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Database: PDB
Entry: 5IT9
LinkDB: 5IT9
Original site: 5IT9 
HEADER    RIBOSOME                                16-MAR-16   5IT9              
TITLE     STRUCTURE OF THE YEAST KLUYVEROMYCES LACTIS SMALL RIBOSOMAL SUBUNIT IN
TITLE    2 COMPLEX WITH THE CRICKET PARALYSIS VIRUS IRES.                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBOSOMAL PROTEIN US2;                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: 40S RIBOSOMAL PROTEIN S0;                                   
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: RIBOSOMAL PROTEIN ES1;                                     
COMPND   7 CHAIN: B;                                                            
COMPND   8 SYNONYM: 40S RIBOSOMAL PROTEIN S1;                                   
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: RIBOSOMAL PROTEIN US5;                                     
COMPND  11 CHAIN: C;                                                            
COMPND  12 SYNONYM: KLLA0F09812P;                                               
COMPND  13 MOL_ID: 4;                                                           
COMPND  14 MOLECULE: RIBOSOMAL PROTEIN US3;                                     
COMPND  15 CHAIN: D;                                                            
COMPND  16 SYNONYM: KLLA0D08305P;                                               
COMPND  17 MOL_ID: 5;                                                           
COMPND  18 MOLECULE: RIBOSOMAL PROTEIN ES4;                                     
COMPND  19 CHAIN: E;                                                            
COMPND  20 SYNONYM: 40S RIBOSOMAL PROTEIN S4;                                   
COMPND  21 MOL_ID: 6;                                                           
COMPND  22 MOLECULE: RIBOSOMAL PROTEIN US7;                                     
COMPND  23 CHAIN: F;                                                            
COMPND  24 SYNONYM: KLLA0D10659P;                                               
COMPND  25 MOL_ID: 7;                                                           
COMPND  26 MOLECULE: RIBOSOMAL PROTEIN ES6;                                     
COMPND  27 CHAIN: G;                                                            
COMPND  28 SYNONYM: 40S RIBOSOMAL PROTEIN S6;                                   
COMPND  29 MOL_ID: 8;                                                           
COMPND  30 MOLECULE: RIBOSOMAL PROTEIN ES7;                                     
COMPND  31 CHAIN: H;                                                            
COMPND  32 SYNONYM: KLLA0C13519P;                                               
COMPND  33 MOL_ID: 9;                                                           
COMPND  34 MOLECULE: RIBOSOMAL PROTEIN ES8;                                     
COMPND  35 CHAIN: I;                                                            
COMPND  36 SYNONYM: 40S RIBOSOMAL PROTEIN S8;                                   
COMPND  37 MOL_ID: 10;                                                          
COMPND  38 MOLECULE: RIBOSOMAL PROTEIN US4;                                     
COMPND  39 CHAIN: J;                                                            
COMPND  40 SYNONYM: KLLA0E23673P;                                               
COMPND  41 MOL_ID: 11;                                                          
COMPND  42 MOLECULE: RIBOSOMAL PROTEIN ES10;                                    
COMPND  43 CHAIN: K;                                                            
COMPND  44 SYNONYM: KLLA0B08173P;                                               
COMPND  45 MOL_ID: 12;                                                          
COMPND  46 MOLECULE: RIBOSOMAL PROTEIN US17;                                    
COMPND  47 CHAIN: L;                                                            
COMPND  48 SYNONYM: KLLA0A10483P;                                               
COMPND  49 MOL_ID: 13;                                                          
COMPND  50 MOLECULE: RIBOSOMAL PROTEIN ES12;                                    
COMPND  51 CHAIN: M;                                                            
COMPND  52 SYNONYM: 40S RIBOSOMAL PROTEIN S12;                                  
COMPND  53 MOL_ID: 14;                                                          
COMPND  54 MOLECULE: RIBOSOMAL PROTEIN US15;                                    
COMPND  55 CHAIN: N;                                                            
COMPND  56 SYNONYM: KLLA0F18040P;                                               
COMPND  57 MOL_ID: 15;                                                          
COMPND  58 MOLECULE: RIBOSOMAL PROTEIN US14;                                    
COMPND  59 CHAIN: O;                                                            
COMPND  60 SYNONYM: 40S RIBOSOMAL PROTEIN S14, RP59;                            
COMPND  61 MOL_ID: 16;                                                          
COMPND  62 MOLECULE: RIBOSOMAL PROTEIN US19;                                    
COMPND  63 CHAIN: P;                                                            
COMPND  64 SYNONYM: KLLA0F07843P;                                               
COMPND  65 MOL_ID: 17;                                                          
COMPND  66 MOLECULE: RIBOSOMAL PROTEIN US9;                                     
COMPND  67 CHAIN: Q;                                                            
COMPND  68 SYNONYM: 40S RIBOSOMAL PROTEIN S16;                                  
COMPND  69 MOL_ID: 18;                                                          
COMPND  70 MOLECULE: RIBOSOMAL PROTEIN ES17;                                    
COMPND  71 CHAIN: R;                                                            
COMPND  72 SYNONYM: KLLA0B01474P;                                               
COMPND  73 MOL_ID: 19;                                                          
COMPND  74 MOLECULE: RIBOSOMAL PROTEIN US13;                                    
COMPND  75 CHAIN: S;                                                            
COMPND  76 SYNONYM: KLLA0B01562P;                                               
COMPND  77 MOL_ID: 20;                                                          
COMPND  78 MOLECULE: RIBOSOMAL PROTEIN ES19;                                    
COMPND  79 CHAIN: T;                                                            
COMPND  80 SYNONYM: KLLA0A07194P;                                               
COMPND  81 MOL_ID: 21;                                                          
COMPND  82 MOLECULE: RIBOSOMAL PROTEIN US10;                                    
COMPND  83 CHAIN: U;                                                            
COMPND  84 SYNONYM: KLLA0F25542P;                                               
COMPND  85 MOL_ID: 22;                                                          
COMPND  86 MOLECULE: RIBOSOMAL PROTEIN ES21;                                    
COMPND  87 CHAIN: V;                                                            
COMPND  88 SYNONYM: 40S RIBOSOMAL PROTEIN S21;                                  
COMPND  89 MOL_ID: 23;                                                          
COMPND  90 MOLECULE: RIBOSOMAL PROTEIN US8;                                     
COMPND  91 CHAIN: W;                                                            
COMPND  92 SYNONYM: 40S RIBOSOMAL PROTEIN S22;                                  
COMPND  93 MOL_ID: 24;                                                          
COMPND  94 MOLECULE: RIBOSOMAL PROTEIN US21;                                    
COMPND  95 CHAIN: X;                                                            
COMPND  96 SYNONYM: RPS23;                                                      
COMPND  97 MOL_ID: 25;                                                          
COMPND  98 MOLECULE: RIBOSOMAL PROTEIN ES24;                                    
COMPND  99 CHAIN: Y;                                                            
COMPND 100 SYNONYM: 40S RIBOSOMAL PROTEIN S24;                                  
COMPND 101 MOL_ID: 26;                                                          
COMPND 102 MOLECULE: RIBOSOMAL PROTEIN ES25;                                    
COMPND 103 CHAIN: Z;                                                            
COMPND 104 SYNONYM: KLLA0B06182P;                                               
COMPND 105 MOL_ID: 27;                                                          
COMPND 106 MOLECULE: RIBOSOMAL PROTEIN ES26;                                    
COMPND 107 CHAIN: a;                                                            
COMPND 108 SYNONYM: KLLA0D05115P;                                               
COMPND 109 MOL_ID: 28;                                                          
COMPND 110 MOLECULE: RIBOSOMAL PROTEIN ES27;                                    
COMPND 111 CHAIN: b;                                                            
COMPND 112 SYNONYM: 40S RIBOSOMAL PROTEIN S27;                                  
COMPND 113 MOL_ID: 29;                                                          
COMPND 114 MOLECULE: RIBOSOMAL PROTEIN ES28;                                    
COMPND 115 CHAIN: c;                                                            
COMPND 116 SYNONYM: 40S RIBOSOMAL PROTEIN S28, S33;                             
COMPND 117 MOL_ID: 30;                                                          
COMPND 118 MOLECULE: RIBOSOMAL PROTEIN ES29;                                    
COMPND 119 CHAIN: d;                                                            
COMPND 120 SYNONYM: 40S RIBOSOMAL PROTEIN S29;                                  
COMPND 121 MOL_ID: 31;                                                          
COMPND 122 MOLECULE: RIBOSOMAL PROTEIN ES30;                                    
COMPND 123 CHAIN: e;                                                            
COMPND 124 SYNONYM: KLLA0C04809P;                                               
COMPND 125 MOL_ID: 32;                                                          
COMPND 126 MOLECULE: RIBOSOMAL PROTEIN ES31;                                    
COMPND 127 CHAIN: f;                                                            
COMPND 128 SYNONYM: UBIQUITIN-40S RIBOSOMAL PROTEIN S27A;                       
COMPND 129 MOL_ID: 33;                                                          
COMPND 130 MOLECULE: RIBOSOMAL PROTEIN RACK1;                                   
COMPND 131 CHAIN: g;                                                            
COMPND 132 SYNONYM: KLLA0E12277P;                                               
COMPND 133 MOL_ID: 34;                                                          
COMPND 134 MOLECULE: 18S RIBOSOMAL RNA;                                         
COMPND 135 CHAIN: 2;                                                            
COMPND 136 MOL_ID: 35;                                                          
COMPND 137 MOLECULE: CRICKET PARALYSIS VIRUS IRES RNA;                          
COMPND 138 CHAIN: i;                                                            
COMPND 139 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: CRICKET PARALYSIS VIRUS;                        
SOURCE 105 ORGANISM_TAXID: 12136;                                               
SOURCE 106 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE 107 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    IRES, RIBOSOME, SMALL, SUBUNIT                                        
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    J.MURRAY,C.G.SAVVA,B.S.SHIN,T.E.DEVER,V.RAMAKRISHNAN,I.S.FERNANDEZ    
REVDAT   3   11-DEC-19 5IT9    1       REMARK LINK   CRYST1 SCALE               
REVDAT   2   02-AUG-17 5IT9    1                                                
REVDAT   1   18-MAY-16 5IT9    0                                                
JRNL        AUTH   J.MURRAY,C.G.SAVVA,B.S.SHIN,T.E.DEVER,V.RAMAKRISHNAN,        
JRNL        AUTH 2 I.S.FERNANDEZ                                                
JRNL        TITL   STRUCTURAL CHARACTERIZATION OF RIBOSOME RECRUITMENT AND      
JRNL        TITL 2 TRANSLOCATION BY TYPE IV IRES.                               
JRNL        REF    ELIFE                         V.   5       2016              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   27159451                                                     
JRNL        DOI    10.7554/ELIFE.13567                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : EPU, EPU, CTFFIND, RELION, REFMAC         
REMARK   3   RECONSTRUCTION SCHEMA  : BACK PROJECTION                           
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : RECIPROCAL                          
REMARK   3   REFINEMENT PROTOCOL          : OTHER                               
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : NULL                                             
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 3.800                          
REMARK   3   NUMBER OF PARTICLES               : 54481                          
REMARK   3   CTF CORRECTION METHOD             : PHASE FLIPPING ONLY            
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 5IT9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-MAR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000219269.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : NULL                              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : KLUYVEROMYCES LACTIS SMALL        
REMARK 245                                    RIBOSOMAL SUBUNIT IN COMPLEX      
REMARK 245                                    WITH THE CRICKET PARALYSIS        
REMARK 245                                    VIRUS IRES                        
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 6.50                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : FEI FALCON II (4K X 4K)        
REMARK 245   MINIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MAXIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : NULL                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 25.00                          
REMARK 245   ILLUMINATION MODE                 : OTHER                          
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 35-MERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: K, L, M, N, O, P, Q, R, S,            
REMARK 350                    AND CHAINS: T, U, V, W, X, Y, Z, a, b, c,         
REMARK 350                    AND CHAINS: d, e, f, g, 2, i                      
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     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     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 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     ARG P 130    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN f 149    CG   CD   OE1  NE2                                  
REMARK 470     LYS f 150    CG   CD   CE   NZ                                   
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       U i6203    O4'  C2'  O2'  C1'  N1   C2   O2                    
REMARK 470       U i6203    N3   C4   O4   C5   C6                              
REMARK 470       A i6204    O4'  C2'  O2'  C1'  N9   C8   N7                    
REMARK 470       A i6204    C5   C6   N6   N1   C2   N3   C4                    
REMARK 470       A i6205    O4'  C2'  O2'  C1'  N9   C8   N7                    
REMARK 470       A i6205    C5   C6   N6   N1   C2   N3   C4                    
REMARK 470       G i6206    O4'  C2'  O2'  C1'  N9   C8   N7                    
REMARK 470       G i6206    C5   C6   O6   N1   C2   N2   N3                    
REMARK 470       G i6206    C4                                                  
REMARK 470       A i6207    O4'  C2'  O2'  C1'  N9   C8   N7                    
REMARK 470       A i6207    C5   C6   N6   N1   C2   N3   C4                    
REMARK 470       A i6208    O4'  C2'  O2'  C1'  N9   C8   N7                    
REMARK 470       A i6208    C5   C6   N6   N1   C2   N3   C4                    
REMARK 470       A i6209    O4'  C2'  O2'  C1'  N9   C8   N7                    
REMARK 470       A i6209    C5   C6   N6   N1   C2   N3   C4                    
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   NZ   LYS e    53     N4     C i  6221              0.71            
REMARK 500   C2     C 2  1044     O6     G 2  1073              0.96            
REMARK 500   N3     C 2  1044     O6     G 2  1073              0.96            
REMARK 500   N2     G 2  1073     N3     C 2  1074              1.07            
REMARK 500   N2     G 2  1073     C4     C 2  1074              1.26            
REMARK 500   O2'    A 2  1229     O2     U 2  1258              1.40            
REMARK 500   CE   LYS e    53     N4     C i  6221              1.41            
REMARK 500   O2     C 2  1044     C6     G 2  1073              1.45            
REMARK 500   O2     C 2  1044     N4     C 2  1074              1.52            
REMARK 500   O2     C 2  1044     O6     G 2  1073              1.63            
REMARK 500   NE2  GLN X    63     OP1    A 2  1753              1.64            
REMARK 500   O2     C 2  1221     O2     U 2  1261              1.67            
REMARK 500   C2     G 2  1073     C4     C 2  1074              1.69            
REMARK 500   NH2  ARG D   116     C2     A i  6220              1.70            
REMARK 500   O    SER Z    63     O    VAL Z    66              1.70            
REMARK 500   N3     C 2  1044     C6     G 2  1073              1.70            
REMARK 500   CZ   ARG D   116     N1     A i  6220              1.70            
REMARK 500   C2     C 2  1044     C6     G 2  1073              1.71            
REMARK 500   O2'    C 2   955     O2'    G 2  1046              1.71            
REMARK 500   O2     C 2  1044     N1     G 2  1073              1.72            
REMARK 500   N1     A 2   480     O4     U 2   506              1.72            
REMARK 500   CZ   ARG D   116     C2     A i  6220              1.74            
REMARK 500   O4     U 2  1292     N1     A 2  1321              1.77            
REMARK 500   NZ   LYS e    53     C4     C i  6221              1.80            
REMARK 500   NE   ARG D   116     N1     A i  6220              1.83            
REMARK 500   N1     A 2  1754     O2'    G i  6189              1.83            
REMARK 500   N    ASP G   155     O5'    A 2    78              1.83            
REMARK 500   O2'    G 2  1082     O2'    G 2  1093              1.84            
REMARK 500   NZ   LYS G   136     OP1    A 2    65              1.87            
REMARK 500   N    ARG G   154     O5'    A 2    78              1.87            
REMARK 500   N3     C 2  1044     N2     G 2  1072              1.90            
REMARK 500   O    GLY J   170     C5'    A 2   511              1.93            
REMARK 500   N2     G i  6183     O4     U i  6211              1.95            
REMARK 500   OP2    G 2   935     N3     C 2  1074              1.96            
REMARK 500   N1     A 2   264     O4     U 2   288              1.98            
REMARK 500   O3'    U 2  1230     O2'    U 2  1257              1.99            
REMARK 500   N6     A 2  1218     O2'    G 2  1263              2.00            
REMARK 500   C4     C 2  1044     O6     G 2  1073              2.00            
REMARK 500   O4     U 2     8     O4     U 2    15              2.01            
REMARK 500   O    MET Z    51     CA   GLU Z    53              2.02            
REMARK 500   NH1  ARG Z    58     NH2  ARG Z   103              2.02            
REMARK 500   C    GLY J   170     OP1    A 2   511              2.03            
REMARK 500   N1     A 2   480     C4     U 2   506              2.04            
REMARK 500   O    GLY J   170     P      A 2   511              2.05            
REMARK 500   O6     G 2   143     N6     A 2   170              2.05            
REMARK 500   O2'    U i  6186     OP2    G i  6188              2.06            
REMARK 500   N1     G 2   513     N4     C 2   542              2.07            
REMARK 500   O    GLY J   170     O5'    A 2   511              2.07            
REMARK 500   O    GLY J   170     OP2    A 2   511              2.07            
REMARK 500   O6     G 2   150     O6     G 2   162              2.08            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      63 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG G 154   CA    ARG G 154   C       0.187                       
REMARK 500      U 2   8   O3'     U 2   9   P      -0.084                       
REMARK 500      U 2  77   O3'     A 2  78   P       0.075                       
REMARK 500      A 2 520   O3'     U 2 521   P      -0.075                       
REMARK 500      U 2 934   O3'     G 2 935   P      -0.122                       
REMARK 500      C 21044   C2      C 21044   O2      0.066                       
REMARK 500      C 21069   O3'     U 21070   P      -0.072                       
REMARK 500      G 21072   C2      G 21072   N2      0.107                       
REMARK 500      G 21073   N1      G 21073   C2     -0.084                       
REMARK 500      G 21073   C6      G 21073   N1     -0.049                       
REMARK 500      G 21073   C2      G 21073   N2     -0.136                       
REMARK 500      G 21073   C6      G 21073   O6     -0.093                       
REMARK 500      C 21074   C4      C 21074   N4      0.104                       
REMARK 500      C i6109   O3'     U i6110   P      -0.116                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG Z  68   N   -  CA  -  C   ANGL. DEV. = -22.1 DEGREES          
REMARK 500      A 2  78   P   -  O5' -  C5' ANGL. DEV. =   9.6 DEGREES          
REMARK 500      A 2  78   C5' -  C4' -  C3' ANGL. DEV. =  11.3 DEGREES          
REMARK 500      A 2  78   C4' -  C3' -  O3' ANGL. DEV. =  15.9 DEGREES          
REMARK 500      A 2 511   O5' -  P   -  OP1 ANGL. DEV. =   7.3 DEGREES          
REMARK 500      U 2 911   N1  -  C1' -  C2' ANGL. DEV. =   8.3 DEGREES          
REMARK 500      C 21044   N1  -  C2  -  O2  ANGL. DEV. =   4.4 DEGREES          
REMARK 500      C 21044   C6  -  N1  -  C1' ANGL. DEV. =  -7.4 DEGREES          
REMARK 500      C 21044   C2  -  N1  -  C1' ANGL. DEV. =   7.9 DEGREES          
REMARK 500      G 21073   N1  -  C2  -  N2  ANGL. DEV. = -15.0 DEGREES          
REMARK 500      G 21073   N1  -  C6  -  O6  ANGL. DEV. =  -4.2 DEGREES          
REMARK 500      C 21074   C2' -  C3' -  O3' ANGL. DEV. =  20.3 DEGREES          
REMARK 500      C 21074   C3' -  C2' -  C1' ANGL. DEV. =   5.1 DEGREES          
REMARK 500      C 21074   N1  -  C1' -  C2' ANGL. DEV. = -10.8 DEGREES          
REMARK 500      C 21076   N1  -  C1' -  C2' ANGL. DEV. =  -7.0 DEGREES          
REMARK 500      G 21082   C3' -  O3' -  P   ANGL. DEV. =  -7.8 DEGREES          
REMARK 500      G 21534   C2' -  C3' -  O3' ANGL. DEV. =   9.7 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    LEU A   9      106.22     63.13                                   
REMARK 500    ALA A  26      -47.71     92.31                                   
REMARK 500    LYS A  27     -175.82     66.84                                   
REMARK 500    ASN A  28      -59.38    -29.90                                   
REMARK 500    PRO A  35       48.00   -107.28                                   
REMARK 500    LYS A  39      130.46     70.10                                   
REMARK 500    ASP A  43       84.78     62.56                                   
REMARK 500    ASP A  72      -47.58   -175.62                                   
REMARK 500    VAL A  73       85.39    -67.38                                   
REMARK 500    THR A 103      110.05     71.65                                   
REMARK 500    ASN A 109       81.72     65.94                                   
REMARK 500    SER A 114       44.87    -94.14                                   
REMARK 500    LEU A 120      111.17   -169.97                                   
REMARK 500    THR A 124      -63.10   -104.91                                   
REMARK 500    ALA A 130      -48.60    -12.76                                   
REMARK 500    LYS A 167      -86.01     69.53                                   
REMARK 500    ARG A 185      104.01     69.08                                   
REMARK 500    GLN A 193      107.48     70.47                                   
REMARK 500    TRP A 195      171.23     59.90                                   
REMARK 500    TYR A 202     -136.81    -87.00                                   
REMARK 500    PHE A 203      161.03     66.53                                   
REMARK 500    VAL B  21      -60.85   -127.09                                   
REMARK 500    ASP B  22       87.62     61.58                                   
REMARK 500    LEU B  54      -59.55     84.99                                   
REMARK 500    LYS B  62       98.51    -60.44                                   
REMARK 500    ASP B  89      -65.30   -107.71                                   
REMARK 500    LYS B  94      -61.36     63.13                                   
REMARK 500    PHE B 100       70.99    -28.05                                   
REMARK 500    TRP B 117       32.17     76.53                                   
REMARK 500    ALA B 139      104.66   -160.32                                   
REMARK 500    ASN B 148      -40.12     86.80                                   
REMARK 500    GLN B 149      127.67    -29.55                                   
REMARK 500    GLN B 177      -63.20     64.22                                   
REMARK 500    LEU B 181      -47.04     71.47                                   
REMARK 500    LYS B 202      -33.97    -37.25                                   
REMARK 500    LEU B 207      151.05     73.60                                   
REMARK 500    ASN B 209      -86.67     58.01                                   
REMARK 500    VAL B 210      110.08     58.11                                   
REMARK 500    ARG B 213      -68.87     68.07                                   
REMARK 500    LEU B 218      -90.44   -101.93                                   
REMARK 500    PRO B 221     -154.76    -81.47                                   
REMARK 500    ASP B 224       78.59     58.19                                   
REMARK 500    TRP C  40      -98.37   -102.60                                   
REMARK 500    VAL C  41      110.23     59.57                                   
REMARK 500    THR C  44      115.45     69.43                                   
REMARK 500    SER C  65       44.40     32.21                                   
REMARK 500    ASP C 111     -125.40   -164.50                                   
REMARK 500    SER C 112       24.27   -147.39                                   
REMARK 500    VAL C 141      120.99    -19.55                                   
REMARK 500    TRP C 149      -64.20     -0.84                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     491 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 ASN A  164     ARG A  165                  148.49                    
REMARK 500 HIS A  168     SER A  169                 -146.98                    
REMARK 500 ASP G  155     TYR G  156                 -144.57                    
REMARK 500 ASP J   66     PRO J   67                 -146.63                    
REMARK 500 PRO O  122     SER O  123                  149.14                    
REMARK 500 GLN Q   40     PRO Q   41                  147.45                    
REMARK 500 TYR Q   49     GLU Q   50                 -146.94                    
REMARK 500 VAL V   13     PRO V   14                 -146.79                    
REMARK 500 ILE W   75     SER W   76                 -149.45                    
REMARK 500 ILE a   83     VAL a   84                  148.12                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG Z  68         0.28    SIDE CHAIN                              
REMARK 500      G 2 561         0.05    SIDE CHAIN                              
REMARK 500      C 2 583         0.05    SIDE CHAIN                              
REMARK 500      C 21044         0.06    SIDE CHAIN                              
REMARK 500      G 21073         0.13    SIDE CHAIN                              
REMARK 500      C 21074         0.12    SIDE CHAIN                              
REMARK 500      G 21269         0.05    SIDE CHAIN                              
REMARK 500      C 21439         0.05    SIDE CHAIN                              
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 G 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN G 176   OE1                                                    
REMARK 620 2   C 2 267   OP1  80.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG T 201  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN T  85   OD1                                                    
REMARK 620 2   A 21467   OP1  95.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN a 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS a  23   SG                                                     
REMARK 620 2 CYS a  26   SG  134.8                                              
REMARK 620 3 CYS a  74   SG  129.9  79.8                                        
REMARK 620 N                    1     2                                         
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 2  43   O3'                                                    
REMARK 620 2   U 2  44   OP1  57.6                                              
REMARK 620 3   U 2  44   OP2  51.4  58.7                                        
REMARK 620 4   A 2  47   OP2 146.2 103.6 146.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21829  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A 2 100   OP2                                                    
REMARK 620 2   U 2 101   OP2  75.6                                              
REMARK 620 3   C 2 360   OP2  76.4 141.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21870  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   C 2 249   OP1                                                    
REMARK 620 2   A 2 250   OP2 105.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21817  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A 2 377   OP2                                                    
REMARK 620 2   U 2 378   OP2  87.0                                              
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  91.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21804  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G 2 551   OP1                                                    
REMARK 620 2   A 2 554   OP2 125.2                                              
REMARK 620 3   A 2 555   OP2 144.0  77.1                                        
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   A 2 622   OP1                                                    
REMARK 620 2   A 2 622   OP2  55.6                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21806  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G 2 623   OP2                                                    
REMARK 620 2   A 21024   OP2 136.6                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21873  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A 2 634   OP1                                                    
REMARK 620 2   A 2 635   OP2  74.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21849  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   U 2 988   OP1                                                    
REMARK 620 2   U 2 988   OP2  53.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21840  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A 2 991   OP2                                                    
REMARK 620 2   G 21010   O6   83.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21809  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A 21004   OP1                                                    
REMARK 620 2   A 21004   OP2  54.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21857  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G 21175   OP1                                                    
REMARK 620 2   G 21175   OP2  77.3                                              
REMARK 620 3   G 21175   O5'  57.0  57.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21860  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A 21195   O3'                                                    
REMARK 620 2   C 21196   OP1  49.5                                              
REMARK 620 N                    1                                               
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   A 21202   OP2  81.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21861  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   U 21268   OP1                                                    
REMARK 620 2   U 21268   OP2  73.4                                              
REMARK 620 N                    1                                               
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   C 21273   OP1                                                    
REMARK 620 2   G 21426   OP1  80.6                                              
REMARK 620 3   G 21427   OP1 144.4 119.9                                        
REMARK 620 4   G 21427   OP2  93.4  74.0  68.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21827  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G 21327   OP2                                                    
REMARK 620 2   G 21329   O6  134.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21863  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G 21537   OP2                                                    
REMARK 620 2   G 21539   O6  108.8                                              
REMARK 620 N                    1                                               
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   G 21627   O3'                                                    
REMARK 620 2   U 21628   OP1  57.4                                              
REMARK 620 3   G 21791   OP1 140.6 156.3                                        
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 21760   OP2                                                    
REMARK 620 2   A 21761   OP2  80.1                                              
REMARK 620 3   G 21765   O2' 145.3  90.4                                        
REMARK 620 4   G 21766   OP2  92.7  94.0  54.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG 21813  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A 21761   OP1                                                    
REMARK 620 2   U 21768   O3' 140.1                                              
REMARK 620 3   U 21769   OP1  82.9  58.7                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG G 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG T 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG X 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN a 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN b 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN f 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1805                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1806                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1808                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1809                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1810                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1811                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1812                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1813                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1814                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1815                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1816                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1817                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1818                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1819                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1820                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1821                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1822                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1823                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1824                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1825                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1826                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1827                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1828                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1829                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1831                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1832                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1833                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1834                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1835                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1836                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1837                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1838                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1839                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1840                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1841                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1842                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1843                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1844                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1845                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1846                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1847                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1849                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1850                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1851                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1853                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1854                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1855                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1857                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1858                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1859                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1860                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1861                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1862                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1863                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1864                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1865                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1866                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1867                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1869                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1870                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1871                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1872                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1873                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1874                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG 2 1875                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-8124   RELATED DB: EMDB                              
DBREF  5IT9 A    2   207  UNP    Q6CN12   RSSA_KLULA       2    207             
DBREF  5IT9 B   20   233  UNP    Q6CWD0   RS3A_KLULA      20    233             
DBREF  5IT9 C   39   255  UNP    Q6CKL3   Q6CKL3_KLULA    39    255             
DBREF  5IT9 D    3   225  UNP    Q6CRK7   Q6CRK7_KLULA     3    225             
DBREF  5IT9 E    2   261  UNP    Q6CWJ2   Q6CWJ2_KLULA     2    261             
DBREF  5IT9 F   22   227  UNP    Q6CRA3   Q6CRA3_KLULA    22    227             
DBREF  5IT9 G    1   226  UNP    Q6CM04   RS6_KLULA        1    226             
DBREF  5IT9 H    4   187  UNP    Q6CTD6   Q6CTD6_KLULA     4    187             
DBREF  5IT9 I    2   201  UNP    Q6CMG3   Q6CMG3_KLULA     2    201             
DBREF  5IT9 J    2   183  UNP    Q6CM18   Q6CM18_KLULA     2    183             
DBREF  5IT9 K    1    96  UNP    Q6CVZ5   Q6CVZ5_KLULA     1     96             
DBREF  5IT9 L    2   156  UNP    Q6CX80   Q6CX80_KLULA     2    156             
DBREF  5IT9 M   13   134  UNP    Q6CLU4   Q6CLU4_KLULA    13    134             
DBREF  5IT9 N    2   151  UNP    Q6CJK0   Q6CJK0_KLULA     2    151             
DBREF  5IT9 O   11   137  UNP    P27069   RS14_KLULA      11    137             
DBREF  5IT9 P    8   130  UNP    Q6CKV4   Q6CKV4_KLULA     8    130             
DBREF  5IT9 Q    3   143  UNP    Q875N2   RS16_KLULA       3    143             
DBREF  5IT9 R    2   130  UNP    Q6CWU3   Q6CWU3_KLULA     2    130             
DBREF  5IT9 S    2   146  UNP    Q6CWT9   Q6CWT9_KLULA     2    146             
DBREF  5IT9 T    2   144  UNP    Q6CXM0   Q6CXM0_KLULA     2    144             
DBREF  5IT9 U   15   120  UNP    Q6CIM1   Q6CIM1_KLULA    12    117             
DBREF  5IT9 V    1    87  UNP    Q6CXT6   RS21_KLULA       1     87             
DBREF  5IT9 W    2   130  UNP    Q6CW21   RS22_KLULA       2    130             
DBREF  5IT9 X    1   145  UNP    Q875M3   Q875M3_KLULC     1    145             
DBREF  5IT9 Y    2   135  UNP    Q6CU44   Q6CU44_KLULA     2    135             
DBREF  5IT9 Z   36   105  UNP    Q6CW78   Q6CW78_KLULA    36    105             
DBREF  5IT9 a    1   100  UNP    Q6CS01   Q6CS01_KLULA     1    100             
DBREF  5IT9 b    1    82  UNP    Q6CNL2   Q6CNL2_KLULA     1     82             
DBREF  5IT9 c    5    67  UNP    P33285   RS28_KLULA       5     67             
DBREF  5IT9 d    4    56  UNP    Q6CPG3   RS29_KLULA       4     56             
DBREF  5IT9 e    9    63  UNP    Q6CUH5   Q6CUH5_KLULA     9     63             
DBREF  5IT9 f   82   150  UNP    P69061   RS27A_KLULA     82    150             
DBREF  5IT9 g    3   326  UNP    Q6CNI7   Q6CNI7_KLULA     3    326             
DBREF  5IT9 2    1  1780  PDB    5IT9     5IT9             1   1780             
DBREF  5IT9 i 6030  6221  GB     8895506  AF218039.1    6030   6221             
SEQADV 5IT9   C i 6176  GB   8895506     U  6176 CONFLICT                       
SEQRES   1 A  206  SER LEU PRO SER THR PHE ASP LEU THR SER GLU ASP ALA          
SEQRES   2 A  206  GLN LEU LEU LEU ALA ALA ARG VAL HIS LEU GLY ALA LYS          
SEQRES   3 A  206  ASN VAL GLN VAL HIS GLN GLU PRO TYR VAL TYR LYS ALA          
SEQRES   4 A  206  ARG PRO ASP GLY VAL ASN VAL ILE ASN VAL GLY LYS THR          
SEQRES   5 A  206  TRP GLU LYS ILE VAL LEU ALA ALA ARG ILE ILE ALA ALA          
SEQRES   6 A  206  ILE PRO ASN PRO GLU ASP VAL VAL ALA ILE SER SER ARG          
SEQRES   7 A  206  THR TYR GLY GLN ARG ALA VAL LEU LYS TYR ALA ALA HIS          
SEQRES   8 A  206  THR GLY ALA THR PRO ILE ALA GLY ARG PHE THR PRO GLY          
SEQRES   9 A  206  SER PHE THR ASN TYR ILE THR ARG SER PHE LYS GLU PRO          
SEQRES  10 A  206  ARG LEU VAL ILE VAL THR ASP PRO ARG SER ASP ALA GLN          
SEQRES  11 A  206  ALA ILE LYS GLU SER SER TYR VAL ASN ILE PRO VAL ILE          
SEQRES  12 A  206  ALA LEU THR ASP LEU ASP SER PRO SER GLU TYR VAL ASP          
SEQRES  13 A  206  VAL ALA ILE PRO CYS ASN ASN ARG GLY LYS HIS SER ILE          
SEQRES  14 A  206  GLY LEU ILE TRP TYR LEU LEU ALA ARG GLU VAL LEU ARG          
SEQRES  15 A  206  LEU ARG GLY ALA LEU PRO ASP ARG THR GLN PRO TRP ALA          
SEQRES  16 A  206  ILE MET PRO ASP LEU TYR PHE TYR ARG ASN PRO                  
SEQRES   1 B  214  VAL VAL ASP PRO PHE THR ARG LYS GLU TRP TYR ASP ILE          
SEQRES   2 B  214  LYS ALA PRO SER THR PHE GLU ASN ARG ASN VAL GLY LYS          
SEQRES   3 B  214  THR LEU VAL ASN LYS SER VAL GLY LEU LYS ASN ALA SER          
SEQRES   4 B  214  ASP SER LEU LYS GLY ARG VAL VAL GLU VAL CYS LEU ALA          
SEQRES   5 B  214  ASP LEU GLN GLY SER GLU ASP HIS SER PHE ARG LYS VAL          
SEQRES   6 B  214  LYS LEU ARG VAL ASP GLU VAL GLN GLY LYS ASN LEU LEU          
SEQRES   7 B  214  THR ASN PHE HIS GLY MET ASP PHE THR THR ASP LYS LEU          
SEQRES   8 B  214  ARG SER MET VAL ARG LYS TRP GLN THR LEU ILE GLU ALA          
SEQRES   9 B  214  ASN VAL THR VAL LYS THR SER ASP ASP TYR VAL LEU ARG          
SEQRES  10 B  214  ILE PHE ALA ILE ALA PHE THR ARG LYS GLN ALA ASN GLN          
SEQRES  11 B  214  VAL LYS ARG THR SER TYR ALA GLN SER SER HIS ILE ARG          
SEQRES  12 B  214  GLN ILE ARG LYS VAL ILE SER GLU ILE LEU THR ARG GLU          
SEQRES  13 B  214  VAL GLN ASN SER THR LEU ALA GLN LEU THR SER LYS LEU          
SEQRES  14 B  214  ILE PRO GLU VAL ILE ASN LYS GLU ILE GLU ASN ALA THR          
SEQRES  15 B  214  LYS ASP ILE PHE PRO LEU GLN ASN VAL HIS ILE ARG LYS          
SEQRES  16 B  214  VAL LYS LEU LEU LYS GLN PRO LYS PHE ASP LEU GLY SER          
SEQRES  17 B  214  LEU LEU SER LEU HIS GLY                                      
SEQRES   1 C  217  GLY TRP VAL PRO VAL THR LYS LEU GLY ARG LEU VAL LYS          
SEQRES   2 C  217  ALA GLY LYS ILE SER SER ILE GLU GLU ILE PHE LEU HIS          
SEQRES   3 C  217  SER LEU PRO VAL LYS GLU PHE GLN ILE ILE ASP GLN LEU          
SEQRES   4 C  217  LEU PRO ASN LEU LYS ASP GLU VAL MET ASN ILE LYS PRO          
SEQRES   5 C  217  VAL GLN LYS GLN THR ARG ALA GLY GLN ARG THR ARG PHE          
SEQRES   6 C  217  LYS ALA VAL VAL VAL VAL GLY ASP SER ASN GLY HIS VAL          
SEQRES   7 C  217  GLY LEU GLY ILE LYS THR ALA LYS GLU VAL ALA GLY ALA          
SEQRES   8 C  217  ILE ARG ALA GLY ILE ILE ILE ALA LYS LEU SER VAL ILE          
SEQRES   9 C  217  PRO ILE ARG ARG GLY TYR TRP GLY THR ASN LEU GLY GLN          
SEQRES  10 C  217  PRO HIS SER LEU ALA THR LYS THR SER GLY LYS CYS GLY          
SEQRES  11 C  217  SER VAL SER VAL ARG LEU ILE PRO ALA PRO ARG GLY SER          
SEQRES  12 C  217  GLY ILE VAL ALA SER PRO ALA VAL LYS LYS LEU MET GLN          
SEQRES  13 C  217  LEU ALA GLY VAL GLU ASP VAL TYR THR SER SER THR GLY          
SEQRES  14 C  217  SER THR ARG THR LEU GLU ASN THR LEU LYS ALA ALA PHE          
SEQRES  15 C  217  VAL ALA ILE GLY ASN THR TYR GLY PHE LEU THR PRO ASN          
SEQRES  16 C  217  LEU TRP GLU VAL GLN ALA LEU THR PRO SER PRO MET ASP          
SEQRES  17 C  217  VAL TYR ALA ASP TYR ALA THR ALA SER                          
SEQRES   1 D  223  ALA ILE ILE SER LYS LYS ARG LYS LEU VAL ALA ASP GLY          
SEQRES   2 D  223  VAL PHE TYR ALA GLU LEU ASN GLU PHE PHE THR ARG GLU          
SEQRES   3 D  223  LEU ALA GLU GLU GLY TYR SER GLY VAL GLU VAL ARG VAL          
SEQRES   4 D  223  THR PRO THR LYS THR GLU ILE ILE ILE ARG ALA THR LYS          
SEQRES   5 D  223  VAL GLN ASP VAL VAL GLY GLU ASN GLY ARG ARG ILE ASN          
SEQRES   6 D  223  GLU LEU THR LEU LEU ILE GLU LYS ARG PHE LYS TYR LYS          
SEQRES   7 D  223  ARG GLY THR ILE ALA LEU TYR ALA GLU ARG VAL HIS ASP          
SEQRES   8 D  223  ARG GLY LEU SER ALA VAL ALA GLN ALA GLU SER MET LYS          
SEQRES   9 D  223  PHE LYS LEU LEU ASN GLY LEU ALA ILE ARG ARG ALA ALA          
SEQRES  10 D  223  TYR GLY VAL VAL ARG TYR VAL MET GLU SER GLY ALA LYS          
SEQRES  11 D  223  GLY CYS GLU VAL VAL ILE SER GLY LYS LEU ARG ALA ALA          
SEQRES  12 D  223  ARG ALA LYS SER MET LYS PHE ALA ASP GLY PHE LEU ILE          
SEQRES  13 D  223  HIS SER GLY GLN PRO VAL ASN ASP PHE ILE GLU THR ALA          
SEQRES  14 D  223  THR ARG HIS VAL LEU LEU ARG GLN GLY VAL LEU GLY ILE          
SEQRES  15 D  223  LYS VAL LYS ILE MET LYS ASP PRO SER ARG ASN THR SER          
SEQRES  16 D  223  GLY PRO LYS ALA LEU PRO ASP ALA VAL THR ILE ILE GLU          
SEQRES  17 D  223  PRO LYS GLU GLU GLU PRO VAL LEU GLU PRO SER VAL LYS          
SEQRES  18 D  223  ASP TYR                                                      
SEQRES   1 E  260  ALA ARG GLY PRO LYS LYS HIS LEU LYS ARG LEU ALA ALA          
SEQRES   2 E  260  PRO HIS HIS TRP MET LEU ASP LYS LEU SER GLY CYS TYR          
SEQRES   3 E  260  ALA PRO ARG PRO SER ALA GLY PRO HIS LYS LEU ARG GLU          
SEQRES   4 E  260  SER LEU PRO LEU ILE VAL PHE LEU ARG ASN ARG LEU LYS          
SEQRES   5 E  260  TYR ALA LEU ASN GLY ARG GLU VAL LYS ALA ILE LEU MET          
SEQRES   6 E  260  GLN ARG HIS VAL LYS VAL ASP GLY LYS VAL ARG THR ASP          
SEQRES   7 E  260  THR THR PHE PRO ALA GLY PHE MET ASP VAL ILE THR LEU          
SEQRES   8 E  260  GLU ALA THR ASN GLU ASN PHE ARG LEU VAL TYR ASP VAL          
SEQRES   9 E  260  LYS GLY ARG PHE ALA VAL HIS ARG ILE THR ASP GLU GLU          
SEQRES  10 E  260  ALA SER TYR LYS LEU ALA LYS VAL LYS LYS VAL GLN LEU          
SEQRES  11 E  260  GLY LYS LYS GLY ILE PRO TYR VAL VAL THR HIS ASP GLY          
SEQRES  12 E  260  ARG THR ILE ARG TYR PRO ASP PRO ASN ILE LYS VAL ASN          
SEQRES  13 E  260  ASP THR VAL LYS VAL ASP LEU ALA THR GLY THR ILE THR          
SEQRES  14 E  260  ASP PHE ILE LYS PHE ASP THR GLY LYS LEU VAL TYR VAL          
SEQRES  15 E  260  THR GLY GLY ARG ASN LEU GLY ARG VAL GLY THR ILE VAL          
SEQRES  16 E  260  HIS ARG GLU ARG HIS GLU GLY GLY PHE ASP LEU VAL HIS          
SEQRES  17 E  260  ILE LYS ASP SER LEU GLU ASN THR PHE VAL THR ARG LEU          
SEQRES  18 E  260  ASN ASN VAL PHE VAL ILE GLY GLU PRO GLY ARG PRO TRP          
SEQRES  19 E  260  ILE SER LEU PRO LYS GLY LYS GLY ILE LYS LEU THR ILE          
SEQRES  20 E  260  SER GLU GLU ARG ASP ARG ARG ARG ALA GLN HIS GLY LEU          
SEQRES   1 F  206  PHE VAL PRO VAL GLU LEU ALA THR THR ILE PRO VAL GLU          
SEQRES   2 F  206  ILE GLN GLN ALA GLN GLN GLU ILE LYS LEU PHE ASN LYS          
SEQRES   3 F  206  TRP SER PHE GLU ASP VAL GLU VAL LYS ASP ALA SER LEU          
SEQRES   4 F  206  VAL ASP TYR ILE GLN ILE SER LYS PRO ILE TYR VAL ALA          
SEQRES   5 F  206  HIS THR ALA GLY ARG TYR ALA ASN LYS ARG PHE ARG LYS          
SEQRES   6 F  206  ALA GLN CYS PRO ILE VAL GLU ARG LEU THR ASN SER LEU          
SEQRES   7 F  206  MET MET ASN GLY ARG ASN ASN GLY LYS LYS LEU LYS ALA          
SEQRES   8 F  206  VAL ARG ILE VAL LYS HIS THR LEU GLU ILE ILE ASN VAL          
SEQRES   9 F  206  LEU THR ASP GLN ASN PRO LEU GLN VAL VAL VAL ASP ALA          
SEQRES  10 F  206  ILE ILE ASN SER GLY PRO ARG GLU ASP THR THR ARG VAL          
SEQRES  11 F  206  GLY GLY GLY GLY ALA ALA ARG ARG GLN ALA VAL ASP VAL          
SEQRES  12 F  206  SER PRO LEU ARG ARG VAL ASN GLN SER ILE ALA LEU LEU          
SEQRES  13 F  206  THR ILE GLY ALA ARG GLU ALA ALA PHE ARG ASN ILE LYS          
SEQRES  14 F  206  THR ILE ALA GLU THR LEU ALA GLU GLU LEU ILE ASN ALA          
SEQRES  15 F  206  ALA LYS GLY SER SER THR SER TYR ALA ILE LYS LYS LYS          
SEQRES  16 F  206  ASP GLU LEU GLU ARG VAL ALA LYS SER ASN ARG                  
SEQRES   1 G  226  MET LYS LEU ASN ILE SER TYR PRO ILE ASN GLY THR GLN          
SEQRES   2 G  226  LYS CYS ILE GLU ILE ASP ASP GLU HIS ARG VAL ARG VAL          
SEQRES   3 G  226  PHE TYR ASP LYS ARG ILE GLY GLN GLU VAL ASP GLY GLU          
SEQRES   4 G  226  SER VAL GLY ASP GLU PHE LYS GLY TYR VAL PHE LYS ILE          
SEQRES   5 G  226  ALA GLY GLY ASN ASP LYS GLN GLY PHE PRO MET LYS GLN          
SEQRES   6 G  226  GLY VAL LEU LEU PRO THR ARG VAL LYS LEU LEU LEU ALA          
SEQRES   7 G  226  LYS GLY HIS SER CYS TYR ARG PRO ARG ARG ASN GLY GLU          
SEQRES   8 G  226  ARG LYS ARG LYS SER VAL ARG GLY ALA ILE VAL GLY PRO          
SEQRES   9 G  226  ASP LEU ALA VAL LEU ALA LEU ILE ILE THR LYS LYS GLY          
SEQRES  10 G  226  GLU GLN GLU ILE GLU GLY ILE THR ASN ASP THR VAL PRO          
SEQRES  11 G  226  LYS ARG LEU GLY PRO LYS ARG ALA ASN ASN ILE ARG LYS          
SEQRES  12 G  226  PHE PHE GLY LEU THR LYS GLU ASP ASP VAL ARG ASP TYR          
SEQRES  13 G  226  VAL ILE ARG ARG GLU VAL THR LYS GLY ASP LYS SER TYR          
SEQRES  14 G  226  THR LYS ALA PRO LYS ILE GLN ARG LEU VAL THR PRO GLN          
SEQRES  15 G  226  ARG LEU GLN ARG LYS ARG GLN GLN LYS SER LEU LYS ILE          
SEQRES  16 G  226  LYS ASN ALA GLN ALA GLN ARG GLU ALA ALA ALA GLU TYR          
SEQRES  17 G  226  ALA GLN LEU LEU ALA LYS ARG LEU SER GLU ARG LYS ALA          
SEQRES  18 G  226  GLU LYS ALA GLU VAL                                          
SEQRES   1 H  184  PRO GLN ALA LYS ILE LEU SER GLN ALA PRO THR GLU LEU          
SEQRES   2 H  184  GLU LEU GLN VAL ALA GLN ALA PHE ILE ASP LEU GLU ASN          
SEQRES   3 H  184  ASN SER PRO GLU LEU LYS ALA ASP LEU ARG ALA LEU GLN          
SEQRES   4 H  184  PHE LYS SER ILE ARG GLU ILE GLU VAL ALA GLY GLY LYS          
SEQRES   5 H  184  LYS ALA LEU ALA VAL PHE VAL PRO VAL PRO SER LEU ALA          
SEQRES   6 H  184  ALA TYR HIS LYS VAL GLN ILE LYS LEU THR ARG GLU LEU          
SEQRES   7 H  184  GLU LYS LYS PHE GLN ASP ARG HIS VAL ILE PHE LEU ALA          
SEQRES   8 H  184  GLU ARG ARG ILE LEU PRO LYS PRO SER ARG LYS SER ARG          
SEQRES   9 H  184  GLN THR GLN LYS ARG PRO ARG SER ARG THR LEU THR ALA          
SEQRES  10 H  184  VAL HIS ASP LYS ILE LEU GLU ASP LEU VAL PHE PRO THR          
SEQRES  11 H  184  GLU ILE VAL GLY LYS ARG VAL ARG TYR LEU VAL GLY GLY          
SEQRES  12 H  184  ASN LYS ILE GLN LYS ILE LEU LEU ASN SER LYS ASP VAL          
SEQRES  13 H  184  GLN HIS ILE ASP ASN LYS LEU GLU SER PHE GLN ALA VAL          
SEQRES  14 H  184  TYR ASN LYS LEU THR GLY LYS GLN ILE VAL PHE GLU ILE          
SEQRES  15 H  184  PRO SER                                                      
SEQRES   1 I  200  GLY ILE SER ARG ASP SER ARG HIS LYS ARG ALA ALA THR          
SEQRES   2 I  200  GLY ALA LYS ARG ALA GLN PHE ARG LYS LYS ARG LYS PHE          
SEQRES   3 I  200  GLU LEU GLY ARG GLN ALA ALA ASN THR LYS ILE GLY THR          
SEQRES   4 I  200  LYS ARG ILE HIS PRO VAL ARG THR ARG GLY GLY ASN GLN          
SEQRES   5 I  200  LYS PHE ARG ALA LEU ARG ILE GLU THR GLY ASN PHE SER          
SEQRES   6 I  200  TRP ALA SER GLU GLY VAL ALA ARG LYS THR ARG ILE THR          
SEQRES   7 I  200  GLY VAL VAL TYR HIS PRO SER ASN ASN GLU LEU VAL ARG          
SEQRES   8 I  200  THR ASN THR LEU THR LYS ALA ALA ILE VAL GLN ILE ASP          
SEQRES   9 I  200  ALA THR PRO PHE ARG GLN TRP TYR GLU SER HIS TYR GLY          
SEQRES  10 I  200  GLN SER LEU GLY LYS LYS LYS ASN THR LYS ALA GLU GLU          
SEQRES  11 I  200  GLU THR ALA THR THR SER LYS ASN THR GLU ARG LYS TRP          
SEQRES  12 I  200  ALA ALA ARG ALA ALA GLU ALA LYS ILE GLU HIS ALA VAL          
SEQRES  13 I  200  ASP SER GLN PHE GLY ALA GLY ARG LEU TYR ALA ALA ILE          
SEQRES  14 I  200  SER SER ARG PRO GLY GLN SER GLY ARG CYS ASP GLY TYR          
SEQRES  15 I  200  ILE LEU GLU GLY GLU GLU LEU ALA PHE TYR LEU ARG ARG          
SEQRES  16 I  200  LEU THR ALA LYS LYS                                          
SEQRES   1 J  182  PRO ARG ALA PRO ARG THR TYR SER LYS THR TYR SER THR          
SEQRES   2 J  182  PRO LYS ARG PRO TYR GLU SER ALA ARG LEU ASP ALA GLU          
SEQRES   3 J  182  LEU LYS LEU ALA GLY GLU TYR GLY LEU LYS ASN LYS ARG          
SEQRES   4 J  182  GLU ILE TYR ARG ILE SER PHE GLN LEU SER LYS ILE ARG          
SEQRES   5 J  182  ARG ALA ALA ARG ASP LEU LEU THR ARG ASP GLU LYS ASP          
SEQRES   6 J  182  PRO LYS ARG LEU PHE GLU GLY ASN ALA LEU ILE ARG ARG          
SEQRES   7 J  182  LEU VAL ARG ILE GLY VAL LEU SER GLU ASP LYS LYS LYS          
SEQRES   8 J  182  LEU ASP TYR VAL LEU ALA LEU LYS VAL GLU ASP PHE LEU          
SEQRES   9 J  182  GLU ARG ARG LEU GLN THR GLN VAL TYR LYS LEU GLY LEU          
SEQRES  10 J  182  ALA LYS SER VAL HIS HIS ALA ARG VAL LEU ILE SER GLN          
SEQRES  11 J  182  ARG HIS ILE ALA VAL GLY LYS GLN ILE VAL ASN ILE PRO          
SEQRES  12 J  182  SER PHE MET VAL ARG LEU GLU SER GLU LYS HIS ILE ASP          
SEQRES  13 J  182  PHE ALA ARG THR SER PRO PHE GLY GLY ALA ARG PRO GLY          
SEQRES  14 J  182  ARG VAL ALA ARG LYS ARG ALA ALA ALA ALA GLY GLY GLU          
SEQRES   1 K   96  MET LEU ILE PRO LYS GLU ASP ARG LYS LYS ILE TYR GLN          
SEQRES   2 K   96  HIS LEU PHE GLN GLU GLY VAL LEU VAL ALA LYS LYS ASP          
SEQRES   3 K   96  PHE ASN GLN PRO LYS HIS GLU GLU ILE ASP THR LYS ASN          
SEQRES   4 K   96  LEU PHE VAL ILE LYS ALA LEU GLN SER LEU THR SER LYS          
SEQRES   5 K   96  GLY PHE VAL LYS THR GLN PHE SER TRP GLN TYR TYR TYR          
SEQRES   6 K   96  TYR THR LEU THR GLU GLU GLY VAL VAL TYR LEU ARG GLU          
SEQRES   7 K   96  TYR LEU ASN LEU PRO GLU HIS ILE PHE PRO ALA THR TYR          
SEQRES   8 K   96  LEU ALA GLY GLN SER                                          
SEQRES   1 L  155  SER THR GLU LEU THR VAL GLN SER GLU ARG ALA PHE GLN          
SEQRES   2 L  155  LYS GLN PRO HIS ILE PHE THR ASN PRO LYS ALA LYS ALA          
SEQRES   3 L  155  ASN ARG LYS THR LYS ARG TRP TYR LYS ASN VAL GLY LEU          
SEQRES   4 L  155  GLY PHE LYS THR PRO LYS THR ALA ILE GLU GLY SER TYR          
SEQRES   5 L  155  ILE ASP LYS LYS CYS PRO PHE THR GLY LEU VAL SER ILE          
SEQRES   6 L  155  ARG GLY LYS ILE LEU THR GLY THR VAL VAL SER THR ARG          
SEQRES   7 L  155  MET HIS ARG THR ILE VAL ILE ARG ARG ASP TYR LEU HIS          
SEQRES   8 L  155  TYR VAL PRO LYS TYR ASN ARG TYR GLU LYS ARG HIS LYS          
SEQRES   9 L  155  ASN VAL PRO ALA HIS VAL SER PRO ALA PHE ARG VAL GLN          
SEQRES  10 L  155  VAL GLY ASP ILE VAL THR VAL GLY GLN CYS ARG PRO ILE          
SEQRES  11 L  155  SER LYS THR VAL ARG PHE ASN VAL LEU LYS VAL ALA SER          
SEQRES  12 L  155  ALA THR GLY LYS ALA ASN LYS GLN PHE ALA LYS PHE              
SEQRES   1 M  122  ALA GLU LEU THR ILE GLU ASP ALA LEU LYS VAL VAL LEU          
SEQRES   2 M  122  ARG THR SER LEU VAL HIS ASP GLY LEU ALA ARG GLY LEU          
SEQRES   3 M  122  ARG GLU SER ALA LYS ALA LEU THR ARG GLY GLU GLY GLN          
SEQRES   4 M  122  LEU ALA VAL LEU VAL GLU SER VAL THR GLU GLU ALA ILE          
SEQRES   5 M  122  SER LYS LEU VAL GLN GLY LEU ALA THR GLU ASN ASN VAL          
SEQRES   6 M  122  PRO LEU ILE LYS VAL ALA ASP ALA LYS GLN LEU GLY GLU          
SEQRES   7 M  122  TRP ALA GLY LEU GLY LYS ILE ASP ARG ASP GLY ASN ALA          
SEQRES   8 M  122  ARG LYS VAL VAL GLY ALA SER VAL VAL VAL VAL LYS ASN          
SEQRES   9 M  122  TRP GLY ALA ASP THR GLN GLU ARG GLU ILE LEU LEU GLU          
SEQRES  10 M  122  HIS PHE SER GLN GLN                                          
SEQRES   1 N  150  GLY ARG MET HIS SER LYS GLY LYS GLY MET SER SER SER          
SEQRES   2 N  150  ALA ILE PRO TYR SER ARG ASN ALA PRO ALA TRP PHE LYS          
SEQRES   3 N  150  GLY SER SER ASP GLY VAL VAL GLU GLN ILE ILE LYS TYR          
SEQRES   4 N  150  ALA ARG LYS GLY LEU THR PRO SER GLN ILE GLY VAL LEU          
SEQRES   5 N  150  LEU ARG ASP ALA HIS GLY VAL THR GLN ALA LYS VAL ILE          
SEQRES   6 N  150  THR GLY ASN LYS ILE LEU ARG ILE LEU LYS SER ASN GLY          
SEQRES   7 N  150  LEU ALA PRO GLU ILE PRO GLU ASP LEU TYR PHE LEU ILE          
SEQRES   8 N  150  LYS LYS ALA VAL SER VAL ARG LYS HIS LEU GLU ARG ASN          
SEQRES   9 N  150  ARG LYS ASP LYS ASP ALA LYS PHE ARG LEU ILE LEU ILE          
SEQRES  10 N  150  GLU SER ARG ILE HIS ARG LEU ALA ARG TYR TYR ARG THR          
SEQRES  11 N  150  VAL SER VAL LEU PRO PRO ASN TRP LYS TYR GLU SER ALA          
SEQRES  12 N  150  THR ALA SER ALA LEU VAL ASN                                  
SEQRES   1 O  127  SER GLN VAL PHE GLY VAL ALA ARG ILE PHE ALA SER PHE          
SEQRES   2 O  127  ASN ASP THR PHE VAL HIS VAL THR ASP LEU SER GLY ARG          
SEQRES   3 O  127  GLU THR ILE ALA ARG VAL THR GLY GLY MET LYS VAL LYS          
SEQRES   4 O  127  ALA ASP ARG ASP GLU SER SER PRO TYR ALA ALA MET LEU          
SEQRES   5 O  127  ALA ALA GLN ASP VAL ALA ALA LYS CYS LYS GLU VAL GLY          
SEQRES   6 O  127  ILE THR ALA VAL HIS ILE LYS ILE ARG ALA THR GLY GLY          
SEQRES   7 O  127  THR ARG SER LYS THR PRO GLY PRO GLY GLY GLN ALA ALA          
SEQRES   8 O  127  LEU ARG ALA LEU ALA ARG SER GLY LEU ARG ILE GLY ARG          
SEQRES   9 O  127  ILE GLU ASP VAL THR PRO VAL PRO SER ASP SER THR ARG          
SEQRES  10 O  127  LYS LYS GLY GLY ARG ARG GLY ARG ARG LEU                      
SEQRES   1 P  123  ARG LYS ARG SER PHE LYS THR TYR SER TYR LYS GLY VAL          
SEQRES   2 P  123  ASP LEU GLU LYS LEU LEU GLU MET PRO THR GLU ASP PHE          
SEQRES   3 P  123  VAL LYS LEU ALA PRO ALA ARG VAL ARG ARG LYS PHE ALA          
SEQRES   4 P  123  ARG GLY LEU SER GLU LYS PRO ALA GLY LEU MET LYS LYS          
SEQRES   5 P  123  LEU ARG ALA ALA LYS LEU SER ALA PRO GLU ASN GLU LYS          
SEQRES   6 P  123  PRO ALA VAL VAL ARG THR HIS LEU ARG ASN MET ILE ILE          
SEQRES   7 P  123  VAL PRO GLU MET ILE GLY SER VAL VAL GLY VAL TYR ASN          
SEQRES   8 P  123  GLY LYS VAL PHE ASN GLN VAL GLU ILE ARG PRO GLU MET          
SEQRES   9 P  123  VAL GLY HIS TYR LEU GLY GLU PHE SER ILE THR TYR THR          
SEQRES  10 P  123  PRO VAL ARG HIS GLY ARG                                      
SEQRES   1 Q  141  THR VAL PRO SER VAL GLN THR PHE GLY LYS LYS LYS SER          
SEQRES   2 Q  141  ALA THR ALA VAL ALA HIS VAL LYS ALA GLY LYS GLY LEU          
SEQRES   3 Q  141  ILE LYS VAL ASN GLY SER PRO ILE THR LEU VAL GLN PRO          
SEQRES   4 Q  141  GLU ILE LEU ARG PHE LYS VAL TYR GLU PRO LEU LEU LEU          
SEQRES   5 Q  141  VAL GLY LEU ASP LYS PHE ALA ASN ILE ASP ILE ARG VAL          
SEQRES   6 Q  141  LYS VAL THR GLY GLY GLY HIS VAL SER GLN VAL TYR ALA          
SEQRES   7 Q  141  ILE ARG GLN ALA ILE ALA LYS GLY LEU VAL ALA TYR HIS          
SEQRES   8 Q  141  GLN LYS PHE VAL ASP GLU GLN SER LYS ASN GLU LEU LYS          
SEQRES   9 Q  141  LYS ALA PHE THR SER TYR ASP ARG THR LEU LEU ILE ALA          
SEQRES  10 Q  141  ASP SER ARG ARG PRO GLU PRO LYS LYS PHE GLY GLY ARG          
SEQRES  11 Q  141  GLY ALA ARG SER ARG PHE GLN LYS SER TYR ARG                  
SEQRES   1 R  129  GLY ARG VAL ARG THR LYS THR VAL LYS ARG ALA SER LYS          
SEQRES   2 R  129  ALA LEU ILE GLU LYS TYR TYR PRO LYS LEU THR MET ASP          
SEQRES   3 R  129  PHE GLN THR ASN LYS ARG LEU CYS ASP GLU ILE ALA THR          
SEQRES   4 R  129  ILE GLN SER LYS ARG LEU ARG ASN LYS ILE ALA GLY TYR          
SEQRES   5 R  129  THR THR HIS LEU MET LYS ARG ILE GLN LYS GLY PRO VAL          
SEQRES   6 R  129  ARG GLY ILE SER PHE LYS LEU GLN GLU GLU GLU ARG GLU          
SEQRES   7 R  129  ARG LYS ASP GLN TYR VAL PRO ASP VAL SER ALA LEU ASP          
SEQRES   8 R  129  LEU SER HIS SER ASN ASP VAL LEU ASN VAL ASP THR GLN          
SEQRES   9 R  129  THR ALA GLU LEU VAL ASN SER LEU GLY LEU LYS LEU PRO          
SEQRES  10 R  129  LEU SER VAL SER SER VAL SER ALA VAL ARG ASP ARG              
SEQRES   1 S  145  SER LEU VAL VAL GLN GLU GLN GLY SER PHE GLN HIS ILE          
SEQRES   2 S  145  LEU ARG LEU LEU ASN THR ASN VAL ASP GLY ASN ILE ASN          
SEQRES   3 S  145  VAL VAL TYR ALA LEU THR THR ILE ARG GLY VAL GLY ARG          
SEQRES   4 S  145  ARG TYR ALA ASN LEU VAL CYS LYS LYS ALA ASP VAL ASP          
SEQRES   5 S  145  LEU HIS LYS ARG ALA GLY GLU LEU THR GLN GLU GLU LEU          
SEQRES   6 S  145  GLU ARG ILE VAL GLN ILE MET GLN ASN PRO THR HIS TYR          
SEQRES   7 S  145  LYS ILE PRO ALA TRP PHE LEU ASN ARG GLN LYS ASP VAL          
SEQRES   8 S  145  ASN ASP GLY LYS ASP TYR HIS SER LEU ALA ASN ASN LEU          
SEQRES   9 S  145  GLU SER LYS LEU ARG ASP ASP LEU GLU ARG LEU LYS LYS          
SEQRES  10 S  145  ILE ARG SER HIS ARG GLY ILE ARG HIS PHE TRP GLY LEU          
SEQRES  11 S  145  ARG VAL ARG GLY GLN HIS THR LYS THR THR GLY ARG ARG          
SEQRES  12 S  145  ARG ALA                                                      
SEQRES   1 T  143  PRO GLY VAL SER VAL ARG ASP VAL PRO ALA GLN ASP PHE          
SEQRES   2 T  143  ILE ASN ASN TYR ALA SER PHE LEU GLN ARG GLN GLY LYS          
SEQRES   3 T  143  LEU GLU VAL PRO GLY TYR VAL ASP ILE VAL LYS THR SER          
SEQRES   4 T  143  ALA GLY ASN GLU LEU PRO PRO GLN ASP SER GLU GLY TRP          
SEQRES   5 T  143  PHE TYR LYS ARG ALA ALA SER VAL ALA ARG HIS ILE TYR          
SEQRES   6 T  143  LEU ARG LYS GLN VAL GLY VAL GLY LYS LEU ASN LYS LEU          
SEQRES   7 T  143  TYR GLY GLY ALA LYS ASN ARG GLY VAL ARG PRO HIS LYS          
SEQRES   8 T  143  HIS VAL ASP ALA SER GLY SER ILE ASN ARG LYS VAL LEU          
SEQRES   9 T  143  GLN SER LEU GLU LYS LEU GLY VAL VAL GLU ILE SER PRO          
SEQRES  10 T  143  LYS GLY GLY ARG ARG ILE SER ASP ASN GLY LEU ARG ASP          
SEQRES  11 T  143  LEU ASP ARG ILE ALA ALA ALA THR LEU GLU ASP GLU GLU          
SEQRES   1 U  106  GLN GLU VAL VAL ILE HIS LYS ILE ARG ILE ASN LEU THR          
SEQRES   2 U  106  SER THR LYS VAL LYS GLN LEU GLU ASN VAL SER ALA ASN          
SEQRES   3 U  106  ILE ILE LYS ASN ALA GLU THR PHE LYS LEU VAL LYS LYS          
SEQRES   4 U  106  GLY PRO VAL ARG LEU PRO THR LYS VAL LEU LYS ILE SER          
SEQRES   5 U  106  THR ARG LYS THR PRO ASN GLY GLU GLY SER LYS THR TRP          
SEQRES   6 U  106  ASP THR TYR GLU MET ARG ILE HIS LYS ARG TYR ILE ASP          
SEQRES   7 U  106  LEU GLU ALA PRO ALA HIS ILE VAL LYS ARG ILE THR GLN          
SEQRES   8 U  106  ILE THR ILE GLU PRO GLY VAL ASP VAL GLU VAL ILE ILE          
SEQRES   9 U  106  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  129  THR ARG THR SER VAL LEU ALA ASP ALA LEU ASN ALA ILE          
SEQRES   2 W  129  ASN ASN ALA GLU LYS THR GLY LYS ARG GLN VAL LEU ILE          
SEQRES   3 W  129  ARG PRO SER SER LYS VAL ILE ILE LYS PHE LEU GLN VAL          
SEQRES   4 W  129  MET GLN LYS HIS GLY TYR ILE GLY GLU PHE GLU TYR ILE          
SEQRES   5 W  129  ASP ASP HIS ARG SER GLY LYS ILE VAL VAL GLN LEU ASN          
SEQRES   6 W  129  GLY ARG LEU ASN LYS CYS GLY VAL ILE SER PRO ARG PHE          
SEQRES   7 W  129  ASN VAL LYS ILE ALA ASP VAL GLU LYS TRP THR ALA ASN          
SEQRES   8 W  129  LEU LEU PRO ALA ARG GLN PHE GLY TYR VAL ILE LEU THR          
SEQRES   9 W  129  THR SER ALA GLY ILE MET ASP HIS GLU GLU ALA HIS ARG          
SEQRES  10 W  129  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  134  SER ASP ALA ILE THR ILE ARG THR ARG LYS VAL ILE SER          
SEQRES   2 Y  134  ASN PRO LEU LEU ALA ARG LYS GLN PHE VAL VAL ASP VAL          
SEQRES   3 Y  134  LEU HIS PRO ASN ARG ALA ASN VAL SER LYS ASP GLU LEU          
SEQRES   4 Y  134  ARG GLU LYS LEU ALA GLU ALA TYR LYS ALA GLU LYS ASP          
SEQRES   5 Y  134  ALA VAL SER VAL PHE GLY PHE ARG THR GLN TYR GLY GLY          
SEQRES   6 Y  134  GLY LYS SER THR GLY PHE GLY LEU VAL TYR ASN SER VAL          
SEQRES   7 Y  134  ALA ASP ALA LYS LYS PHE GLU PRO ALA TYR ARG LEU VAL          
SEQRES   8 Y  134  ARG TYR GLY LEU ALA GLU LYS VAL GLU LYS ALA SER ARG          
SEQRES   9 Y  134  GLN GLN ARG LYS GLN ARG LYS ASN ARG GLY LYS LYS ILE          
SEQRES  10 Y  134  PHE GLY THR GLY LYS SER ILE ALA LYS LYS ALA ALA ARG          
SEQRES  11 Y  134  ARG ASN ALA ASP                                              
SEQRES   1 Z   70  ALA LYS HIS ALA VAL VAL LEU ASP GLN ASP LYS PHE ASP          
SEQRES   2 Z   70  ARG ILE MET LYS GLU ALA PRO THR TYR ARG TYR VAL SER          
SEQRES   3 Z   70  VAL SER VAL LEU VAL ASP ARG PHE LYS LEU GLY GLY SER          
SEQRES   4 Z   70  LEU ALA ARG VAL ALA LEU ARG HIS LEU GLU ASN GLU GLY          
SEQRES   5 Z   70  ILE ILE LYS PRO VAL SER LYS HIS SER LYS GLN ALA ILE          
SEQRES   6 Z   70  TYR THR ARG ALA THR                                          
SEQRES   1 a  100  MET PRO LYS LYS ARG ALA SER ASN GLY ARG ASN LYS LYS          
SEQRES   2 a  100  GLY ARG GLY HIS VAL LYS PRO VAL ARG CYS VAL ASN CYS          
SEQRES   3 a  100  SER ARG SER VAL PRO LYS ASP LYS ALA ILE LYS ARG MET          
SEQRES   4 a  100  ALA ILE ARG ASN ILE VAL GLU ALA ALA ALA ILE ARG ASP          
SEQRES   5 a  100  LEU SER GLU ALA SER VAL TYR ALA GLU TYR ALA LEU PRO          
SEQRES   6 a  100  LYS THR TYR ASN LYS LEU HIS TYR CYS ILE SER CYS ALA          
SEQRES   7 a  100  ILE HIS ALA ARG ILE VAL ARG VAL ARG SER ARG THR ASP          
SEQRES   8 a  100  ARG ARG ILE ARG ALA PRO PRO GLN ARG                          
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   63  THR PRO VAL THR LEU ALA LYS VAL ILE LYS VAL LEU GLY          
SEQRES   2 c   63  ARG THR GLY SER ARG GLY GLY VAL THR GLN VAL ARG VAL          
SEQRES   3 c   63  GLU PHE LEU GLU ASP THR THR ARG THR ILE VAL ARG ASN          
SEQRES   4 c   63  VAL LYS GLY PRO VAL ARG GLU GLY ASP ILE LEU VAL LEU          
SEQRES   5 c   63  MET GLU SER GLU ARG GLU ALA ARG ARG LEU ARG                  
SEQRES   1 d   53  GLU ASN VAL TRP TYR SER HIS PRO ARG LYS PHE GLY LYS          
SEQRES   2 d   53  GLY SER ARG GLN CYS ARG ILE SER GLY SER HIS SER GLY          
SEQRES   3 d   53  LEU ILE ARG LYS TYR GLY LEU ASN ILE ASP ARG GLN SER          
SEQRES   4 d   53  PHE ARG GLU LYS ALA ASN ASP ILE GLY PHE TYR LYS TYR          
SEQRES   5 d   53  ARG                                                          
SEQRES   1 e   55  ALA ARG ALA GLY LYS VAL LYS SER GLN THR PRO LYS VAL          
SEQRES   2 e   55  GLU LYS GLN GLU LYS PRO LYS GLN PRO LYS GLY ARG ALA          
SEQRES   3 e   55  TYR LYS ARG LEU LEU TYR THR ARG ARG PHE VAL ASN VAL          
SEQRES   4 e   55  THR LEU THR ASN GLY LYS ARG LYS MET ASN PRO SER PRO          
SEQRES   5 e   55  SER SER GLN                                                  
SEQRES   1 f   69  LYS LYS VAL TYR THR THR PRO LYS LYS ILE ARG HIS LYS          
SEQRES   2 f   69  HIS LYS LYS VAL LYS LEU ALA VAL LEU ASN TYR TYR LYS          
SEQRES   3 f   69  VAL ASP ASP GLU GLY LYS VAL ALA LYS LEU ARG LYS GLU          
SEQRES   4 f   69  CYS PRO ASN CYS GLY PRO GLY ILE PHE LEU ALA ASN HIS          
SEQRES   5 f   69  GLY ASP ARG PHE TYR CYS GLY LYS CYS HIS SER THR PHE          
SEQRES   6 f   69  ALA THR GLN LYS                                              
SEQRES   1 g  324  SER SER ASN ILE MET LEU VAL LEU ARG GLY THR LEU GLU          
SEQRES   2 g  324  GLY HIS ASN GLY TRP VAL THR SER LEU SER THR SER ALA          
SEQRES   3 g  324  ALA GLN PRO ASN LEU LEU VAL SER GLY SER ARG ASP LYS          
SEQRES   4 g  324  THR LEU ILE SER TRP ARG LEU THR GLU ASN GLU GLN GLN          
SEQRES   5 g  324  PHE GLY VAL PRO VAL ARG SER TYR LYS GLY HIS SER HIS          
SEQRES   6 g  324  ILE VAL GLN ASP VAL VAL VAL SER ALA ASP GLY ASN TYR          
SEQRES   7 g  324  ALA VAL SER ALA SER TRP ASP LYS THR LEU ARG LEU TRP          
SEQRES   8 g  324  ASN LEU ALA THR GLY ASN SER GLU ALA ARG PHE VAL GLY          
SEQRES   9 g  324  HIS THR GLY ASP VAL LEU SER VAL ALA ILE ASP ALA ASN          
SEQRES  10 g  324  SER SER LYS ILE ILE SER ALA SER ARG ASP LYS THR ILE          
SEQRES  11 g  324  ARG VAL TRP ASN THR VAL GLY ASP CYS ALA TYR VAL LEU          
SEQRES  12 g  324  LEU GLY HIS THR ASP TRP VAL THR LYS VAL ARG VAL ALA          
SEQRES  13 g  324  PRO LYS ASN LEU GLU ASP GLY GLU VAL ASP ASP GLY ARG          
SEQRES  14 g  324  ILE THR PHE VAL SER ALA GLY MET ASP LYS ILE VAL ARG          
SEQRES  15 g  324  SER TRP SER LEU ASN GLU ASP SER TYR ARG ILE GLU ALA          
SEQRES  16 g  324  ASP PHE ILE GLY HIS ASN ASN TYR ILE ASN VAL VAL GLN          
SEQRES  17 g  324  PRO SER PRO ASP GLY SER LEU ALA ALA SER ALA GLY LYS          
SEQRES  18 g  324  ASP GLY GLN ILE TYR VAL TRP ASN LEU LYS HIS LYS SER          
SEQRES  19 g  324  ALA PHE MET ASN PHE ASP ALA LYS ASP GLU VAL PHE ALA          
SEQRES  20 g  324  LEU ALA PHE SER PRO SER ARG PHE TRP LEU THR ALA ALA          
SEQRES  21 g  324  THR ALA SER GLY ILE LYS ILE TYR ASP LEU GLU ASN GLU          
SEQRES  22 g  324  VAL LEU ILE ASP GLU LEU LYS PRO GLU PHE ALA GLY TYR          
SEQRES  23 g  324  THR LYS ALA GLN ASP PRO HIS ALA VAL SER LEU ALA TRP          
SEQRES  24 g  324  SER ALA ASP GLY GLN THR LEU PHE ALA GLY TYR THR ASP          
SEQRES  25 g  324  ASN VAL ILE ARG VAL TRP GLN VAL MET THR ALA ASN              
SEQRES   1 2 1780    U   A   U   C   U   G   G   U   U   G   A   U   C          
SEQRES   2 2 1780    C   U   G   C   C   A   G   U   A   G   U   C   A          
SEQRES   3 2 1780    U   A   U   G   C   U   U   G   U   C   U   C   A          
SEQRES   4 2 1780    A   A   G   A   U   U   A   A   G   C   C   A   U          
SEQRES   5 2 1780    G   C   A   U   G   U   C   U   A   A   G   U   A          
SEQRES   6 2 1780    U   A   A   G   C   A   A   U   U   U   A   U   A          
SEQRES   7 2 1780    C   A   G   U   G   A   A   A   C   U   G   C   G          
SEQRES   8 2 1780    A   A   U   G   G   C   U   C   A   U   U   A   A          
SEQRES   9 2 1780    A   U   C   A   G   U   U   A   U   C   G   U   U          
SEQRES  10 2 1780    U   A   U   U   U   G   A   U   A   G   U   U   C          
SEQRES  11 2 1780    C   U   U   U   A   C   U   A   C   A   U   G   G          
SEQRES  12 2 1780    A   U   A   U   C   U   G   U   G   G   U   A   A          
SEQRES  13 2 1780    U   U   C   U   A   G   A   G   C   U   A   A   U          
SEQRES  14 2 1780    A   C   A   U   G   C   U   U   A   A   A   A   U          
SEQRES  15 2 1780    C   U   C   G   A   C   C   C   U   U   U   G   G          
SEQRES  16 2 1780    A   A   G   A   G   A   U   G   U   A   U   U   U          
SEQRES  17 2 1780    A   U   U   A   G   A   U   A   A   A   A   A   A          
SEQRES  18 2 1780    U   C   A   A   U   G   U   C   U   U   C   G   G          
SEQRES  19 2 1780    A   C   U   C   C   U   U   G   A   U   G   A   U          
SEQRES  20 2 1780    U   C   A   U   A   A   U   A   A   C   U   U   U          
SEQRES  21 2 1780    U   C   G   A   A   U   C   G   C   A   U   G   G          
SEQRES  22 2 1780    C   C   U   U   G   U   G   C   U   G   G   C   G          
SEQRES  23 2 1780    A   U   G   G   U   U   C   A   U   U   C   A   A          
SEQRES  24 2 1780    A   U   U   U   C   U   G   C   C   C   U   A   U          
SEQRES  25 2 1780    C   A   A   C   U   U   U   C   G   A   U   G   G          
SEQRES  26 2 1780    U   A   G   G   A   U   A   G   U   G   G   C   C          
SEQRES  27 2 1780    U   A   C   C   A   U   G   G   U   U   U   C   A          
SEQRES  28 2 1780    A   C   G   G   G   U   A   A   C   G   G   G   G          
SEQRES  29 2 1780    A   A   U   A   A   G   G   G   U   U   C   G   A          
SEQRES  30 2 1780    U   U   C   C   G   G   A   G   A   G   G   G   A          
SEQRES  31 2 1780    G   C   C   U   G   A   G   A   A   A   C   G   G          
SEQRES  32 2 1780    C   U   A   C   C   A   C   A   U   C   C   A   A          
SEQRES  33 2 1780    G   G   A   A   G   G   C   A   G   C   A   G   G          
SEQRES  34 2 1780    C   G   C   G   C   A   A   A   U   U   A   C   C          
SEQRES  35 2 1780    C   A   A   U   C   C   U   A   A   U   U   C   A          
SEQRES  36 2 1780    G   G   G   A   G   G   U   A   G   U   G   A   C          
SEQRES  37 2 1780    A   A   U   A   A   A   U   A   A   C   G   A   U          
SEQRES  38 2 1780    A   C   A   G   G   G   C   C   C   A   U   U   C          
SEQRES  39 2 1780    G   G   G   U   C   U   U   G   U   A   A   U   U          
SEQRES  40 2 1780    G   G   A   A   U   G   A   G   U   A   C   A   A          
SEQRES  41 2 1780    U   G   U   A   A   A   U   A   C   C   U   U   A          
SEQRES  42 2 1780    A   C   G   A   G   G   A   A   C   A   A   C   U          
SEQRES  43 2 1780    G   G   A   G   G   G   C   A   A   G   U   C   U          
SEQRES  44 2 1780    G   G   U   G   C   C   A   G   C   A   G   C   C          
SEQRES  45 2 1780    G   C   G   G   U   A   A   U   U   C   C   A   G          
SEQRES  46 2 1780    C   U   C   C   A   G   U   A   G   C   G   U   A          
SEQRES  47 2 1780    U   A   U   U   A   A   A   G   U   U   G   U   U          
SEQRES  48 2 1780    G   C   A   G   U   U   A   A   A   A   A   G   C          
SEQRES  49 2 1780    U   C   G   U   A   G   U   U   G   A   A   C   U          
SEQRES  50 2 1780    U   U   G   G   G   U   C   U   G   G   U   U   G          
SEQRES  51 2 1780    U   C   C   G   G   U   C   G   G   U   U   U   U          
SEQRES  52 2 1780    U   C   A   A   C   C   G   G   A   U   C   U   U          
SEQRES  53 2 1780    U   C   C   U   U   C   U   G   G   C   U   A   A          
SEQRES  54 2 1780    C   C   U   G   U   A   C   U   C   C   U   U   G          
SEQRES  55 2 1780    U   G   G   G   U   G   C   A   G   G   C   G   A          
SEQRES  56 2 1780    A   C   C   A   G   G   A   C   U   U   U   U   A          
SEQRES  57 2 1780    C   U   U   U   G   A   A   A   A   A   A   U   U          
SEQRES  58 2 1780    A   G   A   G   U   G   U   U   C   A   A   A   G          
SEQRES  59 2 1780    C   A   G   G   C   G   A   A   A   G   C   U   C          
SEQRES  60 2 1780    G   A   A   U   A   U   A   U   U   A   G   C   A          
SEQRES  61 2 1780    U   G   G   A   A   U   A   A   U   G   G   A   A          
SEQRES  62 2 1780    U   A   G   G   A   C   G   U   U   U   G   G   U          
SEQRES  63 2 1780    U   C   U   A   U   U   U   U   G   U   U   G   G          
SEQRES  64 2 1780    U   U   U   C   U   A   G   G   A   C   C   A   U          
SEQRES  65 2 1780    C   G   U   A   A   U   G   A   U   U   A   A   U          
SEQRES  66 2 1780    A   G   G   G   A   C   G   G   U   C   G   G   G          
SEQRES  67 2 1780    G   G   C   A   U   C   A   G   U   A   U   U   C          
SEQRES  68 2 1780    A   A   U   U   G   U   C   A   G   A   G   G   U          
SEQRES  69 2 1780    G   A   A   A   U   U   C   U   U   G   G   A   U          
SEQRES  70 2 1780    U   U   A   U   U   G   A   A   G   A   C   U   A          
SEQRES  71 2 1780    A   C   U   A   C   U   G   C   G   A   A   A   G          
SEQRES  72 2 1780    C   A   U   U   U   G   C   C   A   A   G   G   A          
SEQRES  73 2 1780    C   G   U   U   U   U   C   A   U   U   A   A   U          
SEQRES  74 2 1780    C   A   A   G   A   A   C   G   A   A   A   G   U          
SEQRES  75 2 1780    U   A   G   G   G   G   A   U   C   G   A   A   G          
SEQRES  76 2 1780    A   U   G   A   U   C   A   G   A   U   A   C   C          
SEQRES  77 2 1780    G   U   C   G   U   A   G   U   C   U   U   A   A          
SEQRES  78 2 1780    C   C   A   U   A   A   A   C   U   A   U   G   C          
SEQRES  79 2 1780    C   G   A   C   U   A   G   G   G   A   U   C   G          
SEQRES  80 2 1780    G   G   U   G   G   U   G   U   U   U   U   U   C          
SEQRES  81 2 1780    U   U   A   U   G   A   C   C   C   A   C   U   C          
SEQRES  82 2 1780    G   G   C   A   C   C   U   U   A   C   G   A   G          
SEQRES  83 2 1780    A   A   A   U   C   A   A   A   G   U   C   U   U          
SEQRES  84 2 1780    U   G   G   G   U   U   C   U   G   G   G   G   G          
SEQRES  85 2 1780    G   A   G   U   A   U   G   G   U   C   G   C   A          
SEQRES  86 2 1780    A   G   G   C   U   G   A   A   A   C   U   U   A          
SEQRES  87 2 1780    A   A   G   G   A   A   U   U   G   A   C   G   G          
SEQRES  88 2 1780    A   A   G   G   G   C   A   C   C   A   C   C   A          
SEQRES  89 2 1780    G   G   A   G   U   G   G   A   G   C   C   U   G          
SEQRES  90 2 1780    C   G   G   C   U   U   A   A   U   U   U   G   A          
SEQRES  91 2 1780    C   U   C   A   A   C   A   C   G   G   G   G   A          
SEQRES  92 2 1780    A   A   C   U   C   A   C   C   A   G   G   U   C          
SEQRES  93 2 1780    C   A   G   A   C   A   C   A   A   U   A   A   G          
SEQRES  94 2 1780    G   A   U   U   G   A   C   A   G   A   U   U   G          
SEQRES  95 2 1780    A   G   A   G   C   U   C   U   U   U   C   U   U          
SEQRES  96 2 1780    G   A   U   U   U   U   G   U   G   G   G   U   G          
SEQRES  97 2 1780    G   U   G   G   U   G   C   A   U   G   G   C   C          
SEQRES  98 2 1780    G   U   U   C   U   U   A   G   U   U   G   G   U          
SEQRES  99 2 1780    G   G   A   G   U   G   A   U   U   U   G   U   C          
SEQRES 100 2 1780    U   G   C   U   U   A   A   U   U   G   C   G   A          
SEQRES 101 2 1780    U   A   A   C   G   A   A   C   G   A   G   A   C          
SEQRES 102 2 1780    C   U   U   A   A   C   C   U   A   C   U   A   A          
SEQRES 103 2 1780    A   U   A   G   G   G   U   U   G   C   U   G   G          
SEQRES 104 2 1780    C   A   C   U   U   G   C   C   G   G   U   U   G          
SEQRES 105 2 1780    A   C   U   C   U   U   C   U   U   A   G   A   G          
SEQRES 106 2 1780    G   G   A   C   U   A   U   C   G   G   U   U   U          
SEQRES 107 2 1780    C   A   A   G   C   C   G   A   U   G   G   A   A          
SEQRES 108 2 1780    G   U   U   U   G   A   G   G   C   A   A   U   A          
SEQRES 109 2 1780    A   C   A   G   G   U   C   U   G   U   G   A   U          
SEQRES 110 2 1780    G   C   C   C   U   U   A   G   A   C   G   U   U          
SEQRES 111 2 1780    C   U   G   G   G   C   C   G   C   A   C   G   C          
SEQRES 112 2 1780    G   C   G   C   U   A   C   A   C   U   G   A   C          
SEQRES 113 2 1780    G   G   A   G   C   C   A   G   C   G   A   G   U          
SEQRES 114 2 1780    A   C   A   A   C   C   U   U   G   G   C   C   G          
SEQRES 115 2 1780    A   G   A   G   G   U   C   U   G   G   G   U   A          
SEQRES 116 2 1780    A   U   C   U   U   G   U   G   A   A   A   C   U          
SEQRES 117 2 1780    C   C   G   U   C   G   U   G   C   U   G   G   G          
SEQRES 118 2 1780    G   A   U   A   G   A   G   C   A   U   U   G   U          
SEQRES 119 2 1780    A   A   U   U   A   U   U   G   C   U   C   U   U          
SEQRES 120 2 1780    C   A   A   C   G   A   G   G   A   A   U   U   C          
SEQRES 121 2 1780    C   U   A   G   U   A   A   G   C   G   C   A   A          
SEQRES 122 2 1780    G   U   C   A   U   C   A   G   C   U   U   G   C          
SEQRES 123 2 1780    G   U   U   G   A   U   U   A   C   G   U   C   C          
SEQRES 124 2 1780    C   U   G   C   C   C   U   U   U   G   U   A   C          
SEQRES 125 2 1780    A   C   A   C   C   G   C   C   C   G   U   C   G          
SEQRES 126 2 1780    C   U   A   G   U   A   C   C   G   A   U   U   G          
SEQRES 127 2 1780    A   A   U   G   G   C   U   U   A   G   U   G   A          
SEQRES 128 2 1780    G   G   C   C   U   C   A   G   G   A   U   U   U          
SEQRES 129 2 1780    G   C   U   U   A   G   A   G   A   A   G   G   G          
SEQRES 130 2 1780    G   G   C   A   A   C   U   C   C   A   U   C   U          
SEQRES 131 2 1780    C   A   G   A   G   C   G   A   A   G   A   A   U          
SEQRES 132 2 1780    C   U   G   G   U   C   A   A   A   C   U   U   G          
SEQRES 133 2 1780    G   U   C   A   U   U   U   A   G   A   G   G   A          
SEQRES 134 2 1780    A   C   U   A   A   A   A   G   U   C   G   U   A          
SEQRES 135 2 1780    A   C   A   A   G   G   U   U   U   C   C   G   U          
SEQRES 136 2 1780    A   G   G   U   G   A   A   C   C   U   G   C   G          
SEQRES 137 2 1780    G   A   A   G   G   A   U   C   A   U   U   A              
SEQRES   1 i  192    A   A   A   A   A   U   G   U   G   A   U   C   U          
SEQRES   2 i  192    U   G   C   U   U   G   U   A   A   A   U   A   C          
SEQRES   3 i  192    A   A   U   U   U   U   G   A   G   A   G   G   U          
SEQRES   4 i  192    U   A   A   U   A   A   A   U   U   A   C   A   A          
SEQRES   5 i  192    G   U   A   G   U   G   C   U   A   U   U   U   U          
SEQRES   6 i  192    U   G   U   A   U   U   U   A   G   G   U   U   A          
SEQRES   7 i  192    G   C   U   A   U   U   U   A   G   C   U   U   U          
SEQRES   8 i  192    A   C   G   U   U   C   C   A   G   G   A   U   G          
SEQRES   9 i  192    C   C   U   A   G   U   G   G   C   A   G   C   C          
SEQRES  10 i  192    C   C   A   C   A   A   U   A   U   C   C   A   G          
SEQRES  11 i  192    G   A   A   G   C   C   C   U   C   U   C   U   G          
SEQRES  12 i  192    C   G   G   C   U   U   U   U   C   A   G   A   U          
SEQRES  13 i  192    U   A   G   G   U   A   G   U   C   G   A   A   A          
SEQRES  14 i  192    A   A   C   C   U   A   A   G   A   A   A   U   U          
SEQRES  15 i  192    U   A   C   C   U   G   C   U   A   C                      
HET     MG  G 301       1                                                       
HET     MG  N 201       1                                                       
HET     MG  T 201       1                                                       
HET     MG  X 201       1                                                       
HET     ZN  a 201       1                                                       
HET     ZN  b 101       1                                                       
HET     ZN  f 501       1                                                       
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                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      ZN ZINC ION                                                         
FORMUL  36   MG    80(MG 2+)                                                    
FORMUL  40   ZN    3(ZN 2+)                                                     
HELIX    1 AA1 THR A   10  ARG A   21  1                                  12    
HELIX    2 AA2 ASN A   49  ILE A   67  1                                  19    
HELIX    3 AA3 ARG A   79  THR A   93  1                                  15    
HELIX    4 AA4 ASP A  129  TYR A  138  1                                  10    
HELIX    5 AA5 HIS A  168  LEU A  184  1                                  17    
HELIX    6 AA6 MET A  198  TYR A  202  5                                   5    
HELIX    7 AA7 ASN B   56  LYS B   62  1                                   7    
HELIX    8 AA8 LEU B   70  GLY B   75  1                                   6    
HELIX    9 AA9 SER B   76  SER B   80  5                                   5    
HELIX   10 AB1 THR B  106  VAL B  114  1                                   9    
HELIX   11 AB2 GLN B  157  VAL B  176  1                                  20    
HELIX   12 AB3 LEU B  181  ILE B  189  1                                   9    
HELIX   13 AB4 GLU B  191  LYS B  202  1                                  12    
HELIX   14 AB5 ASP B  224  HIS B  232  1                                   9    
HELIX   15 AB6 THR C   44  GLY C   53  1                                  10    
HELIX   16 AB7 SER C   57  HIS C   64  1                                   8    
HELIX   17 AB8 PHE C   71  LEU C   78  1                                   8    
HELIX   18 AB9 GLU C  125  VAL C  141  1                                  17    
HELIX   19 AC1 SER C  186  GLY C  197  1                                  12    
HELIX   20 AC2 THR C  211  TYR C  227  1                                  17    
HELIX   21 AC3 THR C  231  TRP C  235  5                                   5    
HELIX   22 AC4 SER C  243  TYR C  248  1                                   6    
HELIX   23 AC5 SER D    6  LEU D   29  1                                  24    
HELIX   24 AC6 LYS D   54  GLY D   60  1                                   7    
HELIX   25 AC7 ARG D   64  LYS D   78  1                                  15    
HELIX   26 AC8 ALA D   98  GLY D  112  1                                  15    
HELIX   27 AC9 ALA D  114  GLY D  130  1                                  17    
HELIX   28 AD1 PRO D  192  ASN D  195  5                                   4    
HELIX   29 AD2 PRO E   15  MET E   19  5                                   5    
HELIX   30 AD3 LYS E   37  SER E   41  5                                   5    
HELIX   31 AD4 PRO E   43  ASN E   50  1                                   8    
HELIX   32 AD5 ASN E   57  ARG E   68  1                                  12    
HELIX   33 AD6 LYS E  133  GLY E  135  5                                   3    
HELIX   34 AD7 GLY E  185  LEU E  189  5                                   5    
HELIX   35 AD8 THR E  247  GLN E  258  1                                  12    
HELIX   36 AD9 PRO F   32  ALA F   38  1                                   7    
HELIX   37 AE1 PHE F   84  CYS F   89  1                                   6    
HELIX   38 AE2 PRO F   90  MET F  100  1                                  11    
HELIX   39 AE3 ASN F  102  ASN F  106  5                                   5    
HELIX   40 AE4 LYS F  108  LEU F  126  1                                  19    
HELIX   41 AE5 ASN F  130  GLY F  143  1                                  14    
HELIX   42 AE6 SER F  165  PHE F  186  1                                  22    
HELIX   43 AE7 THR F  191  LYS F  205  1                                  15    
HELIX   44 AE8 SER F  210  ASN F  226  1                                  17    
HELIX   45 AE9 ASP G   20  ARG G   25  1                                   6    
HELIX   46 AF1 ARG G  137  GLY G  146  1                                  10    
HELIX   47 AF2 THR G  148  ASP G  152  5                                   5    
HELIX   48 AF3 THR G  180  ALA G  224  1                                  45    
HELIX   49 AF4 THR H   14  ASN H   29  1                                  16    
HELIX   50 AF5 GLU H   33  ALA H   40  1                                   8    
HELIX   51 AF6 SER H   66  GLN H   74  1                                   9    
HELIX   52 AF7 GLN H   74  PHE H   85  1                                  12    
HELIX   53 AF8 THR H  117  VAL H  130  1                                  14    
HELIX   54 AF9 HIS H  161  THR H  177  1                                  17    
HELIX   55 AG1 ASN I   88  THR I   93  1                                   6    
HELIX   56 AG2 ALA I  106  TYR I  117  1                                  12    
HELIX   57 AG3 SER I  137  ARG I  147  1                                  11    
HELIX   58 AG4 HIS I  155  GLY I  164  1                                  10    
HELIX   59 AG5 ARG I  173  GLY I  178  1                                   6    
HELIX   60 AG6 GLU I  186  LYS I  201  1                                  16    
HELIX   61 AG7 GLU J   20  TYR J   34  1                                  15    
HELIX   62 AG8 ASN J   38  ARG J   62  1                                  25    
HELIX   63 AG9 ASP J   66  GLY J   84  1                                  19    
HELIX   64 AH1 LYS J  100  ARG J  107  1                                   8    
HELIX   65 AH2 ARG J  108  LYS J  115  1                                   8    
HELIX   66 AH3 VAL J  122  GLN J  131  1                                  10    
HELIX   67 AH4 ARG J  171  GLU J  183  1                                  13    
HELIX   68 AH5 PRO K    4  GLY K   19  1                                  16    
HELIX   69 AH6 LYS K   38  LYS K   52  1                                  15    
HELIX   70 AH7 PHE K   59  TRP K   61  5                                   3    
HELIX   71 AH8 THR K   69  ASN K   81  1                                  13    
HELIX   72 AH9 PRO L   45  GLY L   51  1                                   7    
HELIX   73 AI1 LEU M   21  ASP M   32  1                                  12    
HELIX   74 AI2 GLY M   37  ARG M   47  1                                  11    
HELIX   75 AI3 VAL M   59  GLU M   61  5                                   3    
HELIX   76 AI4 GLU M   62  ASN M   75  1                                  14    
HELIX   77 AI5 ALA M   85  GLY M   93  1                                   9    
HELIX   78 AI6 THR M  121  GLN M  133  1                                  13    
HELIX   79 AI7 SER N   29  GLY N   44  1                                  16    
HELIX   80 AI8 THR N   46  HIS N   58  1                                  13    
HELIX   81 AI9 GLN N   62  THR N   67  1                                   6    
HELIX   82 AJ1 ILE N   71  GLY N   79  1                                   9    
HELIX   83 AJ2 PRO N   85  ASN N  105  1                                  21    
HELIX   84 AJ3 ASP N  108  SER N  133  1                                  26    
HELIX   85 AJ4 SER N  143  ASN N  151  1                                   9    
HELIX   86 AJ5 THR O   43  VAL O   48  1                                   6    
HELIX   87 AJ6 SER O   56  GLY O   75  1                                  20    
HELIX   88 AJ7 PRO O   96  GLY O  109  1                                  14    
HELIX   89 AJ8 ASP P   21  LEU P   26  1                                   6    
HELIX   90 AJ9 MET P   28  LEU P   36  1                                   9    
HELIX   91 AK1 PRO P   38  ARG P   47  1                                  10    
HELIX   92 AK2 ALA P   54  SER P   66  1                                  13    
HELIX   93 AK3 VAL P   86  ILE P   90  5                                   5    
HELIX   94 AK4 LEU P  116  SER P  120  5                                   5    
HELIX   95 AK5 LEU Q   44  GLY Q   56  1                                  13    
HELIX   96 AK6 LEU Q   57  ALA Q   61  5                                   5    
HELIX   97 AK7 HIS Q   74  VAL Q   97  1                                  24    
HELIX   98 AK8 ASP Q   98  TYR Q  112  1                                  15    
HELIX   99 AK9 THR R    6  TYR R   20  1                                  15    
HELIX  100 AL1 ASP R   27  ALA R   39  1                                  13    
HELIX  101 AL2 LYS R   44  LYS R   63  1                                  20    
HELIX  102 AL3 LYS R   72  TYR R   84  1                                  13    
HELIX  103 AL4 ASP R  103  GLY R  114  1                                  12    
HELIX  104 AL5 ASN S   27  ILE S   35  1                                   9    
HELIX  105 AL6 GLY S   39  ASP S   51  1                                  13    
HELIX  106 AL7 THR S   62  ASN S   75  1                                  14    
HELIX  107 AL8 ALA S  102  ARG S  120  1                                  19    
HELIX  108 AL9 SER S  121  GLY S  130  1                                  10    
HELIX  109 AM1 ALA T   11  GLY T   26  1                                  16    
HELIX  110 AM2 TRP T   53  ARG T   68  1                                  16    
HELIX  111 AM3 GLY T   72  GLY T   81  1                                  10    
HELIX  112 AM4 SER T   97  GLY T  112  1                                  16    
HELIX  113 AM5 SER T  125  GLU T  144  1                                  20    
HELIX  114 AM6 LYS U   30  LYS U   49  1                                  20    
HELIX  115 AM7 PRO U   96  ILE U  106  1                                  11    
HELIX  116 AM8 SER V   56  GLY V   63  1                                   8    
HELIX  117 AM9 GLU V   64  GLY V   77  1                                  14    
HELIX  118 AN1 SER W    5  GLY W   21  1                                  17    
HELIX  119 AN2 SER W   31  GLY W   45  1                                  15    
HELIX  120 AN3 ALA W   84  LEU W   94  1                                  11    
HELIX  121 AN4 ASP W  112  HIS W  120  1                                   9    
HELIX  122 AN5 SER X   11  TRP X   24  1                                  14    
HELIX  123 AN6 GLU X   26  GLY X   35  1                                  10    
HELIX  124 AN7 GLY X   35  SER X   40  1                                   6    
HELIX  125 AN8 CYS X   92  ASP X   97  1                                   6    
HELIX  126 AN9 SER X  131  GLU X  138  1                                   8    
HELIX  127 AO1 SER Y   36  LYS Y   49  1                                  14    
HELIX  128 AO2 GLU Y   51  ASP Y   53  5                                   3    
HELIX  129 AO3 SER Y   78  GLU Y   86  1                                   9    
HELIX  130 AO4 PRO Y   87  GLY Y   95  1                                   9    
HELIX  131 AO5 SER Y  104  ILE Y  118  1                                  15    
HELIX  132 AO6 THR Y  121  ASP Y  135  1                                  15    
HELIX  133 AO7 ASP Z   43  LYS Z   52  1                                  10    
HELIX  134 AO8 SER Z   61  VAL Z   66  1                                   6    
HELIX  135 AO9 GLY Z   72  GLU Z   84  1                                  13    
HELIX  136 AP1 ALA a   48  SER a   57  1                                  10    
HELIX  137 AP2 CYS a   74  HIS a   80  1                                   7    
HELIX  138 AP3 ARG a   89  ILE a   94  5                                   6    
HELIX  139 AP4 THR b   11  LYS b   18  1                                   8    
HELIX  140 AP5 ARG d   32  LEU d   36  5                                   5    
HELIX  141 AP6 ARG d   40  ALA d   47  1                                   8    
HELIX  142 AP7 GLY e   12  THR e   18  1                                   7    
HELIX  143 AP8 GLY e   32  PHE e   44  1                                  13    
SHEET    1 AA1 5 ILE A  98  ALA A  99  0                                        
SHEET    2 AA1 5 VAL A  73  SER A  77  1  N  SER A  77   O  ILE A  98           
SHEET    3 AA1 5 LEU A 120  ILE A 122  1  O  ILE A 122   N  VAL A  74           
SHEET    4 AA1 5 VAL A 143  ALA A 145  1  O  ILE A 144   N  VAL A 121           
SHEET    5 AA1 5 ASP A 157  ALA A 159  1  O  ASP A 157   N  VAL A 143           
SHEET    1 AA2 5 LYS B  45  VAL B  48  0                                        
SHEET    2 AA2 5 GLU B  28  LYS B  33 -1  N  GLU B  28   O  VAL B  48           
SHEET    3 AA2 5 LEU B  96  ASP B 104  1  O  LEU B  96   N  LYS B  33           
SHEET    4 AA2 5 LYS B  83  VAL B  91 -1  N  LYS B  83   O  ASP B 104           
SHEET    5 AA2 5 VAL B  65  CYS B  69 -1  N  VAL B  66   O  LEU B  86           
SHEET    1 AA3 3 LEU B 120  ILE B 121  0                                        
SHEET    2 AA3 3 ILE B 140  PHE B 142 -1  O  ALA B 141   N  ILE B 121           
SHEET    3 AA3 3 GLN B 208  HIS B 211 -1  O  HIS B 211   N  ILE B 140           
SHEET    1 AA4 3 VAL B 125  LYS B 128  0                                        
SHEET    2 AA4 3 VAL B 134  ILE B 137 -1  O  LEU B 135   N  VAL B 127           
SHEET    3 AA4 3 VAL B 215  LEU B 217 -1  O  LYS B 216   N  ARG B 136           
SHEET    1 AA5 4 LYS C  82  GLN C  94  0                                        
SHEET    2 AA5 4 GLN C  99  GLY C 110 -1  O  VAL C 108   N  GLU C  84           
SHEET    3 AA5 4 HIS C 115  ALA C 123 -1  O  GLY C 119   N  VAL C 107           
SHEET    4 AA5 4 ILE C 142  PRO C 143 -1  O  ILE C 142   N  VAL C 116           
SHEET    1 AA6 2 ARG C 146  GLY C 147  0                                        
SHEET    2 AA6 2 SER C 158  LEU C 159 -1  O  SER C 158   N  GLY C 147           
SHEET    1 AA7 4 THR C 163  SER C 164  0                                        
SHEET    2 AA7 4 ARG C 173  PRO C 176 -1  O  LEU C 174   N  THR C 163           
SHEET    3 AA7 4 VAL C 201  THR C 203 -1  O  TYR C 202   N  ILE C 175           
SHEET    4 AA7 4 ILE C 183  VAL C 184  1  N  VAL C 184   O  VAL C 201           
SHEET    1 AA8 2 VAL C 170  SER C 171  0                                        
SHEET    2 AA8 2 THR C 206  GLY C 207 -1  O  THR C 206   N  SER C 171           
SHEET    1 AA9 3 TYR D  34  VAL D  41  0                                        
SHEET    2 AA9 3 THR D  46  ALA D  52 -1  O  ILE D  49   N  GLU D  38           
SHEET    3 AA9 3 ILE D  84  GLU D  89  1  O  ALA D  85   N  ILE D  48           
SHEET    1 AB1 4 LYS D 148  GLY D 155  0                                        
SHEET    2 AB1 4 ALA D 131  GLY D 140 -1  N  GLY D 140   O  LYS D 148           
SHEET    3 AB1 4 VAL D 181  LYS D 190 -1  O  LYS D 187   N  GLU D 135           
SHEET    4 AB1 4 ILE D 168  LEU D 176 -1  N  GLU D 169   O  ILE D 188           
SHEET    1 AB2 5 LYS D 223  ASP D 224  0                                        
SHEET    2 AB2 5 ILE g 195  PHE g 199 -1  O  ASP g 198   N  LYS D 223           
SHEET    3 AB2 5 VAL g 183  LEU g 188 -1  N  SER g 185   O  ALA g 197           
SHEET    4 AB2 5 ILE g 172  GLY g 178 -1  N  SER g 176   O  ARG g 184           
SHEET    5 AB2 5 VAL g 152  ALA g 158 -1  N  ALA g 158   O  THR g 173           
SHEET    1 AB3 2 LEU E   9  LYS E  10  0                                        
SHEET    2 AB3 2 TYR E  27  ALA E  28 -1  O  ALA E  28   N  LEU E   9           
SHEET    1 AB4 4 VAL E  70  VAL E  72  0                                        
SHEET    2 AB4 4 VAL E  89  LEU E  92 -1  O  THR E  91   N  LYS E  71           
SHEET    3 AB4 4 GLU E  97  TYR E 103 -1  O  PHE E  99   N  ILE E  90           
SHEET    4 AB4 4 PHE E 109  ILE E 114 -1  O  ALA E 110   N  VAL E 102           
SHEET    1 AB5 3 LYS E 122  LYS E 125  0                                        
SHEET    2 AB5 3 THR E 159  VAL E 162 -1  O  VAL E 162   N  LYS E 122           
SHEET    3 AB5 3 ASP E 171  ILE E 173 -1  O  ILE E 173   N  THR E 159           
SHEET    1 AB6 3 LYS E 128  LEU E 131  0                                        
SHEET    2 AB6 3 PRO E 137  VAL E 140 -1  O  TYR E 138   N  GLN E 130           
SHEET    3 AB6 3 THR E 146  ARG E 148 -1  O  ILE E 147   N  VAL E 139           
SHEET    1 AB7 3 VAL E 192  GLY E 193  0                                        
SHEET    2 AB7 3 VAL E 181  VAL E 183 -1  N  VAL E 181   O  GLY E 193           
SHEET    3 AB7 3 VAL E 225  VAL E 227 -1  O  PHE E 226   N  TYR E 182           
SHEET    1 AB8 2 LEU E 207  LYS E 211  0                                        
SHEET    2 AB8 2 THR E 217  ARG E 221 -1  O  PHE E 218   N  ILE E 210           
SHEET    1 AB9 2 GLY E 229  GLU E 230  0                                        
SHEET    2 AB9 2 ARG E 233  PRO E 234 -1  O  ARG E 233   N  GLU E 230           
SHEET    1 AC1 2 GLU F 146  ARG F 150  0                                        
SHEET    2 AC1 2 ARG F 159  ASP F 163 -1  O  VAL F 162   N  ASP F 147           
SHEET    1 AC2 5 THR G  12  GLU G  17  0                                        
SHEET    2 AC2 5 LYS G   2  TYR G   7 -1  N  ILE G   5   O  LYS G  14           
SHEET    3 AC2 5 LEU G 106  LYS G 115  1  O  LEU G 111   N  ASN G   4           
SHEET    4 AC2 5 VAL G  49  ASP G  57 -1  N  LYS G  51   O  ILE G 112           
SHEET    5 AC2 5 GLN G  34  ASP G  37 -1  N  VAL G  36   O  PHE G  50           
SHEET    1 AC3 2 ARG G  72  LEU G  77  0                                        
SHEET    2 AC3 2 LYS G  93  ARG G  98 -1  O  VAL G  97   N  VAL G  73           
SHEET    1 AC4 2 ARG G 160  THR G 163  0                                        
SHEET    2 AC4 2 SER G 168  LYS G 171 -1  O  TYR G 169   N  VAL G 162           
SHEET    1 AC5 3 SER H  45  GLU H  50  0                                        
SHEET    2 AC5 3 LYS H  56  VAL H  62 -1  O  ALA H  57   N  ILE H  49           
SHEET    3 AC5 3 ARG H  88  ALA H  94  1  O  ILE H  91   N  LEU H  58           
SHEET    1 AC6 6 GLN H 180  GLU H 184  0                                        
SHEET    2 AC6 6 LYS H 148  LEU H 154  1  N  ILE H 152   O  VAL H 182           
SHEET    3 AC6 6 ILE H 135  TYR H 142 -1  N  GLY H 137   O  LEU H 153           
SHEET    4 AC6 6 ILE W  47  ILE W  53 -1  O  PHE W  50   N  TYR H 142           
SHEET    5 AC6 6 LYS W  60  LEU W  65 -1  O  GLN W  64   N  GLU W  49           
SHEET    6 AC6 6 GLN W  24  ILE W  27 -1  N  ILE W  27   O  ILE W  61           
SHEET    1 AC7 2 ARG I  42  HIS I  44  0                                        
SHEET    2 AC7 2 ARG I  56  LEU I  58 -1  O  LEU I  58   N  ARG I  42           
SHEET    1 AC8 2 ARG I  47  THR I  48  0                                        
SHEET    2 AC8 2 GLY I  51  GLN I  53 -1  O  GLY I  51   N  THR I  48           
SHEET    1 AC9 4 ILE I  78  TYR I  83  0                                        
SHEET    2 AC9 4 ILE I 101  ILE I 104 -1  O  ILE I 101   N  TYR I  83           
SHEET    3 AC9 4 LEU I 166  ILE I 170 -1  O  ALA I 168   N  VAL I 102           
SHEET    4 AC9 4 GLY I 182  ILE I 184 -1  O  TYR I 183   N  ALA I 169           
SHEET    1 AD1 3 LEU K  21  LYS K  24  0                                        
SHEET    2 AD1 3 TYR K  63  LEU K  68 -1  O  TYR K  64   N  ALA K  23           
SHEET    3 AD1 3 VAL K  55  GLN K  58 -1  N  GLN K  58   O  TYR K  65           
SHEET    1 AD2 6 ILE L  70  SER L  77  0                                        
SHEET    2 AD2 6 THR L  83  ARG L  87 -1  O  VAL L  85   N  VAL L  76           
SHEET    3 AD2 6 ASN L 106  HIS L 110 -1  O  ALA L 109   N  ILE L  84           
SHEET    4 AD2 6 PHE L 137  VAL L 142  1  O  VAL L 139   N  HIS L 110           
SHEET    5 AD2 6 ILE L 122  GLN L 127 -1  N  THR L 124   O  LYS L 141           
SHEET    6 AD2 6 ILE L  70  SER L  77 -1  N  LEU L  71   O  VAL L 125           
SHEET    1 AD3 2 TYR L  90  VAL L  94  0                                        
SHEET    2 AD3 2 ARG L  99  ARG L 103 -1  O  ARG L 103   N  TYR L  90           
SHEET    1 AD4 3 LEU M  34  ARG M  36  0                                        
SHEET    2 AD4 3 VAL M 112  VAL M 114 -1  O  VAL M 113   N  ALA M  35           
SHEET    3 AD4 3 LEU M  52  VAL M  54 -1  N  VAL M  54   O  VAL M 112           
SHEET    1 AD5 4 ASP O  25  THR O  26  0                                        
SHEET    2 AD5 4 ILE O  19  SER O  22 -1  N  SER O  22   O  ASP O  25           
SHEET    3 AD5 4 LYS O  82  ARG O  84  1  O  LYS O  82   N  ILE O  19           
SHEET    4 AD5 4 GLU O 116  ASP O 117  1  O  GLU O 116   N  ILE O  83           
SHEET    1 AD6 2 VAL O  30  THR O  31  0                                        
SHEET    2 AD6 2 THR O  38  ALA O  40 -1  O  ILE O  39   N  VAL O  30           
SHEET    1 AD7 2 ALA O  78  VAL O  79  0                                        
SHEET    2 AD7 2 ARG O 111  ILE O 112  1  O  ARG O 111   N  VAL O  79           
SHEET    1 AD8 3 VAL P  76  THR P  78  0                                        
SHEET    2 AD8 3 VAL P  93  TYR P  97  1  O  VAL P  93   N  VAL P  76           
SHEET    3 AD8 3 PHE P 102  GLU P 106 -1  O  VAL P 105   N  VAL P  94           
SHEET    1 AD9 5 VAL Q   7  LYS Q  13  0                                        
SHEET    2 AD9 5 ALA Q  16  ALA Q  24 -1  O  ALA Q  20   N  THR Q   9           
SHEET    3 AD9 5 ILE Q  63  THR Q  70 -1  O  THR Q  70   N  THR Q  17           
SHEET    4 AD9 5 ILE Q  29  VAL Q  31  1  N  LYS Q  30   O  ILE Q  65           
SHEET    5 AD9 5 SER Q  34  PRO Q  35 -1  O  SER Q  34   N  VAL Q  31           
SHEET    1 AE1 2 LEU S  15  LEU S  17  0                                        
SHEET    2 AE1 2 THR S  20  VAL S  22 -1  O  THR S  20   N  LEU S  17           
SHEET    1 AE2 2 VAL T 114  ILE T 116  0                                        
SHEET    2 AE2 2 ARG T 122  ILE T 124 -1  O  ARG T 123   N  GLU T 115           
SHEET    1 AE3 4 VAL U  51  ARG U  68  0                                        
SHEET    2 AE3 4 TRP U  79  GLU U  94 -1  O  TYR U  82   N  ILE U  65           
SHEET    3 AE3 4 ILE U  22  SER U  28 -1  N  ILE U  22   O  LEU U  93           
SHEET    4 AE3 4 ASP U 113  VAL U 116 -1  O  ASP U 113   N  THR U  27           
SHEET    1 AE4 3 VAL U  51  ARG U  68  0                                        
SHEET    2 AE4 3 TRP U  79  GLU U  94 -1  O  TYR U  82   N  ILE U  65           
SHEET    3 AE4 3 TYR d  53  LYS d  54 -1  O  TYR d  53   N  GLU U  83           
SHEET    1 AE5 2 VAL V  32  ALA V  37  0                                        
SHEET    2 AE5 2 TYR V  50  LEU V  55 -1  O  TYR V  53   N  ILE V  34           
SHEET    1 AE6 3 GLY W 109  MET W 111  0                                        
SHEET    2 AE6 3 LEU W 104  THR W 106 -1  N  LEU W 104   O  MET W 111           
SHEET    3 AE6 3 LYS W 124  ILE W 125 -1  O  LYS W 124   N  THR W 105           
SHEET    1 AE7 6 HIS X  48  ILE X  57  0                                        
SHEET    2 AE7 6 CYS X  71  LEU X  76 -1  O  ARG X  73   N  GLU X  55           
SHEET    3 AE7 6 LYS X  82  PHE X  86 -1  O  VAL X  83   N  VAL X  74           
SHEET    4 AE7 6 PHE X 122  VAL X 127  1  O  VAL X 124   N  PHE X  86           
SHEET    5 AE7 6 GLU X 101  GLY X 106 -1  N  LEU X 103   O  VAL X 125           
SHEET    6 AE7 6 HIS X  48  ILE X  57 -1  N  ALA X  49   O  LEU X 104           
SHEET    1 AE8 4 ILE Y   7  ASN Y  15  0                                        
SHEET    2 AE8 4 ARG Y  20  LEU Y  28 -1  O  ARG Y  20   N  ASN Y  15           
SHEET    3 AE8 4 LYS Y  68  TYR Y  76 -1  O  GLY Y  73   N  PHE Y  23           
SHEET    4 AE8 4 VAL Y  55  THR Y  62 -1  N  PHE Y  58   O  PHE Y  72           
SHEET    1 AE9 2 ILE Z  89  PRO Z  91  0                                        
SHEET    2 AE9 2 TYR Z 101  ARG Z 103 -1  O  THR Z 102   N  LYS Z  90           
SHEET    1 AF1 2 PRO a  20  ARG a  22  0                                        
SHEET    2 AF1 2 SER a  29  PRO a  31 -1  O  VAL a  30   N  VAL a  21           
SHEET    1 AF2 2 LYS a  37  ASN a  43  0                                        
SHEET    2 AF2 2 LYS a  66  HIS a  72 -1  O  ASN a  69   N  ALA a  40           
SHEET    1 AF3 3 ILE b  43  PHE b  47  0                                        
SHEET    2 AF3 3 PHE b  32  LYS b  36 -1  N  VAL b  35   O  THR b  44           
SHEET    3 AF3 3 SER b  78  ARG b  80 -1  O  SER b  78   N  LYS b  36           
SHEET    1 AF4 2 CYS b  64  THR b  65  0                                        
SHEET    2 AF4 2 LYS b  72  LEU b  73 -1  O  LYS b  72   N  THR b  65           
SHEET    1 AF5 4 THR c  39  VAL c  44  0                                        
SHEET    2 AF5 4 VAL c  25  GLU c  31 -1  N  VAL c  28   O  ARG c  42           
SHEET    3 AF5 4 THR c   8  THR c  19 -1  N  THR c  19   O  VAL c  25           
SHEET    4 AF5 4 ILE c  53  LEU c  56 -1  O  LEU c  56   N  THR c   8           
SHEET    1 AF6 2 LEU d  30  ILE d  31  0                                        
SHEET    2 AF6 2 ILE d  38  ASP d  39 -1  O  ILE d  38   N  ILE d  31           
SHEET    1 AF7 2 ALA f 131  HIS f 133  0                                        
SHEET    2 AF7 2 ARG f 136  TYR f 138 -1  O  TYR f 138   N  ALA f 131           
SHEET    1 AF8 4 VAL g   9  LEU g  14  0                                        
SHEET    2 AF8 4 ILE g 317  GLN g 321 -1  O  VAL g 319   N  GLY g  12           
SHEET    3 AF8 4 THR g 307  TYR g 312 -1  N  ALA g 310   O  ARG g 318           
SHEET    4 AF8 4 ALA g 296  TRP g 301 -1  N  ALA g 300   O  PHE g 309           
SHEET    1 AF9 4 SER g  23  SER g  25  0                                        
SHEET    2 AF9 4 LEU g  33  GLY g  37 -1  O  GLY g  37   N  SER g  23           
SHEET    3 AF9 4 LEU g  43  LEU g  48 -1  O  ILE g  44   N  SER g  36           
SHEET    4 AF9 4 GLY g  56  SER g  61 -1  O  ARG g  60   N  SER g  45           
SHEET    1 AG1 4 VAL g  69  VAL g  74  0                                        
SHEET    2 AG1 4 TYR g  80  SER g  85 -1  O  VAL g  82   N  VAL g  73           
SHEET    3 AG1 4 LEU g  90  ASN g  94 -1  O  TRP g  93   N  ALA g  81           
SHEET    4 AG1 4 ASN g  99  PHE g 104 -1  O  ALA g 102   N  LEU g  92           
SHEET    1 AG2 4 VAL g 111  ALA g 115  0                                        
SHEET    2 AG2 4 ILE g 123  SER g 127 -1  O  ALA g 126   N  SER g 113           
SHEET    3 AG2 4 ILE g 132  TRP g 135 -1  O  ARG g 133   N  SER g 125           
SHEET    4 AG2 4 CYS g 141  LEU g 145 -1  O  LEU g 145   N  ILE g 132           
SHEET    1 AG3 4 ILE g 206  PRO g 211  0                                        
SHEET    2 AG3 4 LEU g 217  GLY g 222 -1  O  ALA g 219   N  GLN g 210           
SHEET    3 AG3 4 GLN g 226  ASN g 231 -1  O  TYR g 228   N  SER g 220           
SHEET    4 AG3 4 SER g 236  ASP g 242 -1  O  PHE g 241   N  ILE g 227           
SHEET    1 AG4 4 VAL g 247  PHE g 252  0                                        
SHEET    2 AG4 4 TRP g 258  THR g 263 -1  O  ALA g 262   N  PHE g 248           
SHEET    3 AG4 4 ILE g 267  ASP g 271 -1  O  TYR g 270   N  LEU g 259           
SHEET    4 AG4 4 VAL g 276  LEU g 281 -1  O  LEU g 281   N  ILE g 267           
LINK         OE1 GLN G 176                MG    MG G 301     1555   1555  2.60  
LINK         OD1 ASN T  85                MG    MG T 201     1555   1555  2.55  
LINK         O   PRO X  64                MG    MG X 201     1555   1555  2.22  
LINK         SG  CYS a  23                ZN    ZN a 201     1555   1555  2.05  
LINK         SG  CYS a  26                ZN    ZN a 201     1555   1555  2.82  
LINK         SG  CYS a  74                ZN    ZN a 201     1555   1555  2.80  
LINK         SG  CYS b  59                ZN    ZN b 101     1555   1555  2.54  
LINK         OP1   G 2  16                MG    MG 21816     1555   1555  2.22  
LINK         OP1   A 2  28                MG    MG 21818     1555   1555  2.56  
LINK         O3'   A 2  43                MG    MG 21822     1555   1555  2.86  
LINK         OP1   U 2  44                MG    MG 21822     1555   1555  2.17  
LINK         OP2   U 2  44                MG    MG 21822     1555   1555  2.90  
LINK         OP2   A 2  47                MG    MG 21822     1555   1555  2.75  
LINK         OP2   C 2  49                MG    MG 21808     1555   1555  2.29  
LINK         O4    U 2  58                MG    MG 21843     1555   1555  2.97  
LINK         OP2   G 2  95                MG    MG 21833     1555   1555  2.32  
LINK         OP1   A 2 100                MG    MG 21805     1555   1555  2.31  
LINK         OP2   A 2 100                MG    MG 21829     1555   1555  2.39  
LINK         OP2   U 2 101                MG    MG 21829     1555   1555  2.23  
LINK         OP1   U 2 118                MG    MG 21869     1555   1555  2.74  
LINK         OP2   A 2 212                MG    MG 21850     1555   1555  2.17  
LINK         OP1   C 2 249                MG    MG 21870     1555   1555  2.05  
LINK         OP2   A 2 250                MG    MG 21870     1555   1555  1.94  
LINK         OP1   C 2 267                MG    MG G 301     1555   1555  2.08  
LINK         OP2   C 2 360                MG    MG 21829     1555   1555  1.94  
LINK         OP1   G 2 361                MG    MG 21802     1555   1555  2.29  
LINK         OP2   A 2 377                MG    MG 21817     1555   1555  2.39  
LINK         OP2   U 2 378                MG    MG 21817     1555   1555  2.46  
LINK         OP2   A 2 400                MG    MG 21815     1555   1555  1.95  
LINK         OP1   G 2 402                MG    MG 21803     1555   1555  2.43  
LINK         OP2   C 2 423                MG    MG 21871     1555   1555  2.25  
LINK         OP2   A 2 459                MG    MG 21836     1555   1555  1.98  
LINK         OP2   G 2 460                MG    MG 21836     1555   1555  2.23  
LINK         OP2   G 2 466                MG    MG 21837     1555   1555  1.93  
LINK         OP1   G 2 551                MG    MG 21804     1555   1555  2.57  
LINK         OP2   A 2 554                MG    MG 21804     1555   1555  2.87  
LINK         OP2   A 2 555                MG    MG 21804     1555   1555  2.34  
LINK         OP2   A 2 603                MG    MG 21872     1555   1555  2.64  
LINK         OP1   A 2 604                MG    MG 21819     1555   1555  2.08  
LINK         OP1   A 2 618                MG    MG 21826     1555   1555  2.44  
LINK         OP2   A 2 620                MG    MG 21824     1555   1555  1.93  
LINK         OP1   A 2 622                MG    MG 21828     1555   1555  2.39  
LINK         OP2   A 2 622                MG    MG 21828     1555   1555  2.99  
LINK         OP2   G 2 623                MG    MG 21806     1555   1555  2.55  
LINK         OP1   A 2 634                MG    MG 21873     1555   1555  2.49  
LINK         OP2   A 2 635                MG    MG 21873     1555   1555  2.15  
LINK         OP2   A 2 760                MG    MG 21844     1555   1555  2.88  
LINK         OP2   A 2 928                MG    MG 21812     1555   1555  1.87  
LINK         OP1   A 2 940                MG    MG 21801     1555   1555  1.83  
LINK         OP2   U 2 967                MG    MG 21874     1555   1555  2.73  
LINK         OP2   A 2 970                MG    MG 21875     1555   1555  2.76  
LINK         OP2   A 2 978                MG    MG 21842     1555   1555  2.74  
LINK         OP1   U 2 988                MG    MG 21849     1555   1555  2.77  
LINK         OP2   U 2 988                MG    MG 21849     1555   1555  2.89  
LINK         OP2   A 2 991                MG    MG 21840     1555   1555  2.87  
LINK         OP1   A 21004                MG    MG 21809     1555   1555  2.66  
LINK         OP2   A 21004                MG    MG 21809     1555   1555  2.95  
LINK         O6    G 21010                MG    MG 21840     1555   1555  2.51  
LINK         OP2   A 21024                MG    MG 21806     1555   1555  2.28  
LINK         OP1   G 21175                MG    MG 21857     1555   1555  1.96  
LINK         OP2   G 21175                MG    MG 21857     1555   1555  2.14  
LINK         O5'   G 21175                MG    MG 21857     1555   1555  2.92  
LINK         O3'   A 21195                MG    MG 21860     1555   1555  2.99  
LINK         OP1   C 21196                MG    MG 21860     1555   1555  3.00  
LINK         OP1   A 21201                MG    MG 21866     1555   1555  2.60  
LINK         OP2   A 21202                MG    MG 21866     1555   1555  1.97  
LINK         OP1   U 21268                MG    MG 21861     1555   1555  2.24  
LINK         OP2   U 21268                MG    MG 21861     1555   1555  2.04  
LINK         OP1   C 21273                MG    MG 21865     1555   1555  1.96  
LINK         OP2   C 21273                MG    MG 21862     1555   1555  1.91  
LINK         OP1   U 21282                MG    MG 21855     1555   1555  2.05  
LINK         OP2   U 21302                MG    MG 21841     1555   1555  2.23  
LINK         OP2   G 21327                MG    MG 21827     1555   1555  1.99  
LINK         OP2   G 21329                MG    MG 21810     1555   1555  2.18  
LINK         O6    G 21329                MG    MG 21827     1555   1555  2.55  
LINK         OP1   G 21426                MG    MG 21865     1555   1555  2.65  
LINK         OP1   G 21427                MG    MG 21865     1555   1555  2.57  
LINK         OP2   G 21427                MG    MG 21865     1555   1555  1.90  
LINK         OP1   A 21467                MG    MG T 201     1555   1555  2.59  
LINK         OP2   G 21537                MG    MG 21863     1555   1555  1.98  
LINK         O6    G 21539                MG    MG 21863     1555   1555  2.24  
LINK         O2    C 21600                MG    MG 21858     1555   1555  2.90  
LINK         O3'   G 21627                MG    MG 21835     1555   1555  2.94  
LINK         OP1   U 21628                MG    MG 21835     1555   1555  1.89  
LINK         O4    U 21726                MG    MG 21834     1555   1555  2.71  
LINK         OP2   A 21760                MG    MG 21823     1555   1555  2.07  
LINK         OP1   A 21761                MG    MG 21813     1555   1555  2.14  
LINK         OP2   A 21761                MG    MG 21823     1555   1555  2.15  
LINK         O2'   G 21765                MG    MG 21823     1555   1555  2.87  
LINK         OP2   G 21766                MG    MG 21823     1555   1555  2.37  
LINK         OP2   U 21768                MG    MG 21832     1555   1555  1.96  
LINK         O3'   U 21768                MG    MG 21813     1555   1555  2.87  
LINK         OP1   U 21769                MG    MG 21813     1555   1555  1.92  
LINK         OP1   G 21791                MG    MG 21835     1555   1555  2.74  
CISPEP   1 ASP R   87    VAL R   88          0        17.33                     
CISPEP   2 LEU R   91    ASP R   92          0         9.96                     
CISPEP   3 LYS Z   52    GLU Z   53          0        -1.30                     
CISPEP   4 VAL Z   66    ASP Z   67          0        -1.23                     
CISPEP   5 ALA Z  104    THR Z  105          0         0.31                     
SITE     1 AC1  2   C 2 267  GLN G 176                                          
SITE     1 AC2  2   A 21467  ASN T  85                                          
SITE     1 AC3  3   G 2 576  PRO X  64    U i6216                               
SITE     1 AC4  4 CYS a  23  CYS a  26  CYS a  74  CYS a  77                    
SITE     1 AC5  4 CYS b  40  CYS b  56  SER b  58  CYS b  59                    
SITE     1 AC6  3 CYS f 121  CYS f 139  CYS f 142                               
SITE     1 AC7  2   A 2 940  HIS a  17                                          
SITE     1 AC8  2   A 2 359    G 2 361                                          
SITE     1 AC9  4   A 2  93    G 2  95    G 2 402  ARG E   3                    
SITE     1 AD1  3   G 2 551    A 2 554    A 2 555                               
SITE     1 AD2  1   A 2 100                                                     
SITE     1 AD3  2   G 2 623    A 21024                                          
SITE     1 AD4  2   C 2  49    A 2 424                                          
SITE     1 AD5  3   A 2 992    A 21004    G 21776                               
SITE     1 AD6  4   A 21328    G 21329    C 21418  SER D 160                    
SITE     1 AD7  1   U 2   9                                                     
SITE     1 AD8  4   A 2 928    A 2 929    C 2 930    U 2 944                    
SITE     1 AD9  5   A 21761    G 21765    G 21766    U 21768                    
SITE     2 AD9  5   U 21769                                                     
SITE     1 AE1  1   G 2 547                                                     
SITE     1 AE2  2   A 2 400  LYS I  23                                          
SITE     1 AE3  2   G 2  16    G 2 609                                          
SITE     1 AE4  2   A 2 377    U 2 378                                          
SITE     1 AE5  1   A 2  28                                                     
SITE     1 AE6  3   G 2 370    A 2 604    G 2 606                               
SITE     1 AE7  2   U 2 995    G 2 996                                          
SITE     1 AE8  2   C 2 426    G 2 428                                          
SITE     1 AE9  3   A 2  43    U 2  44    A 2  47                               
SITE     1 AF1  5   U 21759    A 21760    A 21761    G 21765                    
SITE     2 AF1  5   G 21766                                                     
SITE     1 AF2  4   U 2 617    A 2 618    A 2 619    A 2 620                    
SITE     1 AF3  1   A 2 579                                                     
SITE     1 AF4  2   A 2 618    A 21029                                          
SITE     1 AF5  2   G 21327    G 21329                                          
SITE     1 AF6  1   A 2 622                                                     
SITE     1 AF7  4   A 2 100    U 2 101    U 2 102    C 2 360                    
SITE     1 AF8  2   G 21108    G 21109                                          
SITE     1 AF9  2   U 21768    A 21792                                          
SITE     1 AG1  1   G 2  95                                                     
SITE     1 AG2  1   U 21726                                                     
SITE     1 AG3  5   G 21627    U 21628    G 21791    A 21792                    
SITE     2 AG3  5 MET a   1                                                     
SITE     1 AG4  2   A 2 459    G 2 460                                          
SITE     1 AG5  1   G 2 466                                                     
SITE     1 AG6  1   A 21415                                                     
SITE     1 AG7  2   A 2 549    C 2 582                                          
SITE     1 AG8  3   A 2 991    C 21009    G 21010                               
SITE     1 AG9  1   U 21302                                                     
SITE     1 AH1  1   A 2 978                                                     
SITE     1 AH2  2   G 2  57    U 2  58                                          
SITE     1 AH3  2   A 2 760    G 2 761                                          
SITE     1 AH4  1   G 21139                                                     
SITE     1 AH5  1   G 2  34                                                     
SITE     1 AH6  1   G 21293                                                     
SITE     1 AH7  1   U 2 988                                                     
SITE     1 AH8  1   A 2 212                                                     
SITE     1 AH9  1   G 2 336                                                     
SITE     1 AI1  1   G 2 382                                                     
SITE     1 AI2  1   G 21392                                                     
SITE     1 AI3  3   C 21158    A 21192    U 21282                               
SITE     1 AI4  3   G 21175    A 21201    C 21455                               
SITE     1 AI5  3   G 21200    A 21598    C 21600                               
SITE     1 AI6  1   U 21430                                                     
SITE     1 AI7  4   A 21195    C 21196    C 21463    U 21601                    
SITE     1 AI8  2   G 21267    U 21268                                          
SITE     1 AI9  3   G 21272    C 21273    G 21426                               
SITE     1 AJ1  2   G 21537    G 21539                                          
SITE     1 AJ2  2   U 21515    U 21520                                          
SITE     1 AJ3  3   C 21273    G 21426    G 21427                               
SITE     1 AJ4  2   A 21201    A 21202                                          
SITE     1 AJ5  2   U 2 512    G 2 513                                          
SITE     1 AJ6  2   U 2 118    A 2 119                                          
SITE     1 AJ7  3   C 2 249    A 2 250    U 2 251                               
SITE     1 AJ8  1   C 2 423                                                     
SITE     1 AJ9  1   A 2 603                                                     
SITE     1 AK1  3   A 2 634    A 2 635    A 2 805                               
SITE     1 AK2  2   C 2 626    U 2 967                                          
SITE     1 AK3  2   A 2 970    G 2 971                                          
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                                                                             
DBGET integrated database retrieval system