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Database: PDB
Entry: 3JAM
LinkDB: 3JAM
Original site: 3JAM 
HEADER    TRANSLATION                             17-JUN-15   3JAM              
TITLE     CRYOEM STRUCTURE OF 40S-EIF1A-EIF1 COMPLEX FROM YEAST                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 18S RRNA;                                                  
COMPND   3 CHAIN: 2;                                                            
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: US2;                                                       
COMPND   6 CHAIN: A;                                                            
COMPND   7 MOL_ID: 3;                                                           
COMPND   8 MOLECULE: ES1;                                                       
COMPND   9 CHAIN: B;                                                            
COMPND  10 MOL_ID: 4;                                                           
COMPND  11 MOLECULE: US5;                                                       
COMPND  12 CHAIN: C;                                                            
COMPND  13 MOL_ID: 5;                                                           
COMPND  14 MOLECULE: US3;                                                       
COMPND  15 CHAIN: D;                                                            
COMPND  16 MOL_ID: 6;                                                           
COMPND  17 MOLECULE: ES4;                                                       
COMPND  18 CHAIN: E;                                                            
COMPND  19 MOL_ID: 7;                                                           
COMPND  20 MOLECULE: US7;                                                       
COMPND  21 CHAIN: F;                                                            
COMPND  22 MOL_ID: 8;                                                           
COMPND  23 MOLECULE: ES6;                                                       
COMPND  24 CHAIN: G;                                                            
COMPND  25 MOL_ID: 9;                                                           
COMPND  26 MOLECULE: ES7;                                                       
COMPND  27 CHAIN: H;                                                            
COMPND  28 MOL_ID: 10;                                                          
COMPND  29 MOLECULE: ES8;                                                       
COMPND  30 CHAIN: I;                                                            
COMPND  31 MOL_ID: 11;                                                          
COMPND  32 MOLECULE: US4;                                                       
COMPND  33 CHAIN: J;                                                            
COMPND  34 MOL_ID: 12;                                                          
COMPND  35 MOLECULE: ES10;                                                      
COMPND  36 CHAIN: K;                                                            
COMPND  37 MOL_ID: 13;                                                          
COMPND  38 MOLECULE: US17;                                                      
COMPND  39 CHAIN: L;                                                            
COMPND  40 MOL_ID: 14;                                                          
COMPND  41 MOLECULE: ES12;                                                      
COMPND  42 CHAIN: M;                                                            
COMPND  43 MOL_ID: 15;                                                          
COMPND  44 MOLECULE: US15;                                                      
COMPND  45 CHAIN: N;                                                            
COMPND  46 MOL_ID: 16;                                                          
COMPND  47 MOLECULE: US11;                                                      
COMPND  48 CHAIN: O;                                                            
COMPND  49 MOL_ID: 17;                                                          
COMPND  50 MOLECULE: US19;                                                      
COMPND  51 CHAIN: P;                                                            
COMPND  52 MOL_ID: 18;                                                          
COMPND  53 MOLECULE: US9;                                                       
COMPND  54 CHAIN: Q;                                                            
COMPND  55 MOL_ID: 19;                                                          
COMPND  56 MOLECULE: ES17;                                                      
COMPND  57 CHAIN: R;                                                            
COMPND  58 MOL_ID: 20;                                                          
COMPND  59 MOLECULE: US13;                                                      
COMPND  60 CHAIN: S;                                                            
COMPND  61 MOL_ID: 21;                                                          
COMPND  62 MOLECULE: ES19;                                                      
COMPND  63 CHAIN: T;                                                            
COMPND  64 MOL_ID: 22;                                                          
COMPND  65 MOLECULE: US10;                                                      
COMPND  66 CHAIN: U;                                                            
COMPND  67 MOL_ID: 23;                                                          
COMPND  68 MOLECULE: ES21;                                                      
COMPND  69 CHAIN: V;                                                            
COMPND  70 MOL_ID: 24;                                                          
COMPND  71 MOLECULE: US8;                                                       
COMPND  72 CHAIN: W;                                                            
COMPND  73 MOL_ID: 25;                                                          
COMPND  74 MOLECULE: US12;                                                      
COMPND  75 CHAIN: X;                                                            
COMPND  76 MOL_ID: 26;                                                          
COMPND  77 MOLECULE: ES24;                                                      
COMPND  78 CHAIN: Y;                                                            
COMPND  79 MOL_ID: 27;                                                          
COMPND  80 MOLECULE: ES25;                                                      
COMPND  81 CHAIN: Z;                                                            
COMPND  82 MOL_ID: 28;                                                          
COMPND  83 MOLECULE: ES26;                                                      
COMPND  84 CHAIN: a;                                                            
COMPND  85 MOL_ID: 29;                                                          
COMPND  86 MOLECULE: ES27;                                                      
COMPND  87 CHAIN: b;                                                            
COMPND  88 MOL_ID: 30;                                                          
COMPND  89 MOLECULE: ES28;                                                      
COMPND  90 CHAIN: c;                                                            
COMPND  91 MOL_ID: 31;                                                          
COMPND  92 MOLECULE: US14;                                                      
COMPND  93 CHAIN: d;                                                            
COMPND  94 MOL_ID: 32;                                                          
COMPND  95 MOLECULE: ES30;                                                      
COMPND  96 CHAIN: e;                                                            
COMPND  97 MOL_ID: 33;                                                          
COMPND  98 MOLECULE: ES31;                                                      
COMPND  99 CHAIN: f;                                                            
COMPND 100 MOL_ID: 34;                                                          
COMPND 101 MOLECULE: RACK1;                                                     
COMPND 102 CHAIN: g;                                                            
COMPND 103 MOL_ID: 35;                                                          
COMPND 104 MOLECULE: EL41;                                                      
COMPND 105 CHAIN: h;                                                            
COMPND 106 MOL_ID: 36;                                                          
COMPND 107 MOLECULE: EIF1A;                                                     
COMPND 108 CHAIN: i;                                                            
COMPND 109 ENGINEERED: YES;                                                     
COMPND 110 MOL_ID: 37;                                                          
COMPND 111 MOLECULE: EIF1;                                                      
COMPND 112 CHAIN: j;                                                            
COMPND 113 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE   3 ORGANISM_TAXID: 28985;                                               
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE   6 ORGANISM_TAXID: 28985;                                               
SOURCE   7 MOL_ID: 3;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE   9 ORGANISM_TAXID: 28985;                                               
SOURCE  10 MOL_ID: 4;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  12 ORGANISM_TAXID: 28985;                                               
SOURCE  13 MOL_ID: 5;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  15 ORGANISM_TAXID: 28985;                                               
SOURCE  16 MOL_ID: 6;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  18 ORGANISM_TAXID: 28985;                                               
SOURCE  19 MOL_ID: 7;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  21 ORGANISM_TAXID: 28985;                                               
SOURCE  22 MOL_ID: 8;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  24 ORGANISM_TAXID: 28985;                                               
SOURCE  25 MOL_ID: 9;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  27 ORGANISM_TAXID: 28985;                                               
SOURCE  28 MOL_ID: 10;                                                          
SOURCE  29 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  30 ORGANISM_TAXID: 28985;                                               
SOURCE  31 MOL_ID: 11;                                                          
SOURCE  32 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  33 ORGANISM_TAXID: 28985;                                               
SOURCE  34 MOL_ID: 12;                                                          
SOURCE  35 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  36 ORGANISM_TAXID: 28985;                                               
SOURCE  37 MOL_ID: 13;                                                          
SOURCE  38 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  39 ORGANISM_TAXID: 28985;                                               
SOURCE  40 MOL_ID: 14;                                                          
SOURCE  41 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  42 ORGANISM_TAXID: 28985;                                               
SOURCE  43 MOL_ID: 15;                                                          
SOURCE  44 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  45 ORGANISM_TAXID: 28985;                                               
SOURCE  46 MOL_ID: 16;                                                          
SOURCE  47 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  48 ORGANISM_TAXID: 28985;                                               
SOURCE  49 MOL_ID: 17;                                                          
SOURCE  50 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  51 ORGANISM_TAXID: 28985;                                               
SOURCE  52 MOL_ID: 18;                                                          
SOURCE  53 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  54 ORGANISM_TAXID: 28985;                                               
SOURCE  55 MOL_ID: 19;                                                          
SOURCE  56 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  57 ORGANISM_TAXID: 28985;                                               
SOURCE  58 MOL_ID: 20;                                                          
SOURCE  59 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  60 ORGANISM_TAXID: 28985;                                               
SOURCE  61 MOL_ID: 21;                                                          
SOURCE  62 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  63 ORGANISM_TAXID: 28985;                                               
SOURCE  64 MOL_ID: 22;                                                          
SOURCE  65 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  66 ORGANISM_TAXID: 28985;                                               
SOURCE  67 MOL_ID: 23;                                                          
SOURCE  68 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  69 ORGANISM_TAXID: 28985;                                               
SOURCE  70 MOL_ID: 24;                                                          
SOURCE  71 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  72 ORGANISM_TAXID: 28985;                                               
SOURCE  73 MOL_ID: 25;                                                          
SOURCE  74 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  75 ORGANISM_TAXID: 28985;                                               
SOURCE  76 MOL_ID: 26;                                                          
SOURCE  77 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  78 ORGANISM_TAXID: 28985;                                               
SOURCE  79 MOL_ID: 27;                                                          
SOURCE  80 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  81 ORGANISM_TAXID: 28985;                                               
SOURCE  82 MOL_ID: 28;                                                          
SOURCE  83 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  84 ORGANISM_TAXID: 28985;                                               
SOURCE  85 MOL_ID: 29;                                                          
SOURCE  86 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  87 ORGANISM_TAXID: 28985;                                               
SOURCE  88 MOL_ID: 30;                                                          
SOURCE  89 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  90 ORGANISM_TAXID: 28985;                                               
SOURCE  91 MOL_ID: 31;                                                          
SOURCE  92 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  93 ORGANISM_TAXID: 28985;                                               
SOURCE  94 MOL_ID: 32;                                                          
SOURCE  95 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  96 ORGANISM_TAXID: 28985;                                               
SOURCE  97 MOL_ID: 33;                                                          
SOURCE  98 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE  99 ORGANISM_TAXID: 28985;                                               
SOURCE 100 MOL_ID: 34;                                                          
SOURCE 101 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE 102 ORGANISM_TAXID: 28985;                                               
SOURCE 103 MOL_ID: 35;                                                          
SOURCE 104 ORGANISM_SCIENTIFIC: KLUYVEROMYCES LACTIS;                           
SOURCE 105 ORGANISM_TAXID: 28985;                                               
SOURCE 106 MOL_ID: 36;                                                          
SOURCE 107 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE 108 ORGANISM_TAXID: 4932;                                                
SOURCE 109 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE 110 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE 111 EXPRESSION_SYSTEM_STRAIN: ROSETTA;                                   
SOURCE 112 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE 113 EXPRESSION_SYSTEM_PLASMID: PTYB2;                                    
SOURCE 114 MOL_ID: 37;                                                          
SOURCE 115 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE 116 ORGANISM_TAXID: 4932;                                                
SOURCE 117 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE 118 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE 119 EXPRESSION_SYSTEM_STRAIN: ROSETTA;                                   
SOURCE 120 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE 121 EXPRESSION_SYSTEM_PLASMID: PTYB2                                     
KEYWDS    EUKARYOTIC TRANSLATION INITIATION, 48S, SMALL RIBOSOME SUBUNIT, 40S,  
KEYWDS   2 43S, TRANSLATION                                                     
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    J.L.LLACER,T.HUSSAIN,V.RAMAKRISHNAN                                   
REVDAT   2   02-SEP-15 3JAM    1       JRNL                                     
REVDAT   1   12-AUG-15 3JAM    0                                                
JRNL        AUTH   J.L.LLACER,T.HUSSAIN,L.MARLER,C.E.AITKEN,A.THAKUR,           
JRNL        AUTH 2 J.R.LORSCH,A.G.HINNEBUSCH,V.RAMAKRISHNAN                     
JRNL        TITL   CONFORMATIONAL DIFFERENCES BETWEEN OPEN AND CLOSED STATES OF 
JRNL        TITL 2 THE EUKARYOTIC TRANSLATION INITIATION COMPLEX.               
JRNL        REF    MOL.CELL                      V.  59   399 2015              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   26212456                                                     
JRNL        DOI    10.1016/J.MOLCEL.2015.06.033                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.46 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : CHIMERA, COOT, REFMAC                     
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 3J80                                
REMARK   3   REFINEMENT SPACE             : RECIPROCAL                          
REMARK   3   REFINEMENT PROTOCOL          : NULL                                
REMARK   3   REFINEMENT TARGET            : R-FACTOR, FSC                       
REMARK   3   OVERALL ANISOTROPIC B VALUE  : 89.000                              
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : LOCAL REFINEMENT                                 
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : 1.340                          
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : 1.340                          
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 3.460                          
REMARK   3   NUMBER OF PARTICLES               : 86055                          
REMARK   3   CTF CORRECTION METHOD             : NULL                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: GOLD-STANDARD                                         
REMARK   4                                                                      
REMARK   4 3JAM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUL-15.                  
REMARK 100 THE RCSB ID CODE IS RCSB160460.                                      
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : VITREOUS ICE (CRYO EM)            
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : ASYMMETRIC                        
REMARK 245   NAME OF SAMPLE                 : INITIATION FACTORS EIF1A AND      
REMARK 245                                    EIF1 BOUND TO THE 40S RIBOSOME    
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 0.17                              
REMARK 245   SAMPLE SUPPORT DETAILS         : QUANTIFOIL R2/2 400 MESH COPPER   
REMARK 245                                    GRIDS WITH 4-5 NM THIN CARBON ON  
REMARK 245                                    TOP                               
REMARK 245   SAMPLE VITRIFICATION DETAILS   : BLOT FOR 2.5 TO 3 SECONDS         
REMARK 245                                    BEFORE PLUNGING INTO LIQUID       
REMARK 245                                    ETHANE (FEI VITROBOT MARK I).     
REMARK 245   SAMPLE BUFFER                  : 20 MM MES-KOH, 40 MM POTASSIUM    
REMARK 245                                    ACETATE, 10 MM AMMONIUM ACETATE,  
REMARK 245                                    8 MM MAGNESIUM ACETATE, 2 MM DTT  
REMARK 245   PH                             : 6.50                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : 28-APR-14                      
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : 2056                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : FEI FALCON II (4K X 4K)        
REMARK 245   MINIMUM DEFOCUS (NM)              : 1500.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 4000.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : 2.70                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 27.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 78000                          
REMARK 245   CALIBRATED MAGNIFICATION          : 104478                         
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : COMPLETE DATASET WAS           
REMARK 245  COLLECTED OVER TWO NON-CONSECUTIVE DAYS.                            
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 37-MERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 2, A, B, C, D, E, F, G, H,            
REMARK 350                    AND CHAINS: I, J, K, L, M, N, O, P, Q,            
REMARK 350                    AND CHAINS: R, S, T, U, V, W, X, Y, Z,            
REMARK 350                    AND CHAINS: a, b, c, d, e, f, g, h, i, j          
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465       C 2   657A                                                     
REMARK 465       G 2   657B                                                     
REMARK 465       A 2   657C                                                     
REMARK 465       C 2   657D                                                     
REMARK 465       U 2   657E                                                     
REMARK 465       U 2   657F                                                     
REMARK 465       U 2   657G                                                     
REMARK 465       A 2   657H                                                     
REMARK 465       U 2   657I                                                     
REMARK 465       G 2   657J                                                     
REMARK 465       U 2   657K                                                     
REMARK 465       C 2   657L                                                     
REMARK 465       G 2   657M                                                     
REMARK 465       C 2   657N                                                     
REMARK 465       G 2   657O                                                     
REMARK 465       C 2   657P                                                     
REMARK 465       A 2   657Q                                                     
REMARK 465       C 2   657R                                                     
REMARK 465       U 2   657S                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ILE A   210                                                      
REMARK 465     GLU A   211                                                      
REMARK 465     GLN A   212                                                      
REMARK 465     GLN A   213                                                      
REMARK 465     THR A   214                                                      
REMARK 465     ALA A   215                                                      
REMARK 465     GLU A   216                                                      
REMARK 465     GLU A   217                                                      
REMARK 465     GLU A   218                                                      
REMARK 465     ALA A   219                                                      
REMARK 465     VAL A   220                                                      
REMARK 465     ALA A   221                                                      
REMARK 465     SER A   222                                                      
REMARK 465     GLY A   223                                                      
REMARK 465     GLU A   224                                                      
REMARK 465     GLN A   225                                                      
REMARK 465     THR A   226                                                      
REMARK 465     GLU A   227                                                      
REMARK 465     GLU A   228                                                      
REMARK 465     ALA A   229                                                      
REMARK 465     VAL A   230                                                      
REMARK 465     ASP A   231                                                      
REMARK 465     ALA A   232                                                      
REMARK 465     THR A   233                                                      
REMARK 465     GLU A   234                                                      
REMARK 465     GLU A   235                                                      
REMARK 465     GLN A   236                                                      
REMARK 465     THR A   237                                                      
REMARK 465     GLU A   238                                                      
REMARK 465     ALA A   239                                                      
REMARK 465     ALA A   240                                                      
REMARK 465     GLU A   241                                                      
REMARK 465     TRP A   242                                                      
REMARK 465     ALA A   243                                                      
REMARK 465     GLU A   244                                                      
REMARK 465     GLU A   245                                                      
REMARK 465     GLY A   246                                                      
REMARK 465     GLN A   247                                                      
REMARK 465     ALA A   248                                                      
REMARK 465     GLN A   249                                                      
REMARK 465     GLU A   250                                                      
REMARK 465     GLU A   251                                                      
REMARK 465     GLU A   252                                                      
REMARK 465     TRP A   253                                                      
REMARK 465     ASN A   254                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B    10                                                      
REMARK 465     LYS B    11                                                      
REMARK 465     GLY B    12                                                      
REMARK 465     LYS B    13                                                      
REMARK 465     LYS B    14                                                      
REMARK 465     GLY B    15                                                      
REMARK 465     LEU B    16                                                      
REMARK 465     LYS B    17                                                      
REMARK 465     LYS B    18                                                      
REMARK 465     GLU B   234                                                      
REMARK 465     ALA B   235                                                      
REMARK 465     SER B   236                                                      
REMARK 465     ALA B   237                                                      
REMARK 465     GLU B   238                                                      
REMARK 465     GLU B   239                                                      
REMARK 465     LYS B   240                                                      
REMARK 465     GLY B   241                                                      
REMARK 465     LYS B   242                                                      
REMARK 465     LYS B   243                                                      
REMARK 465     VAL B   244                                                      
REMARK 465     ALA B   245                                                      
REMARK 465     GLY B   246                                                      
REMARK 465     PHE B   247                                                      
REMARK 465     LYS B   248                                                      
REMARK 465     ASP B   249                                                      
REMARK 465     GLU B   250                                                      
REMARK 465     ILE B   251                                                      
REMARK 465     LEU B   252                                                      
REMARK 465     GLU B   253                                                      
REMARK 465     THR B   254                                                      
REMARK 465     VAL B   255                                                      
REMARK 465     MET C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     ALA C     3                                                      
REMARK 465     PRO C     4                                                      
REMARK 465     GLN C     5                                                      
REMARK 465     ALA C     6                                                      
REMARK 465     GLN C     7                                                      
REMARK 465     GLY C     8                                                      
REMARK 465     GLN C     9                                                      
REMARK 465     GLN C    10                                                      
REMARK 465     ALA C    11                                                      
REMARK 465     PRO C    12                                                      
REMARK 465     ARG C    13                                                      
REMARK 465     ARG C    14                                                      
REMARK 465     GLY C    15                                                      
REMARK 465     GLY C    16                                                      
REMARK 465     PHE C    17                                                      
REMARK 465     GLY C    18                                                      
REMARK 465     GLY C    19                                                      
REMARK 465     ALA C    20                                                      
REMARK 465     ASN C    21                                                      
REMARK 465     ARG C    22                                                      
REMARK 465     GLY C    23                                                      
REMARK 465     GLY C    24                                                      
REMARK 465     ARG C    25                                                      
REMARK 465     GLY C    26                                                      
REMARK 465     GLY C    27                                                      
REMARK 465     ARG C    28                                                      
REMARK 465     ARG C    29                                                      
REMARK 465     GLY C    30                                                      
REMARK 465     GLY C    31                                                      
REMARK 465     ARG C    32                                                      
REMARK 465     ARG C    33                                                      
REMARK 465     ASP C    34                                                      
REMARK 465     GLN C    35                                                      
REMARK 465     GLU C    36                                                      
REMARK 465     GLU C    37                                                      
REMARK 465     LYS C    38                                                      
REMARK 465     LYS C   256                                                      
REMARK 465     LYS C   257                                                      
REMARK 465     LYS C   258                                                      
REMARK 465     LEU C   259                                                      
REMARK 465     MET D     1                                                      
REMARK 465     VAL D     2                                                      
REMARK 465     ARG D   226                                                      
REMARK 465     PRO D   227                                                      
REMARK 465     THR D   228                                                      
REMARK 465     GLU D   229                                                      
REMARK 465     PRO D   230                                                      
REMARK 465     VAL D   231                                                      
REMARK 465     GLU D   232                                                      
REMARK 465     ALA D   233                                                      
REMARK 465     ALA D   234                                                      
REMARK 465     GLU D   235                                                      
REMARK 465     SER D   236                                                      
REMARK 465     ALA D   237                                                      
REMARK 465     MET E     1                                                      
REMARK 465     MET F     1                                                      
REMARK 465     SER F     2                                                      
REMARK 465     GLU F     3                                                      
REMARK 465     HIS F     4                                                      
REMARK 465     GLU F     5                                                      
REMARK 465     ALA F     6                                                      
REMARK 465     GLN F     7                                                      
REMARK 465     VAL F     8                                                      
REMARK 465     GLU F     9                                                      
REMARK 465     VAL F    10                                                      
REMARK 465     GLU F    11                                                      
REMARK 465     VAL F    12                                                      
REMARK 465     GLN F    13                                                      
REMARK 465     GLU F    14                                                      
REMARK 465     ASP F    15                                                      
REMARK 465     PHE F    16                                                      
REMARK 465     GLU F    17                                                      
REMARK 465     VAL F    18                                                      
REMARK 465     VAL F    19                                                      
REMARK 465     GLN F    20                                                      
REMARK 465     GLU F    21                                                      
REMARK 465     ARG G   227                                                      
REMARK 465     LYS G   228                                                      
REMARK 465     ARG G   229                                                      
REMARK 465     ARG G   230                                                      
REMARK 465     ALA G   231                                                      
REMARK 465     SER G   232                                                      
REMARK 465     SER G   233                                                      
REMARK 465     LEU G   234                                                      
REMARK 465     LYS G   235                                                      
REMARK 465     ALA G   236                                                      
REMARK 465     MET H     1                                                      
REMARK 465     SER H     2                                                      
REMARK 465     ASP H     3                                                      
REMARK 465     GLU H   188                                                      
REMARK 465     THR H   189                                                      
REMARK 465     HIS H   190                                                      
REMARK 465     MET I     1                                                      
REMARK 465     LYS I   124                                                      
REMARK 465     LYS I   125                                                      
REMARK 465     ASN I   126                                                      
REMARK 465     THR I   127                                                      
REMARK 465     LYS I   128                                                      
REMARK 465     ALA I   129                                                      
REMARK 465     GLU I   130                                                      
REMARK 465     GLU I   131                                                      
REMARK 465     GLU I   132                                                      
REMARK 465     THR I   133                                                      
REMARK 465     ALA I   134                                                      
REMARK 465     THR I   135                                                      
REMARK 465     MET J     1                                                      
REMARK 465     GLU J   184                                                      
REMARK 465     ALA J   185                                                      
REMARK 465     ASP J   186                                                      
REMARK 465     GLU J   187                                                      
REMARK 465     GLU J   188                                                      
REMARK 465     GLY K    97                                                      
REMARK 465     ASP K    98                                                      
REMARK 465     GLN K    99                                                      
REMARK 465     ARG K   100                                                      
REMARK 465     PRO K   101                                                      
REMARK 465     GLN K   102                                                      
REMARK 465     GLY K   103                                                      
REMARK 465     LYS K   104                                                      
REMARK 465     LYS K   105                                                      
REMARK 465     TYR K   106                                                      
REMARK 465     MET L     1                                                      
REMARK 465     MET M     1                                                      
REMARK 465     SER M     2                                                      
REMARK 465     ASP M     3                                                      
REMARK 465     VAL M     4                                                      
REMARK 465     GLU M     5                                                      
REMARK 465     GLU M     6                                                      
REMARK 465     VAL M     7                                                      
REMARK 465     GLN M     8                                                      
REMARK 465     GLN M     9                                                      
REMARK 465     VAL M    10                                                      
REMARK 465     PRO M    11                                                      
REMARK 465     VAL M    12                                                      
REMARK 465     MET N     1                                                      
REMARK 465     MET O     1                                                      
REMARK 465     ALA O     2                                                      
REMARK 465     ASN O     3                                                      
REMARK 465     VAL O     4                                                      
REMARK 465     VAL O     5                                                      
REMARK 465     GLN O     6                                                      
REMARK 465     ALA O     7                                                      
REMARK 465     LYS O     8                                                      
REMARK 465     ASP O     9                                                      
REMARK 465     ASN O    10                                                      
REMARK 465     MET P     1                                                      
REMARK 465     SER P     2                                                      
REMARK 465     GLU P     3                                                      
REMARK 465     ALA P     4                                                      
REMARK 465     ALA P     5                                                      
REMARK 465     ALA P     6                                                      
REMARK 465     PRO P     7                                                      
REMARK 465     ALA P   131                                                      
REMARK 465     GLY P   132                                                      
REMARK 465     ALA P   133                                                      
REMARK 465     THR P   134                                                      
REMARK 465     THR P   135                                                      
REMARK 465     SER P   136                                                      
REMARK 465     ARG P   137                                                      
REMARK 465     PHE P   138                                                      
REMARK 465     ILE P   139                                                      
REMARK 465     PRO P   140                                                      
REMARK 465     LEU P   141                                                      
REMARK 465     ARG P   142                                                      
REMARK 465     MET Q     1                                                      
REMARK 465     SER Q     2                                                      
REMARK 465     MET R     1                                                      
REMARK 465     VAL R   127                                                      
REMARK 465     ARG R   128                                                      
REMARK 465     ASP R   129                                                      
REMARK 465     ARG R   130                                                      
REMARK 465     ARG R   131                                                      
REMARK 465     PHE R   132                                                      
REMARK 465     ARG R   133                                                      
REMARK 465     LYS R   134                                                      
REMARK 465     ARG R   135                                                      
REMARK 465     ASN R   136                                                      
REMARK 465     MET S     1                                                      
REMARK 465     MET T     1                                                      
REMARK 465     MET U     4                                                      
REMARK 465     SER U     5                                                      
REMARK 465     GLN U     6                                                      
REMARK 465     VAL U     7                                                      
REMARK 465     GLU U     8                                                      
REMARK 465     LYS U     9                                                      
REMARK 465     LYS U    10                                                      
REMARK 465     SER U    11                                                      
REMARK 465     GLU U    12                                                      
REMARK 465     GLN U    13                                                      
REMARK 465     GLN U    14                                                      
REMARK 465     MET W     1                                                      
REMARK 465     MET X     1                                                      
REMARK 465     MET Y     1                                                      
REMARK 465     MET Z     1                                                      
REMARK 465     PRO Z     2                                                      
REMARK 465     PRO Z     3                                                      
REMARK 465     LYS Z     4                                                      
REMARK 465     GLN Z     5                                                      
REMARK 465     GLN Z     6                                                      
REMARK 465     LEU Z     7                                                      
REMARK 465     SER Z     8                                                      
REMARK 465     LYS Z     9                                                      
REMARK 465     ALA Z    10                                                      
REMARK 465     ALA Z    11                                                      
REMARK 465     LYS Z    12                                                      
REMARK 465     ALA Z    13                                                      
REMARK 465     ALA Z    14                                                      
REMARK 465     ALA Z    15                                                      
REMARK 465     ALA Z    16                                                      
REMARK 465     MET Z    17                                                      
REMARK 465     ALA Z    18                                                      
REMARK 465     GLY Z    19                                                      
REMARK 465     GLY Z    20                                                      
REMARK 465     LYS Z    21                                                      
REMARK 465     LYS Z    22                                                      
REMARK 465     SER Z    23                                                      
REMARK 465     LYS Z    24                                                      
REMARK 465     LYS Z    25                                                      
REMARK 465     LYS Z    26                                                      
REMARK 465     TRP Z    27                                                      
REMARK 465     SER Z    28                                                      
REMARK 465     LYS Z    29                                                      
REMARK 465     LYS Z    30                                                      
REMARK 465     SER Z    31                                                      
REMARK 465     HIS Z    32                                                      
REMARK 465     LYS Z    33                                                      
REMARK 465     ASP Z    34                                                      
REMARK 465     LYS Z    35                                                      
REMARK 465     ALA Z   106                                                      
REMARK 465     SER Z   107                                                      
REMARK 465     GLU Z   108                                                      
REMARK 465     MET a     1                                                      
REMARK 465     ARG a   100                                                      
REMARK 465     PRO a   101                                                      
REMARK 465     ARG a   102                                                      
REMARK 465     PHE a   103                                                      
REMARK 465     ASN a   104                                                      
REMARK 465     ARG a   105                                                      
REMARK 465     ASP a   106                                                      
REMARK 465     ASN a   107                                                      
REMARK 465     LYS a   108                                                      
REMARK 465     VAL a   109                                                      
REMARK 465     SER a   110                                                      
REMARK 465     PRO a   111                                                      
REMARK 465     ALA a   112                                                      
REMARK 465     ASP a   113                                                      
REMARK 465     ALA a   114                                                      
REMARK 465     ALA a   115                                                      
REMARK 465     LYS a   116                                                      
REMARK 465     LYS a   117                                                      
REMARK 465     ALA a   118                                                      
REMARK 465     LEU a   119                                                      
REMARK 465     MET b     1                                                      
REMARK 465     MET c     1                                                      
REMARK 465     ASP c     2                                                      
REMARK 465     THR c     3                                                      
REMARK 465     LYS c     4                                                      
REMARK 465     MET d     1                                                      
REMARK 465     ALA d     2                                                      
REMARK 465     HIS d     3                                                      
REMARK 465     MET e     1                                                      
REMARK 465     GLY e     2                                                      
REMARK 465     LYS e     3                                                      
REMARK 465     VAL e     4                                                      
REMARK 465     HIS e     5                                                      
REMARK 465     GLY e     6                                                      
REMARK 465     SER e     7                                                      
REMARK 465     LEU e     8                                                      
REMARK 465     SER e    62                                                      
REMARK 465     GLN e    63                                                      
REMARK 465     MET f     1                                                      
REMARK 465     GLN f     2                                                      
REMARK 465     ILE f     3                                                      
REMARK 465     PHE f     4                                                      
REMARK 465     VAL f     5                                                      
REMARK 465     LYS f     6                                                      
REMARK 465     THR f     7                                                      
REMARK 465     LEU f     8                                                      
REMARK 465     THR f     9                                                      
REMARK 465     GLY f    10                                                      
REMARK 465     LYS f    11                                                      
REMARK 465     THR f    12                                                      
REMARK 465     ILE f    13                                                      
REMARK 465     THR f    14                                                      
REMARK 465     LEU f    15                                                      
REMARK 465     GLU f    16                                                      
REMARK 465     VAL f    17                                                      
REMARK 465     GLU f    18                                                      
REMARK 465     SER f    19                                                      
REMARK 465     SER f    20                                                      
REMARK 465     ASP f    21                                                      
REMARK 465     THR f    22                                                      
REMARK 465     ILE f    23                                                      
REMARK 465     ASP f    24                                                      
REMARK 465     ASN f    25                                                      
REMARK 465     VAL f    26                                                      
REMARK 465     LYS f    27                                                      
REMARK 465     SER f    28                                                      
REMARK 465     LYS f    29                                                      
REMARK 465     ILE f    30                                                      
REMARK 465     GLN f    31                                                      
REMARK 465     ASP f    32                                                      
REMARK 465     LYS f    33                                                      
REMARK 465     GLU f    34                                                      
REMARK 465     GLY f    35                                                      
REMARK 465     ILE f    36                                                      
REMARK 465     PRO f    37                                                      
REMARK 465     PRO f    38                                                      
REMARK 465     ASP f    39                                                      
REMARK 465     GLN f    40                                                      
REMARK 465     GLN f    41                                                      
REMARK 465     ARG f    42                                                      
REMARK 465     LEU f    43                                                      
REMARK 465     ILE f    44                                                      
REMARK 465     PHE f    45                                                      
REMARK 465     ALA f    46                                                      
REMARK 465     GLY f    47                                                      
REMARK 465     LYS f    48                                                      
REMARK 465     GLN f    49                                                      
REMARK 465     LEU f    50                                                      
REMARK 465     GLU f    51                                                      
REMARK 465     ASP f    52                                                      
REMARK 465     GLY f    53                                                      
REMARK 465     ARG f    54                                                      
REMARK 465     THR f    55                                                      
REMARK 465     LEU f    56                                                      
REMARK 465     SER f    57                                                      
REMARK 465     ASP f    58                                                      
REMARK 465     TYR f    59                                                      
REMARK 465     ASN f    60                                                      
REMARK 465     ILE f    61                                                      
REMARK 465     GLN f    62                                                      
REMARK 465     LYS f    63                                                      
REMARK 465     GLU f    64                                                      
REMARK 465     SER f    65                                                      
REMARK 465     THR f    66                                                      
REMARK 465     LEU f    67                                                      
REMARK 465     HIS f    68                                                      
REMARK 465     LEU f    69                                                      
REMARK 465     VAL f    70                                                      
REMARK 465     LEU f    71                                                      
REMARK 465     ARG f    72                                                      
REMARK 465     LEU f    73                                                      
REMARK 465     ARG f    74                                                      
REMARK 465     GLY f    75                                                      
REMARK 465     GLY f    76                                                      
REMARK 465     GLY f    77                                                      
REMARK 465     LYS f    78                                                      
REMARK 465     LYS f    79                                                      
REMARK 465     ARG f    80                                                      
REMARK 465     LYS f    81                                                      
REMARK 465     MET g     1                                                      
REMARK 465     SER g     2                                                      
REMARK 465     GLU g   163                                                      
REMARK 465     ASP g   164                                                      
REMARK 465     GLY g   165                                                      
REMARK 465     GLU g   166                                                      
REMARK 465     GLU g   190                                                      
REMARK 465     ASP g   191                                                      
REMARK 465     MET i     1                                                      
REMARK 465     GLY i     2                                                      
REMARK 465     LYS i     3                                                      
REMARK 465     LYS i     4                                                      
REMARK 465     ASN i     5                                                      
REMARK 465     THR i     6                                                      
REMARK 465     LYS i     7                                                      
REMARK 465     GLY i     8                                                      
REMARK 465     GLY i     9                                                      
REMARK 465     LYS i    10                                                      
REMARK 465     LYS i    11                                                      
REMARK 465     GLY i    12                                                      
REMARK 465     ARG i    13                                                      
REMARK 465     ARG i    14                                                      
REMARK 465     GLY i    15                                                      
REMARK 465     LYS i    16                                                      
REMARK 465     ASN i    17                                                      
REMARK 465     ASP i    18                                                      
REMARK 465     SER i    19                                                      
REMARK 465     ASP i    20                                                      
REMARK 465     GLY i    21                                                      
REMARK 465     THR i   118                                                      
REMARK 465     ASP i   119                                                      
REMARK 465     ASN i   120                                                      
REMARK 465     PHE i   121                                                      
REMARK 465     GLY i   122                                                      
REMARK 465     PHE i   123                                                      
REMARK 465     GLU i   124                                                      
REMARK 465     SER i   125                                                      
REMARK 465     ASP i   126                                                      
REMARK 465     GLU i   127                                                      
REMARK 465     ASP i   128                                                      
REMARK 465     VAL i   129                                                      
REMARK 465     ASN i   130                                                      
REMARK 465     PHE i   131                                                      
REMARK 465     GLU i   132                                                      
REMARK 465     PHE i   133                                                      
REMARK 465     GLY i   134                                                      
REMARK 465     ASN i   135                                                      
REMARK 465     ALA i   136                                                      
REMARK 465     ASP i   137                                                      
REMARK 465     GLU i   138                                                      
REMARK 465     ASP i   139                                                      
REMARK 465     ASP i   140                                                      
REMARK 465     GLU i   141                                                      
REMARK 465     GLU i   142                                                      
REMARK 465     GLY i   143                                                      
REMARK 465     GLU i   144                                                      
REMARK 465     ASP i   145                                                      
REMARK 465     GLU i   146                                                      
REMARK 465     GLU i   147                                                      
REMARK 465     LEU i   148                                                      
REMARK 465     ASP i   149                                                      
REMARK 465     ILE i   150                                                      
REMARK 465     ASP i   151                                                      
REMARK 465     ASP i   152                                                      
REMARK 465     ILE i   153                                                      
REMARK 465     MET j     1                                                      
REMARK 465     SER j     2                                                      
REMARK 465     ILE j     3                                                      
REMARK 465     GLU j     4                                                      
REMARK 465     ASN j     5                                                      
REMARK 465     LEU j     6                                                      
REMARK 465     LYS j     7                                                      
REMARK 465     SER j     8                                                      
REMARK 465     PHE j     9                                                      
REMARK 465     ASP j    10                                                      
REMARK 465     PRO j    11                                                      
REMARK 465     PHE j    12                                                      
REMARK 465     ALA j    13                                                      
REMARK 465     ASP j    14                                                      
REMARK 465     THR j    15                                                      
REMARK 465     GLY j    16                                                      
REMARK 465     ASP j    17                                                      
REMARK 465     ASP j    18                                                      
REMARK 465     GLU j    19                                                      
REMARK 465     THR j    20                                                      
REMARK 465     ALA j    21                                                      
REMARK 465     THR j    22                                                      
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       A 21692    N9   C8   N7   C5   C6   N6   N1                    
REMARK 470       A 21692    C2   N3   C4                                        
REMARK 470       G 21693    N9   C8   N7   C5   C6   O6   N1                    
REMARK 470       G 21693    C2   N2   N3   C4                                   
REMARK 470       G 21694    N9   C8   N7   C5   C6   O6   N1                    
REMARK 470       G 21694    C2   N2   N3   C4                                   
REMARK 470       G 21695    N9   C8   N7   C5   C6   O6   N1                    
REMARK 470       G 21695    C2   N2   N3   C4                                   
REMARK 470       G 21696    N9   C8   N7   C5   C6   O6   N1                    
REMARK 470       G 21696    C2   N2   N3   C4                                   
REMARK 470       G 21697    N9   C8   N7   C5   C6   O6   N1                    
REMARK 470       G 21697    C2   N2   N3   C4                                   
REMARK 470       C 21698    N1   C2   O2   N3   C4   N4   C5                    
REMARK 470       C 21698    C6                                                  
REMARK 470       A 21699    N9   C8   N7   C5   C6   N6   N1                    
REMARK 470       A 21699    C2   N3   C4                                        
REMARK 470       A 21700    N9   C8   N7   C5   C6   N6   N1                    
REMARK 470       A 21700    C2   N3   C4                                        
REMARK 470       C 21701    N1   C2   O2   N3   C4   N4   C5                    
REMARK 470       C 21701    C6                                                  
REMARK 470       U 21702    N1   C2   O2   N3   C4   O4   C5                    
REMARK 470       U 21702    C6                                                  
REMARK 470       C 21703    N1   C2   O2   N3   C4   N4   C5                    
REMARK 470       C 21703    C6                                                  
REMARK 470       C 21704    N1   C2   O2   N3   C4   N4   C5                    
REMARK 470       C 21704    C6                                                  
REMARK 470       A 21705    N9   C8   N7   C5   C6   N6   N1                    
REMARK 470       A 21705    C2   N3   C4                                        
REMARK 470     LYS A  27    CG   CD   CE   NZ                                   
REMARK 470     GLU A 209    CG   CD   OE1  OE2                                  
REMARK 470     LYS B   5    CG   CD   CE   NZ                                   
REMARK 470     ASN B   6    CG   OD1  ND2                                       
REMARK 470     LYS B   7    CG   CD   CE   NZ                                   
REMARK 470     LEU B   9    CG   CD1  CD2                                       
REMARK 470     ARG B  19    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS I 123    CG   CD   CE   NZ                                   
REMARK 470     ARG P 130    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN R  97    CG   OD1  ND2                                       
REMARK 470     GLN f 149    CG   CD   OE1  NE2                                  
REMARK 470     LYS f 150    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   N1     A 2   991     O4     U 2  1011              1.40            
REMARK 500   N1     A 2   480     O4     U 2   506              1.62            
REMARK 500   O4     U 2  1079     N1     A 2  1090              1.66            
REMARK 500   N3     U 2   628     N6     A 2   969              1.77            
REMARK 500   N1     A 2   864     O4     U 2   964              1.83            
REMARK 500   N6     A 2    51     N3     U 2   439              1.83            
REMARK 500   O4     U 2  1292     N1     A 2  1321              1.86            
REMARK 500   N1     A 2    51     O4     U 2   439              1.87            
REMARK 500   N3     U 2  1593     N6     A 2  1598              1.90            
REMARK 500   O4     U 2  1593     N1     A 2  1598              1.90            
REMARK 500   O4     U 2  1037     N1     A 2  1091              1.98            
REMARK 500   O2'    U 2  1319     OP1    A 2  1321              2.04            
REMARK 500   N1     A 2   480     C4     U 2   506              2.13            
REMARK 500   C2     A 2   991     O4     U 2  1011              2.14            
REMARK 500   C2     A 2   480     O4     U 2   506              2.16            
REMARK 500   N3     U 2     8     N6     A 2  1138              2.18            
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 21315   C2' -  C3' -  O3' ANGL. DEV. =  11.4 DEGREES          
REMARK 500      G 21534   C2' -  C3' -  O3' ANGL. DEV. =   9.8 DEGREES          
REMARK 500    LEU B 181   CA  -  CB  -  CG  ANGL. DEV. =  15.6 DEGREES          
REMARK 500    PRO D 220   C   -  N   -  CA  ANGL. DEV. =  10.4 DEGREES          
REMARK 500    LEU H 118   CA  -  CB  -  CG  ANGL. DEV. =  14.1 DEGREES          
REMARK 500    LEU I  29   CA  -  CB  -  CG  ANGL. DEV. =  15.9 DEGREES          
REMARK 500    LEU I 190   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES          
REMARK 500    PRO K  88   C   -  N   -  CA  ANGL. DEV. =   9.2 DEGREES          
REMARK 500    LEU S 105   CA  -  CB  -  CG  ANGL. DEV. =  16.1 DEGREES          
REMARK 500    PRO X  64   C   -  N   -  CD  ANGL. DEV. = -14.2 DEGREES          
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    SER A   5      -27.77     61.16                                   
REMARK 500    LEU A   9       88.23    -69.63                                   
REMARK 500    ARG A  21       47.00     78.45                                   
REMARK 500    LYS A  27      158.24     66.80                                   
REMARK 500    LYS A  39      176.25     58.93                                   
REMARK 500    PRO A  42      -19.98    -46.32                                   
REMARK 500    TYR A  81        2.21    -64.19                                   
REMARK 500    THR A  93     -175.19    -66.07                                   
REMARK 500    ALA A  95      125.02     46.34                                   
REMARK 500    THR A 103      102.73     67.84                                   
REMARK 500    ASN A 109       87.72     61.06                                   
REMARK 500    LEU A 120      135.07   -173.91                                   
REMARK 500    ASP A 129       41.74   -100.29                                   
REMARK 500    LEU A 149       49.58    -83.88                                   
REMARK 500    ASP A 150      -37.85   -156.97                                   
REMARK 500    VAL A 158      106.92     84.36                                   
REMARK 500    LYS A 167      -71.87     68.02                                   
REMARK 500    TRP A 195      133.14     68.17                                   
REMARK 500    TYR A 202     -113.92    -81.69                                   
REMARK 500    PHE A 203     -151.03     55.07                                   
REMARK 500    PRO A 207      107.04    -50.35                                   
REMARK 500    GLU A 208      -34.04   -140.66                                   
REMARK 500    ASP B  22       77.64     63.43                                   
REMARK 500    VAL B  43      -67.79    -94.42                                   
REMARK 500    LEU B  54      104.81     61.02                                   
REMARK 500    LYS B  55       63.88    101.62                                   
REMARK 500    SER B  60       49.46    -89.84                                   
REMARK 500    LEU B  61      -49.86   -138.60                                   
REMARK 500    ASP B  89      -58.82   -124.18                                   
REMARK 500    LYS B  94      -54.87     70.32                                   
REMARK 500    TRP B 117       15.13     82.27                                   
REMARK 500    ASP B 131     -132.90    -86.81                                   
REMARK 500    ALA B 147       83.89    -56.50                                   
REMARK 500    ASN B 148      -25.27    167.05                                   
REMARK 500    THR B 153      -86.75   -119.63                                   
REMARK 500    SER B 154       53.35     82.07                                   
REMARK 500    GLN B 177      -22.86     66.46                                   
REMARK 500    SER B 179      170.47     97.99                                   
REMARK 500    GLU B 191       58.78     39.77                                   
REMARK 500    PRO B 206      -64.12    -24.76                                   
REMARK 500    LEU B 207      145.61     66.99                                   
REMARK 500    LYS B 214      114.23     64.37                                   
REMARK 500    PRO B 221     -124.44    -72.23                                   
REMARK 500    LYS B 222     -113.27    -81.45                                   
REMARK 500    PHE B 223      -51.64   -127.65                                   
REMARK 500    ASP B 224       86.87     52.82                                   
REMARK 500    SER B 230       -8.22    -57.91                                   
REMARK 500    THR C  44      137.97     68.27                                   
REMARK 500    ASN C  80       47.73   -107.33                                   
REMARK 500    ASP C 111     -104.95   -104.45                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     485 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 PHE K   87     PRO K   88                 -148.67                    
REMARK 500 MET P   28     PRO P   29                 -149.85                    
REMARK 500 GLN Q   40     PRO Q   41                  138.98                    
REMARK 500 GLN X   63     PRO X   64                 -134.74                    
REMARK 500 HIS Y   29     PRO Y   30                 -147.64                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    VAL C 141        24.6      L          L   OUTSIDE RANGE           
REMARK 500    ILE F  66        24.9      L          L   OUTSIDE RANGE           
REMARK 500    SER H  31        24.9      L          L   OUTSIDE RANGE           
REMARK 500    GLN H  74        23.0      L          L   OUTSIDE RANGE           
REMARK 500    PHE H 131        23.5      L          L   OUTSIDE RANGE           
REMARK 500    THR L   6        24.7      L          L   OUTSIDE RANGE           
REMARK 500    ILE L  54        23.6      L          L   OUTSIDE RANGE           
REMARK 500    VAL Q  39        24.3      L          L   OUTSIDE RANGE           
REMARK 500    GLN Q  40        24.3      L          L   OUTSIDE RANGE           
REMARK 500    PHE R  71        23.9      L          L   OUTSIDE RANGE           
REMARK 500    ILE W  83        23.9      L          L   OUTSIDE RANGE           
REMARK 500    ASN Y  31        24.1      L          L   OUTSIDE RANGE           
REMARK 500    LYS Z  97        24.3      L          L   OUTSIDE RANGE           
REMARK 500    HIS f 143        24.9      L          L   OUTSIDE RANGE           
REMARK 500    GLU j  73        24.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21865  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G 21427   OP2                                                    
REMARK 620 2   C 21273   OP1 113.7                                              
REMARK 620 3   G 21426   OP1  95.3 106.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21826  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G 21327   OP2                                                    
REMARK 620 2   G 21329   O6  130.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21874  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A 2 914   OP2                                                    
REMARK 620 2   G 2 894   O6  131.9                                              
REMARK 620 3   U 2 916   O4  131.7  79.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21803  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A 2 554   OP2                                                    
REMARK 620 2   A 2 555   OP2  87.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21818  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A 2 604   OP1                                                    
REMARK 620 2   G 2 606   OP1  81.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21812  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   U 21769   OP1                                                    
REMARK 620 2   A 21761   OP1  90.8                                              
REMARK 620 3   G 21765   O3' 161.3 106.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21828  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   U 2 101   OP2                                                    
REMARK 620 2   C 2 360   OP2 160.2                                              
REMARK 620 3   A 2 100   OP2  85.0  81.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21823  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A 2 620   OP2                                                    
REMARK 620 2   A 2 618   OP2 149.1                                              
REMARK 620 3   A 2 619   OP2  66.5  82.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21835  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   C 2 267   OP1                                                    
REMARK 620 2 GLN G 176   OE1 120.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21834  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   U 21628   OP1                                                    
REMARK 620 2   G 21791   OP1 143.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21864  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   U 21520   OP2                                                    
REMARK 620 2   U 21518   O2  123.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21869  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   C 2 249   OP1                                                    
REMARK 620 2   A 2 250   OP2  92.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21836  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A 2 459   OP2                                                    
REMARK 620 2   G 2 460   OP2  85.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21872  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A 2 635   OP2                                                    
REMARK 620 2   A 2 634   OP1  75.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21822  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A 21761   OP2                                                    
REMARK 620 2   A 21760   OP2  93.7                                              
REMARK 620 3   G 21766   OP2  91.3  91.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21816  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A 2 377   OP2                                                    
REMARK 620 2   U 2 378   OP2  87.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN a 500  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS a  26   SG                                                     
REMARK 620 2 CYS a  77   SG   99.4                                              
REMARK 620 3 CYS a  23   SG  129.6 113.4                                        
REMARK 620 4 CYS a  74   SG  110.3  95.9 103.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21866  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A 21201   OP1                                                    
REMARK 620 2   C 21597   O2  119.5                                              
REMARK 620 3   A 21202   OP2  62.6 118.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21830  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G 21109   OP2                                                    
REMARK 620 2   G 21108   OP1  73.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21862  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G 21426   OP2                                                    
REMARK 620 2   C 21273   OP2  69.1                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1805                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1807                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1809                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1811                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1812                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1814                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1815                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1816                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1817                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1818                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1819                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1820                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1821                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1822                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1823                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1824                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1825                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1826                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1827                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1828                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1830                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1831                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1832                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1833                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1834                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1835                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1836                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1837                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1841                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1842                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1844                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1845                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1846                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1849                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1850                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1852                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1854                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1855                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1856                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1857                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1858                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1859                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1860                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1861                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1862                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1863                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1864                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1865                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1866                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1868                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1869                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1870                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1871                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1872                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1874                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1875                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1876                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG 2 1877                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN a 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN b 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG f 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN f 202                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-3047   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-3048   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-3049   RELATED DB: EMDB                              
REMARK 900 RELATED ID: 3J80   RELATED DB: PDB                                   
REMARK 900 YEAST 40S-EIF1-EIF1A AT LOWER RESOLUTION, FITTED INTO AN EM          
REMARK 900 MAP WITH AN EXTRA COMPONENT NOT FOUND IN EMD-3047                    
REMARK 900 RELATED ID: 3JAP   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3JAQ   RELATED DB: PDB                                   
DBREF1 3JAM 2    1  1798  GB                   NC_006040.1                      
DBREF2 3JAM 2     NC_006040.1                   1505732     1507530             
DBREF  3JAM A    1   254  UNP    Q6CN12   RSSA_KLULA       1    254             
DBREF  3JAM B    1   255  UNP    Q6CWD0   RS3A_KLULA       1    255             
DBREF  3JAM C    1   259  UNP    Q6CKL3   Q6CKL3_KLULA     1    259             
DBREF  3JAM D    1   237  UNP    Q6CRK7   Q6CRK7_KLULA     1    237             
DBREF  3JAM E    1   261  UNP    Q6CWJ2   Q6CWJ2_KLULA     1    261             
DBREF  3JAM F    1   227  UNP    Q6CRA3   Q6CRA3_KLULA     1    227             
DBREF  3JAM G    1   236  UNP    Q6CM04   RS6_KLULA        1    236             
DBREF  3JAM H    1   190  UNP    Q6CTD6   Q6CTD6_KLULA     1    190             
DBREF  3JAM I    1   201  UNP    Q6CMG3   Q6CMG3_KLULA     1    201             
DBREF  3JAM J    1   188  UNP    Q6CM18   Q6CM18_KLULA     1    188             
DBREF  3JAM K    1   106  UNP    Q6CVZ5   Q6CVZ5_KLULA     1    106             
DBREF  3JAM L    1   156  UNP    Q6CX80   Q6CX80_KLULA     1    156             
DBREF  3JAM M    1   134  UNP    Q6CLU4   Q6CLU4_KLULA     1    134             
DBREF  3JAM N    1   151  UNP    Q6CJK0   Q6CJK0_KLULA     1    151             
DBREF  3JAM O    1   137  UNP    P27069   RS14_KLULA       1    137             
DBREF  3JAM P    1   142  UNP    Q6CKV4   Q6CKV4_KLULA     1    142             
DBREF  3JAM Q    1   143  UNP    Q875N2   RS16_KLULA       1    143             
DBREF  3JAM R    1   136  UNP    Q6CWU3   Q6CWU3_KLULA     1    136             
DBREF  3JAM S    1   146  UNP    Q6CWT9   Q6CWT9_KLULA     1    146             
DBREF  3JAM T    1   144  UNP    Q6CXM0   Q6CXM0_KLULA     1    144             
DBREF  3JAM U    4   120  UNP    Q6CIM1   Q6CIM1_KLULA     1    117             
DBREF  3JAM V    1    87  UNP    Q6CXT6   RS21_KLULA       1     87             
DBREF  3JAM W    1   130  UNP    Q6CW21   RS22_KLULA       1    130             
DBREF  3JAM X    1   145  UNP    F2Z602   F2Z602_KLULA     1    145             
DBREF  3JAM Y    1   135  UNP    Q6CU44   Q6CU44_KLULA     1    135             
DBREF  3JAM Z    1   108  UNP    Q6CW78   Q6CW78_KLULA     1    108             
DBREF  3JAM a    1   119  UNP    Q6CS01   Q6CS01_KLULA     1    119             
DBREF  3JAM b    1    82  UNP    Q6CNL2   Q6CNL2_KLULA     1     82             
DBREF  3JAM c    1    67  UNP    P33285   RS28_KLULA       1     67             
DBREF  3JAM d    1    56  UNP    Q6CPG3   RS29_KLULA       1     56             
DBREF  3JAM e    1    63  UNP    Q6CUH5   Q6CUH5_KLULA     1     63             
DBREF  3JAM f    1   150  UNP    P69061   RS27A_KLULA      1    150             
DBREF  3JAM g    1   326  UNP    Q6CNI7   Q6CNI7_KLULA     1    326             
DBREF  3JAM h    1    25  UNP    P0CX86   RL41A_YEAST      1     25             
DBREF  3JAM i    1   153  UNP    P38912   IF1A_YEAST       1    153             
DBREF  3JAM j    1   108  UNP    P32911   SUI1_YEAST       1    108             
SEQRES   1 2 1799    U   A   U   C   U   G   G   U   U   G   A   U   C          
SEQRES   2 2 1799    C   U   G   C   C   A   G   U   A   G   U   C   A          
SEQRES   3 2 1799    U   A   U   G   C   U   U   G   U   C   U   C   A          
SEQRES   4 2 1799    A   A   G   A   U   U   A   A   G   C   C   A   U          
SEQRES   5 2 1799    G   C   A   U   G   U   C   U   A   A   G   U   A          
SEQRES   6 2 1799    U   A   A   G   C   A   A   U   U   U   A   U   A          
SEQRES   7 2 1799    C   A   G   U   G   A   A   A   C   U   G   C   G          
SEQRES   8 2 1799    A   A   U   G   G   C   U   C   A   U   U   A   A          
SEQRES   9 2 1799    A   U   C   A   G   U   U   A   U   C   G   U   U          
SEQRES  10 2 1799    U   A   U   U   U   G   A   U   A   G   U   U   C          
SEQRES  11 2 1799    C   U   U   U   A   C   U   A   C   A   U   G   G          
SEQRES  12 2 1799    A   U   A   U   C   U   G   U   G   G   U   A   A          
SEQRES  13 2 1799    U   U   C   U   A   G   A   G   C   U   A   A   U          
SEQRES  14 2 1799    A   C   A   U   G   C   U   U   A   A   A   A   U          
SEQRES  15 2 1799    C   U   C   G   A   C   C   C   U   U   U   G   G          
SEQRES  16 2 1799    A   A   G   A   G   A   U   G   U   A   U   U   U          
SEQRES  17 2 1799    A   U   U   A   G   A   U   A   A   A   A   A   A          
SEQRES  18 2 1799    U   C   A   A   U   G   U   C   U   U   C   G   G          
SEQRES  19 2 1799    A   C   U   C   C   U   U   G   A   U   G   A   U          
SEQRES  20 2 1799    U   C   A   U   A   A   U   A   A   C   U   U   U          
SEQRES  21 2 1799    U   C   G   A   A   U   C   G   C   A   U   G   G          
SEQRES  22 2 1799    C   C   U   U   G   U   G   C   U   G   G   C   G          
SEQRES  23 2 1799    A   U   G   G   U   U   C   A   U   U   C   A   A          
SEQRES  24 2 1799    A   U   U   U   C   U   G   C   C   C   U   A   U          
SEQRES  25 2 1799    C   A   A   C   U   U   U   C   G   A   U   G   G          
SEQRES  26 2 1799    U   A   G   G   A   U   A   G   U   G   G   C   C          
SEQRES  27 2 1799    U   A   C   C   A   U   G   G   U   U   U   C   A          
SEQRES  28 2 1799    A   C   G   G   G   U   A   A   C   G   G   G   G          
SEQRES  29 2 1799    A   A   U   A   A   G   G   G   U   U   C   G   A          
SEQRES  30 2 1799    U   U   C   C   G   G   A   G   A   G   G   G   A          
SEQRES  31 2 1799    G   C   C   U   G   A   G   A   A   A   C   G   G          
SEQRES  32 2 1799    C   U   A   C   C   A   C   A   U   C   C   A   A          
SEQRES  33 2 1799    G   G   A   A   G   G   C   A   G   C   A   G   G          
SEQRES  34 2 1799    C   G   C   G   C   A   A   A   U   U   A   C   C          
SEQRES  35 2 1799    C   A   A   U   C   C   U   A   A   U   U   C   A          
SEQRES  36 2 1799    G   G   G   A   G   G   U   A   G   U   G   A   C          
SEQRES  37 2 1799    A   A   U   A   A   A   U   A   A   C   G   A   U          
SEQRES  38 2 1799    A   C   A   G   G   G   C   C   C   A   U   U   C          
SEQRES  39 2 1799    G   G   G   U   C   U   U   G   U   A   A   U   U          
SEQRES  40 2 1799    G   G   A   A   U   G   A   G   U   A   C   A   A          
SEQRES  41 2 1799    U   G   U   A   A   A   U   A   C   C   U   U   A          
SEQRES  42 2 1799    A   C   G   A   G   G   A   A   C   A   A   C   U          
SEQRES  43 2 1799    G   G   A   G   G   G   C   A   A   G   U   C   U          
SEQRES  44 2 1799    G   G   U   G   C   C   A   G   C   A   G   C   C          
SEQRES  45 2 1799    G   C   G   G   U   A   A   U   U   C   C   A   G          
SEQRES  46 2 1799    C   U   C   C   A   G   U   A   G   C   G   U   A          
SEQRES  47 2 1799    U   A   U   U   A   A   A   G   U   U   G   U   U          
SEQRES  48 2 1799    G   C   A   G   U   U   A   A   A   A   A   G   C          
SEQRES  49 2 1799    U   C   G   U   A   G   U   U   G   A   A   C   U          
SEQRES  50 2 1799    U   U   G   G   G   U   C   U   G   G   U   U   G          
SEQRES  51 2 1799    U   C   C   G   G   U   C   C   G   A   C   U   U          
SEQRES  52 2 1799    U   A   U   G   U   C   G   C   G   C   A   C   U          
SEQRES  53 2 1799    G   G   U   U   U   U   U   C   A   A   C   C   G          
SEQRES  54 2 1799    G   A   U   C   U   U   U   C   C   U   U   C   U          
SEQRES  55 2 1799    G   G   C   U   A   A   C   C   U   G   U   A   C          
SEQRES  56 2 1799    U   C   C   U   U   G   U   G   G   G   U   G   C          
SEQRES  57 2 1799    A   G   G   C   G   A   A   C   C   A   G   G   A          
SEQRES  58 2 1799    C   U   U   U   U   A   C   U   U   U   G   A   A          
SEQRES  59 2 1799    A   A   A   A   U   U   A   G   A   G   U   G   U          
SEQRES  60 2 1799    U   C   A   A   A   G   C   A   G   G   C   G   A          
SEQRES  61 2 1799    A   A   G   C   U   C   G   A   A   U   A   U   A          
SEQRES  62 2 1799    U   U   A   G   C   A   U   G   G   A   A   U   A          
SEQRES  63 2 1799    A   U   G   G   A   A   U   A   G   G   A   C   G          
SEQRES  64 2 1799    U   U   U   G   G   U   U   C   U   A   U   U   U          
SEQRES  65 2 1799    U   G   U   U   G   G   U   U   U   C   U   A   G          
SEQRES  66 2 1799    G   A   C   C   A   U   C   G   U   A   A   U   G          
SEQRES  67 2 1799    A   U   U   A   A   U   A   G   G   G   A   C   G          
SEQRES  68 2 1799    G   U   C   G   G   G   G   G   C   A   U   C   A          
SEQRES  69 2 1799    G   U   A   U   U   C   A   A   U   U   G   U   C          
SEQRES  70 2 1799    A   G   A   G   G   U   G   A   A   A   U   U   C          
SEQRES  71 2 1799    U   U   G   G   A   U   U   U   A   U   U   G   A          
SEQRES  72 2 1799    A   G   A   C   U   A   A   C   U   A   C   U   G          
SEQRES  73 2 1799    C   G   A   A   A   G   C   A   U   U   U   G   C          
SEQRES  74 2 1799    C   A   A   G   G   A   C   G   U   U   U   U   C          
SEQRES  75 2 1799    A   U   U   A   A   U   C   A   A   G   A   A   C          
SEQRES  76 2 1799    G   A   A   A   G   U   U   A   G   G   G   G   A          
SEQRES  77 2 1799    U   C   G   A   A   G   A   U   G   A   U   C   A          
SEQRES  78 2 1799    G   A   U   A   C   C   G   U   C   G   U   A   G          
SEQRES  79 2 1799    U   C   U   U   A   A   C   C   A   U   A   A   A          
SEQRES  80 2 1799    C   U   A   U   G   C   C   G   A   C   U   A   G          
SEQRES  81 2 1799    G   G   A   U   C   G   G   G   U   G   G   U   G          
SEQRES  82 2 1799    U   U   U   U   U   C   U   U   A   U   G   A   C          
SEQRES  83 2 1799    C   C   A   C   U   C   G   G   C   A   C   C   U          
SEQRES  84 2 1799    U   A   C   G   A   G   A   A   A   U   C   A   A          
SEQRES  85 2 1799    A   G   U   C   U   U   U   G   G   G   U   U   C          
SEQRES  86 2 1799    U   G   G   G   G   G   G   A   G   U   A   U   G          
SEQRES  87 2 1799    G   U   C   G   C   A   A   G   G   C   U   G   A          
SEQRES  88 2 1799    A   A   C   U   U   A   A   A   G   G   A   A   U          
SEQRES  89 2 1799    U   G   A   C   G   G   A   A   G   G   G   C   A          
SEQRES  90 2 1799    C   C   A   C   C   A   G   G   A   G   U   G   G          
SEQRES  91 2 1799    A   G   C   C   U   G   C   G   G   C   U   U   A          
SEQRES  92 2 1799    A   U   U   U   G   A   C   U   C   A   A   C   A          
SEQRES  93 2 1799    C   G   G   G   G   A   A   A   C   U   C   A   C          
SEQRES  94 2 1799    C   A   G   G   U   C   C   A   G   A   C   A   C          
SEQRES  95 2 1799    A   A   U   A   A   G   G   A   U   U   G   A   C          
SEQRES  96 2 1799    A   G   A   U   U   G   A   G   A   G   C   U   C          
SEQRES  97 2 1799    U   U   U   C   U   U   G   A   U   U   U   U   G          
SEQRES  98 2 1799    U   G   G   G   U   G   G   U   G   G   U   G   C          
SEQRES  99 2 1799    A   U   G   G   C   C   G   U   U   C   U   U   A          
SEQRES 100 2 1799    G   U   U   G   G   U   G   G   A   G   U   G   A          
SEQRES 101 2 1799    U   U   U   G   U   C   U   G   C   U   U   A   A          
SEQRES 102 2 1799    U   U   G   C   G   A   U   A   A   C   G   A   A          
SEQRES 103 2 1799    C   G   A   G   A   C   C   U   U   A   A   C   C          
SEQRES 104 2 1799    U   A   C   U   A   A   A   U   A   G   G   G   U          
SEQRES 105 2 1799    U   G   C   U   G   G   C   A   C   U   U   G   C          
SEQRES 106 2 1799    C   G   G   U   U   G   A   C   U   C   U   U   C          
SEQRES 107 2 1799    U   U   A   G   A   G   G   G   A   C   U   A   U          
SEQRES 108 2 1799    C   G   G   U   U   U   C   A   A   G   C   C   G          
SEQRES 109 2 1799    A   U   G   G   A   A   G   U   U   U   G   A   G          
SEQRES 110 2 1799    G   C   A   A   U   A   A   C   A   G   G   U   C          
SEQRES 111 2 1799    U   G   U   G   A   U   G   C   C   C   U   U   A          
SEQRES 112 2 1799    G   A   C   G   U   U   C   U   G   G   G   C   C          
SEQRES 113 2 1799    G   C   A   C   G   C   G   C   G   C   U   A   C          
SEQRES 114 2 1799    A   C   U   G   A   C   G   G   A   G   C   C   A          
SEQRES 115 2 1799    G   C   G   A   G   U   A   C   A   A   C   C   U          
SEQRES 116 2 1799    U   G   G   C   C   G   A   G   A   G   G   U   C          
SEQRES 117 2 1799    U   G   G   G   U   A   A   U   C   U   U   G   U          
SEQRES 118 2 1799    G   A   A   A   C   U   C   C   G   U   C   G   U          
SEQRES 119 2 1799    G   C   U   G   G   G   G   A   U   A   G   A   G          
SEQRES 120 2 1799    C   A   U   U   G   U   A   A   U   U   A   U   U          
SEQRES 121 2 1799    G   C   U   C   U   U   C   A   A   C   G   A   G          
SEQRES 122 2 1799    G   A   A   U   U   C   C   U   A   G   U   A   A          
SEQRES 123 2 1799    G   C   G   C   A   A   G   U   C   A   U   C   A          
SEQRES 124 2 1799    G   C   U   U   G   C   G   U   U   G   A   U   U          
SEQRES 125 2 1799    A   C   G   U   C   C   C   U   G   C   C   C   U          
SEQRES 126 2 1799    U   U   G   U   A   C   A   C   A   C   C   G   C          
SEQRES 127 2 1799    C   C   G   U   C   G   C   U   A   G   U   A   C          
SEQRES 128 2 1799    C   G   A   U   U   G   A   A   U   G   G   C   U          
SEQRES 129 2 1799    U   A   G   U   G   A   G   G   C   C   U   C   A          
SEQRES 130 2 1799    G   G   A   U   U   U   G   C   U   U   A   G   A          
SEQRES 131 2 1799    G   A   A   G   G   G   G   G   C   A   A   C   U          
SEQRES 132 2 1799    C   C   A   U   C   U   C   A   G   A   G   C   G          
SEQRES 133 2 1799    A   A   G   A   A   U   C   U   G   G   U   C   A          
SEQRES 134 2 1799    A   A   C   U   U   G   G   U   C   A   U   U   U          
SEQRES 135 2 1799    A   G   A   G   G   A   A   C   U   A   A   A   A          
SEQRES 136 2 1799    G   U   C   G   U   A   A   C   A   A   G   G   U          
SEQRES 137 2 1799    U   U   C   C   G   U   A   G   G   U   G   A   A          
SEQRES 138 2 1799    C   C   U   G   C   G   G   A   A   G   G   A   U          
SEQRES 139 2 1799    C   A   U   U   A                                          
SEQRES   1 A  254  MET SER LEU PRO SER THR PHE ASP LEU THR SER GLU ASP          
SEQRES   2 A  254  ALA GLN LEU LEU LEU ALA ALA ARG VAL HIS LEU GLY ALA          
SEQRES   3 A  254  LYS ASN VAL GLN VAL HIS GLN GLU PRO TYR VAL TYR LYS          
SEQRES   4 A  254  ALA ARG PRO ASP GLY VAL ASN VAL ILE ASN VAL GLY LYS          
SEQRES   5 A  254  THR TRP GLU LYS ILE VAL LEU ALA ALA ARG ILE ILE ALA          
SEQRES   6 A  254  ALA ILE PRO ASN PRO GLU ASP VAL VAL ALA ILE SER SER          
SEQRES   7 A  254  ARG THR TYR GLY GLN ARG ALA VAL LEU LYS TYR ALA ALA          
SEQRES   8 A  254  HIS THR GLY ALA THR PRO ILE ALA GLY ARG PHE THR PRO          
SEQRES   9 A  254  GLY SER PHE THR ASN TYR ILE THR ARG SER PHE LYS GLU          
SEQRES  10 A  254  PRO ARG LEU VAL ILE VAL THR ASP PRO ARG SER ASP ALA          
SEQRES  11 A  254  GLN ALA ILE LYS GLU SER SER TYR VAL ASN ILE PRO VAL          
SEQRES  12 A  254  ILE ALA LEU THR ASP LEU ASP SER PRO SER GLU TYR VAL          
SEQRES  13 A  254  ASP VAL ALA ILE PRO CYS ASN ASN ARG GLY LYS HIS SER          
SEQRES  14 A  254  ILE GLY LEU ILE TRP TYR LEU LEU ALA ARG GLU VAL LEU          
SEQRES  15 A  254  ARG LEU ARG GLY ALA LEU PRO ASP ARG THR GLN PRO TRP          
SEQRES  16 A  254  ALA ILE MET PRO ASP LEU TYR PHE TYR ARG ASN PRO GLU          
SEQRES  17 A  254  GLU ILE GLU GLN GLN THR ALA GLU GLU GLU ALA VAL ALA          
SEQRES  18 A  254  SER GLY GLU GLN THR GLU GLU ALA VAL ASP ALA THR GLU          
SEQRES  19 A  254  GLU GLN THR GLU ALA ALA GLU TRP ALA GLU GLU GLY GLN          
SEQRES  20 A  254  ALA GLN GLU GLU GLU TRP ASN                                  
SEQRES   1 B  255  MET ALA VAL GLY LYS ASN LYS ARG LEU SER LYS GLY LYS          
SEQRES   2 B  255  LYS GLY LEU LYS LYS ARG VAL VAL ASP PRO PHE THR ARG          
SEQRES   3 B  255  LYS GLU TRP TYR ASP ILE LYS ALA PRO SER THR PHE GLU          
SEQRES   4 B  255  ASN ARG ASN VAL GLY LYS THR LEU VAL ASN LYS SER VAL          
SEQRES   5 B  255  GLY LEU LYS ASN ALA SER ASP SER LEU LYS GLY ARG VAL          
SEQRES   6 B  255  VAL GLU VAL CYS LEU ALA ASP LEU GLN GLY SER GLU ASP          
SEQRES   7 B  255  HIS SER PHE ARG LYS VAL LYS LEU ARG VAL ASP GLU VAL          
SEQRES   8 B  255  GLN GLY LYS ASN LEU LEU THR ASN PHE HIS GLY MET ASP          
SEQRES   9 B  255  PHE THR THR ASP LYS LEU ARG SER MET VAL ARG LYS TRP          
SEQRES  10 B  255  GLN THR LEU ILE GLU ALA ASN VAL THR VAL LYS THR SER          
SEQRES  11 B  255  ASP ASP TYR VAL LEU ARG ILE PHE ALA ILE ALA PHE THR          
SEQRES  12 B  255  ARG LYS GLN ALA ASN GLN VAL LYS ARG THR SER TYR ALA          
SEQRES  13 B  255  GLN SER SER HIS ILE ARG GLN ILE ARG LYS VAL ILE SER          
SEQRES  14 B  255  GLU ILE LEU THR ARG GLU VAL GLN ASN SER THR LEU ALA          
SEQRES  15 B  255  GLN LEU THR SER LYS LEU ILE PRO GLU VAL ILE ASN LYS          
SEQRES  16 B  255  GLU ILE GLU ASN ALA THR LYS ASP ILE PHE PRO LEU GLN          
SEQRES  17 B  255  ASN VAL HIS ILE ARG LYS VAL LYS LEU LEU LYS GLN PRO          
SEQRES  18 B  255  LYS PHE ASP LEU GLY SER LEU LEU SER LEU HIS GLY GLU          
SEQRES  19 B  255  ALA SER ALA GLU GLU LYS GLY LYS LYS VAL ALA GLY PHE          
SEQRES  20 B  255  LYS ASP GLU ILE LEU GLU THR VAL                              
SEQRES   1 C  259  MET SER ALA PRO GLN ALA GLN GLY GLN GLN ALA PRO ARG          
SEQRES   2 C  259  ARG GLY GLY PHE GLY GLY ALA ASN ARG GLY GLY ARG GLY          
SEQRES   3 C  259  GLY ARG ARG GLY GLY ARG ARG ASP GLN GLU GLU LYS GLY          
SEQRES   4 C  259  TRP VAL PRO VAL THR LYS LEU GLY ARG LEU VAL LYS ALA          
SEQRES   5 C  259  GLY LYS ILE SER SER ILE GLU GLU ILE PHE LEU HIS SER          
SEQRES   6 C  259  LEU PRO VAL LYS GLU PHE GLN ILE ILE ASP GLN LEU LEU          
SEQRES   7 C  259  PRO ASN LEU LYS ASP GLU VAL MET ASN ILE LYS PRO VAL          
SEQRES   8 C  259  GLN LYS GLN THR ARG ALA GLY GLN ARG THR ARG PHE LYS          
SEQRES   9 C  259  ALA VAL VAL VAL VAL GLY ASP SER ASN GLY HIS VAL GLY          
SEQRES  10 C  259  LEU GLY ILE LYS THR ALA LYS GLU VAL ALA GLY ALA ILE          
SEQRES  11 C  259  ARG ALA GLY ILE ILE ILE ALA LYS LEU SER VAL ILE PRO          
SEQRES  12 C  259  ILE ARG ARG GLY TYR TRP GLY THR ASN LEU GLY GLN PRO          
SEQRES  13 C  259  HIS SER LEU ALA THR LYS THR SER GLY LYS CYS GLY SER          
SEQRES  14 C  259  VAL SER VAL ARG LEU ILE PRO ALA PRO ARG GLY SER GLY          
SEQRES  15 C  259  ILE VAL ALA SER PRO ALA VAL LYS LYS LEU MET GLN LEU          
SEQRES  16 C  259  ALA GLY VAL GLU ASP VAL TYR THR SER SER THR GLY SER          
SEQRES  17 C  259  THR ARG THR LEU GLU ASN THR LEU LYS ALA ALA PHE VAL          
SEQRES  18 C  259  ALA ILE GLY ASN THR TYR GLY PHE LEU THR PRO ASN LEU          
SEQRES  19 C  259  TRP GLU VAL GLN ALA LEU THR PRO SER PRO MET ASP VAL          
SEQRES  20 C  259  TYR ALA ASP TYR ALA THR ALA SER LYS LYS LYS LEU              
SEQRES   1 D  237  MET VAL ALA ILE ILE SER LYS LYS ARG LYS LEU VAL ALA          
SEQRES   2 D  237  ASP GLY VAL PHE TYR ALA GLU LEU ASN GLU PHE PHE THR          
SEQRES   3 D  237  ARG GLU LEU ALA GLU GLU GLY TYR SER GLY VAL GLU VAL          
SEQRES   4 D  237  ARG VAL THR PRO THR LYS THR GLU ILE ILE ILE ARG ALA          
SEQRES   5 D  237  THR LYS VAL GLN ASP VAL VAL GLY GLU ASN GLY ARG ARG          
SEQRES   6 D  237  ILE ASN GLU LEU THR LEU LEU ILE GLU LYS ARG PHE LYS          
SEQRES   7 D  237  TYR LYS ARG GLY THR ILE ALA LEU TYR ALA GLU ARG VAL          
SEQRES   8 D  237  HIS ASP ARG GLY LEU SER ALA VAL ALA GLN ALA GLU SER          
SEQRES   9 D  237  MET LYS PHE LYS LEU LEU ASN GLY LEU ALA ILE ARG ARG          
SEQRES  10 D  237  ALA ALA TYR GLY VAL VAL ARG TYR VAL MET GLU SER GLY          
SEQRES  11 D  237  ALA LYS GLY CYS GLU VAL VAL ILE SER GLY LYS LEU ARG          
SEQRES  12 D  237  ALA ALA ARG ALA LYS SER MET LYS PHE ALA ASP GLY PHE          
SEQRES  13 D  237  LEU ILE HIS SER GLY GLN PRO VAL ASN ASP PHE ILE GLU          
SEQRES  14 D  237  THR ALA THR ARG HIS VAL LEU LEU ARG GLN GLY VAL LEU          
SEQRES  15 D  237  GLY ILE LYS VAL LYS ILE MET LYS ASP PRO SER ARG ASN          
SEQRES  16 D  237  THR SER GLY PRO LYS ALA LEU PRO ASP ALA VAL THR ILE          
SEQRES  17 D  237  ILE GLU PRO LYS GLU GLU GLU PRO VAL LEU GLU PRO SER          
SEQRES  18 D  237  VAL LYS ASP TYR ARG PRO THR GLU PRO VAL GLU ALA ALA          
SEQRES  19 D  237  GLU SER ALA                                                  
SEQRES   1 E  261  MET ALA ARG GLY PRO LYS LYS HIS LEU LYS ARG LEU ALA          
SEQRES   2 E  261  ALA PRO HIS HIS TRP MET LEU ASP LYS LEU SER GLY CYS          
SEQRES   3 E  261  TYR ALA PRO ARG PRO SER ALA GLY PRO HIS LYS LEU ARG          
SEQRES   4 E  261  GLU SER LEU PRO LEU ILE VAL PHE LEU ARG ASN ARG LEU          
SEQRES   5 E  261  LYS TYR ALA LEU ASN GLY ARG GLU VAL LYS ALA ILE LEU          
SEQRES   6 E  261  MET GLN ARG HIS VAL LYS VAL ASP GLY LYS VAL ARG THR          
SEQRES   7 E  261  ASP THR THR PHE PRO ALA GLY PHE MET ASP VAL ILE THR          
SEQRES   8 E  261  LEU GLU ALA THR ASN GLU ASN PHE ARG LEU VAL TYR ASP          
SEQRES   9 E  261  VAL LYS GLY ARG PHE ALA VAL HIS ARG ILE THR ASP GLU          
SEQRES  10 E  261  GLU ALA SER TYR LYS LEU ALA LYS VAL LYS LYS VAL GLN          
SEQRES  11 E  261  LEU GLY LYS LYS GLY ILE PRO TYR VAL VAL THR HIS ASP          
SEQRES  12 E  261  GLY ARG THR ILE ARG TYR PRO ASP PRO ASN ILE LYS VAL          
SEQRES  13 E  261  ASN ASP THR VAL LYS VAL ASP LEU ALA THR GLY THR ILE          
SEQRES  14 E  261  THR ASP PHE ILE LYS PHE ASP THR GLY LYS LEU VAL TYR          
SEQRES  15 E  261  VAL THR GLY GLY ARG ASN LEU GLY ARG VAL GLY THR ILE          
SEQRES  16 E  261  VAL HIS ARG GLU ARG HIS GLU GLY GLY PHE ASP LEU VAL          
SEQRES  17 E  261  HIS ILE LYS ASP SER LEU GLU ASN THR PHE VAL THR ARG          
SEQRES  18 E  261  LEU ASN ASN VAL PHE VAL ILE GLY GLU PRO GLY ARG PRO          
SEQRES  19 E  261  TRP ILE SER LEU PRO LYS GLY LYS GLY ILE LYS LEU THR          
SEQRES  20 E  261  ILE SER GLU GLU ARG ASP ARG ARG ARG ALA GLN HIS GLY          
SEQRES  21 E  261  LEU                                                          
SEQRES   1 F  227  MET SER GLU HIS GLU ALA GLN VAL GLU VAL GLU VAL GLN          
SEQRES   2 F  227  GLU ASP PHE GLU VAL VAL GLN GLU PHE VAL PRO VAL GLU          
SEQRES   3 F  227  LEU ALA THR THR ILE PRO VAL GLU ILE GLN GLN ALA GLN          
SEQRES   4 F  227  GLN GLU ILE LYS LEU PHE ASN LYS TRP SER PHE GLU ASP          
SEQRES   5 F  227  VAL GLU VAL LYS ASP ALA SER LEU VAL ASP TYR ILE GLN          
SEQRES   6 F  227  ILE SER LYS PRO ILE TYR VAL ALA HIS THR ALA GLY ARG          
SEQRES   7 F  227  TYR ALA ASN LYS ARG PHE ARG LYS ALA GLN CYS PRO ILE          
SEQRES   8 F  227  VAL GLU ARG LEU THR ASN SER LEU MET MET ASN GLY ARG          
SEQRES   9 F  227  ASN ASN GLY LYS LYS LEU LYS ALA VAL ARG ILE VAL LYS          
SEQRES  10 F  227  HIS THR LEU GLU ILE ILE ASN VAL LEU THR ASP GLN ASN          
SEQRES  11 F  227  PRO LEU GLN VAL VAL VAL ASP ALA ILE ILE ASN SER GLY          
SEQRES  12 F  227  PRO ARG GLU ASP THR THR ARG VAL GLY GLY GLY GLY ALA          
SEQRES  13 F  227  ALA ARG ARG GLN ALA VAL ASP VAL SER PRO LEU ARG ARG          
SEQRES  14 F  227  VAL ASN GLN SER ILE ALA LEU LEU THR ILE GLY ALA ARG          
SEQRES  15 F  227  GLU ALA ALA PHE ARG ASN ILE LYS THR ILE ALA GLU THR          
SEQRES  16 F  227  LEU ALA GLU GLU LEU ILE ASN ALA ALA LYS GLY SER SER          
SEQRES  17 F  227  THR SER TYR ALA ILE LYS LYS LYS ASP GLU LEU GLU ARG          
SEQRES  18 F  227  VAL ALA LYS SER ASN ARG                                      
SEQRES   1 G  236  MET LYS LEU ASN ILE SER TYR PRO ILE ASN GLY THR GLN          
SEQRES   2 G  236  LYS CYS ILE GLU ILE ASP ASP GLU HIS ARG VAL ARG VAL          
SEQRES   3 G  236  PHE TYR ASP LYS ARG ILE GLY GLN GLU VAL ASP GLY GLU          
SEQRES   4 G  236  SER VAL GLY ASP GLU PHE LYS GLY TYR VAL PHE LYS ILE          
SEQRES   5 G  236  ALA GLY GLY ASN ASP LYS GLN GLY PHE PRO MET LYS GLN          
SEQRES   6 G  236  GLY VAL LEU LEU PRO THR ARG VAL LYS LEU LEU LEU ALA          
SEQRES   7 G  236  LYS GLY HIS SER CYS TYR ARG PRO ARG ARG ASN GLY GLU          
SEQRES   8 G  236  ARG LYS ARG LYS SER VAL ARG GLY ALA ILE VAL GLY PRO          
SEQRES   9 G  236  ASP LEU ALA VAL LEU ALA LEU ILE ILE THR LYS LYS GLY          
SEQRES  10 G  236  GLU GLN GLU ILE GLU GLY ILE THR ASN ASP THR VAL PRO          
SEQRES  11 G  236  LYS ARG LEU GLY PRO LYS ARG ALA ASN ASN ILE ARG LYS          
SEQRES  12 G  236  PHE PHE GLY LEU THR LYS GLU ASP ASP VAL ARG ASP TYR          
SEQRES  13 G  236  VAL ILE ARG ARG GLU VAL THR LYS GLY ASP LYS SER TYR          
SEQRES  14 G  236  THR LYS ALA PRO LYS ILE GLN ARG LEU VAL THR PRO GLN          
SEQRES  15 G  236  ARG LEU GLN ARG LYS ARG GLN GLN LYS SER LEU LYS ILE          
SEQRES  16 G  236  LYS ASN ALA GLN ALA GLN ARG GLU ALA ALA ALA GLU TYR          
SEQRES  17 G  236  ALA GLN LEU LEU ALA LYS ARG LEU SER GLU ARG LYS ALA          
SEQRES  18 G  236  GLU LYS ALA GLU VAL ARG LYS ARG ARG ALA SER SER LEU          
SEQRES  19 G  236  LYS ALA                                                      
SEQRES   1 H  190  MET SER ASP PRO GLN ALA LYS ILE LEU SER GLN ALA PRO          
SEQRES   2 H  190  THR GLU LEU GLU LEU GLN VAL ALA GLN ALA PHE ILE ASP          
SEQRES   3 H  190  LEU GLU ASN ASN SER PRO GLU LEU LYS ALA ASP LEU ARG          
SEQRES   4 H  190  ALA LEU GLN PHE LYS SER ILE ARG GLU ILE GLU VAL ALA          
SEQRES   5 H  190  GLY GLY LYS LYS ALA LEU ALA VAL PHE VAL PRO VAL PRO          
SEQRES   6 H  190  SER LEU ALA ALA TYR HIS LYS VAL GLN ILE LYS LEU THR          
SEQRES   7 H  190  ARG GLU LEU GLU LYS LYS PHE GLN ASP ARG HIS VAL ILE          
SEQRES   8 H  190  PHE LEU ALA GLU ARG ARG ILE LEU PRO LYS PRO SER ARG          
SEQRES   9 H  190  LYS SER ARG GLN THR GLN LYS ARG PRO ARG SER ARG THR          
SEQRES  10 H  190  LEU THR ALA VAL HIS ASP LYS ILE LEU GLU ASP LEU VAL          
SEQRES  11 H  190  PHE PRO THR GLU ILE VAL GLY LYS ARG VAL ARG TYR LEU          
SEQRES  12 H  190  VAL GLY GLY ASN LYS ILE GLN LYS ILE LEU LEU ASN SER          
SEQRES  13 H  190  LYS ASP VAL GLN HIS ILE ASP ASN LYS LEU GLU SER PHE          
SEQRES  14 H  190  GLN ALA VAL TYR ASN LYS LEU THR GLY LYS GLN ILE VAL          
SEQRES  15 H  190  PHE GLU ILE PRO SER GLU THR HIS                              
SEQRES   1 I  201  MET GLY ILE SER ARG ASP SER ARG HIS LYS ARG ALA ALA          
SEQRES   2 I  201  THR GLY ALA LYS ARG ALA GLN PHE ARG LYS LYS ARG LYS          
SEQRES   3 I  201  PHE GLU LEU GLY ARG GLN ALA ALA ASN THR LYS ILE GLY          
SEQRES   4 I  201  THR LYS ARG ILE HIS PRO VAL ARG THR ARG GLY GLY ASN          
SEQRES   5 I  201  GLN LYS PHE ARG ALA LEU ARG ILE GLU THR GLY ASN PHE          
SEQRES   6 I  201  SER TRP ALA SER GLU GLY VAL ALA ARG LYS THR ARG ILE          
SEQRES   7 I  201  THR GLY VAL VAL TYR HIS PRO SER ASN ASN GLU LEU VAL          
SEQRES   8 I  201  ARG THR ASN THR LEU THR LYS ALA ALA ILE VAL GLN ILE          
SEQRES   9 I  201  ASP ALA THR PRO PHE ARG GLN TRP TYR GLU SER HIS TYR          
SEQRES  10 I  201  GLY GLN SER LEU GLY LYS LYS LYS ASN THR LYS ALA GLU          
SEQRES  11 I  201  GLU GLU THR ALA THR THR SER LYS ASN THR GLU ARG LYS          
SEQRES  12 I  201  TRP ALA ALA ARG ALA ALA GLU ALA LYS ILE GLU HIS ALA          
SEQRES  13 I  201  VAL ASP SER GLN PHE GLY ALA GLY ARG LEU TYR ALA ALA          
SEQRES  14 I  201  ILE SER SER ARG PRO GLY GLN SER GLY ARG CYS ASP GLY          
SEQRES  15 I  201  TYR ILE LEU GLU GLY GLU GLU LEU ALA PHE TYR LEU ARG          
SEQRES  16 I  201  ARG LEU THR ALA LYS LYS                                      
SEQRES   1 J  188  MET PRO ARG ALA PRO ARG THR TYR SER LYS THR TYR SER          
SEQRES   2 J  188  THR PRO LYS ARG PRO TYR GLU SER ALA ARG LEU ASP ALA          
SEQRES   3 J  188  GLU LEU LYS LEU ALA GLY GLU TYR GLY LEU LYS ASN LYS          
SEQRES   4 J  188  ARG GLU ILE TYR ARG ILE SER PHE GLN LEU SER LYS ILE          
SEQRES   5 J  188  ARG ARG ALA ALA ARG ASP LEU LEU THR ARG ASP GLU LYS          
SEQRES   6 J  188  ASP PRO LYS ARG LEU PHE GLU GLY ASN ALA LEU ILE ARG          
SEQRES   7 J  188  ARG LEU VAL ARG ILE GLY VAL LEU SER GLU ASP LYS LYS          
SEQRES   8 J  188  LYS LEU ASP TYR VAL LEU ALA LEU LYS VAL GLU ASP PHE          
SEQRES   9 J  188  LEU GLU ARG ARG LEU GLN THR GLN VAL TYR LYS LEU GLY          
SEQRES  10 J  188  LEU ALA LYS SER VAL HIS HIS ALA ARG VAL LEU ILE SER          
SEQRES  11 J  188  GLN ARG HIS ILE ALA VAL GLY LYS GLN ILE VAL ASN ILE          
SEQRES  12 J  188  PRO SER PHE MET VAL ARG LEU GLU SER GLU LYS HIS ILE          
SEQRES  13 J  188  ASP PHE ALA ARG THR SER PRO PHE GLY GLY ALA ARG PRO          
SEQRES  14 J  188  GLY ARG VAL ALA ARG LYS ARG ALA ALA ALA ALA GLY GLY          
SEQRES  15 J  188  GLU GLU ALA ASP GLU GLU                                      
SEQRES   1 K  106  MET LEU ILE PRO LYS GLU ASP ARG LYS LYS ILE TYR GLN          
SEQRES   2 K  106  HIS LEU PHE GLN GLU GLY VAL LEU VAL ALA LYS LYS ASP          
SEQRES   3 K  106  PHE ASN GLN PRO LYS HIS GLU GLU ILE ASP THR LYS ASN          
SEQRES   4 K  106  LEU PHE VAL ILE LYS ALA LEU GLN SER LEU THR SER LYS          
SEQRES   5 K  106  GLY PHE VAL LYS THR GLN PHE SER TRP GLN TYR TYR TYR          
SEQRES   6 K  106  TYR THR LEU THR GLU GLU GLY VAL VAL TYR LEU ARG GLU          
SEQRES   7 K  106  TYR LEU ASN LEU PRO GLU HIS ILE PHE PRO ALA THR TYR          
SEQRES   8 K  106  LEU ALA GLY GLN SER GLY ASP GLN ARG PRO GLN GLY LYS          
SEQRES   9 K  106  LYS TYR                                                      
SEQRES   1 L  156  MET SER THR GLU LEU THR VAL GLN SER GLU ARG ALA PHE          
SEQRES   2 L  156  GLN LYS GLN PRO HIS ILE PHE THR ASN PRO LYS ALA LYS          
SEQRES   3 L  156  ALA ASN ARG LYS THR LYS ARG TRP TYR LYS ASN VAL GLY          
SEQRES   4 L  156  LEU GLY PHE LYS THR PRO LYS THR ALA ILE GLU GLY SER          
SEQRES   5 L  156  TYR ILE ASP LYS LYS CYS PRO PHE THR GLY LEU VAL SER          
SEQRES   6 L  156  ILE ARG GLY LYS ILE LEU THR GLY THR VAL VAL SER THR          
SEQRES   7 L  156  ARG MET HIS ARG THR ILE VAL ILE ARG ARG ASP TYR LEU          
SEQRES   8 L  156  HIS TYR VAL PRO LYS TYR ASN ARG TYR GLU LYS ARG HIS          
SEQRES   9 L  156  LYS ASN VAL PRO ALA HIS VAL SER PRO ALA PHE ARG VAL          
SEQRES  10 L  156  GLN VAL GLY ASP ILE VAL THR VAL GLY GLN CYS ARG PRO          
SEQRES  11 L  156  ILE SER LYS THR VAL ARG PHE ASN VAL LEU LYS VAL ALA          
SEQRES  12 L  156  SER ALA THR GLY LYS ALA ASN LYS GLN PHE ALA LYS PHE          
SEQRES   1 M  134  MET SER ASP VAL GLU GLU VAL GLN GLN VAL PRO VAL ALA          
SEQRES   2 M  134  GLU LEU THR ILE GLU ASP ALA LEU LYS VAL VAL LEU ARG          
SEQRES   3 M  134  THR SER LEU VAL HIS ASP GLY LEU ALA ARG GLY LEU ARG          
SEQRES   4 M  134  GLU SER ALA LYS ALA LEU THR ARG GLY GLU GLY GLN LEU          
SEQRES   5 M  134  ALA VAL LEU VAL GLU SER VAL THR GLU GLU ALA ILE SER          
SEQRES   6 M  134  LYS LEU VAL GLN GLY LEU ALA THR GLU ASN ASN VAL PRO          
SEQRES   7 M  134  LEU ILE LYS VAL ALA ASP ALA LYS GLN LEU GLY GLU TRP          
SEQRES   8 M  134  ALA GLY LEU GLY LYS ILE ASP ARG ASP GLY ASN ALA ARG          
SEQRES   9 M  134  LYS VAL VAL GLY ALA SER VAL VAL VAL VAL LYS ASN TRP          
SEQRES  10 M  134  GLY ALA ASP THR GLN GLU ARG GLU ILE LEU LEU GLU HIS          
SEQRES  11 M  134  PHE SER GLN GLN                                              
SEQRES   1 N  151  MET GLY ARG MET HIS SER LYS GLY LYS GLY MET SER SER          
SEQRES   2 N  151  SER ALA ILE PRO TYR SER ARG ASN ALA PRO ALA TRP PHE          
SEQRES   3 N  151  LYS GLY SER SER ASP GLY VAL VAL GLU GLN ILE ILE LYS          
SEQRES   4 N  151  TYR ALA ARG LYS GLY LEU THR PRO SER GLN ILE GLY VAL          
SEQRES   5 N  151  LEU LEU ARG ASP ALA HIS GLY VAL THR GLN ALA LYS VAL          
SEQRES   6 N  151  ILE THR GLY ASN LYS ILE LEU ARG ILE LEU LYS SER ASN          
SEQRES   7 N  151  GLY LEU ALA PRO GLU ILE PRO GLU ASP LEU TYR PHE LEU          
SEQRES   8 N  151  ILE LYS LYS ALA VAL SER VAL ARG LYS HIS LEU GLU ARG          
SEQRES   9 N  151  ASN ARG LYS ASP LYS ASP ALA LYS PHE ARG LEU ILE LEU          
SEQRES  10 N  151  ILE GLU SER ARG ILE HIS ARG LEU ALA ARG TYR TYR ARG          
SEQRES  11 N  151  THR VAL SER VAL LEU PRO PRO ASN TRP LYS TYR GLU SER          
SEQRES  12 N  151  ALA THR ALA SER ALA LEU VAL ASN                              
SEQRES   1 O  137  MET ALA ASN VAL VAL GLN ALA LYS ASP ASN SER GLN VAL          
SEQRES   2 O  137  PHE GLY VAL ALA ARG ILE PHE ALA SER PHE ASN ASP THR          
SEQRES   3 O  137  PHE VAL HIS VAL THR ASP LEU SER GLY ARG GLU THR ILE          
SEQRES   4 O  137  ALA ARG VAL THR GLY GLY MET LYS VAL LYS ALA ASP ARG          
SEQRES   5 O  137  ASP GLU SER SER PRO TYR ALA ALA MET LEU ALA ALA GLN          
SEQRES   6 O  137  ASP VAL ALA ALA LYS CYS LYS GLU VAL GLY ILE THR ALA          
SEQRES   7 O  137  VAL HIS ILE LYS ILE ARG ALA THR GLY GLY THR ARG SER          
SEQRES   8 O  137  LYS THR PRO GLY PRO GLY GLY GLN ALA ALA LEU ARG ALA          
SEQRES   9 O  137  LEU ALA ARG SER GLY LEU ARG ILE GLY ARG ILE GLU ASP          
SEQRES  10 O  137  VAL THR PRO VAL PRO SER ASP SER THR ARG LYS LYS GLY          
SEQRES  11 O  137  GLY ARG ARG GLY ARG ARG LEU                                  
SEQRES   1 P  142  MET SER GLU ALA ALA ALA PRO ARG LYS ARG SER PHE LYS          
SEQRES   2 P  142  THR TYR SER TYR LYS GLY VAL ASP LEU GLU LYS LEU LEU          
SEQRES   3 P  142  GLU MET PRO THR GLU ASP PHE VAL LYS LEU ALA PRO ALA          
SEQRES   4 P  142  ARG VAL ARG ARG LYS PHE ALA ARG GLY LEU SER GLU LYS          
SEQRES   5 P  142  PRO ALA GLY LEU MET LYS LYS LEU ARG ALA ALA LYS LEU          
SEQRES   6 P  142  SER ALA PRO GLU ASN GLU LYS PRO ALA VAL VAL ARG THR          
SEQRES   7 P  142  HIS LEU ARG ASN MET ILE ILE VAL PRO GLU MET ILE GLY          
SEQRES   8 P  142  SER VAL VAL GLY VAL TYR ASN GLY LYS VAL PHE ASN GLN          
SEQRES   9 P  142  VAL GLU ILE ARG PRO GLU MET VAL GLY HIS TYR LEU GLY          
SEQRES  10 P  142  GLU PHE SER ILE THR TYR THR PRO VAL ARG HIS GLY ARG          
SEQRES  11 P  142  ALA GLY ALA THR THR SER ARG PHE ILE PRO LEU ARG              
SEQRES   1 Q  143  MET SER THR VAL PRO SER VAL GLN THR PHE GLY LYS LYS          
SEQRES   2 Q  143  LYS SER ALA THR ALA VAL ALA HIS VAL LYS ALA GLY LYS          
SEQRES   3 Q  143  GLY LEU ILE LYS VAL ASN GLY SER PRO ILE THR LEU VAL          
SEQRES   4 Q  143  GLN PRO GLU ILE LEU ARG PHE LYS VAL TYR GLU PRO LEU          
SEQRES   5 Q  143  LEU LEU VAL GLY LEU ASP LYS PHE ALA ASN ILE ASP ILE          
SEQRES   6 Q  143  ARG VAL LYS VAL THR GLY GLY GLY HIS VAL SER GLN VAL          
SEQRES   7 Q  143  TYR ALA ILE ARG GLN ALA ILE ALA LYS GLY LEU VAL ALA          
SEQRES   8 Q  143  TYR HIS GLN LYS PHE VAL ASP GLU GLN SER LYS ASN GLU          
SEQRES   9 Q  143  LEU LYS LYS ALA PHE THR SER TYR ASP ARG THR LEU LEU          
SEQRES  10 Q  143  ILE ALA ASP SER ARG ARG PRO GLU PRO LYS LYS PHE GLY          
SEQRES  11 Q  143  GLY ARG GLY ALA ARG SER ARG PHE GLN LYS SER TYR ARG          
SEQRES   1 R  136  MET GLY ARG VAL ARG THR LYS THR VAL LYS ARG ALA SER          
SEQRES   2 R  136  LYS ALA LEU ILE GLU LYS TYR TYR PRO LYS LEU THR MET          
SEQRES   3 R  136  ASP PHE GLN THR ASN LYS ARG LEU CYS ASP GLU ILE ALA          
SEQRES   4 R  136  THR ILE GLN SER LYS ARG LEU ARG ASN LYS ILE ALA GLY          
SEQRES   5 R  136  TYR THR THR HIS LEU MET LYS ARG ILE GLN LYS GLY PRO          
SEQRES   6 R  136  VAL ARG GLY ILE SER PHE LYS LEU GLN GLU GLU GLU ARG          
SEQRES   7 R  136  GLU ARG LYS ASP GLN TYR VAL PRO ASP VAL SER ALA LEU          
SEQRES   8 R  136  ASP LEU SER HIS SER ASN ASP VAL LEU ASN VAL ASP THR          
SEQRES   9 R  136  GLN THR ALA GLU LEU VAL ASN SER LEU GLY LEU LYS LEU          
SEQRES  10 R  136  PRO LEU SER VAL SER SER VAL SER ALA VAL ARG ASP ARG          
SEQRES  11 R  136  ARG PHE ARG LYS ARG ASN                                      
SEQRES   1 S  146  MET SER LEU VAL VAL GLN GLU GLN GLY SER PHE GLN HIS          
SEQRES   2 S  146  ILE LEU ARG LEU LEU ASN THR ASN VAL ASP GLY ASN ILE          
SEQRES   3 S  146  ASN VAL VAL TYR ALA LEU THR THR ILE ARG GLY VAL GLY          
SEQRES   4 S  146  ARG ARG TYR ALA ASN LEU VAL CYS LYS LYS ALA ASP VAL          
SEQRES   5 S  146  ASP LEU HIS LYS ARG ALA GLY GLU LEU THR GLN GLU GLU          
SEQRES   6 S  146  LEU GLU ARG ILE VAL GLN ILE MET GLN ASN PRO THR HIS          
SEQRES   7 S  146  TYR LYS ILE PRO ALA TRP PHE LEU ASN ARG GLN LYS ASP          
SEQRES   8 S  146  VAL ASN ASP GLY LYS ASP TYR HIS SER LEU ALA ASN ASN          
SEQRES   9 S  146  LEU GLU SER LYS LEU ARG ASP ASP LEU GLU ARG LEU LYS          
SEQRES  10 S  146  LYS ILE ARG SER HIS ARG GLY ILE ARG HIS PHE TRP GLY          
SEQRES  11 S  146  LEU ARG VAL ARG GLY GLN HIS THR LYS THR THR GLY ARG          
SEQRES  12 S  146  ARG ARG ALA                                                  
SEQRES   1 T  144  MET PRO GLY VAL SER VAL ARG ASP VAL PRO ALA GLN ASP          
SEQRES   2 T  144  PHE ILE ASN ASN TYR ALA SER PHE LEU GLN ARG GLN GLY          
SEQRES   3 T  144  LYS LEU GLU VAL PRO GLY TYR VAL ASP ILE VAL LYS THR          
SEQRES   4 T  144  SER ALA GLY ASN GLU LEU PRO PRO GLN ASP SER GLU GLY          
SEQRES   5 T  144  TRP PHE TYR LYS ARG ALA ALA SER VAL ALA ARG HIS ILE          
SEQRES   6 T  144  TYR LEU ARG LYS GLN VAL GLY VAL GLY LYS LEU ASN LYS          
SEQRES   7 T  144  LEU TYR GLY GLY ALA LYS ASN ARG GLY VAL ARG PRO HIS          
SEQRES   8 T  144  LYS HIS VAL ASP ALA SER GLY SER ILE ASN ARG LYS VAL          
SEQRES   9 T  144  LEU GLN SER LEU GLU LYS LEU GLY VAL VAL GLU ILE SER          
SEQRES  10 T  144  PRO LYS GLY GLY ARG ARG ILE SER ASP ASN GLY LEU ARG          
SEQRES  11 T  144  ASP LEU ASP ARG ILE ALA ALA ALA THR LEU GLU ASP GLU          
SEQRES  12 T  144  GLU                                                          
SEQRES   1 U  117  MET SER GLN VAL GLU LYS LYS SER GLU GLN GLN GLN GLU          
SEQRES   2 U  117  VAL VAL ILE HIS LYS ILE ARG ILE ASN LEU THR SER THR          
SEQRES   3 U  117  LYS VAL LYS GLN LEU GLU ASN VAL SER ALA ASN ILE ILE          
SEQRES   4 U  117  LYS ASN ALA GLU THR PHE LYS LEU VAL LYS LYS GLY PRO          
SEQRES   5 U  117  VAL ARG LEU PRO THR LYS VAL LEU LYS ILE SER THR ARG          
SEQRES   6 U  117  LYS THR PRO ASN GLY GLU GLY SER LYS THR TRP ASP THR          
SEQRES   7 U  117  TYR GLU MET ARG ILE HIS LYS ARG TYR ILE ASP LEU GLU          
SEQRES   8 U  117  ALA PRO ALA HIS ILE VAL LYS ARG ILE THR GLN ILE THR          
SEQRES   9 U  117  ILE GLU PRO GLY VAL ASP VAL GLU VAL ILE ILE ALA ALA          
SEQRES   1 V   87  MET GLU ASN ASP LYS GLY GLN LEU VAL GLU LEU TYR VAL          
SEQRES   2 V   87  PRO ARG LYS CYS SER ALA THR ASN ARG ILE ILE LYS ALA          
SEQRES   3 V   87  LYS ASP HIS SER SER VAL GLN ILE ASN ILE ALA GLN VAL          
SEQRES   4 V   87  ASP GLU GLU GLY ARG ALA ILE PRO GLY GLU TYR VAL THR          
SEQRES   5 V   87  TYR ALA LEU SER GLY TYR ILE ARG ALA ARG GLY GLU ALA          
SEQRES   6 V   87  ASP ASP SER LEU ASN ARG LEU ALA GLN GLN ASP GLY LEU          
SEQRES   7 V   87  LEU LYS ASN VAL TRP SER TYR SER ARG                          
SEQRES   1 W  130  MET THR ARG THR SER VAL LEU ALA ASP ALA LEU ASN ALA          
SEQRES   2 W  130  ILE ASN ASN ALA GLU LYS THR GLY LYS ARG GLN VAL LEU          
SEQRES   3 W  130  ILE ARG PRO SER SER LYS VAL ILE ILE LYS PHE LEU GLN          
SEQRES   4 W  130  VAL MET GLN LYS HIS GLY TYR ILE GLY GLU PHE GLU TYR          
SEQRES   5 W  130  ILE ASP ASP HIS ARG SER GLY LYS ILE VAL VAL GLN LEU          
SEQRES   6 W  130  ASN GLY ARG LEU ASN LYS CYS GLY VAL ILE SER PRO ARG          
SEQRES   7 W  130  PHE ASN VAL LYS ILE ALA ASP VAL GLU LYS TRP THR ALA          
SEQRES   8 W  130  ASN LEU LEU PRO ALA ARG GLN PHE GLY TYR VAL ILE LEU          
SEQRES   9 W  130  THR THR SER ALA GLY ILE MET ASP HIS GLU GLU ALA HIS          
SEQRES  10 W  130  ARG LYS HIS VAL SER GLY LYS ILE LEU GLY PHE VAL TYR          
SEQRES   1 X  145  MET GLY LYS GLY LYS PRO ARG GLY LEU ASN SER ALA ARG          
SEQRES   2 X  145  LYS LEU ARG VAL HIS ARG ARG ASN ASN ARG TRP ALA GLU          
SEQRES   3 X  145  THR THR TYR LYS LYS ARG LEU LEU GLY THR ALA PHE LYS          
SEQRES   4 X  145  SER SER PRO PHE GLY GLY SER SER HIS ALA LYS GLY ILE          
SEQRES   5 X  145  VAL LEU GLU LYS ILE GLY ILE GLU SER LYS GLN PRO ASN          
SEQRES   6 X  145  SER ALA ILE ARG LYS CYS VAL ARG VAL GLN LEU ILE LYS          
SEQRES   7 X  145  ASN GLY LYS LYS VAL THR ALA PHE VAL PRO ASN ASP GLY          
SEQRES   8 X  145  CYS LEU ASN PHE VAL ASP GLU ASN ASP GLU VAL LEU LEU          
SEQRES   9 X  145  ALA GLY PHE GLY ARG LYS GLY LYS ALA LYS GLY ASP ILE          
SEQRES  10 X  145  PRO GLY VAL ARG PHE LYS VAL VAL LYS VAL SER GLY VAL          
SEQRES  11 X  145  SER LEU LEU ALA LEU TRP LYS GLU LYS LYS GLU LYS PRO          
SEQRES  12 X  145  ARG SER                                                      
SEQRES   1 Y  135  MET SER ASP ALA ILE THR ILE ARG THR ARG LYS VAL ILE          
SEQRES   2 Y  135  SER ASN PRO LEU LEU ALA ARG LYS GLN PHE VAL VAL ASP          
SEQRES   3 Y  135  VAL LEU HIS PRO ASN ARG ALA ASN VAL SER LYS ASP GLU          
SEQRES   4 Y  135  LEU ARG GLU LYS LEU ALA GLU ALA TYR LYS ALA GLU LYS          
SEQRES   5 Y  135  ASP ALA VAL SER VAL PHE GLY PHE ARG THR GLN TYR GLY          
SEQRES   6 Y  135  GLY GLY LYS SER THR GLY PHE GLY LEU VAL TYR ASN SER          
SEQRES   7 Y  135  VAL ALA ASP ALA LYS LYS PHE GLU PRO ALA TYR ARG LEU          
SEQRES   8 Y  135  VAL ARG TYR GLY LEU ALA GLU LYS VAL GLU LYS ALA SER          
SEQRES   9 Y  135  ARG GLN GLN ARG LYS GLN ARG LYS ASN ARG GLY LYS LYS          
SEQRES  10 Y  135  ILE PHE GLY THR GLY LYS SER ILE ALA LYS LYS ALA ALA          
SEQRES  11 Y  135  ARG ARG ASN ALA ASP                                          
SEQRES   1 Z  108  MET PRO PRO LYS GLN GLN LEU SER LYS ALA ALA LYS ALA          
SEQRES   2 Z  108  ALA ALA ALA MET ALA GLY GLY LYS LYS SER LYS LYS LYS          
SEQRES   3 Z  108  TRP SER LYS LYS SER HIS LYS ASP LYS ALA LYS HIS ALA          
SEQRES   4 Z  108  VAL VAL LEU ASP GLN ASP LYS PHE ASP ARG ILE MET LYS          
SEQRES   5 Z  108  GLU ALA PRO THR TYR ARG TYR VAL SER VAL SER VAL LEU          
SEQRES   6 Z  108  VAL ASP ARG PHE LYS LEU GLY GLY SER LEU ALA ARG VAL          
SEQRES   7 Z  108  ALA LEU ARG HIS LEU GLU ASN GLU GLY ILE ILE LYS PRO          
SEQRES   8 Z  108  VAL SER LYS HIS SER LYS GLN ALA ILE TYR THR ARG ALA          
SEQRES   9 Z  108  THR ALA SER GLU                                              
SEQRES   1 a  119  MET PRO LYS LYS ARG ALA SER ASN GLY ARG ASN LYS LYS          
SEQRES   2 a  119  GLY ARG GLY HIS VAL LYS PRO VAL ARG CYS VAL ASN CYS          
SEQRES   3 a  119  SER ARG SER VAL PRO LYS ASP LYS ALA ILE LYS ARG MET          
SEQRES   4 a  119  ALA ILE ARG ASN ILE VAL GLU ALA ALA ALA ILE ARG ASP          
SEQRES   5 a  119  LEU SER GLU ALA SER VAL TYR ALA GLU TYR ALA LEU PRO          
SEQRES   6 a  119  LYS THR TYR ASN LYS LEU HIS TYR CYS ILE SER CYS ALA          
SEQRES   7 a  119  ILE HIS ALA ARG ILE VAL ARG VAL ARG SER ARG THR ASP          
SEQRES   8 a  119  ARG ARG ILE ARG ALA PRO PRO GLN ARG PRO ARG PHE ASN          
SEQRES   9 a  119  ARG ASP ASN LYS VAL SER PRO ALA ASP ALA ALA LYS LYS          
SEQRES  10 a  119  ALA LEU                                                      
SEQRES   1 b   82  MET VAL LEU VAL GLN ASP LEU LEU HIS PRO THR ALA ALA          
SEQRES   2 b   82  SER GLU ALA ARG LYS HIS LYS LEU LYS THR LEU VAL GLN          
SEQRES   3 b   82  SER PRO ARG SER HIS PHE LEU ASP VAL LYS CYS PRO GLY          
SEQRES   4 b   82  CYS LEU ASN ILE THR THR VAL PHE SER HIS ALA GLN THR          
SEQRES   5 b   82  ALA VAL THR CYS GLU SER CYS SER THR VAL LEU CYS THR          
SEQRES   6 b   82  PRO THR GLY GLY LYS ALA LYS LEU SER GLU GLY THR SER          
SEQRES   7 b   82  PHE ARG ARG LYS                                              
SEQRES   1 c   67  MET ASP THR LYS THR PRO VAL THR LEU ALA LYS VAL ILE          
SEQRES   2 c   67  LYS VAL LEU GLY ARG THR GLY SER ARG GLY GLY VAL THR          
SEQRES   3 c   67  GLN VAL ARG VAL GLU PHE LEU GLU ASP THR THR ARG THR          
SEQRES   4 c   67  ILE VAL ARG ASN VAL LYS GLY PRO VAL ARG GLU GLY ASP          
SEQRES   5 c   67  ILE LEU VAL LEU MET GLU SER GLU ARG GLU ALA ARG ARG          
SEQRES   6 c   67  LEU ARG                                                      
SEQRES   1 d   56  MET ALA HIS GLU ASN VAL TRP TYR SER HIS PRO ARG LYS          
SEQRES   2 d   56  PHE GLY LYS GLY SER ARG GLN CYS ARG ILE SER GLY SER          
SEQRES   3 d   56  HIS SER GLY LEU ILE ARG LYS TYR GLY LEU ASN ILE ASP          
SEQRES   4 d   56  ARG GLN SER PHE ARG GLU LYS ALA ASN ASP ILE GLY PHE          
SEQRES   5 d   56  TYR LYS TYR ARG                                              
SEQRES   1 e   63  MET GLY LYS VAL HIS GLY SER LEU ALA ARG ALA GLY LYS          
SEQRES   2 e   63  VAL LYS SER GLN THR PRO LYS VAL GLU LYS GLN GLU LYS          
SEQRES   3 e   63  PRO LYS GLN PRO LYS GLY ARG ALA TYR LYS ARG LEU LEU          
SEQRES   4 e   63  TYR THR ARG ARG PHE VAL ASN VAL THR LEU THR ASN GLY          
SEQRES   5 e   63  LYS ARG LYS MET ASN PRO SER PRO SER SER GLN                  
SEQRES   1 f  150  MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE          
SEQRES   2 f  150  THR LEU GLU VAL GLU SER SER ASP THR ILE ASP ASN VAL          
SEQRES   3 f  150  LYS SER LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP          
SEQRES   4 f  150  GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP          
SEQRES   5 f  150  GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER          
SEQRES   6 f  150  THR LEU HIS LEU VAL LEU ARG LEU ARG GLY GLY GLY LYS          
SEQRES   7 f  150  LYS ARG LYS LYS LYS VAL TYR THR THR PRO LYS LYS ILE          
SEQRES   8 f  150  ARG HIS LYS HIS LYS LYS VAL LYS LEU ALA VAL LEU ASN          
SEQRES   9 f  150  TYR TYR LYS VAL ASP ASP GLU GLY LYS VAL ALA LYS LEU          
SEQRES  10 f  150  ARG LYS GLU CYS PRO ASN CYS GLY PRO GLY ILE PHE LEU          
SEQRES  11 f  150  ALA ASN HIS GLY ASP ARG PHE TYR CYS GLY LYS CYS HIS          
SEQRES  12 f  150  SER THR PHE ALA THR GLN LYS                                  
SEQRES   1 g  326  MET SER SER SER ASN ILE MET LEU VAL LEU ARG GLY THR          
SEQRES   2 g  326  LEU GLU GLY HIS ASN GLY TRP VAL THR SER LEU SER THR          
SEQRES   3 g  326  SER ALA ALA GLN PRO ASN LEU LEU VAL SER GLY SER ARG          
SEQRES   4 g  326  ASP LYS THR LEU ILE SER TRP ARG LEU THR GLU ASN GLU          
SEQRES   5 g  326  GLN GLN PHE GLY VAL PRO VAL ARG SER TYR LYS GLY HIS          
SEQRES   6 g  326  SER HIS ILE VAL GLN ASP VAL VAL VAL SER ALA ASP GLY          
SEQRES   7 g  326  ASN TYR ALA VAL SER ALA SER TRP ASP LYS THR LEU ARG          
SEQRES   8 g  326  LEU TRP ASN LEU ALA THR GLY ASN SER GLU ALA ARG PHE          
SEQRES   9 g  326  VAL GLY HIS THR GLY ASP VAL LEU SER VAL ALA ILE ASP          
SEQRES  10 g  326  ALA ASN SER SER LYS ILE ILE SER ALA SER ARG ASP LYS          
SEQRES  11 g  326  THR ILE ARG VAL TRP ASN THR VAL GLY ASP CYS ALA TYR          
SEQRES  12 g  326  VAL LEU LEU GLY HIS THR ASP TRP VAL THR LYS VAL ARG          
SEQRES  13 g  326  VAL ALA PRO LYS ASN LEU GLU ASP GLY GLU VAL ASP ASP          
SEQRES  14 g  326  GLY ARG ILE THR PHE VAL SER ALA GLY MET ASP LYS ILE          
SEQRES  15 g  326  VAL ARG SER TRP SER LEU ASN GLU ASP SER TYR ARG ILE          
SEQRES  16 g  326  GLU ALA ASP PHE ILE GLY HIS ASN ASN TYR ILE ASN VAL          
SEQRES  17 g  326  VAL GLN PRO SER PRO ASP GLY SER LEU ALA ALA SER ALA          
SEQRES  18 g  326  GLY LYS ASP GLY GLN ILE TYR VAL TRP ASN LEU LYS HIS          
SEQRES  19 g  326  LYS SER ALA PHE MET ASN PHE ASP ALA LYS ASP GLU VAL          
SEQRES  20 g  326  PHE ALA LEU ALA PHE SER PRO SER ARG PHE TRP LEU THR          
SEQRES  21 g  326  ALA ALA THR ALA SER GLY ILE LYS ILE TYR ASP LEU GLU          
SEQRES  22 g  326  ASN GLU VAL LEU ILE ASP GLU LEU LYS PRO GLU PHE ALA          
SEQRES  23 g  326  GLY TYR THR LYS ALA GLN ASP PRO HIS ALA VAL SER LEU          
SEQRES  24 g  326  ALA TRP SER ALA ASP GLY GLN THR LEU PHE ALA GLY TYR          
SEQRES  25 g  326  THR ASP ASN VAL ILE ARG VAL TRP GLN VAL MET THR ALA          
SEQRES  26 g  326  ASN                                                          
SEQRES   1 h   25  MET ARG ALA LYS TRP ARG LYS LYS ARG THR ARG ARG LEU          
SEQRES   2 h   25  LYS ARG LYS ARG ARG LYS VAL ARG ALA ARG SER LYS              
SEQRES   1 i  153  MET GLY LYS LYS ASN THR LYS GLY GLY LYS LYS GLY ARG          
SEQRES   2 i  153  ARG GLY LYS ASN ASP SER ASP GLY PRO LYS ARG GLU LEU          
SEQRES   3 i  153  ILE TYR LYS GLU GLU GLY GLN GLU TYR ALA GLN ILE THR          
SEQRES   4 i  153  LYS MET LEU GLY ASN GLY ARG VAL GLU ALA SER CYS PHE          
SEQRES   5 i  153  ASP GLY ASN LYS ARG MET ALA HIS ILE ARG GLY LYS LEU          
SEQRES   6 i  153  ARG LYS LYS VAL TRP MET GLY GLN GLY ASP ILE ILE LEU          
SEQRES   7 i  153  VAL SER LEU ARG ASP PHE GLN ASP ASP GLN CYS ASP VAL          
SEQRES   8 i  153  VAL HIS LYS TYR ASN LEU ASP GLU ALA ARG THR LEU LYS          
SEQRES   9 i  153  ASN GLN GLY GLU LEU PRO GLU ASN ALA LYS ILE ASN GLU          
SEQRES  10 i  153  THR ASP ASN PHE GLY PHE GLU SER ASP GLU ASP VAL ASN          
SEQRES  11 i  153  PHE GLU PHE GLY ASN ALA ASP GLU ASP ASP GLU GLU GLY          
SEQRES  12 i  153  GLU ASP GLU GLU LEU ASP ILE ASP ASP ILE                      
SEQRES   1 j  108  MET SER ILE GLU ASN LEU LYS SER PHE ASP PRO PHE ALA          
SEQRES   2 j  108  ASP THR GLY ASP ASP GLU THR ALA THR SER ASN TYR ILE          
SEQRES   3 j  108  HIS ILE ARG ILE GLN GLN ARG ASN GLY ARG LYS THR LEU          
SEQRES   4 j  108  THR THR VAL GLN GLY VAL PRO GLU GLU TYR ASP LEU LYS          
SEQRES   5 j  108  ARG ILE LEU LYS VAL LEU LYS LYS ASP PHE ALA CYS ASN          
SEQRES   6 j  108  GLY ASN ILE VAL LYS ASP PRO GLU MET GLY GLU ILE ILE          
SEQRES   7 j  108  GLN LEU GLN GLY ASP GLN ARG ALA LYS VAL CYS GLU PHE          
SEQRES   8 j  108  MET ILE SER GLN LEU GLY LEU GLN LYS LYS ASN ILE LYS          
SEQRES   9 j  108  ILE HIS GLY PHE                                              
HET     MG  21801       1                                                       
HET     MG  21802       1                                                       
HET     MG  21803       1                                                       
HET     MG  21804       1                                                       
HET     MG  21805       1                                                       
HET     MG  21806       1                                                       
HET     MG  21807       1                                                       
HET     MG  21808       1                                                       
HET     MG  21809       1                                                       
HET     MG  21810       1                                                       
HET     MG  21811       1                                                       
HET     MG  21812       1                                                       
HET     MG  21813       1                                                       
HET     MG  21814       1                                                       
HET     MG  21815       1                                                       
HET     MG  21816       1                                                       
HET     MG  21817       1                                                       
HET     MG  21818       1                                                       
HET     MG  21819       1                                                       
HET     MG  21820       1                                                       
HET     MG  21821       1                                                       
HET     MG  21822       1                                                       
HET     MG  21823       1                                                       
HET     MG  21824       1                                                       
HET     MG  21825       1                                                       
HET     MG  21826       1                                                       
HET     MG  21827       1                                                       
HET     MG  21828       1                                                       
HET     MG  21829       1                                                       
HET     MG  21830       1                                                       
HET     MG  21831       1                                                       
HET     MG  21832       1                                                       
HET     MG  21833       1                                                       
HET     MG  21834       1                                                       
HET     MG  21835       1                                                       
HET     MG  21836       1                                                       
HET     MG  21837       1                                                       
HET     MG  21838       1                                                       
HET     MG  21839       1                                                       
HET     MG  21840       1                                                       
HET     MG  21841       1                                                       
HET     MG  21842       1                                                       
HET     MG  21843       1                                                       
HET     MG  21844       1                                                       
HET     MG  21845       1                                                       
HET     MG  21846       1                                                       
HET     MG  21847       1                                                       
HET     MG  21848       1                                                       
HET     MG  21849       1                                                       
HET     MG  21850       1                                                       
HET     MG  21851       1                                                       
HET     MG  21852       1                                                       
HET     MG  21853       1                                                       
HET     MG  21854       1                                                       
HET     MG  21855       1                                                       
HET     MG  21856       1                                                       
HET     MG  21857       1                                                       
HET     MG  21858       1                                                       
HET     MG  21859       1                                                       
HET     MG  21860       1                                                       
HET     MG  21861       1                                                       
HET     MG  21862       1                                                       
HET     MG  21863       1                                                       
HET     MG  21864       1                                                       
HET     MG  21865       1                                                       
HET     MG  21866       1                                                       
HET     MG  21867       1                                                       
HET     MG  21868       1                                                       
HET     MG  21869       1                                                       
HET     MG  21870       1                                                       
HET     MG  21871       1                                                       
HET     MG  21872       1                                                       
HET     MG  21873       1                                                       
HET     MG  21874       1                                                       
HET     MG  21875       1                                                       
HET     MG  21876       1                                                       
HET     MG  21877       1                                                       
HET     MG  21878       1                                                       
HET     MG  J 201       1                                                       
HET     ZN  a 500       1                                                       
HET     ZN  b 101       1                                                       
HET     MG  f 201       1                                                       
HET     ZN  f 202       1                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      ZN ZINC ION                                                         
FORMUL  38   MG    80(MG 2+)                                                    
FORMUL  17   ZN    3(ZN 2+)                                                     
HELIX    1   1 THR A   10  ARG A   21  1                                  12    
HELIX    2   2 ASN A   49  ILE A   67  1                                  19    
HELIX    3   3 ASN A   69  GLU A   71  5                                   3    
HELIX    4   4 ARG A   79  THR A   93  1                                  15    
HELIX    5   5 ASP A  129  TYR A  138  1                                  10    
HELIX    6   6 LYS A  167  GLY A  186  1                                  20    
HELIX    7   7 ASP B   22  THR B   25  5                                   4    
HELIX    8   8 LEU B   70  GLY B   75  1                                   6    
HELIX    9   9 SER B   76  SER B   80  5                                   5    
HELIX   10  10 THR B  106  VAL B  114  1                                   9    
HELIX   11  11 GLN B  157  VAL B  176  1                                  20    
HELIX   12  12 THR B  180  ILE B  189  1                                  10    
HELIX   13  13 GLU B  191  LYS B  202  1                                  12    
HELIX   14  14 ASP B  224  SER B  230  1                                   7    
HELIX   15  15 THR C   44  GLY C   53  1                                  10    
HELIX   16  16 SER C   57  HIS C   64  1                                   8    
HELIX   17  17 GLU C   70  LEU C   78  1                                   9    
HELIX   18  18 GLU C  125  VAL C  141  1                                  17    
HELIX   19  19 SER C  186  GLY C  197  1                                  12    
HELIX   20  20 THR C  211  THR C  226  1                                  16    
HELIX   21  21 THR C  231  TRP C  235  5                                   5    
HELIX   22  22 SER C  243  TYR C  248  1                                   6    
HELIX   23  23 SER D    6  LEU D   29  1                                  24    
HELIX   24  24 LYS D   54  GLY D   60  1                                   7    
HELIX   25  25 ARG D   64  LYS D   78  1                                  15    
HELIX   26  26 SER D   97  GLY D  112  1                                  16    
HELIX   27  27 ALA D  114  GLY D  130  1                                  17    
HELIX   28  28 GLN D  162  PHE D  167  1                                   6    
HELIX   29  29 PRO E   15  MET E   19  5                                   5    
HELIX   30  30 LYS E   37  SER E   41  5                                   5    
HELIX   31  31 PRO E   43  ARG E   51  1                                   9    
HELIX   32  32 ASN E   57  GLN E   67  1                                  11    
HELIX   33  33 THR E  115  SER E  120  1                                   6    
HELIX   34  34 LYS E  133  GLY E  135  5                                   3    
HELIX   35  35 THR E  247  GLN E  258  1                                  12    
HELIX   36  36 PRO F   32  ALA F   38  1                                   7    
HELIX   37  37 PRO F   90  MET F  100  1                                  11    
HELIX   38  38 LYS F  108  LEU F  126  1                                  19    
HELIX   39  39 ASN F  130  ASN F  141  1                                  12    
HELIX   40  40 SER F  165  PHE F  186  1                                  22    
HELIX   41  41 THR F  191  LYS F  205  1                                  15    
HELIX   42  42 SER F  210  ARG F  227  1                                  18    
HELIX   43  43 ASP G   20  ARG G   25  1                                   6    
HELIX   44  44 VAL G   26  TYR G   28  5                                   3    
HELIX   45  45 ARG G  137  GLY G  146  1                                  10    
HELIX   46  46 VAL G  153  VAL G  157  5                                   5    
HELIX   47  47 THR G  180  LYS G  223  1                                  44    
HELIX   48  48 GLU H   15  LEU H   27  1                                  13    
HELIX   49  49 GLU H   28  LYS H   35  5                                   8    
HELIX   50  50 SER H   66  GLN H   74  1                                   9    
HELIX   51  51 GLN H   74  PHE H   85  1                                  12    
HELIX   52  52 THR H  117  VAL H  130  1                                  14    
HELIX   53  53 ASP H  158  ASP H  163  1                                   6    
HELIX   54  54 LYS H  165  THR H  177  1                                  13    
HELIX   55  55 ASN I   87  ASN I   94  1                                   8    
HELIX   56  56 ALA I  106  TYR I  117  1                                  12    
HELIX   57  57 SER I  137  ARG I  147  1                                  11    
HELIX   58  58 GLU I  154  GLY I  164  1                                  11    
HELIX   59  59 ARG I  173  GLY I  178  1                                   6    
HELIX   60  60 GLU I  186  LYS I  201  1                                  16    
HELIX   61  61 GLU J   20  GLY J   35  1                                  16    
HELIX   62  62 ASN J   38  ARG J   62  1                                  25    
HELIX   63  63 ASP J   66  GLY J   84  1                                  19    
HELIX   64  64 SER J   87  LYS J   91  5                                   5    
HELIX   65  65 ASP J   94  LYS J  100  5                                   7    
HELIX   66  66 VAL J  101  GLU J  106  1                                   6    
HELIX   67  67 ARG J  108  LEU J  116  1                                   9    
HELIX   68  68 SER J  121  GLN J  131  1                                  11    
HELIX   69  69 ARG J  171  GLY J  182  1                                  12    
HELIX   70  70 PRO K    4  GLY K   19  1                                  16    
HELIX   71  71 LYS K   38  LYS K   52  1                                  15    
HELIX   72  72 THR K   69  ASN K   81  1                                  13    
HELIX   73  73 PRO L   45  GLY L   51  1                                   7    
HELIX   74  74 GLU M   18  ASP M   32  1                                  15    
HELIX   75  75 GLY M   37  ARG M   47  1                                  11    
HELIX   76  76 GLU M   62  ASN M   75  1                                  14    
HELIX   77  77 ALA M   85  GLY M   93  1                                   9    
HELIX   78  78 GLU M  125  GLN M  133  1                                   9    
HELIX   79  79 SER N   29  GLY N   44  1                                  16    
HELIX   80  80 THR N   46  HIS N   58  1                                  13    
HELIX   81  81 GLN N   62  THR N   67  1                                   6    
HELIX   82  82 LYS N   70  GLY N   79  1                                  10    
HELIX   83  83 PRO N   85  ASN N  105  1                                  21    
HELIX   84  84 ASP N  108  SER N  133  1                                  26    
HELIX   85  85 SER N  143  ASN N  151  1                                   9    
HELIX   86  86 THR O   43  VAL O   48  1                                   6    
HELIX   87  87 ASP O   51  SER O   55  5                                   5    
HELIX   88  88 SER O   56  GLY O   75  1                                  20    
HELIX   89  89 GLY O   98  ARG O  107  1                                  10    
HELIX   90  90 ASP P   21  LEU P   26  1                                   6    
HELIX   91  91 MET P   28  ALA P   37  1                                  10    
HELIX   92  92 PRO P   38  ARG P   47  1                                  10    
HELIX   93  93 PRO P   53  SER P   66  1                                  14    
HELIX   94  94 LEU P  116  ILE P  121  1                                   6    
HELIX   95  95 LEU Q   44  LEU Q   54  1                                  11    
HELIX   96  96 GLY Q   56  PHE Q   60  5                                   5    
HELIX   97  97 HIS Q   74  VAL Q   97  1                                  24    
HELIX   98  98 ASP Q   98  TYR Q  112  1                                  15    
HELIX   99  99 THR R    6  TYR R   21  1                                  16    
HELIX  100 100 ASP R   27  ALA R   39  1                                  13    
HELIX  101 101 SER R   43  GLN R   62  1                                  20    
HELIX  102 102 PHE R   71  GLN R   83  1                                  13    
HELIX  103 103 ASP R  103  GLY R  114  1                                  12    
HELIX  104 104 ALA S   31  ILE S   35  5                                   5    
HELIX  105 105 ARG S   40  ASP S   51  1                                  12    
HELIX  106 106 THR S   62  ASN S   75  1                                  14    
HELIX  107 107 ASN S  104  ARG S  120  1                                  17    
HELIX  108 108 SER S  121  GLY S  130  1                                  10    
HELIX  109 109 SER T    5  VAL T    9  5                                   5    
HELIX  110 110 PRO T   10  GLY T   26  1                                  17    
HELIX  111 111 TRP T   53  ARG T   68  1                                  16    
HELIX  112 112 GLY T   72  GLY T   81  1                                  10    
HELIX  113 113 SER T   97  GLY T  112  1                                  16    
HELIX  114 114 SER T  125  GLU T  144  1                                  20    
HELIX  115 115 LYS U   30  LYS U   49  1                                  20    
HELIX  116 116 PRO U   96  ILE U  106  1                                  11    
HELIX  117 117 SER V   56  GLY V   63  1                                   8    
HELIX  118 118 GLU V   64  GLN V   74  1                                  11    
HELIX  119 119 SER W    5  THR W   20  1                                  16    
HELIX  120 120 SER W   31  GLY W   45  1                                  15    
HELIX  121 121 LYS W   82  ALA W   84  5                                   3    
HELIX  122 122 ASP W   85  LEU W   94  1                                  10    
HELIX  123 123 HIS W  113  HIS W  120  1                                   8    
HELIX  124 124 ALA X   12  TRP X   24  1                                  13    
HELIX  125 125 GLU X   26  GLY X   35  1                                  10    
HELIX  126 126 GLY X   35  SER X   40  1                                   6    
HELIX  127 127 CYS X   92  VAL X   96  5                                   5    
HELIX  128 128 LEU X  132  LYS X  137  1                                   6    
HELIX  129 129 SER Y   36  LYS Y   49  1                                  14    
HELIX  130 130 GLU Y   51  ASP Y   53  5                                   3    
HELIX  131 131 SER Y   78  GLU Y   86  1                                   9    
HELIX  132 132 PRO Y   87  GLY Y   95  1                                   9    
HELIX  133 133 SER Y  104  LYS Y  117  1                                  14    
HELIX  134 134 GLY Y  122  ASP Y  135  1                                  14    
HELIX  135 135 GLN Z   44  LYS Z   52  1                                   9    
HELIX  136 136 SER Z   61  ARG Z   68  1                                   8    
HELIX  137 137 LEU Z   75  ASN Z   85  1                                  11    
HELIX  138 138 ALA a   49  SER a   57  1                                   9    
HELIX  139 139 CYS a   74  ALA a   81  1                                   8    
HELIX  140 140 THR b   11  LYS b   18  1                                   8    
HELIX  141 141 ARG d   32  LEU d   36  5                                   5    
HELIX  142 142 ARG d   40  LYS d   46  1                                   7    
HELIX  143 143 LYS d   46  GLY d   51  1                                   6    
HELIX  144 144 GLY e   12  THR e   18  1                                   7    
HELIX  145 145 GLY e   32  PHE e   44  1                                  13    
HELIX  146 146 ARG h    2  LYS h   25  1                                  24    
HELIX  147 147 GLY i   63  ARG i   66  5                                   4    
HELIX  148 148 LEU i   97  GLY i  107  1                                  11    
HELIX  149 149 ASP j   50  ALA j   63  1                                  14    
HELIX  150 150 ARG j   85  GLN j   95  1                                  11    
SHEET    1   A 2 VAL A  37  ALA A  40  0                                        
SHEET    2   A 2 ASN A  46  ILE A  48 -1  O  VAL A  47   N  TYR A  38           
SHEET    1   B 4 THR A  96  ALA A  99  0                                        
SHEET    2   B 4 VAL A  73  SER A  77  1  N  VAL A  73   O  THR A  96           
SHEET    3   B 4 LEU A 120  VAL A 123  1  O  ILE A 122   N  ILE A  76           
SHEET    4   B 4 VAL A 143  ALA A 145  1  O  ILE A 144   N  VAL A 121           
SHEET    1   C 6 ASN B  42  ASN B  49  0                                        
SHEET    2   C 6 LYS B  27  LYS B  33 -1  N  GLU B  28   O  VAL B  48           
SHEET    3   C 6 ASN B  95  PHE B 105  1  O  LEU B  96   N  LYS B  33           
SHEET    4   C 6 VAL B 215  LYS B 219 -1  O  VAL B 215   N  MET B 103           
SHEET    5   C 6 VAL B 134  PHE B 142 -1  N  ARG B 136   O  LYS B 216           
SHEET    6   C 6 LEU B 120  LYS B 128 -1  N  ILE B 121   O  ALA B 141           
SHEET    1   D 6 VAL B  65  CYS B  69  0                                        
SHEET    2   D 6 ARG B  82  VAL B  91 -1  O  VAL B  84   N  VAL B  68           
SHEET    3   D 6 ASN B  95  PHE B 105 -1  O  GLY B 102   N  LYS B  85           
SHEET    4   D 6 VAL B 215  LYS B 219 -1  O  VAL B 215   N  MET B 103           
SHEET    5   D 6 VAL B 134  PHE B 142 -1  N  ARG B 136   O  LYS B 216           
SHEET    6   D 6 GLN B 208  HIS B 211 -1  O  HIS B 211   N  ILE B 140           
SHEET    1   E 4 LYS C  82  GLN C  94  0                                        
SHEET    2   E 4 GLN C  99  GLY C 110 -1  O  VAL C 108   N  GLU C  84           
SHEET    3   E 4 HIS C 115  ALA C 123 -1  O  LYS C 121   N  ALA C 105           
SHEET    4   E 4 ILE C 142  PRO C 143 -1  O  ILE C 142   N  VAL C 116           
SHEET    1   F 2 ARG C 146  GLY C 147  0                                        
SHEET    2   F 2 SER C 158  LEU C 159 -1  O  SER C 158   N  GLY C 147           
SHEET    1   G 4 THR C 163  CYS C 167  0                                        
SHEET    2   G 4 VAL C 170  PRO C 176 -1  O  LEU C 174   N  THR C 163           
SHEET    3   G 4 VAL C 201  THR C 206 -1  O  TYR C 202   N  ILE C 175           
SHEET    4   G 4 ILE C 183  VAL C 184  1  N  VAL C 184   O  VAL C 201           
SHEET    1   H 3 TYR D  34  VAL D  41  0                                        
SHEET    2   H 3 THR D  46  ALA D  52 -1  O  ARG D  51   N  SER D  35           
SHEET    3   H 3 ILE D  84  GLU D  89  1  O  TYR D  87   N  ILE D  50           
SHEET    1   I 4 MET D 150  GLY D 155  0                                        
SHEET    2   I 4 GLY D 133  SER D 139 -1  N  VAL D 136   O  PHE D 152           
SHEET    3   I 4 GLY D 180  MET D 189 -1  O  LYS D 185   N  VAL D 137           
SHEET    4   I 4 ILE D 168  LEU D 177 -1  N  VAL D 175   O  LEU D 182           
SHEET    1   J 5 LYS D 223  ASP D 224  0                                        
SHEET    2   J 5 ILE g 195  ILE g 200 -1  O  ASP g 198   N  LYS D 223           
SHEET    3   J 5 ILE g 182  LEU g 188 -1  N  SER g 185   O  ALA g 197           
SHEET    4   J 5 ILE g 172  GLY g 178 -1  N  PHE g 174   O  TRP g 186           
SHEET    5   J 5 VAL g 152  VAL g 157 -1  N  LYS g 154   O  ALA g 177           
SHEET    1   K 4 VAL E  70  VAL E  72  0                                        
SHEET    2   K 4 VAL E  89  LEU E  92 -1  O  THR E  91   N  LYS E  71           
SHEET    3   K 4 ASN E  98  ARG E 100 -1  O  PHE E  99   N  ILE E  90           
SHEET    4   K 4 ARG E 113  ILE E 114 -1  O  ILE E 114   N  ASN E  98           
SHEET    1   L 2 VAL E 102  TYR E 103  0                                        
SHEET    2   L 2 PHE E 109  ALA E 110 -1  O  ALA E 110   N  VAL E 102           
SHEET    1   M 5 THR E 146  ARG E 148  0                                        
SHEET    2   M 5 PRO E 137  THR E 141 -1  N  VAL E 139   O  ILE E 147           
SHEET    3   M 5 LYS E 122  LEU E 131 -1  N  GLN E 130   O  TYR E 138           
SHEET    4   M 5 THR E 159  VAL E 162 -1  O  VAL E 162   N  LYS E 122           
SHEET    5   M 5 ILE E 169  ILE E 173 -1  O  THR E 170   N  LYS E 161           
SHEET    1   N 4 VAL E 192  GLY E 193  0                                        
SHEET    2   N 4 LEU E 180  VAL E 183 -1  N  VAL E 181   O  GLY E 193           
SHEET    3   N 4 VAL E 225  GLU E 230 -1  O  PHE E 226   N  TYR E 182           
SHEET    4   N 4 ARG E 233  PRO E 234 -1  O  ARG E 233   N  GLU E 230           
SHEET    1   O 3 HIS E 197  ARG E 198  0                                        
SHEET    2   O 3 LEU E 207  ILE E 210 -1  O  HIS E 209   N  HIS E 197           
SHEET    3   O 3 PHE E 218  ARG E 221 -1  O  PHE E 218   N  ILE E 210           
SHEET    1   P 6 GLU F 146  THR F 149  0                                        
SHEET    2   P 6 GLN F 160  VAL F 164 -1  O  VAL F 162   N  ASP F 147           
SHEET    3   P 6 VAL c  41  LYS c  45  1  O  LYS c  45   N  ASP F 163           
SHEET    4   P 6 VAL c  25  PHE c  32 -1  N  THR c  26   O  VAL c  44           
SHEET    5   P 6 THR c   8  THR c  19 -1  N  LYS c  14   O  ARG c  29           
SHEET    6   P 6 ILE c  53  LEU c  56 -1  O  LEU c  54   N  ALA c  10           
SHEET    1   Q 5 THR G  12  GLU G  17  0                                        
SHEET    2   Q 5 LYS G   2  TYR G   7 -1  N  ILE G   5   O  LYS G  14           
SHEET    3   Q 5 LEU G 106  LYS G 115  1  O  ALA G 107   N  LYS G   2           
SHEET    4   Q 5 VAL G  49  ASP G  57 -1  N  ALA G  53   O  ALA G 110           
SHEET    5   Q 5 GLN G  34  ASP G  37 -1  N  VAL G  36   O  PHE G  50           
SHEET    1   R 2 VAL G  73  LEU G  77  0                                        
SHEET    2   R 2 LYS G  93  VAL G  97 -1  O  LYS G  93   N  LEU G  77           
SHEET    1   S 2 ARG G 160  THR G 163  0                                        
SHEET    2   S 2 SER G 168  LYS G 171 -1  O  TYR G 169   N  VAL G 162           
SHEET    1   T 3 ILE H  46  GLU H  50  0                                        
SHEET    2   T 3 LYS H  56  VAL H  60 -1  O  ALA H  59   N  ARG H  47           
SHEET    3   T 3 VAL H  90  ILE H  91  1  O  ILE H  91   N  VAL H  60           
SHEET    1   U 6 GLN H 180  GLU H 184  0                                        
SHEET    2   U 6 LYS H 148  LEU H 154  1  N  ILE H 152   O  VAL H 182           
SHEET    3   U 6 ILE H 135  TYR H 142 -1  N  ARG H 139   O  LYS H 151           
SHEET    4   U 6 PHE W  50  ILE W  53 -1  O  PHE W  50   N  TYR H 142           
SHEET    5   U 6 LYS W  60  GLN W  64 -1  O  VAL W  62   N  GLU W  51           
SHEET    6   U 6 GLN W  24  ILE W  27 -1  N  ILE W  27   O  ILE W  61           
SHEET    1   V 2 HIS I  44  THR I  48  0                                        
SHEET    2   V 2 GLY I  51  ARG I  56 -1  O  LYS I  54   N  VAL I  46           
SHEET    1   W 6 THR I  62  TRP I  67  0                                        
SHEET    2   W 6 VAL I  72  TYR I  83 -1  O  VAL I  72   N  TRP I  67           
SHEET    3   W 6 ILE I 101  ILE I 104 -1  O  GLN I 103   N  THR I  79           
SHEET    4   W 6 LEU I 166  ILE I 170 -1  O  ALA I 168   N  VAL I 102           
SHEET    5   W 6 ASP I 181  ILE I 184 -1  O  TYR I 183   N  ALA I 169           
SHEET    6   W 6 THR I  62  TRP I  67  1  N  SER I  66   O  ILE I 184           
SHEET    1   X 3 VAL K  20  LYS K  24  0                                        
SHEET    2   X 3 TYR K  63  LEU K  68 -1  O  TYR K  66   N  LEU K  21           
SHEET    3   X 3 VAL K  55  GLN K  58 -1  N  LYS K  56   O  THR K  67           
SHEET    1   Y 6 ILE L  70  SER L  77  0                                        
SHEET    2   Y 6 THR L  83  ARG L  87 -1  O  VAL L  85   N  VAL L  76           
SHEET    3   Y 6 ASN L 106  HIS L 110 -1  O  VAL L 107   N  ILE L  86           
SHEET    4   Y 6 PHE L 137  VAL L 142  1  O  VAL L 139   N  HIS L 110           
SHEET    5   Y 6 ILE L 122  GLN L 127 -1  N  GLY L 126   O  ASN L 138           
SHEET    6   Y 6 ILE L  70  SER L  77 -1  N  GLY L  73   O  VAL L 123           
SHEET    1   Z 2 TYR L  90  VAL L  94  0                                        
SHEET    2   Z 2 ARG L  99  ARG L 103 -1  O  ARG L 103   N  TYR L  90           
SHEET    1  AA 2 LEU M  34  ARG M  36  0                                        
SHEET    2  AA 2 VAL M 112  VAL M 114 -1  O  VAL M 113   N  ALA M  35           
SHEET    1  AB 2 ALA M  53  VAL M  54  0                                        
SHEET    2  AB 2 LEU M  79  ILE M  80  1  O  ILE M  80   N  ALA M  53           
SHEET    1  AC 5 THR O  26  PHE O  27  0                                        
SHEET    2  AC 5 ILE O  19  ALA O  21 -1  N  PHE O  20   O  PHE O  27           
SHEET    3  AC 5 ALA O  78  ARG O  84  1  O  ARG O  84   N  ALA O  21           
SHEET    4  AC 5 PHE O  14  VAL O  16  1  N  GLY O  15   O  HIS O  80           
SHEET    5  AC 5 THR O  31  ASP O  32 -1  O  THR O  31   N  VAL O  16           
SHEET    1  AD 4 THR O  26  PHE O  27  0                                        
SHEET    2  AD 4 ILE O  19  ALA O  21 -1  N  PHE O  20   O  PHE O  27           
SHEET    3  AD 4 ALA O  78  ARG O  84  1  O  ARG O  84   N  ALA O  21           
SHEET    4  AD 4 ARG O 111  ASP O 117  1  O  GLU O 116   N  ILE O  83           
SHEET    1  AE 3 VAL P  76  THR P  78  0                                        
SHEET    2  AE 3 VAL P  94  VAL P  96  1  O  GLY P  95   N  THR P  78           
SHEET    3  AE 3 ASN P 103  VAL P 105 -1  O  ASN P 103   N  VAL P  96           
SHEET    1  AF 5 SER Q   6  LYS Q  13  0                                        
SHEET    2  AF 5 ALA Q  16  ALA Q  24 -1  O  VAL Q  22   N  VAL Q   7           
SHEET    3  AF 5 ILE Q  63  THR Q  70 -1  O  THR Q  70   N  THR Q  17           
SHEET    4  AF 5 ILE Q  29  VAL Q  31  1  N  LYS Q  30   O  VAL Q  67           
SHEET    5  AF 5 SER Q  34  PRO Q  35 -1  O  SER Q  34   N  VAL Q  31           
SHEET    1  AG 2 LEU R 100  VAL R 102  0                                        
SHEET    2  AG 2 LEU R 119  VAL R 121  1  O  SER R 120   N  VAL R 102           
SHEET    1  AH 2 LEU S  15  ARG S  16  0                                        
SHEET    2  AH 2 ASN S  21  VAL S  22 -1  O  VAL S  22   N  LEU S  15           
SHEET    1  AI 2 ALA T  83  LYS T  84  0                                        
SHEET    2  AI 2 LYS T  92  HIS T  93 -1  O  LYS T  92   N  LYS T  84           
SHEET    1  AJ 2 VAL T 114  ILE T 116  0                                        
SHEET    2  AJ 2 ARG T 122  ILE T 124 -1  O  ARG T 123   N  GLU T 115           
SHEET    1  AK 4 ASP U 113  VAL U 116  0                                        
SHEET    2  AK 4 ILE U  22  SER U  28 -1  N  THR U  27   O  ASP U 113           
SHEET    3  AK 4 TRP U  79  GLU U  94 -1  O  HIS U  87   N  SER U  28           
SHEET    4  AK 4 VAL U  51  ARG U  57 -1  N  VAL U  56   O  TYR U  90           
SHEET    1  AL 3 VAL U  51  ARG U  57  0                                        
SHEET    2  AL 3 TRP U  79  GLU U  94 -1  O  TYR U  90   N  VAL U  56           
SHEET    3  AL 3 LYS U  61  LEU U  63 -1  N  LEU U  63   O  MET U  84           
SHEET    1  AM 3 LYS U  61  LEU U  63  0                                        
SHEET    2  AM 3 TRP U  79  GLU U  94 -1  O  MET U  84   N  LEU U  63           
SHEET    3  AM 3 SER U  66  ARG U  68 -1  N  THR U  67   O  ASP U  80           
SHEET    1  AN 3 SER U  66  ARG U  68  0                                        
SHEET    2  AN 3 TRP U  79  GLU U  94 -1  O  ASP U  80   N  THR U  67           
SHEET    3  AN 3 TYR d  53  LYS d  54 -1  O  TYR d  53   N  GLU U  83           
SHEET    1  AO 4 TYR d  53  LYS d  54  0                                        
SHEET    2  AO 4 TRP U  79  GLU U  94 -1  N  GLU U  83   O  TYR d  53           
SHEET    3  AO 4 ILE U  22  SER U  28 -1  N  SER U  28   O  HIS U  87           
SHEET    4  AO 4 ASP U 113  VAL U 116 -1  O  ASP U 113   N  THR U  27           
SHEET    1  AP 2 VAL V  32  ALA V  37  0                                        
SHEET    2  AP 2 TYR V  50  LEU V  55 -1  O  VAL V  51   N  ILE V  36           
SHEET    1  AQ 3 GLY W 109  ASP W 112  0                                        
SHEET    2  AQ 3 TYR W 101  THR W 106 -1  N  LEU W 104   O  MET W 111           
SHEET    3  AQ 3 LYS W 124  VAL W 129 -1  O  VAL W 129   N  TYR W 101           
SHEET    1  AR 7 PHE X 122  LYS X 123  0                                        
SHEET    2  AR 7 LYS X  82  PHE X  86  1  N  PHE X  86   O  PHE X 122           
SHEET    3  AR 7 CYS X  71  LEU X  76 -1  N  VAL X  74   O  VAL X  83           
SHEET    4  AR 7 HIS X  48  ILE X  57 -1  N  ILE X  52   O  GLN X  75           
SHEET    5  AR 7 GLU X 101  ALA X 105 -1  O  LEU X 104   N  ALA X  49           
SHEET    6  AR 7 LYS X 126  VAL X 127 -1  O  LYS X 126   N  LEU X 103           
SHEET    7  AR 7 VAL X 130  SER X 131 -1  O  VAL X 130   N  VAL X 127           
SHEET    1  AS 4 ILE Y   7  ASN Y  15  0                                        
SHEET    2  AS 4 ARG Y  20  LEU Y  28 -1  O  GLN Y  22   N  ILE Y  13           
SHEET    3  AS 4 LYS Y  68  TYR Y  76 -1  O  GLY Y  73   N  PHE Y  23           
SHEET    4  AS 4 VAL Y  55  THR Y  62 -1  N  PHE Y  58   O  PHE Y  72           
SHEET    1  AT 2 ILE Z  89  HIS Z  95  0                                        
SHEET    2  AT 2 GLN Z  98  ARG Z 103 -1  O  THR Z 102   N  LYS Z  90           
SHEET    1  AU 2 PRO a  20  VAL a  21  0                                        
SHEET    2  AU 2 VAL a  30  PRO a  31 -1  O  VAL a  30   N  VAL a  21           
SHEET    1  AV 2 LYS a  37  ASN a  43  0                                        
SHEET    2  AV 2 LYS a  66  HIS a  72 -1  O  LEU a  71   N  ARG a  38           
SHEET    1  AW 3 ILE b  43  PHE b  47  0                                        
SHEET    2  AW 3 PHE b  32  LYS b  36 -1  N  VAL b  35   O  THR b  44           
SHEET    3  AW 3 SER b  78  ARG b  81 -1  O  ARG b  80   N  ASP b  34           
SHEET    1  AX 2 CYS b  64  THR b  65  0                                        
SHEET    2  AX 2 LYS b  72  LEU b  73 -1  O  LYS b  72   N  THR b  65           
SHEET    1  AY 2 LEU d  30  ILE d  31  0                                        
SHEET    2  AY 2 ILE d  38  ASP d  39 -1  O  ILE d  38   N  ILE d  31           
SHEET    1  AZ 2 TYR f 106  LYS f 107  0                                        
SHEET    2  AZ 2 ALA f 115  LYS f 116 -1  O  ALA f 115   N  LYS f 107           
SHEET    1  BA 4 VAL g   9  LEU g  14  0                                        
SHEET    2  BA 4 ILE g 317  GLN g 321 -1  O  VAL g 319   N  ARG g  11           
SHEET    3  BA 4 THR g 307  TYR g 312 -1  N  LEU g 308   O  TRP g 320           
SHEET    4  BA 4 ALA g 296  TRP g 301 -1  N  SER g 298   O  GLY g 311           
SHEET    1  BB 4 SER g  23  SER g  25  0                                        
SHEET    2  BB 4 LEU g  33  GLY g  37 -1  O  GLY g  37   N  SER g  23           
SHEET    3  BB 4 LEU g  43  LEU g  48 -1  O  ILE g  44   N  SER g  36           
SHEET    4  BB 4 GLY g  56  SER g  61 -1  O  VAL g  59   N  SER g  45           
SHEET    1  BC 4 VAL g  69  VAL g  74  0                                        
SHEET    2  BC 4 TYR g  80  SER g  85 -1  O  VAL g  82   N  VAL g  73           
SHEET    3  BC 4 LEU g  90  ASN g  94 -1  O  TRP g  93   N  ALA g  81           
SHEET    4  BC 4 ASN g  99  PHE g 104 -1  O  PHE g 104   N  LEU g  90           
SHEET    1  BD 4 VAL g 111  ILE g 116  0                                        
SHEET    2  BD 4 LYS g 122  SER g 127 -1  O  ALA g 126   N  SER g 113           
SHEET    3  BD 4 ILE g 132  ASN g 136 -1  O  ARG g 133   N  SER g 125           
SHEET    4  BD 4 CYS g 141  LEU g 145 -1  O  ALA g 142   N  VAL g 134           
SHEET    1  BE 4 ILE g 206  PRO g 211  0                                        
SHEET    2  BE 4 LEU g 217  GLY g 222 -1  O  ALA g 221   N  VAL g 208           
SHEET    3  BE 4 GLN g 226  ASN g 231 -1  O  TRP g 230   N  ALA g 218           
SHEET    4  BE 4 ASN g 240  ASP g 242 -1  O  PHE g 241   N  ILE g 227           
SHEET    1  BF 4 ALA g 249  PHE g 252  0                                        
SHEET    2  BF 4 TRP g 258  ALA g 262 -1  O  ALA g 262   N  ALA g 249           
SHEET    3  BF 4 ILE g 267  ASP g 271 -1  O  LYS g 268   N  ALA g 261           
SHEET    4  BF 4 LEU g 277  LEU g 281 -1  O  ASP g 279   N  ILE g 269           
SHEET    1  BG 6 GLN i  33  GLY i  43  0                                        
SHEET    2  BG 6 ARG i  46  CYS i  51 -1  O  GLU i  48   N  THR i  39           
SHEET    3  BG 6 LYS i  56  ILE i  61 -1  O  ARG i  57   N  ALA i  49           
SHEET    4  BG 6 GLN i  88  LYS i  94  1  O  CYS i  89   N  HIS i  60           
SHEET    5  BG 6 ILE i  76  LEU i  81 -1  N  LEU i  78   O  VAL i  92           
SHEET    6  BG 6 GLN i  33  GLY i  43 -1  N  ALA i  36   O  ILE i  77           
SHEET    1  BH 5 ASN j  67  VAL j  69  0                                        
SHEET    2  BH 5 ILE j  77  GLN j  81 -1  O  ILE j  77   N  VAL j  69           
SHEET    3  BH 5 THR j  38  GLN j  43 -1  N  THR j  40   O  LEU j  80           
SHEET    4  BH 5 ILE j  26  GLN j  32 -1  N  GLN j  31   O  LEU j  39           
SHEET    5  BH 5 ILE j 103  ILE j 105  1  O  LYS j 104   N  ILE j  26           
LINK         OP2   G 21427                MG    MG 21865     1555   1555  1.89  
LINK         OP1   A 2 618                MG    MG 21825     1555   1555  1.89  
LINK         OP2   G 21327                MG    MG 21826     1555   1555  1.93  
LINK         OP2   A 2 914                MG    MG 21874     1555   1555  1.94  
LINK         OP1   C 21273                MG    MG 21865     1555   1555  1.96  
LINK         OP2   A 2 554                MG    MG 21803     1555   1555  1.96  
LINK         OP2   A 2  47                MG    MG 21821     1555   1555  1.98  
LINK         OP2   C 2 423                MG    MG 21870     1555   1555  1.99  
LINK         OP1   G 2 361                MG    MG 21801     1555   1555  1.99  
LINK         OP1   A 2 604                MG    MG 21818     1555   1555  2.02  
LINK         OP1   U 21769                MG    MG 21812     1555   1555  2.02  
LINK         OP2   U 2 101                MG    MG 21828     1555   1555  2.04  
LINK         OP2   A 21024                MG    MG 21805     1555   1555  2.06  
LINK         OP2   A 2 400                MG    MG 21814     1555   1555  2.06  
LINK         OP2   A 2 620                MG    MG 21823     1555   1555  2.09  
LINK         OP1   G 21426                MG    MG 21865     1555   1555  2.11  
LINK         OP1   C 2 267                MG    MG 21835     1555   1555  2.11  
LINK         OP1   A 21761                MG    MG 21812     1555   1555  2.11  
LINK         OP1   G 2 402                MG    MG 21802     1555   1555  2.14  
LINK         OP1   U 21628                MG    MG 21834     1555   1555  2.14  
LINK         OP2   U 21768                MG    MG 21831     1555   1555  2.15  
LINK         OP2   C 2 360                MG    MG 21828     1555   1555  2.16  
LINK         OP2   A 2 978                MG    MG 21842     1555   1555  2.17  
LINK         OP2   A 2 928                MG    MG 21811     1555   1555  2.17  
LINK         OP2   U 21520                MG    MG 21864     1555   1555  2.17  
LINK         OP2   A 2 618                MG    MG 21823     1555   1555  2.20  
LINK         O6    G 2 894                MG    MG 21874     1555   1555  2.23  
LINK         OP1   C 2 249                MG    MG 21869     1555   1555  2.24  
LINK         OP2   U 2 967                MG    MG 21876     1555   1555  2.25  
LINK         OP2   A 2 250                MG    MG 21869     1555   1555  2.25  
LINK         OP1   G 21791                MG    MG 21834     1555   1555  2.26  
LINK         OP2   A 2 100                MG    MG 21828     1555   1555  2.26  
LINK         OP2   A 2 514                MG    MG 21846     1555   1555  2.27  
LINK         OP2   G 21329                MG    MG 21809     1555   1555  2.27  
LINK         OP1   A 2  28                MG    MG 21817     1555   1555  2.28  
LINK         OP2   A 2 459                MG    MG 21836     1555   1555  2.28  
LINK         OP2   A 2 635                MG    MG 21872     1555   1555  2.28  
LINK         OP1   G 2  16                MG    MG 21815     1555   1555  2.29  
LINK         OP1   A 2 634                MG    MG 21872     1555   1555  2.30  
LINK         OP2   G 2  95                MG    MG 21832     1555   1555  2.31  
LINK         OP2   A 21761                MG    MG 21822     1555   1555  2.32  
LINK         OP2   G 2 460                MG    MG 21836     1555   1555  2.32  
LINK         OP2   A 2 377                MG    MG 21816     1555   1555  2.33  
LINK         O6    G 21329                MG    MG 21826     1555   1555  2.33  
LINK         SG  CYS a  26                ZN    ZN a 500     1555   1555  2.33  
LINK         SG  CYS a  77                ZN    ZN a 500     1555   1555  2.34  
LINK         OP1   A 2 100                MG    MG 21804     1555   1555  2.34  
LINK         O4    U 2 916                MG    MG 21874     1555   1555  2.35  
LINK         OP2   C 2  49                MG    MG 21807     1555   1555  2.37  
LINK         OP2   U 2 378                MG    MG 21816     1555   1555  2.39  
LINK         OP2   A 2 970                MG    MG 21877     1555   1555  2.39  
LINK         OP1   U 2 988                MG    MG 21849     1555   1555  2.42  
LINK         OP2   A 2 555                MG    MG 21803     1555   1555  2.44  
LINK         OP2   U 21302                MG    MG 21841     1555   1555  2.44  
LINK         OP2   A 2 603                MG    MG 21871     1555   1555  2.46  
LINK         OP2   A 21760                MG    MG 21822     1555   1555  2.46  
LINK         SG  CYS a  23                ZN    ZN a 500     1555   1555  2.49  
LINK         OP1   U 21282                MG    MG 21855     1555   1555  2.49  
LINK         OP2   A 2 760                MG    MG 21844     1555   1555  2.51  
LINK         OP2   G 21766                MG    MG 21822     1555   1555  2.52  
LINK         OP1   A 21201                MG    MG 21866     1555   1555  2.52  
LINK         OP2   G 21109                MG    MG 21830     1555   1555  2.56  
LINK         O2    U 21518                MG    MG 21864     1555   1555  2.58  
LINK         OP1   U 2 118                MG    MG 21868     1555   1555  2.59  
LINK         OP2   G 21426                MG    MG 21862     1555   1555  2.62  
LINK         OE1 GLN G 176                MG    MG 21835     1555   1555  2.62  
LINK         O3'   G 21765                MG    MG 21812     1555   1555  2.63  
LINK         OP1   C 21455                MG    MG 21857     1555   1555  2.67  
LINK         SG  CYS a  74                ZN    ZN a 500     1555   1555  2.67  
LINK         OP2   C 21273                MG    MG 21862     1555   1555  2.71  
LINK         OP2   A 2 619                MG    MG 21823     1555   1555  2.80  
LINK         OP2   G 2 466                MG    MG 21837     1555   1555  2.86  
LINK         O2    C 21597                MG    MG 21866     1555   1555  2.87  
LINK         OP1   G 21108                MG    MG 21830     1555   1555  2.90  
LINK         OP1   A 2 622                MG    MG 21827     1555   1555  2.96  
LINK         OP2   A 21202                MG    MG 21866     1555   1555  2.96  
LINK         OP2   U 21003                MG    MG 21819     1555   1555  2.96  
LINK         OP1   A 21467                MG    MG 21856     1555   1555  2.98  
LINK         OP1   G 2 606                MG    MG 21818     1555   1555  3.00  
SITE     1 AC1  1   G 2 361                                                     
SITE     1 AC2  2   G 2  95    G 2 402                                          
SITE     1 AC3  3   G 2 551    A 2 554    A 2 555                               
SITE     1 AC4  1   A 2 100                                                     
SITE     1 AC5  1   A 21024                                                     
SITE     1 AC6  2   C 2  49    A 2 424                                          
SITE     1 AC7  1   G 21329                                                     
SITE     1 AC8  1   A 2 928                                                     
SITE     1 AC9  5   A 21761    G 21765    G 21766    U 21768                    
SITE     2 AC9  5   U 21769                                                     
SITE     1 BC1  2   A 2 386    A 2 400                                          
SITE     1 BC2  1   G 2  16                                                     
SITE     1 BC3  2   A 2 377    U 2 378                                          
SITE     1 BC4  1   A 2  28                                                     
SITE     1 BC5  3   G 2 370    A 2 604    G 2 606                               
SITE     1 BC6  1   U 21003                                                     
SITE     1 BC7  1   C 2 426                                                     
SITE     1 BC8  2   U 2  44    A 2  47                                          
SITE     1 BC9  5   U 21759    A 21760    A 21761    G 21765                    
SITE     2 BC9  5   G 21766                                                     
SITE     1 CC1  4   U 2 617    A 2 618    A 2 619    A 2 620                    
SITE     1 CC2  2   U 2 562    A 2 579                                          
SITE     1 CC3  1   A 2 618                                                     
SITE     1 CC4  2   G 21327    G 21329                                          
SITE     1 CC5  1   A 2 622                                                     
SITE     1 CC6  4   A 2 100    U 2 101    U 2 102    C 2 360                    
SITE     1 CC7  2   G 21108    G 21109                                          
SITE     1 CC8  1   U 21768                                                     
SITE     1 CC9  1   G 2  95                                                     
SITE     1 DC1  4   G 21670    G 21671    G 21725    U 21726                    
SITE     1 DC2  2   U 21628    G 21791                                          
SITE     1 DC3  4   U 2 169    U 2 266    C 2 267  GLN G 176                    
SITE     1 DC4  2   A 2 459    G 2 460                                          
SITE     1 DC5  1   G 2 466                                                     
SITE     1 DC6  1   U 21302                                                     
SITE     1 DC7  1   A 2 978                                                     
SITE     1 DC8  1   A 2 760                                                     
SITE     1 DC9  2   U 2   8    G 21139                                          
SITE     1 EC1  2   A 2 514    C 2 530                                          
SITE     1 EC2  2   U 2 988    C 2 989                                          
SITE     1 EC3  1   A 2 212                                                     
SITE     1 EC4  1   U 2 934                                                     
SITE     1 EC5  1   G 21392                                                     
SITE     1 EC6  2   C 21158    U 21282                                          
SITE     1 EC7  2   A 21467  ASN T  85                                          
SITE     1 EC8  2   A 21201    C 21455                                          
SITE     1 EC9  3   G 21200    A 21598    C 21600                               
SITE     1 FC1  1   C 21429                                                     
SITE     1 FC2  3   A 21195    C 21196  LYS U  77                               
SITE     1 FC3  2   G 21267    U 21268                                          
SITE     1 FC4  3   G 21272    C 21273    G 21426                               
SITE     1 FC5  2   G 21539    C 21566                                          
SITE     1 FC6  2   U 21518    U 21520                                          
SITE     1 FC7  3   C 21273    G 21426    G 21427                               
SITE     1 FC8  3   A 21201    A 21202    C 21597                               
SITE     1 FC9  2   U 2 118  ASN I  52                                          
SITE     1 GC1  2   C 2 249    A 2 250                                          
SITE     1 GC2  1   C 2 423                                                     
SITE     1 GC3  1   A 2 603                                                     
SITE     1 GC4  2   A 2 634    A 2 635                                          
SITE     1 GC5  3   G 2 894    A 2 914    U 2 916                               
SITE     1 GC6  2   G 2 941  GLY a  16                                          
SITE     1 GC7  1   U 2 967                                                     
SITE     1 GC8  1   A 2 970                                                     
SITE     1 GC9  4 CYS a  23  CYS a  26  CYS a  74  CYS a  77                    
SITE     1 HC1  4 CYS b  37  GLY b  39  CYS b  40  CYS b  59                    
SITE     1 HC2  2 TYR f  85  THR f  87                                          
SITE     1 HC3  5 CYS f 121  ILE f 128  CYS f 139  LYS f 141                    
SITE     2 HC3  5 CYS f 142                                                     
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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