G   G   G   A   C   C   U          
SEQRES 108 A 2927    A   A   G   C   C   G   A   G   G   C   C   G   A          
SEQRES 109 A 2927    A   A   G   G   C   G   U   A   G   G   C   G   A          
SEQRES 110 A 2927    U   G   G   A   C   A   A   C   A   G   G   U   U          
SEQRES 111 A 2927    G   A   U   A   U   U   C   C   U   G   U   A   C          
SEQRES 112 A 2927    C   A   C   C   U   C   C   U   C   A   C   C   A          
SEQRES 113 A 2927    U   U   U   G   A   G   C   A   A   U   G   G   G          
SEQRES 114 A 2927    G   G   G   A   C   G   C   A   G   G   A   G   G          
SEQRES 115 A 2927    A   U   A   G   G   G   U   A   A   G   C   G   C          
SEQRES 116 A 2927    G   G   U   A   U   U   G   G   A   U   A   U   C          
SEQRES 117 A 2927    C   G   C   G   U   C   C   A   A   G   C   A   G          
SEQRES 118 A 2927    U   U   A   G   G   C   U   G   G   G   A   A   A          
SEQRES 119 A 2927    U   A   G   G   C   A   A   A   U   C   C   G   U          
SEQRES 120 A 2927    U   U   C   C   C   A   U   A   A   G   G   C   U          
SEQRES 121 A 2927    G   A   G   C   U   G   U   G   A   U   G   G   C          
SEQRES 122 A 2927    G   A   G   C   G   A   A   A   U   A   U   A   G          
SEQRES 123 A 2927    U   A   G   C   G   A   A   G   U   U   C   C   U          
SEQRES 124 A 2927    G   A   U   U   C   C   A   C   A   C   U   G   C          
SEQRES 125 A 2927    C   A   A   G   A   A   A   A   G   C   C   U   C          
SEQRES 126 A 2927    U   A   G   C   G   A   G   G   U   G   A   G   A          
SEQRES 127 A 2927    G   G   U   G   C   C   C   G   U   A   C   C   G          
SEQRES 128 A 2927    C   A   A   A   C   C   G   A   C   A   C   A   G          
SEQRES 129 A 2927    G   U   A   G   G   C   G   A   G   G   A   G   A          
SEQRES 130 A 2927    G   A   A   U   C   C   U   A   A   G   G   U   G          
SEQRES 131 A 2927    A   U   C   G   A   G   A   G   A   A   C   U   C          
SEQRES 132 A 2927    U   C   G   U   U   A   A   G   G   A   A   C   U          
SEQRES 133 A 2927    C   G   G   C   A   A   A   A   U   G   A   C   C          
SEQRES 134 A 2927    C   C   G   U   A   A   C   U   U   C   G   G   G          
SEQRES 135 A 2927    A   G   A   A   G   G   G   G   U   G   C   U   C          
SEQRES 136 A 2927    U   G   U   U   A   G   G   G   U   G   C   A   A          
SEQRES 137 A 2927    G   C   C   C   G   A   G   A   G   A   G   C   C          
SEQRES 138 A 2927    G   C   A   G   U   G   A   A   U   A   G   G   C          
SEQRES 139 A 2927    C   C   A   G   G   C   G   A   C   U   G   U   U          
SEQRES 140 A 2927    U   A   G   C   A   A   A   A   A   C   A   C   A          
SEQRES 141 A 2927    G   G   U   C   U   C   U   G   C   G   A   A   G          
SEQRES 142 A 2927    C   C   G   U   A   A   G   G   C   G   A   A   G          
SEQRES 143 A 2927    U   A   U   A   G   G   G   G   C   U   G   A   C          
SEQRES 144 A 2927    G   C   C   U   G   C   C   C   G   G   U   G   C          
SEQRES 145 A 2927    U   G   G   A   A   G   G   U   U   A   A   G   A          
SEQRES 146 A 2927    G   G   A   G   C   G   C   U   U   A   G   C   G          
SEQRES 147 A 2927    U   A   A   G   C   G   A   A   G   G   U   G   C          
SEQRES 148 A 2927    G   A   A   U   U   G   A   A   G   C   C   C   C          
SEQRES 149 A 2927    A   G   U   A   A   A   C   G   G   C   G   G   C          
SEQRES 150 A 2927    C   G   U   A   A   C   U   A   U   A   A   C   G          
SEQRES 151 A 2927    G   U   C   C   U   A   A   G   G   U   A   G   C          
SEQRES 152 A 2927    G   A   A   A   U   U   C   C   U   U   G   U   C          
SEQRES 153 A 2927    G   G   G   U   A   A   G   U   U   C   C   G   A          
SEQRES 154 A 2927    C   C   C   G   C   A   C   G   A   A   A   G   G          
SEQRES 155 A 2927    C   G   C   A   A   C   G   A   U   C   U   G   G          
SEQRES 156 A 2927    G   C   A   C   U   G   U   C   U   C   A   A   C          
SEQRES 157 A 2927    G   A   G   A   G   A   C   U   C   G   G   U   G          
SEQRES 158 A 2927    A   A   A   U   U   A   U   A   G   U   A   C   C          
SEQRES 159 A 2927    U   G   U   G   A   A   G   A   U   G   C   A   G          
SEQRES 160 A 2927    G   U   U   A   C   C   C   G   C   G   A   C   A          
SEQRES 161 A 2927    G   G   A   C   G   G   A   A   A   G   A   C   C          
SEQRES 162 A 2927    C   C   G   U   G   G   A   G   C   U   U   U   A          
SEQRES 163 A 2927    C   U   G   C   A   G   C   C   U   G   A   U   A          
SEQRES 164 A 2927    U   U   G   A   A   U   G   U   U   G   G   U   A          
SEQRES 165 A 2927    C   A   G   C   U   U   G   U   A   C   A   G   G          
SEQRES 166 A 2927    A   U   A   G   G   U   A   G   G   A   G   C   C          
SEQRES 167 A 2927    U   U   G   G   A   A   A   C   C   G   G   A   G          
SEQRES 168 A 2927    C   G   C   C   A   G   C   U   U   C   G   G   U          
SEQRES 169 A 2927    G   G   A   G   G   C   A   U   C   G   G   U   G          
SEQRES 170 A 2927    G   G   A   U   A   C   U   A   C   C   C   U   G          
SEQRES 171 A 2927    G   C   U   G   U   A   U   U   G   A   C   C   U          
SEQRES 172 A 2927    U   C   U   A   A   C   C   C   G   C   C   G   C          
SEQRES 173 A 2927    C   C   U   U   A   U   C   G   G   G   C   G   G          
SEQRES 174 A 2927    G   G   A   G   A   C   A   G   U   G   U   C   A          
SEQRES 175 A 2927    G   G   U   G   G   G   C   A   G   U   U   U   G          
SEQRES 176 A 2927    A   C   U   G   G   G   G   C   G   G   U   C   G          
SEQRES 177 A 2927    C   C   U   C   C   U   A   A   A   A   G   G   U          
SEQRES 178 A 2927    A   A   C   G   G   A   G   G   C   G   C   C   C          
SEQRES 179 A 2927    A   A   A   G   G   U   U   C   C   C   U   C   A          
SEQRES 180 A 2927    G   A   A   U   G   G   U   U   G   G   A   A   A          
SEQRES 181 A 2927    U   C   A   U   U   C   G   C   A   G   A   G   U          
SEQRES 182 A 2927    G   U   A   A   A   G   G   C   A   C   A   A   G          
SEQRES 183 A 2927    G   G   A   G   C   U   U   G   A   C   U   G   C          
SEQRES 184 A 2927    G   A   G   A   C   C   U   A   C   A   A   G   U          
SEQRES 185 A 2927    C   G   A   G   C   A   G   G   G   A   C   G   A          
SEQRES 186 A 2927    A   A   G   U   C   G   G   G   C   U   U   A   G          
SEQRES 187 A 2927    U   G   A   U   C   C   G   G   U   G   G   U   U          
SEQRES 188 A 2927    C   C   G   C   A   U   G   G   A   A   G   G   G          
SEQRES 189 A 2927    C   C   A   U   C   G   C   U   C   A   A   C   G          
SEQRES 190 A 2927    G   A   U   A   A   A   A   G   C   U   A   C   C          
SEQRES 191 A 2927    C   C   G   G   G   G   A   U   A   A   C   A   G          
SEQRES 192 A 2927    G   C   U   U   A   U   C   U   C   C   C   C   C          
SEQRES 193 A 2927    A   A   G   A   G   U   C   C   A   C   A   U   C          
SEQRES 194 A 2927    G   A   C   G   G   G   G   A   G   G   U   U   U          
SEQRES 195 A 2927    G   G   C   A   C   C   U   C   G   A   U   G   U          
SEQRES 196 A 2927    C   G   G   C   U   C   A   U   C   G   C   A   U          
SEQRES 197 A 2927    C   C   U   G   G   G   G   C   U   G   U   A   G          
SEQRES 198 A 2927    U   C   A   G   U   C   C   C   A   A   G   G   G          
SEQRES 199 A 2927    U   U   G   G   G   C   U   G   U   U   C   G   C          
SEQRES 200 A 2927    C   C   A   U   U   A   A   A   G   C   G   G   U          
SEQRES 201 A 2927    A   C   G   C   G   A   G   C   U   G   G   G   U          
SEQRES 202 A 2927    U   C   A   G   A   A   C   G   U   C   G   U   G          
SEQRES 203 A 2927    A   G   A   C   A   G   U   U   C   G   G   U   C          
SEQRES 204 A 2927    C   C   U   A   U   C   C   G   U   C   G   C   G          
SEQRES 205 A 2927    G   G   C   G   C   A   G   G   A   A   A   U   U          
SEQRES 206 A 2927    U   G   A   G   A   G   G   A   G   C   U   G   U          
SEQRES 207 A 2927    C   C   U   U   A   G   U   A   C   G   A   G   A          
SEQRES 208 A 2927    G   G   A   C   C   G   G   G   A   U   G   G   A          
SEQRES 209 A 2927    C   G   C   A   C   C   G   C   U   G   G   U   G          
SEQRES 210 A 2927    U   A   C   C   A   G   U   U   G   U   U   C   U          
SEQRES 211 A 2927    G   C   C   A   A   G   G   G   C   A   U   C   G          
SEQRES 212 A 2927    C   U   G   G   G   U   A   G   C   U   A   U   G          
SEQRES 213 A 2927    U   G   C   G   G   A   C   G   G   G   A   U   A          
SEQRES 214 A 2927    A   G   U   G   C   U   G   A   A   A   G   C   A          
SEQRES 215 A 2927    U   C   U   A   A   G   C   A   U   G   A   A   G          
SEQRES 216 A 2927    C   C   C   C   C   C   U   C   A   A   G   A   U          
SEQRES 217 A 2927    G   A   G   A   U   U   U   C   C   C   A   U   U          
SEQRES 218 A 2927    C   C   G   C   A   A   G   G   A   A   G   U   A          
SEQRES 219 A 2927    A   G   A   U   C   C   C   U   G   A   A   A   G          
SEQRES 220 A 2927    A   U   G   A   U   C   A   G   G   U   U   G   A          
SEQRES 221 A 2927    U   A   G   G   U   C   U   G   A   G   G   U   G          
SEQRES 222 A 2927    G   A   A   G   U   G   U   G   G   C   G   A   C          
SEQRES 223 A 2927    A   C   A   U   G   G   A   G   C   U   G   A   C          
SEQRES 224 A 2927    A   G   A   U   A   C   U   A   A   U   C   G   A          
SEQRES 225 A 2927    U   C   G   A   G   G   A   C   U   U   A   A   C          
SEQRES 226 A 2927    C   A                                                      
SEQRES   1 B  119    U   U   U   G   G   U   G   G   C   G   A   U   A          
SEQRES   2 B  119    G   C   G   A   A   G   A   G   G   U   C   A   C          
SEQRES   3 B  119    A   C   C   C   G   U   U   C   C   C   A   U   A          
SEQRES   4 B  119    C   C   G   A   A   C   A   C   G   G   A   A   G          
SEQRES   5 B  119    U   U   A   A   G   C   U   C   U   U   C   A   G          
SEQRES   6 B  119    C   G   C   C   G   A   U   G   G   U   A   G   U          
SEQRES   7 B  119    C   G   G   G   G   G   U   U   U   C   C   C   C          
SEQRES   8 B  119    C   U   G   U   G   A   G   A   G   U   A   G   G          
SEQRES   9 B  119    A   C   G   C   C   G   C   C   A   A   G   C   A          
SEQRES  10 B  119    A   G                                                      
SEQRES   1 C  277  MET ALA ILE LYS LYS TYR LYS PRO THR SER ASN GLY ARG          
SEQRES   2 C  277  ARG GLY MET THR THR SER ASP PHE ALA GLU ILE THR THR          
SEQRES   3 C  277  ASP LYS PRO GLU LYS SER LEU LEU ALA PRO LEU HIS LYS          
SEQRES   4 C  277  LYS GLY GLY ARG ASN ASN GLN GLY LYS LEU THR VAL ARG          
SEQRES   5 C  277  HIS GLN GLY GLY GLY HIS LYS ARG GLN TYR ARG VAL ILE          
SEQRES   6 C  277  ASP PHE LYS ARG ASP LYS ASP GLY ILE PRO GLY ARG VAL          
SEQRES   7 C  277  ALA THR VAL GLU TYR ASP PRO ASN ARG SER ALA ASN ILE          
SEQRES   8 C  277  ALA LEU ILE ASN TYR ALA ASP GLY GLU LYS ARG TYR ILE          
SEQRES   9 C  277  LEU ALA PRO LYS GLY ILE GLN VAL GLY THR GLU ILE MET          
SEQRES  10 C  277  SER GLY PRO GLU ALA ASP ILE LYS VAL GLY ASN ALA LEU          
SEQRES  11 C  277  PRO LEU ILE ASN ILE PRO VAL GLY THR VAL VAL HIS ASN          
SEQRES  12 C  277  ILE GLU LEU LYS PRO GLY LYS GLY GLY GLN LEU VAL ARG          
SEQRES  13 C  277  SER ALA GLY THR SER ALA GLN VAL LEU GLY LYS GLU GLY          
SEQRES  14 C  277  LYS TYR VAL LEU VAL ARG LEU ASN SER GLY GLU VAL ARG          
SEQRES  15 C  277  MET ILE LEU SER ALA CYS ARG ALA SER ILE GLY GLN VAL          
SEQRES  16 C  277  GLY ASN GLU GLN HIS GLU LEU ILE ASN ILE GLY LYS ALA          
SEQRES  17 C  277  GLY ARG SER ARG TRP LYS GLY ILE ARG PRO THR VAL ARG          
SEQRES  18 C  277  GLY SER VAL MET ASN PRO ASN ASP HIS PRO HIS GLY GLY          
SEQRES  19 C  277  GLY GLU GLY ARG ALA PRO ILE GLY ARG LYS SER PRO MET          
SEQRES  20 C  277  SER PRO TRP GLY LYS PRO THR LEU GLY PHE LYS THR ARG          
SEQRES  21 C  277  LYS LYS LYS ASN LYS SER ASP LYS PHE ILE VAL ARG ARG          
SEQRES  22 C  277  ARG LYS ASN LYS                                              
SEQRES   1 D  209  MET THR LYS GLY ILE LEU GLY ARG LYS ILE GLY MET THR          
SEQRES   2 D  209  GLN VAL PHE ALA GLU ASN GLY ASP LEU ILE PRO VAL THR          
SEQRES   3 D  209  VAL ILE GLU ALA ALA PRO ASN VAL VAL LEU GLN LYS LYS          
SEQRES   4 D  209  THR ALA GLU ASN ASP GLY TYR GLU ALA ILE GLN LEU GLY          
SEQRES   5 D  209  PHE ASP ASP LYS ARG GLU LYS LEU SER ASN LYS PRO GLU          
SEQRES   6 D  209  LYS GLY HIS VAL ALA LYS ALA GLU THR ALA PRO LYS ARG          
SEQRES   7 D  209  PHE VAL LYS GLU LEU ARG GLY VAL GLU MET ASP ALA TYR          
SEQRES   8 D  209  GLU VAL GLY GLN GLU VAL LYS VAL GLU ILE PHE SER ALA          
SEQRES   9 D  209  GLY GLU ILE VAL ASP VAL THR GLY VAL SER LYS GLY LYS          
SEQRES  10 D  209  GLY PHE GLN GLY ALA ILE LYS ARG HIS GLY GLN SER ARG          
SEQRES  11 D  209  GLY PRO MET SER HIS GLY SER ARG TYR HIS ARG ARG PRO          
SEQRES  12 D  209  GLY SER MET GLY PRO VAL ASP PRO ASN ARG VAL PHE LYS          
SEQRES  13 D  209  GLY LYS LEU LEU PRO GLY ARG MET GLY GLY GLU GLN ILE          
SEQRES  14 D  209  THR VAL GLN ASN LEU GLU ILE VAL LYS VAL ASP ALA GLU          
SEQRES  15 D  209  ARG ASN LEU LEU LEU ILE LYS GLY ASN VAL PRO GLY ALA          
SEQRES  16 D  209  LYS LYS SER LEU ILE THR VAL LYS SER ALA VAL LYS SER          
SEQRES  17 D  209  LYS                                                          
SEQRES   1 E  207  MET PRO LYS VAL ALA LEU TYR ASN GLN ASN GLY SER THR          
SEQRES   2 E  207  ALA GLY ASP ILE GLU LEU ASN ALA SER VAL PHE GLY ILE          
SEQRES   3 E  207  GLU PRO ASN GLU SER VAL VAL PHE ASP ALA ILE LEU MET          
SEQRES   4 E  207  GLN ARG ALA SER LEU ARG GLN GLY THR HIS LYS VAL LYS          
SEQRES   5 E  207  ASN ARG SER GLU VAL ARG GLY GLY GLY ARG LYS PRO TRP          
SEQRES   6 E  207  ARG GLN LYS GLY THR GLY ARG ALA ARG GLN GLY SER ILE          
SEQRES   7 E  207  ARG SER PRO GLN TRP ARG GLY GLY GLY VAL VAL PHE GLY          
SEQRES   8 E  207  PRO THR PRO ARG SER TYR SER TYR LYS LEU PRO LYS LYS          
SEQRES   9 E  207  VAL ARG ARG LEU ALA ILE LYS SER VAL LEU SER SER LYS          
SEQRES  10 E  207  VAL ILE ASP ASN ASN ILE ILE VAL LEU GLU ASP LEU THR          
SEQRES  11 E  207  LEU ASP THR ALA LYS THR LYS GLU MET ALA ALA ILE LEU          
SEQRES  12 E  207  LYS GLY LEU SER VAL GLU LYS LYS ALA LEU ILE VAL THR          
SEQRES  13 E  207  ALA ASP ALA ASN GLU ALA VAL ALA LEU SER ALA ARG ASN          
SEQRES  14 E  207  ILE PRO GLY VAL THR VAL VAL GLU ALA ASN GLY ILE ASN          
SEQRES  15 E  207  VAL LEU ASP VAL VAL ASN HIS GLU LYS LEU LEU ILE THR          
SEQRES  16 E  207  LYS ALA ALA VAL GLU LYS VAL GLU GLU VAL LEU ALA              
SEQRES   1 F  179  MET ASN ARG LEU LYS GLU LYS TYR ASN LYS GLU ILE ALA          
SEQRES   2 F  179  PRO ALA LEU MET THR LYS PHE ASN TYR ASP SER VAL MET          
SEQRES   3 F  179  GLN VAL PRO LYS ILE GLU LYS ILE VAL ILE ASN MET GLY          
SEQRES   4 F  179  VAL GLY ASP ALA VAL GLN ASN ALA LYS ALA ILE ASP SER          
SEQRES   5 F  179  ALA VAL GLU GLU LEU THR PHE ILE ALA GLY GLN LYS PRO          
SEQRES   6 F  179  VAL VAL THR ARG ALA LYS LYS SER ILE ALA GLY PHE ARG          
SEQRES   7 F  179  LEU ARG GLU GLY MET PRO ILE GLY ALA LYS VAL THR LEU          
SEQRES   8 F  179  ARG GLY GLU ARG MET TYR ASP PHE LEU ASP LYS LEU ILE          
SEQRES   9 F  179  SER VAL SER LEU PRO ARG VAL ARG ASP PHE ARG GLY VAL          
SEQRES  10 F  179  SER LYS LYS SER PHE ASP GLY ARG GLY ASN TYR THR LEU          
SEQRES  11 F  179  GLY ILE LYS GLU GLN LEU ILE PHE PRO GLU ILE ASP TYR          
SEQRES  12 F  179  ASP LYS VAL THR LYS VAL ARG GLY MET ASP ILE VAL ILE          
SEQRES  13 F  179  VAL THR THR ALA ASN THR ASP GLU GLU ALA ARG GLU LEU          
SEQRES  14 F  179  LEU THR GLN VAL GLY MET PRO PHE GLN LYS                      
SEQRES   1 G  179  MET SER ARG VAL GLY LYS LYS LEU LEU GLU ILE PRO SER          
SEQRES   2 G  179  ASP VAL THR VAL THR LEU ASN ASP ASN ASN THR VAL ALA          
SEQRES   3 G  179  VAL LYS GLY PRO LYS GLY GLU LEU THR ARG THR PHE HIS          
SEQRES   4 G  179  PRO ASP MET GLU ILE LYS VAL GLU ASP ASN VAL LEU THR          
SEQRES   5 G  179  VAL ALA ARG PRO SER ASP GLN LYS GLU HIS ARG ALA LEU          
SEQRES   6 G  179  HIS GLY THR THR ARG SER LEU LEU GLY ASN MET VAL GLU          
SEQRES   7 G  179  GLY VAL SER LYS GLY PHE GLU ARG GLY LEU GLU LEU VAL          
SEQRES   8 G  179  GLY VAL GLY TYR ARG ALA SER LYS SER GLY ASN LYS LEU          
SEQRES   9 G  179  VAL LEU ASN VAL GLY TYR SER HIS PRO VAL GLU ILE VAL          
SEQRES  10 G  179  PRO GLU GLU GLY ILE GLU ILE GLU VAL PRO SER GLN THR          
SEQRES  11 G  179  LYS VAL VAL VAL LYS GLY THR ASP LYS GLU ARG VAL GLY          
SEQRES  12 G  179  ALA ILE ALA ALA ASN ILE ARG ALA VAL ARG SER PRO GLU          
SEQRES  13 G  179  PRO TYR LYS GLY LYS GLY ILE ARG TYR GLU GLY GLU VAL          
SEQRES  14 G  179  VAL ARG ARG LYS GLU GLY LYS SER ALA LYS                      
SEQRES   1 J  145  MET ARG THR THR PRO MET ALA ASN ALA SER THR ILE GLU          
SEQRES   2 J  145  ARG LYS TRP LEU VAL VAL ASP ALA ALA GLY LYS THR LEU          
SEQRES   3 J  145  GLY ARG LEU SER SER GLU VAL ALA ALA ILE LEU ARG GLY          
SEQRES   4 J  145  LYS HIS LYS PRO THR TYR THR PRO HIS VAL ASP THR GLY          
SEQRES   5 J  145  ASP HIS VAL ILE ILE ILE ASN ALA GLU LYS ILE GLU LEU          
SEQRES   6 J  145  THR GLY LYS LYS LEU THR ASP LYS ILE TYR TYR ARG HIS          
SEQRES   7 J  145  THR GLN HIS PRO GLY GLY LEU LYS SER ARG THR ALA LEU          
SEQRES   8 J  145  GLU MET ARG THR ASN TYR PRO GLU LYS MET LEU GLU LEU          
SEQRES   9 J  145  ALA ILE LYS GLY MET LEU PRO LYS GLY SER LEU GLY ARG          
SEQRES  10 J  145  GLN MET PHE LYS LYS LEU ASN VAL TYR ARG GLY SER GLU          
SEQRES  11 J  145  HIS PRO HIS GLU ALA GLN LYS PRO GLU VAL TYR GLU LEU          
SEQRES  12 J  145  ARG GLY                                                      
SEQRES   1 K  122  MET ILE GLN GLN GLU THR ARG LEU LYS VAL ALA ASP ASN          
SEQRES   2 K  122  SER GLY ALA ARG GLU VAL LEU THR ILE LYS VAL LEU GLY          
SEQRES   3 K  122  GLY SER GLY ARG LYS THR ALA ASN ILE GLY ASP VAL ILE          
SEQRES   4 K  122  VAL CYS THR VAL LYS GLN ALA THR PRO GLY GLY VAL VAL          
SEQRES   5 K  122  LYS LYS GLY GLU VAL VAL LYS ALA VAL ILE VAL ARG THR          
SEQRES   6 K  122  LYS SER GLY ALA ARG ARG SER ASP GLY SER TYR ILE SER          
SEQRES   7 K  122  PHE ASP GLU ASN ALA CYS VAL ILE ILE ARG ASP ASP LYS          
SEQRES   8 K  122  SER PRO ARG GLY THR ARG ILE PHE GLY PRO VAL ALA ARG          
SEQRES   9 K  122  GLU LEU ARG GLU ASN ASN PHE MET LYS ILE VAL SER LEU          
SEQRES  10 K  122  ALA PRO GLU VAL ILE                                          
SEQRES   1 L  146  MET LYS LEU HIS GLU LEU LYS PRO SER GLU GLY SER ARG          
SEQRES   2 L  146  LYS THR ARG ASN ARG VAL GLY ARG GLY ILE GLY SER GLY          
SEQRES   3 L  146  ASN GLY LYS THR ALA GLY LYS GLY HIS LYS GLY GLN ASN          
SEQRES   4 L  146  ALA ARG SER GLY GLY GLY VAL ARG PRO GLY PHE GLU GLY          
SEQRES   5 L  146  GLY GLN MET PRO LEU PHE GLN ARG LEU PRO LYS ARG GLY          
SEQRES   6 L  146  PHE THR ASN ILE ASN ARG LYS GLU TYR ALA VAL VAL ASN          
SEQRES   7 L  146  LEU ASP LYS LEU ASN GLY PHE ALA GLU GLY THR GLU VAL          
SEQRES   8 L  146  THR PRO GLU LEU LEU LEU GLU THR GLY VAL ILE SER LYS          
SEQRES   9 L  146  LEU ASN ALA GLY VAL LYS ILE LEU GLY ASN GLY LYS LEU          
SEQRES  10 L  146  GLU LYS LYS LEU THR VAL LYS ALA ASN LYS PHE SER ALA          
SEQRES  11 L  146  SER ALA LYS GLU ALA VAL GLU ALA ALA GLY GLY THR ALA          
SEQRES  12 L  146  GLU VAL ILE                                                  
SEQRES   1 N  120  MET SER TYR ARG LYS LEU GLY ARG THR SER ALA GLN ARG          
SEQRES   2 N  120  LYS ALA MET LEU ARG ASP LEU THR THR ASP LEU ILE ILE          
SEQRES   3 N  120  ASN GLU ARG ILE GLU THR THR GLU THR ARG ALA LYS GLU          
SEQRES   4 N  120  LEU ARG SER VAL VAL GLU LYS MET ILE THR LEU GLY LYS          
SEQRES   5 N  120  ARG GLY ASP LEU HIS ALA ARG ARG GLN ALA ALA ALA TYR          
SEQRES   6 N  120  ILE ARG ASN GLU VAL ALA ASN GLU GLU ASN ASN GLN ASP          
SEQRES   7 N  120  ALA LEU GLN LYS LEU PHE SER ASP ILE ALA THR ARG TYR          
SEQRES   8 N  120  GLU GLU ARG GLN GLY GLY TYR THR ARG ILE MET LYS LEU          
SEQRES   9 N  120  GLY PRO ARG ARG GLY ASP GLY ALA PRO MET ALA ILE ILE          
SEQRES  10 N  120  GLU LEU VAL                                                  
SEQRES   1 O  120  MET ILE THR LYS THR SER LYS ASN ALA ALA ARG LEU LYS          
SEQRES   2 O  120  ARG HIS ALA ARG VAL ARG ALA LYS LEU SER GLY THR ALA          
SEQRES   3 O  120  GLU ARG PRO ARG LEU ASN VAL PHE ARG SER ASN LYS HIS          
SEQRES   4 O  120  ILE TYR ALA GLN ILE ILE ASP ASP VAL ASN GLY VAL THR          
SEQRES   5 O  120  LEU ALA SER ALA SER THR LEU ASP LYS ASP LEU ASN VAL          
SEQRES   6 O  120  GLU SER THR GLY ASP THR SER ALA ALA THR LYS VAL GLY          
SEQRES   7 O  120  GLU LEU VAL ALA LYS ARG ALA ALA GLU LYS GLY ILE SER          
SEQRES   8 O  120  ASP VAL VAL PHE ASP ARG GLY GLY TYR LEU TYR HIS GLY          
SEQRES   9 O  120  ARG VAL LYS ALA LEU ALA ASP ALA ALA ARG GLU ALA GLY          
SEQRES  10 O  120  LEU LYS PHE                                                  
SEQRES   1 P  115  MET GLN LYS LEU ILE GLU ASP ILE THR LYS GLU GLN LEU          
SEQRES   2 P  115  ARG THR ASP LEU PRO ALA PHE ARG PRO GLY ASP THR LEU          
SEQRES   3 P  115  ARG VAL HIS VAL LYS VAL VAL GLU GLY ASN ARG GLU ARG          
SEQRES   4 P  115  ILE GLN ILE PHE GLU GLY VAL VAL ILE LYS ARG ARG GLY          
SEQRES   5 P  115  GLY GLY ILE SER GLU THR PHE THR VAL ARG LYS ILE SER          
SEQRES   6 P  115  TYR GLY VAL GLY VAL GLU ARG THR PHE PRO VAL HIS THR          
SEQRES   7 P  115  PRO LYS ILE ALA LYS ILE GLU VAL VAL ARG TYR GLY LYS          
SEQRES   8 P  115  VAL ARG ARG ALA LYS LEU TYR TYR LEU ARG GLU LEU ARG          
SEQRES   9 P  115  GLY LYS ALA ALA ARG ILE LYS GLU ILE ARG ARG                  
SEQRES   1 Q  119  MET PRO ARG VAL LYS GLY GLY THR VAL THR ARG LYS ARG          
SEQRES   2 Q  119  ARG LYS LYS VAL LEU LYS LEU ALA LYS GLY TYR PHE GLY          
SEQRES   3 Q  119  SER LYS HIS THR LEU TYR LYS VAL ALA ASN GLN GLN VAL          
SEQRES   4 Q  119  MET LYS SER GLY ASN TYR ALA PHE ARG ASP ARG ARG GLN          
SEQRES   5 Q  119  LYS LYS ARG ASP PHE ARG LYS LEU TRP ILE THR ARG ILE          
SEQRES   6 Q  119  ASN ALA ALA ALA ARG MET ASN GLY LEU SER TYR SER ARG          
SEQRES   7 Q  119  LEU MET HIS GLY LEU LYS LEU SER GLY ILE GLU VAL ASN          
SEQRES   8 Q  119  ARG LYS MET LEU ALA ASP LEU ALA VAL ASN ASP LEU THR          
SEQRES   9 Q  119  ALA PHE ASN GLN LEU ALA ASP ALA ALA LYS ALA GLN LEU          
SEQRES  10 Q  119  ASN LYS                                                      
SEQRES   1 R  102  MET TYR ALA ILE ILE LYS THR GLY GLY LYS GLN ILE LYS          
SEQRES   2 R  102  VAL GLU GLU GLY GLN THR VAL TYR ILE GLU LYS LEU ALA          
SEQRES   3 R  102  ALA GLU ALA GLY GLU THR VAL THR PHE GLU ASP VAL LEU          
SEQRES   4 R  102  PHE VAL GLY GLY ASP ASN VAL LYS VAL GLY ASN PRO THR          
SEQRES   5 R  102  VAL GLU GLY ALA THR VAL THR ALA LYS VAL GLU LYS GLN          
SEQRES   6 R  102  GLY ARG ALA LYS LYS ILE THR VAL PHE ARG TYR LYS PRO          
SEQRES   7 R  102  LYS LYS ASN VAL HIS LYS LYS GLN GLY HIS ARG GLN PRO          
SEQRES   8 R  102  TYR THR LYS VAL THR ILE GLU LYS ILE ASN ALA                  
SEQRES   1 S  113  MET GLN ALA LYS ALA VAL ALA ARG THR VAL ARG ILE ALA          
SEQRES   2 S  113  PRO ARG LYS ALA ARG LEU VAL MET ASP LEU ILE ARG GLY          
SEQRES   3 S  113  LYS GLN VAL GLY GLU ALA VAL SER ILE LEU ASN LEU THR          
SEQRES   4 S  113  PRO ARG ALA ALA SER PRO ILE ILE GLU LYS VAL LEU LYS          
SEQRES   5 S  113  SER ALA ILE ALA ASN ALA GLU HIS ASN TYR GLU MET ASP          
SEQRES   6 S  113  ALA ASN ASN LEU VAL ILE SER GLN ALA PHE VAL ASP GLU          
SEQRES   7 S  113  GLY PRO THR LEU LYS ARG PHE ARG PRO ARG ALA MET GLY          
SEQRES   8 S  113  ARG ALA SER GLN ILE ASN LYS ARG THR SER HIS ILE THR          
SEQRES   9 S  113  ILE VAL VAL SER GLU LYS LYS GLU GLY                          
SEQRES   1 T   95  MET LYS ASP PRO ARG ASP VAL LEU LYS ARG PRO VAL ILE          
SEQRES   2 T   95  THR GLU ARG SER ALA ASP LEU MET THR GLU LYS LYS TYR          
SEQRES   3 T   95  THR PHE GLU VAL ASP VAL ARG ALA ASN LYS THR GLU VAL          
SEQRES   4 T   95  LYS ASP ALA VAL GLU SER ILE PHE GLY VAL LYS VAL ASP          
SEQRES   5 T   95  LYS VAL ASN ILE MET ASN TYR LYS GLY LYS SER LYS ARG          
SEQRES   6 T   95  VAL GLY ARG TYR THR GLY MET THR SER ARG ARG ARG LYS          
SEQRES   7 T   95  ALA ILE VAL LYS LEU THR ALA ASP SER LYS GLU ILE GLU          
SEQRES   8 T   95  ILE PHE GLU ALA                                              
SEQRES   1 U  103  MET HIS VAL LYS LYS GLY ASP LYS VAL MET VAL ILE SER          
SEQRES   2 U  103  GLY LYS ASP LYS GLY LYS GLN GLY THR ILE LEU ALA ALA          
SEQRES   3 U  103  PHE PRO LYS LYS ASP ARG VAL LEU VAL GLU GLY VAL ASN          
SEQRES   4 U  103  MET VAL LYS LYS HIS SER LYS PRO THR GLN ALA ASN PRO          
SEQRES   5 U  103  GLN GLY GLY ILE SER ASN GLN GLU ALA PRO ILE HIS VAL          
SEQRES   6 U  103  SER ASN VAL MET PRO LEU ASP PRO LYS THR GLY GLU VAL          
SEQRES   7 U  103  THR ARG VAL GLY TYR LYS VAL GLU ASP GLY LYS LYS VAL          
SEQRES   8 U  103  ARG VAL ALA LYS LYS SER GLY GLN VAL LEU ASP LYS              
SEQRES   1 X   66  MET LYS ALA ASN GLU ILE ARG ASP LEU THR THR ALA GLU          
SEQRES   2 X   66  ILE GLU GLN LYS VAL LYS SER LEU LYS GLU GLU LEU PHE          
SEQRES   3 X   66  ASN LEU ARG PHE GLN LEU ALA THR GLY GLN LEU GLU ASN          
SEQRES   4 X   66  THR ALA ARG ILE ARG GLU VAL ARG LYS ALA ILE ALA ARG          
SEQRES   5 X   66  MET LYS THR VAL ILE ARG GLU ARG GLU ILE ALA ALA ASN          
SEQRES   6 X   66  LYS                                                          
SEQRES   1 Y   59  MET ALA LYS LEU GLU ILE THR LEU LYS ARG SER VAL ILE          
SEQRES   2 Y   59  GLY ARG PRO GLU ASP GLN ARG VAL THR VAL ARG THR LEU          
SEQRES   3 Y   59  GLY LEU LYS LYS THR ASN GLN THR VAL VAL HIS GLU ASP          
SEQRES   4 Y   59  ASN ALA ALA ILE ARG GLY MET ILE ASN LYS VAL SER HIS          
SEQRES   5 Y   59  LEU VAL SER VAL LYS GLU GLN                                  
HELIX    1   1 SER 0    9  ARG 0   17  1                                   9    
HELIX    2   2 ASN 2    8  HIS 2   16  1                                   9    
HELIX    3   3 GLY 2   17  MET 2   22  1                                   6    
HELIX    4   4 SER 2   24  GLY 2   38  1                                  15    
HELIX    5   5 GLY 5    5  ASP 5   16  1                                  12    
HELIX    6   6 ASP 5   22  VAL 5   30  1                                   9    
HELIX    7   7 LYS 5   54  GLN 5   58  5                                   5    
HELIX    8   8 GLU 5  181  ALA 5  199  1                                  19    
HELIX    9   9 ALA 6   21  GLY 6   25  5                                   5    
HELIX   10  10 ASN 6   34  ALA 6   47  1                                  14    
HELIX   11  11 PRO 6   74  GLY 6   84  1                                  11    
HELIX   12  12 LYS 6  101  LYS 6  112  1                                  12    
HELIX   13  13 MET 6  113  LEU 6  116  5                                   4    
HELIX   14  14 ASP 6  120  GLY 6  136  1                                  17    
HELIX   15  15 ASN D   62  LYS D   71  1                                  10    
HELIX   16  16 ASN E   29  ALA E   36  1                                   8    
HELIX   17  17 ILE E   37  ALA E   42  1                                   6    
HELIX   18  18 PRO E  102  ASP E  120  1                                  19    
HELIX   19  19 LYS E  135  LEU E  146  1                                  12    
HELIX   20  20 VAL E  183  ASN E  188  1                                   6    
HELIX   21  21 THR E  195  ALA E  207  1                                  13    
HELIX   22  22 ASN F    2  ILE F   12  1                                  11    
HELIX   23  23 ILE F   12  PHE F   20  1                                   9    
HELIX   24  24 ASP F   23  VAL F   28  1                                   6    
HELIX   25  25 ASP F   51  GLY F   62  1                                  12    
HELIX   26  26 GLY F   93  VAL F  106  1                                  14    
HELIX   27  27 GLN G   59  GLY G   83  1                                  25    
HELIX   28  28 ASP G  138  ALA G  151  1                                  14    
HELIX   29  29 ALA J    7  ILE J   12  1                                   6    
HELIX   30  30 GLY J   27  ARG J   38  1                                  12    
HELIX   31  31 GLY J   67  ASP J   72  1                                   6    
HELIX   32  32 THR J   89  THR J   95  1                                   7    
HELIX   33  33 LYS J  100  GLY J  108  1                                   9    
HELIX   34  34 GLY J  113  LYS J  121  1                                   9    
HELIX   35  35 PRO J  132  LYS J  137  5                                   6    
HELIX   36  36 ARG K  104  ASN K  109  1                                   6    
HELIX   37  37 PHE K  111  ALA K  118  1                                   8    
HELIX   38  38 ASP L   80  PHE L   85  5                                   6    
HELIX   39  39 SER L  129  ALA L  138  1                                  10    
HELIX   40  40 THR N    9  GLU N   28  1                                  20    
HELIX   41  41 GLU N   34  GLY N   54  1                                  21    
HELIX   42  42 ASP N   55  ALA N   63  1                                   9    
HELIX   43  43 ALA N   64  ILE N   66  5                                   3    
HELIX   44  44 ALA N   79  ASP N   86  1                                   8    
HELIX   45  45 ASP N   86  GLU N   92  1                                   7    
HELIX   46  46 LEU O   12  ARG O   19  1                                   8    
HELIX   47  47 THR O   71  ALA O   86  1                                  16    
HELIX   48  48 ALA O   86  SER O   91  1                                   6    
HELIX   49  49 HIS O  103  GLU O  115  1                                  13    
HELIX   50  50 LEU P    4  THR P    9  1                                   6    
HELIX   51  51 THR Q    8  LEU Q   20  1                                  13    
HELIX   52  52 LEU Q   31  MET Q   71  1                                  41    
HELIX   53  53 SER Q   75  GLY Q   87  1                                  13    
HELIX   54  54 MET Q   94  ALA Q   96  5                                   3    
HELIX   55  55 ASP Q   97  ASP Q  102  1                                   6    
HELIX   56  56 ASP Q  102  GLN Q  116  1                                  15    
HELIX   57  57 ALA S   13  ILE S   24  1                                  12    
HELIX   58  58 GLN S   28  LEU S   38  1                                  11    
HELIX   59  59 ALA S   43  GLU S   63  1                                  21    
HELIX   60  60 ASP S   65  ASN S   67  5                                   3    
HELIX   61  61 THR T   14  THR T   22  1                                   9    
HELIX   62  62 ASN T   35  PHE T   47  1                                  13    
HELIX   63  63 LYS X    2  LEU X    9  1                                   8    
HELIX   64  64 THR X   10  ARG X   29  1                                  20    
HELIX   65  65 ASN X   39  GLU X   61  1                                  23    
HELIX   66  66 PRO Y   16  LEU Y   26  1                                  11    
HELIX   67  67 ALA Y   41  VAL Y   50  1                                  10    
HELIX   68  68 SER Y   51  VAL Y   54  5                                   4    
SHEET    1   A 2 THR 0  28  GLU 0  29  0                                        
SHEET    2   A 2 MET 0  36  LYS 0  37 -1  O  LYS 0  37   N  THR 0  28           
SHEET    1   B 3 GLU 5  43  VAL 5  44  0                                        
SHEET    2   B 3 ALA 5 213  THR 5 215 -1  O  THR 5 215   N  GLU 5  43           
SHEET    3   B 3 GLY 5 221  LYS 5 223 -1  O  VAL 5 222   N  VAL 5 214           
SHEET    1   C 3 VAL 6   9  PRO 6  14  0                                        
SHEET    2   C 3 ILE 6  53  SER 6  59 -1  O  ILE 6  58   N  VAL 6   9           
SHEET    3   C 3 THR 6  67  THR 6  70 -1  O  ILE 6  69   N  GLU 6  57           
SHEET    1   D 2 ILE C   3  LYS C   5  0                                        
SHEET    2   D 2 THR C  17  SER C  19 -1  O  THR C  18   N  LYS C   4           
SHEET    1   E 2 HIS C  38  LYS C  39  0                                        
SHEET    2   E 2 ARG C  60  GLN C  61 -1  O  ARG C  60   N  LYS C  39           
SHEET    1   F 5 ILE C  65  ASP C  66  0                                        
SHEET    2   F 5 LYS C 101  LEU C 105  1  O  TYR C 103   N  ASP C  66           
SHEET    3   F 5 ILE C  91  TYR C  96 -1  N  ALA C  92   O  ILE C 104           
SHEET    4   F 5 GLY C  76  GLU C  82 -1  N  ARG C  77   O  ASN C  95           
SHEET    5   F 5 GLU C 115  ILE C 116 -1  O  ILE C 116   N  GLY C  76           
SHEET    1   G 3 ALA C 129  PRO C 131  0                                        
SHEET    2   G 3 ARG C 189  ILE C 192 -1  O  ALA C 190   N  LEU C 130           
SHEET    3   G 3 VAL C 141  HIS C 142 -1  N  HIS C 142   O  SER C 191           
SHEET    1   H 3 GLN C 163  GLU C 168  0                                        
SHEET    2   H 3 TYR C 171  ARG C 175 -1  O  ARG C 175   N  GLN C 163           
SHEET    3   H 3 VAL C 181  LEU C 185 -1  O  ILE C 184   N  VAL C 172           
SHEET    1   I 8 THR D  13  VAL D  15  0                                        
SHEET    2   I 8 ILE D  23  ALA D  30 -1  O  VAL D  25   N  THR D  13           
SHEET    3   I 8 LEU D 185  LYS D 189 -1  O  ILE D 188   N  THR D  26           
SHEET    4   I 8 GLN D 168  ASP D 180 -1  N  GLU D 175   O  LYS D 189           
SHEET    5   I 8 ILE D 107  VAL D 113 -1  N  VAL D 108   O  LEU D 174           
SHEET    6   I 8 LEU D 199  SER D 204 -1  O  LYS D 203   N  ASP D 109           
SHEET    7   I 8 GLY D   4  LYS D   9 -1  N  GLY D   7   O  ILE D 200           
SHEET    8   I 8 ILE D  23  ALA D  30 -1  O  GLU D  29   N  ARG D   8           
SHEET    1   J 4 VAL D  80  ARG D  84  0                                        
SHEET    2   J 4 ALA D  48  GLY D  52 -1  N  ILE D  49   O  LEU D  83           
SHEET    3   J 4 ASN D  33  LYS D  39 -1  N  LEU D  36   O  GLN D  50           
SHEET    4   J 4 GLN D  95  GLU D  96 -1  O  GLU D  96   N  ASN D  33           
SHEET    1   K 2 GLY D 116  GLN D 120  0                                        
SHEET    2   K 2 GLY D 162  GLY D 165 -1  O  MET D 164   N  GLY D 118           
SHEET    1   L 2 LYS E   3  VAL E   4  0                                        
SHEET    2   L 2 ILE E  17  GLU E  18 -1  O  ILE E  17   N  VAL E   4           
SHEET    1   M 3 ILE F  31  ASN F  37  0                                        
SHEET    2   M 3 ASP F 153  THR F 158 -1  O  ASP F 153   N  ASN F  37           
SHEET    3   M 3 TYR F 128  GLY F 131 -1  N  LEU F 130   O  ILE F 154           
SHEET    1   N 3 THR G  16  THR G  18  0                                        
SHEET    2   N 3 THR G  24  GLY G  29 -1  O  ALA G  26   N  THR G  18           
SHEET    3   N 3 GLY G  32  THR G  37 -1  O  LEU G  34   N  VAL G  27           
SHEET    1   O 2 GLU G  43  GLU G  47  0                                        
SHEET    2   O 2 VAL G  50  ALA G  54 -1  O  ALA G  54   N  GLU G  43           
SHEET    1   P 4 ILE G 122  SER G 128  0                                        
SHEET    2   P 4 LYS G 131  GLY G 136 -1  O  LYS G 135   N  GLU G 123           
SHEET    3   P 4 PHE G  84  VAL G  91 -1  N  LEU G  88   O  VAL G 132           
SHEET    4   P 4 GLY G 162  ARG G 164 -1  O  ARG G 164   N  GLU G  89           
SHEET    1   Q 3 TYR G  95  SER G 100  0                                        
SHEET    2   Q 3 LYS G 103  VAL G 108 -1  O  VAL G 105   N  SER G  98           
SHEET    3   Q 3 VAL G 114  ILE G 116 -1  O  VAL G 114   N  LEU G 106           
SHEET    1   R 2 TRP J  16  VAL J  19  0                                        
SHEET    2   R 2 HIS J  54  ILE J  57  1  O  ILE J  56   N  VAL J  19           
SHEET    1   S 2 TYR J  75  HIS J  78  0                                        
SHEET    2   S 2 LEU J  85  ARG J  88 -1  O  LYS J  86   N  ARG J  77           
SHEET    1   T 6 ARG K   7  VAL K  10  0                                        
SHEET    2   T 6 ALA K  16  VAL K  24 -1  O  VAL K  19   N  LEU K   8           
SHEET    3   T 6 VAL K  38  ALA K  46 -1  O  VAL K  40   N  LYS K  23           
SHEET    4   T 6 VAL K  57  ARG K  64 -1  O  VAL K  58   N  CYS K  41           
SHEET    5   T 6 ALA K  83  ILE K  87 -1  O  VAL K  85   N  VAL K  61           
SHEET    6   T 6 ARG K   7  VAL K  10  1  N  LYS K   9   O  CYS K  84           
SHEET    1   U 3 ALA L  75  VAL L  77  0                                        
SHEET    2   U 3 VAL L 109  ILE L 111  1  O  LYS L 110   N  ALA L  75           
SHEET    3   U 3 LYS L 127  PHE L 128  1  O  LYS L 127   N  ILE L 111           
SHEET    1   V 3 ILE N  30  THR N  33  0                                        
SHEET    2   V 3 MET N 114  GLU N 118 -1  O  ILE N 117   N  ILE N  30           
SHEET    3   V 3 ARG N 100  MET N 102 -1  N  ARG N 100   O  GLU N 118           
SHEET    1   W 2 ALA R   3  THR R   7  0                                        
SHEET    2   W 2 LYS R  10  VAL R  14 -1  O  LYS R  10   N  THR R   7           
SHEET    1   X 4 GLN R  18  ILE R  22  0                                        
SHEET    2   X 4 THR R  93  ASN R 101 -1  O  ILE R  97   N  GLN R  18           
SHEET    3   X 4 THR R  57  VAL R  62 -1  N  LYS R  61   O  THR R  96           
SHEET    4   X 4 THR R  32  PHE R  35 -1  N  PHE R  35   O  VAL R  58           
SHEET    1   Y 2 ILE R  71  PHE R  74  0                                        
SHEET    2   Y 2 LYS R  85  HIS R  88 -1  O  GLN R  86   N  VAL R  73           
SHEET    1   Z 3 GLN S   2  ALA S   5  0                                        
SHEET    2   Z 3 HIS S 102  GLU S 109 -1  O  VAL S 107   N  ALA S   3           
SHEET    3   Z 3 LEU S  69  ASP S  77 -1  N  GLN S  73   O  VAL S 106           
SHEET    1  AA 4 LEU T   8  PRO T  11  0                                        
SHEET    2  AA 4 LYS T  25  VAL T  30 -1  O  GLU T  29   N  ARG T  10           
SHEET    3  AA 4 ARG T  76  LYS T  82 -1  O  ALA T  79   N  PHE T  28           
SHEET    4  AA 4 VAL T  54  TYR T  59 -1  N  MET T  57   O  LYS T  78           
SHEET    1  AB 2 VAL U   9  MET U  10  0                                        
SHEET    2  AB 2 VAL U  65  SER U  66 -1  O  SER U  66   N  VAL U   9           
SHEET    1  AC 2 LEU Y   4  ILE Y   6  0                                        
SHEET    2  AC 2 VAL Y  35  HIS Y  37 -1  O  HIS Y  37   N  LEU Y   4           
CISPEP   1 ASP D   89    ALA D   90          0        15.73                     
CISPEP   2 TYR D  139    HIS D  140          0        -5.92                     
CISPEP   3 ASN G   22    ASN G   23          0       -14.12                     
CISPEP   4 VAL R   48    GLY R   49          0        -3.53                     
CISPEP   5 ASP U   87    GLY U   88          0       -28.98                     
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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