GenomeNet

Database: PDB
Entry: 3J7Y
LinkDB: 3J7Y
Original site: 3J7Y 
HEADER    RIBOSOME                                26-AUG-14   3J7Y              
TITLE     STRUCTURE OF THE LARGE RIBOSOMAL SUBUNIT FROM HUMAN MITOCHONDRIA      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 16S RRNA;                                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 MOL_ID: 2;                                                           
COMPND   5 MOLECULE: MT-TRNAVAL;                                                
COMPND   6 CHAIN: B;                                                            
COMPND   7 MOL_ID: 3;                                                           
COMPND   8 MOLECULE: UL2;                                                       
COMPND   9 CHAIN: D;                                                            
COMPND  10 MOL_ID: 4;                                                           
COMPND  11 MOLECULE: UL3;                                                       
COMPND  12 CHAIN: E;                                                            
COMPND  13 MOL_ID: 5;                                                           
COMPND  14 MOLECULE: UL4;                                                       
COMPND  15 CHAIN: F;                                                            
COMPND  16 MOL_ID: 6;                                                           
COMPND  17 MOLECULE: BL9;                                                       
COMPND  18 CHAIN: H;                                                            
COMPND  19 MOL_ID: 7;                                                           
COMPND  20 MOLECULE: UL10;                                                      
COMPND  21 CHAIN: I;                                                            
COMPND  22 MOL_ID: 8;                                                           
COMPND  23 MOLECULE: UL11;                                                      
COMPND  24 CHAIN: J;                                                            
COMPND  25 MOL_ID: 9;                                                           
COMPND  26 MOLECULE: UL13;                                                      
COMPND  27 CHAIN: K;                                                            
COMPND  28 MOL_ID: 10;                                                          
COMPND  29 MOLECULE: UL14;                                                      
COMPND  30 CHAIN: L;                                                            
COMPND  31 MOL_ID: 11;                                                          
COMPND  32 MOLECULE: UL15;                                                      
COMPND  33 CHAIN: M;                                                            
COMPND  34 MOL_ID: 12;                                                          
COMPND  35 MOLECULE: UL16;                                                      
COMPND  36 CHAIN: N;                                                            
COMPND  37 MOL_ID: 13;                                                          
COMPND  38 MOLECULE: BL17;                                                      
COMPND  39 CHAIN: O;                                                            
COMPND  40 MOL_ID: 14;                                                          
COMPND  41 MOLECULE: UL18;                                                      
COMPND  42 CHAIN: P;                                                            
COMPND  43 MOL_ID: 15;                                                          
COMPND  44 MOLECULE: BL19;                                                      
COMPND  45 CHAIN: Q;                                                            
COMPND  46 MOL_ID: 16;                                                          
COMPND  47 MOLECULE: BL20;                                                      
COMPND  48 CHAIN: R;                                                            
COMPND  49 MOL_ID: 17;                                                          
COMPND  50 MOLECULE: BL21;                                                      
COMPND  51 CHAIN: S;                                                            
COMPND  52 MOL_ID: 18;                                                          
COMPND  53 MOLECULE: UL22;                                                      
COMPND  54 CHAIN: T;                                                            
COMPND  55 MOL_ID: 19;                                                          
COMPND  56 MOLECULE: UL23;                                                      
COMPND  57 CHAIN: U;                                                            
COMPND  58 MOL_ID: 20;                                                          
COMPND  59 MOLECULE: UL24;                                                      
COMPND  60 CHAIN: V;                                                            
COMPND  61 MOL_ID: 21;                                                          
COMPND  62 MOLECULE: BL27;                                                      
COMPND  63 CHAIN: W;                                                            
COMPND  64 MOL_ID: 22;                                                          
COMPND  65 MOLECULE: BL28;                                                      
COMPND  66 CHAIN: X;                                                            
COMPND  67 MOL_ID: 23;                                                          
COMPND  68 MOLECULE: UL29;                                                      
COMPND  69 CHAIN: Y;                                                            
COMPND  70 MOL_ID: 24;                                                          
COMPND  71 MOLECULE: UL30;                                                      
COMPND  72 CHAIN: Z;                                                            
COMPND  73 MOL_ID: 25;                                                          
COMPND  74 MOLECULE: BL32;                                                      
COMPND  75 CHAIN: 0;                                                            
COMPND  76 MOL_ID: 26;                                                          
COMPND  77 MOLECULE: BL33;                                                      
COMPND  78 CHAIN: 1;                                                            
COMPND  79 MOL_ID: 27;                                                          
COMPND  80 MOLECULE: BL34;                                                      
COMPND  81 CHAIN: 2;                                                            
COMPND  82 MOL_ID: 28;                                                          
COMPND  83 MOLECULE: BL35;                                                      
COMPND  84 CHAIN: 3;                                                            
COMPND  85 MOL_ID: 29;                                                          
COMPND  86 MOLECULE: BL36;                                                      
COMPND  87 CHAIN: 4;                                                            
COMPND  88 MOL_ID: 30;                                                          
COMPND  89 MOLECULE: ML37;                                                      
COMPND  90 CHAIN: 5;                                                            
COMPND  91 MOL_ID: 31;                                                          
COMPND  92 MOLECULE: ML38;                                                      
COMPND  93 CHAIN: 6;                                                            
COMPND  94 MOL_ID: 32;                                                          
COMPND  95 MOLECULE: ML39;                                                      
COMPND  96 CHAIN: 7;                                                            
COMPND  97 MOL_ID: 33;                                                          
COMPND  98 MOLECULE: ML40;                                                      
COMPND  99 CHAIN: 8;                                                            
COMPND 100 MOL_ID: 34;                                                          
COMPND 101 MOLECULE: ML41;                                                      
COMPND 102 CHAIN: 9;                                                            
COMPND 103 MOL_ID: 35;                                                          
COMPND 104 MOLECULE: ML42;                                                      
COMPND 105 CHAIN: a;                                                            
COMPND 106 MOL_ID: 36;                                                          
COMPND 107 MOLECULE: ML43;                                                      
COMPND 108 CHAIN: b;                                                            
COMPND 109 MOL_ID: 37;                                                          
COMPND 110 MOLECULE: ML44;                                                      
COMPND 111 CHAIN: c;                                                            
COMPND 112 MOL_ID: 38;                                                          
COMPND 113 MOLECULE: ML45;                                                      
COMPND 114 CHAIN: d;                                                            
COMPND 115 MOL_ID: 39;                                                          
COMPND 116 MOLECULE: ML46;                                                      
COMPND 117 CHAIN: e;                                                            
COMPND 118 MOL_ID: 40;                                                          
COMPND 119 MOLECULE: ML48;                                                      
COMPND 120 CHAIN: f;                                                            
COMPND 121 MOL_ID: 41;                                                          
COMPND 122 MOLECULE: ML49;                                                      
COMPND 123 CHAIN: g;                                                            
COMPND 124 MOL_ID: 42;                                                          
COMPND 125 MOLECULE: ML50;                                                      
COMPND 126 CHAIN: h;                                                            
COMPND 127 MOL_ID: 43;                                                          
COMPND 128 MOLECULE: ML51;                                                      
COMPND 129 CHAIN: i;                                                            
COMPND 130 MOL_ID: 44;                                                          
COMPND 131 MOLECULE: ML52;                                                      
COMPND 132 CHAIN: j;                                                            
COMPND 133 MOL_ID: 45;                                                          
COMPND 134 MOLECULE: ML53;                                                      
COMPND 135 CHAIN: k;                                                            
COMPND 136 MOL_ID: 46;                                                          
COMPND 137 MOLECULE: ML63;                                                      
COMPND 138 CHAIN: o;                                                            
COMPND 139 MOL_ID: 47;                                                          
COMPND 140 MOLECULE: ICT1;                                                      
COMPND 141 CHAIN: p;                                                            
COMPND 142 MOL_ID: 48;                                                          
COMPND 143 MOLECULE: CRIF1;                                                     
COMPND 144 CHAIN: q;                                                            
COMPND 145 MOL_ID: 49;                                                          
COMPND 146 MOLECULE: BS18A;                                                     
COMPND 147 CHAIN: r;                                                            
COMPND 148 MOL_ID: 50;                                                          
COMPND 149 MOLECULE: MS30;                                                      
COMPND 150 CHAIN: s;                                                            
COMPND 151 MOL_ID: 51;                                                          
COMPND 152 MOLECULE: UNKNOWN PROTEIN;                                           
COMPND 153 CHAIN: t                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 CELL_LINE: HEK293;                                                   
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   8 ORGANISM_COMMON: HUMAN;                                              
SOURCE   9 ORGANISM_TAXID: 9606;                                                
SOURCE  10 CELL_LINE: HEK293;                                                   
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 CELL_LINE: HEK293;                                                   
SOURCE  16 MOL_ID: 4;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  18 ORGANISM_COMMON: HUMAN;                                              
SOURCE  19 ORGANISM_TAXID: 9606;                                                
SOURCE  20 CELL_LINE: HEK293;                                                   
SOURCE  21 MOL_ID: 5;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606;                                                
SOURCE  25 CELL_LINE: HEK293;                                                   
SOURCE  26 MOL_ID: 6;                                                           
SOURCE  27 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  28 ORGANISM_COMMON: HUMAN;                                              
SOURCE  29 ORGANISM_TAXID: 9606;                                                
SOURCE  30 CELL_LINE: HEK293;                                                   
SOURCE  31 MOL_ID: 7;                                                           
SOURCE  32 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  33 ORGANISM_COMMON: HUMAN;                                              
SOURCE  34 ORGANISM_TAXID: 9606;                                                
SOURCE  35 CELL_LINE: HEK293;                                                   
SOURCE  36 MOL_ID: 8;                                                           
SOURCE  37 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  38 ORGANISM_COMMON: HUMAN;                                              
SOURCE  39 ORGANISM_TAXID: 9606;                                                
SOURCE  40 CELL_LINE: HEK293;                                                   
SOURCE  41 MOL_ID: 9;                                                           
SOURCE  42 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  43 ORGANISM_COMMON: HUMAN;                                              
SOURCE  44 ORGANISM_TAXID: 9606;                                                
SOURCE  45 CELL_LINE: HEK293;                                                   
SOURCE  46 MOL_ID: 10;                                                          
SOURCE  47 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  48 ORGANISM_COMMON: HUMAN;                                              
SOURCE  49 ORGANISM_TAXID: 9606;                                                
SOURCE  50 CELL_LINE: HEK293;                                                   
SOURCE  51 MOL_ID: 11;                                                          
SOURCE  52 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  53 ORGANISM_COMMON: HUMAN;                                              
SOURCE  54 ORGANISM_TAXID: 9606;                                                
SOURCE  55 CELL_LINE: HEK293;                                                   
SOURCE  56 MOL_ID: 12;                                                          
SOURCE  57 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  58 ORGANISM_COMMON: HUMAN;                                              
SOURCE  59 ORGANISM_TAXID: 9606;                                                
SOURCE  60 CELL_LINE: HEK293;                                                   
SOURCE  61 MOL_ID: 13;                                                          
SOURCE  62 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  63 ORGANISM_COMMON: HUMAN;                                              
SOURCE  64 ORGANISM_TAXID: 9606;                                                
SOURCE  65 CELL_LINE: HEK293;                                                   
SOURCE  66 MOL_ID: 14;                                                          
SOURCE  67 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  68 ORGANISM_COMMON: HUMAN;                                              
SOURCE  69 ORGANISM_TAXID: 9606;                                                
SOURCE  70 CELL_LINE: HEK293;                                                   
SOURCE  71 MOL_ID: 15;                                                          
SOURCE  72 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  73 ORGANISM_COMMON: HUMAN;                                              
SOURCE  74 ORGANISM_TAXID: 9606;                                                
SOURCE  75 CELL_LINE: HEK293;                                                   
SOURCE  76 MOL_ID: 16;                                                          
SOURCE  77 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  78 ORGANISM_COMMON: HUMAN;                                              
SOURCE  79 ORGANISM_TAXID: 9606;                                                
SOURCE  80 CELL_LINE: HEK293;                                                   
SOURCE  81 MOL_ID: 17;                                                          
SOURCE  82 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  83 ORGANISM_COMMON: HUMAN;                                              
SOURCE  84 ORGANISM_TAXID: 9606;                                                
SOURCE  85 CELL_LINE: HEK293;                                                   
SOURCE  86 MOL_ID: 18;                                                          
SOURCE  87 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  88 ORGANISM_COMMON: HUMAN;                                              
SOURCE  89 ORGANISM_TAXID: 9606;                                                
SOURCE  90 CELL_LINE: HEK293;                                                   
SOURCE  91 MOL_ID: 19;                                                          
SOURCE  92 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  93 ORGANISM_COMMON: HUMAN;                                              
SOURCE  94 ORGANISM_TAXID: 9606;                                                
SOURCE  95 CELL_LINE: HEK293;                                                   
SOURCE  96 MOL_ID: 20;                                                          
SOURCE  97 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  98 ORGANISM_COMMON: HUMAN;                                              
SOURCE  99 ORGANISM_TAXID: 9606;                                                
SOURCE 100 CELL_LINE: HEK293;                                                   
SOURCE 101 MOL_ID: 21;                                                          
SOURCE 102 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 103 ORGANISM_COMMON: HUMAN;                                              
SOURCE 104 ORGANISM_TAXID: 9606;                                                
SOURCE 105 CELL_LINE: HEK293;                                                   
SOURCE 106 MOL_ID: 22;                                                          
SOURCE 107 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 108 ORGANISM_COMMON: HUMAN;                                              
SOURCE 109 ORGANISM_TAXID: 9606;                                                
SOURCE 110 CELL_LINE: HEK293;                                                   
SOURCE 111 MOL_ID: 23;                                                          
SOURCE 112 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 113 ORGANISM_COMMON: HUMAN;                                              
SOURCE 114 ORGANISM_TAXID: 9606;                                                
SOURCE 115 CELL_LINE: HEK293;                                                   
SOURCE 116 MOL_ID: 24;                                                          
SOURCE 117 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 118 ORGANISM_COMMON: HUMAN;                                              
SOURCE 119 ORGANISM_TAXID: 9606;                                                
SOURCE 120 CELL_LINE: HEK293;                                                   
SOURCE 121 MOL_ID: 25;                                                          
SOURCE 122 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 123 ORGANISM_COMMON: HUMAN;                                              
SOURCE 124 ORGANISM_TAXID: 9606;                                                
SOURCE 125 CELL_LINE: HEK293;                                                   
SOURCE 126 MOL_ID: 26;                                                          
SOURCE 127 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 128 ORGANISM_COMMON: HUMAN;                                              
SOURCE 129 ORGANISM_TAXID: 9606;                                                
SOURCE 130 CELL_LINE: HEK293;                                                   
SOURCE 131 MOL_ID: 27;                                                          
SOURCE 132 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 133 ORGANISM_COMMON: HUMAN;                                              
SOURCE 134 ORGANISM_TAXID: 9606;                                                
SOURCE 135 CELL_LINE: HEK293;                                                   
SOURCE 136 MOL_ID: 28;                                                          
SOURCE 137 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 138 ORGANISM_COMMON: HUMAN;                                              
SOURCE 139 ORGANISM_TAXID: 9606;                                                
SOURCE 140 CELL_LINE: HEK293;                                                   
SOURCE 141 MOL_ID: 29;                                                          
SOURCE 142 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 143 ORGANISM_COMMON: HUMAN;                                              
SOURCE 144 ORGANISM_TAXID: 9606;                                                
SOURCE 145 CELL_LINE: HEK293;                                                   
SOURCE 146 MOL_ID: 30;                                                          
SOURCE 147 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 148 ORGANISM_COMMON: HUMAN;                                              
SOURCE 149 ORGANISM_TAXID: 9606;                                                
SOURCE 150 CELL_LINE: HEK293;                                                   
SOURCE 151 MOL_ID: 31;                                                          
SOURCE 152 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 153 ORGANISM_COMMON: HUMAN;                                              
SOURCE 154 ORGANISM_TAXID: 9606;                                                
SOURCE 155 CELL_LINE: HEK293;                                                   
SOURCE 156 MOL_ID: 32;                                                          
SOURCE 157 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 158 ORGANISM_COMMON: HUMAN;                                              
SOURCE 159 ORGANISM_TAXID: 9606;                                                
SOURCE 160 CELL_LINE: HEK293;                                                   
SOURCE 161 MOL_ID: 33;                                                          
SOURCE 162 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 163 ORGANISM_COMMON: HUMAN;                                              
SOURCE 164 ORGANISM_TAXID: 9606;                                                
SOURCE 165 CELL_LINE: HEK293;                                                   
SOURCE 166 MOL_ID: 34;                                                          
SOURCE 167 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 168 ORGANISM_COMMON: HUMAN;                                              
SOURCE 169 ORGANISM_TAXID: 9606;                                                
SOURCE 170 CELL_LINE: HEK293;                                                   
SOURCE 171 MOL_ID: 35;                                                          
SOURCE 172 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 173 ORGANISM_COMMON: HUMAN;                                              
SOURCE 174 ORGANISM_TAXID: 9606;                                                
SOURCE 175 CELL_LINE: HEK293;                                                   
SOURCE 176 MOL_ID: 36;                                                          
SOURCE 177 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 178 ORGANISM_COMMON: HUMAN;                                              
SOURCE 179 ORGANISM_TAXID: 9606;                                                
SOURCE 180 CELL_LINE: HEK293;                                                   
SOURCE 181 MOL_ID: 37;                                                          
SOURCE 182 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 183 ORGANISM_COMMON: HUMAN;                                              
SOURCE 184 ORGANISM_TAXID: 9606;                                                
SOURCE 185 CELL_LINE: HEK293;                                                   
SOURCE 186 MOL_ID: 38;                                                          
SOURCE 187 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 188 ORGANISM_COMMON: HUMAN;                                              
SOURCE 189 ORGANISM_TAXID: 9606;                                                
SOURCE 190 CELL_LINE: HEK293;                                                   
SOURCE 191 MOL_ID: 39;                                                          
SOURCE 192 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 193 ORGANISM_COMMON: HUMAN;                                              
SOURCE 194 ORGANISM_TAXID: 9606;                                                
SOURCE 195 CELL_LINE: HEK293;                                                   
SOURCE 196 MOL_ID: 40;                                                          
SOURCE 197 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 198 ORGANISM_COMMON: HUMAN;                                              
SOURCE 199 ORGANISM_TAXID: 9606;                                                
SOURCE 200 CELL_LINE: HEK293;                                                   
SOURCE 201 MOL_ID: 41;                                                          
SOURCE 202 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 203 ORGANISM_COMMON: HUMAN;                                              
SOURCE 204 ORGANISM_TAXID: 9606;                                                
SOURCE 205 CELL_LINE: HEK293;                                                   
SOURCE 206 MOL_ID: 42;                                                          
SOURCE 207 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 208 ORGANISM_COMMON: HUMAN;                                              
SOURCE 209 ORGANISM_TAXID: 9606;                                                
SOURCE 210 CELL_LINE: HEK293;                                                   
SOURCE 211 MOL_ID: 43;                                                          
SOURCE 212 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 213 ORGANISM_COMMON: HUMAN;                                              
SOURCE 214 ORGANISM_TAXID: 9606;                                                
SOURCE 215 CELL_LINE: HEK293;                                                   
SOURCE 216 MOL_ID: 44;                                                          
SOURCE 217 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 218 ORGANISM_COMMON: HUMAN;                                              
SOURCE 219 ORGANISM_TAXID: 9606;                                                
SOURCE 220 CELL_LINE: HEK293;                                                   
SOURCE 221 MOL_ID: 45;                                                          
SOURCE 222 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 223 ORGANISM_COMMON: HUMAN;                                              
SOURCE 224 ORGANISM_TAXID: 9606;                                                
SOURCE 225 CELL_LINE: HEK293;                                                   
SOURCE 226 MOL_ID: 46;                                                          
SOURCE 227 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 228 ORGANISM_COMMON: HUMAN;                                              
SOURCE 229 ORGANISM_TAXID: 9606;                                                
SOURCE 230 CELL_LINE: HEK293;                                                   
SOURCE 231 MOL_ID: 47;                                                          
SOURCE 232 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 233 ORGANISM_COMMON: HUMAN;                                              
SOURCE 234 ORGANISM_TAXID: 9606;                                                
SOURCE 235 CELL_LINE: HEK293;                                                   
SOURCE 236 MOL_ID: 48;                                                          
SOURCE 237 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 238 ORGANISM_COMMON: HUMAN;                                              
SOURCE 239 ORGANISM_TAXID: 9606;                                                
SOURCE 240 CELL_LINE: HEK293;                                                   
SOURCE 241 MOL_ID: 49;                                                          
SOURCE 242 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 243 ORGANISM_COMMON: HUMAN;                                              
SOURCE 244 ORGANISM_TAXID: 9606;                                                
SOURCE 245 CELL_LINE: HEK293;                                                   
SOURCE 246 MOL_ID: 50;                                                          
SOURCE 247 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 248 ORGANISM_COMMON: HUMAN;                                              
SOURCE 249 ORGANISM_TAXID: 9606;                                                
SOURCE 250 CELL_LINE: HEK293;                                                   
SOURCE 251 MOL_ID: 51;                                                          
SOURCE 252 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 253 ORGANISM_COMMON: HUMAN;                                              
SOURCE 254 ORGANISM_TAXID: 9606;                                                
SOURCE 255 CELL_LINE: HEK293                                                    
KEYWDS    MITOCHONDRIA, LARGE SUBUNIT, RRNA, TRNA, RIBOSOME                     
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    A.BROWN,A.AMUNTS,X.C.BAI,Y.SUGIMOTO,P.C.EDWARDS,G.MURSHUDOV,          
AUTHOR   2 S.H.W.SCHERES,V.RAMAKRISHNAN                                         
REVDAT   3   18-JUL-18 3J7Y    1       REMARK                                   
REVDAT   2   19-NOV-14 3J7Y    1       JRNL                                     
REVDAT   1   15-OCT-14 3J7Y    0                                                
JRNL        AUTH   A.BROWN,A.AMUNTS,X.C.BAI,Y.SUGIMOTO,P.C.EDWARDS,G.MURSHUDOV, 
JRNL        AUTH 2 S.H.SCHERES,V.RAMAKRISHNAN                                   
JRNL        TITL   STRUCTURE OF THE LARGE RIBOSOMAL SUBUNIT FROM HUMAN          
JRNL        TITL 2 MITOCHONDRIA.                                                
JRNL        REF    SCIENCE                       V. 346   718 2014              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   25278503                                                     
JRNL        DOI    10.1126/SCIENCE.1258026                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : CTFFIND, EMAN, RELION                     
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : NULL                                
REMARK   3   REFINEMENT PROTOCOL          : NULL                                
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)    : 1.340                          
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 3.400                          
REMARK   3   NUMBER OF PARTICLES               : 107679                         
REMARK   3   CTF CORRECTION METHOD             : NULL                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: FINAL RESOLUTION WAS CALCULATED USING A SOFT MASK     
REMARK   3  OVER THE LARGE SUBUNIT                                              
REMARK   4                                                                      
REMARK   4 3J7Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-SEP-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000160364.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : VITREOUS ICE (CRYO EM)            
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : HUMAN MITOCHONDRIAL RIBOSOME;     
REMARK 245                                    LARGE SUBUNIT OF THE HUMAN        
REMARK 245                                    MITOCHONDRIAL RIBOSOME            
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 0.23                              
REMARK 245   SAMPLE SUPPORT DETAILS         : 30 SECONDS ON GLOW-DISCHARGED     
REMARK 245                                    HOLEY CARBON GRIDS (QUANTIFOIL    
REMARK 245                                    R2/2) WITH HOME-MADE CONTINUOUS   
REMARK 245                                    CARBON FILM                       
REMARK 245   SAMPLE VITRIFICATION DETAILS   : BLOT 2.5 SECONDS BEFORE           
REMARK 245                                    PLUNGING INTO LIQUID ETHANE       
REMARK 245                                    (FEI VITROBOT MARK II).           
REMARK 245   SAMPLE BUFFER                  : 20 MM HEPES-KOH, PH 7.45, 100     
REMARK 245                                    MM POTASSIUM CHLORIDE, 20 MM      
REMARK 245                                    MAGNESIUM ACETATE, 2 MM DTT       
REMARK 245   PH                             : 7.45                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : 12-APR-14                      
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : 85.00                          
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : FEI FALCON II (4K X 4K)        
REMARK 245   MINIMUM DEFOCUS (NM)              : 1500.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 3500.00                        
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                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 59000                          
REMARK 245   CALIBRATED MAGNIFICATION          : 104478                         
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: 51-MERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, E, F, H, I, J, K, L,         
REMARK 350                    AND CHAINS: M, N, O, P, Q, R, S, T, U,            
REMARK 350                    AND CHAINS: V, W, X, Y, Z, 0, 1, 2, 3, 4,         
REMARK 350                    AND CHAINS: 5, 6, 7, 8, 9, a, b, c, d,            
REMARK 350                    AND CHAINS: e, f, g, h, i, j, k, o, p, q,         
REMARK 350                    AND CHAINS: r, s, t                               
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 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 6  99    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR 6 100    OG1  CG2                                            
REMARK 470     GLN 6 101    CG   CD   OE1  NE2                                  
REMARK 470     GLN 6 102    CG   CD   OE1  NE2                                  
REMARK 470     LEU 6 103    CG   CD1  CD2                                       
REMARK 470     LEU 6 104    CG   CD1  CD2                                       
REMARK 470     GLU 6 105    CG   CD   OE1  OE2                                  
REMARK 470     ARG 6 106    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS 6 107    CG   CD   CE   NZ                                   
REMARK 470     GLN 6 108    CG   CD   OE1  NE2                                  
REMARK 470     ILE 6 110    CG1  CG2  CD1                                       
REMARK 470     GLN 6 111    CG   CD   OE1  NE2                                  
REMARK 470     GLU 6 112    CG   CD   OE1  OE2                                  
REMARK 470     LEU 6 113    CG   CD1  CD2                                       
REMARK 470     ARG 6 114    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN 6 116    CG   OD1  ND2                                       
REMARK 470     VAL 6 117    CG1  CG2                                            
REMARK 470     GLU 6 118    CG   CD   OE1  OE2                                  
REMARK 470     GLU 6 120    CG   CD   OE1  OE2                                  
REMARK 470     ARG 6 121    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG 6 124    CG   CD   NE   CZ   NH1  NH2                        
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   SG   CYS 4    79    ZN     ZN 4   200              1.69            
REMARK 500   CG2  THR H    53     CG2  THR H    86              1.71            
REMARK 500   CE   MET k    76     CG   MET k    86              1.71            
REMARK 500   NH1  ARG K   154     OE2  GLU K   157              1.86            
REMARK 500   C2     A A  2556     O2     U A  2559              1.86            
REMARK 500   CG2  THR H    53     OG1  THR H    86              2.02            
REMARK 500   O2'    G A  2995     O2'    U A  3041              2.03            
REMARK 500   SG   CYS 0   110     O    GLU 0   112              2.05            
REMARK 500   NH1  ARG Q   244     CD1  LEU Q   247              2.11            
REMARK 500   NH1  ARG K   154     CD   GLU K   157              2.14            
REMARK 500   O4     U A  2731     N1     A A  2918              2.17            
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    GLU D 199   CD    GLU D 199   OE1     0.123                       
REMARK 500    GLU O  43   CD    GLU O  43   OE1     0.082                       
REMARK 500    GLU O  70   CD    GLU O  70   OE2     0.081                       
REMARK 500    GLU P 151   CD    GLU P 151   OE1     0.153                       
REMARK 500    GLU P 151   CD    GLU P 151   OE2     0.199                       
REMARK 500    GLU Q 256   CG    GLU Q 256   CD      0.140                       
REMARK 500    GLU R  23   CD    GLU R  23   OE1     0.091                       
REMARK 500    GLU R  23   CD    GLU R  23   OE2     0.206                       
REMARK 500    GLU U  47   CD    GLU U  47   OE1     0.098                       
REMARK 500    GLU U  47   CD    GLU U  47   OE2     0.133                       
REMARK 500    ASP V 176   CG    ASP V 176   OD1     0.147                       
REMARK 500    ASP Y  97   CG    ASP Y  97   OD2     0.167                       
REMARK 500    GLU Z  51   CD    GLU Z  51   OE1     0.082                       
REMARK 500    ASP 0 108   CG    ASP 0 108   OD1     0.163                       
REMARK 500    ASP 0 108   CG    ASP 0 108   OD2     0.171                       
REMARK 500    GLN 6  63   CD    GLN 6  63   NE2     0.179                       
REMARK 500    GLU 6 140   CD    GLU 6 140   OE1     0.069                       
REMARK 500    ASN 6 191   CG    ASN 6 191   OD1     0.191                       
REMARK 500    ASP 7 259   CG    ASP 7 259   OD2     0.153                       
REMARK 500    GLN 9  90   CD    GLN 9  90   OE1     0.158                       
REMARK 500    GLU 9  94   CD    GLU 9  94   OE1     0.126                       
REMARK 500    GLU 9  94   CD    GLU 9  94   OE2     0.070                       
REMARK 500    GLU 9 120   CD    GLU 9 120   OE1     0.074                       
REMARK 500    GLU 9 120   CD    GLU 9 120   OE2     0.068                       
REMARK 500    GLU b  78   CD    GLU b  78   OE1     0.089                       
REMARK 500    GLU b  78   CD    GLU b  78   OE2     0.162                       
REMARK 500    GLU b  86   CD    GLU b  86   OE1     0.150                       
REMARK 500    GLU b  86   CD    GLU b  86   OE2     0.110                       
REMARK 500    GLU c  44   CD    GLU c  44   OE1     0.089                       
REMARK 500    GLU c 295   CD    GLU c 295   OE2     0.068                       
REMARK 500    GLU e 180   CD    GLU e 180   OE2     0.167                       
REMARK 500    GLU f 123   CD    GLU f 123   OE1     0.158                       
REMARK 500    GLU f 123   CD    GLU f 123   OE2     0.157                       
REMARK 500    GLU f 168   CD    GLU f 168   OE1     0.075                       
REMARK 500    ARG o  15   CZ    ARG o  15   NH1     0.089                       
REMARK 500    GLU q 118   CG    GLU q 118   CD      0.101                       
REMARK 500    ASP s 318   CG    ASP s 318   OD1     0.154                       
REMARK 500    ASP s 318   CG    ASP s 318   OD2     0.198                       
REMARK 500    GLU s 403   CD    GLU s 403   OE2     0.079                       
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      A A1772   C2' -  C3' -  O3' ANGL. DEV. =  12.2 DEGREES          
REMARK 500      G A2174   C2' -  C3' -  O3' ANGL. DEV. =  11.8 DEGREES          
REMARK 500      A A2374   C2' -  C3' -  O3' ANGL. DEV. =  11.2 DEGREES          
REMARK 500      G A2421   C2' -  C3' -  O3' ANGL. DEV. =   9.7 DEGREES          
REMARK 500      A A2507   C2' -  C3' -  O3' ANGL. DEV. =  10.1 DEGREES          
REMARK 500    ASP 0 108   CB  -  CG  -  OD2 ANGL. DEV. =  -6.9 DEGREES          
REMARK 500    ARG 3 169   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    LEU c 241   CA  -  CB  -  CG  ANGL. DEV. =  15.0 DEGREES          
REMARK 500    ARG o  15   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 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    PHE D  63       91.86   -164.36                                   
REMARK 500    LYS D  67        1.20    -54.72                                   
REMARK 500    ALA D 173       70.34     62.78                                   
REMARK 500    ILE D 207       61.22     63.26                                   
REMARK 500    ASN D 221     -138.64     58.20                                   
REMARK 500    LYS D 231       -9.65    -59.41                                   
REMARK 500    LEU D 266       -4.55    -59.19                                   
REMARK 500    SER E  54     -179.54    -68.72                                   
REMARK 500    ASP E  82      -84.04    -69.94                                   
REMARK 500    TRP E  85      164.57     62.81                                   
REMARK 500    ASP E 126      -93.10     60.98                                   
REMARK 500    CYS E 127       95.91     59.92                                   
REMARK 500    LYS E 141      -55.66   -166.62                                   
REMARK 500    SER E 153       99.01    -61.06                                   
REMARK 500    ARG E 154      -35.07    -39.92                                   
REMARK 500    LEU E 170      151.51     69.97                                   
REMARK 500    HIS E 231        0.35    108.96                                   
REMARK 500    THR E 234     -106.83    -91.02                                   
REMARK 500    LYS E 235       39.14    -90.37                                   
REMARK 500    ALA E 244       88.75   -174.42                                   
REMARK 500    THR E 245      159.98     67.63                                   
REMARK 500    PRO E 317      -70.69    -78.73                                   
REMARK 500    ASP E 322       96.27    -62.46                                   
REMARK 500    ASP E 324      -30.89     87.17                                   
REMARK 500    GLU E 326      140.19     74.14                                   
REMARK 500    ARG F  59      153.99     70.49                                   
REMARK 500    GLN F  74       86.47    -64.28                                   
REMARK 500    VAL F  77       69.67   -104.54                                   
REMARK 500    LEU F  79      118.65   -167.31                                   
REMARK 500    ALA F  88       34.30   -150.70                                   
REMARK 500    TRP F 128      148.59     59.63                                   
REMARK 500    ARG F 142        2.67     91.93                                   
REMARK 500    GLU F 194      102.26   -164.23                                   
REMARK 500    THR F 222      -67.47     79.81                                   
REMARK 500    HIS F 223      -40.49     99.95                                   
REMARK 500    GLU F 225       54.18    -97.21                                   
REMARK 500    LEU F 283      -59.52     69.77                                   
REMARK 500    TYR F 290      171.08     62.66                                   
REMARK 500    TRP H  60       -7.57     89.70                                   
REMARK 500    LYS H  61      112.21     68.97                                   
REMARK 500    LEU H  64      101.23     78.33                                   
REMARK 500    ARG H  75       -9.91    -55.78                                   
REMARK 500    GLU H 103     -129.81     41.19                                   
REMARK 500    ARG H 122      -68.59   -131.30                                   
REMARK 500    ALA H 132       23.48    -78.97                                   
REMARK 500    GLU H 135      -71.19    -49.61                                   
REMARK 500    THR I  51       36.30    -95.51                                   
REMARK 500    HIS I  61      146.61     79.56                                   
REMARK 500    VAL I 102      -41.57    174.57                                   
REMARK 500    LYS I 120       98.26    -55.41                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     461 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 SER F  140     ILE F  141                  146.89                    
REMARK 500 GLY K   82     TYR K   83                 -149.68                    
REMARK 500 GLU k   61     PRO k   62                 -141.15                    
REMARK 500 ALA o   63     ALA o   64                 -149.07                    
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    ASN 6 191         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610       A A 3301                                                       
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 A3365  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   U A2115   OP2                                                    
REMARK 620 2   C A2114   OP1  86.3                                              
REMARK 620 3   C A2100   OP1 163.8  79.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A3342  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   U A3037   OP1                                                    
REMARK 620 2   C A2474   OP2  91.5                                              
REMARK 620 3   A A2473   OP2  89.0  90.3                                        
REMARK 620 4   U A2475   O4  155.0 113.2  94.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A3305  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   C A1726   OP2                                                    
REMARK 620 2   C A1725   OP1  86.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A3339  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A3063   OP1                                                    
REMARK 620 2   A A3064   OP1  85.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A3335  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   C A2603   OP1                                                    
REMARK 620 2   A A2604   OP2 115.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A3317  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A A1961   OP1                                                    
REMARK 620 2   A A2430   OP1 127.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A3351  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   C A2986   OP1                                                    
REMARK 620 2   A A2935   OP1  94.2                                              
REMARK 620 3   G A1851   O6   91.7 138.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A3349  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A2733   OP2                                                    
REMARK 620 2   G A2732   OP2 112.2                                              
REMARK 620 3   G A2732   O5'  72.1  50.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A3320  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A A2452   OP2                                                    
REMARK 620 2   A A2451   OP2  90.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A3324  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A A2313   OP2                                                    
REMARK 620 2   A A2668   OP1  81.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A3363  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A2917   OP2                                                    
REMARK 620 2   A A2918   OP2 114.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN r 200  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS r  70   SG                                                     
REMARK 620 2 CYS r 108   SG   86.6                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A3347  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A2719   OP2                                                    
REMARK 620 2   A A2720   OP2  82.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A3313  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A A1994   OP2                                                    
REMARK 620 2   A A3076   OP1  87.8                                              
REMARK 620 3   A A1993   OP2 112.7  82.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A3309  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   C A1942   OP2                                                    
REMARK 620 2   A A1971   OP2 126.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A3315  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   U A2253   OP2                                                    
REMARK 620 2   C A2252   OP1  78.0                                              
REMARK 620 3   U A2141   OP1  75.0  77.7                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A3337  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A A2468   OP1                                                    
REMARK 620 2   A A2469   OP2  78.9                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A3304  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A A1757   OP2                                                    
REMARK 620 2   U A1758   O4   94.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A3356  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   U A3102   OP1                                                    
REMARK 620 2   A A2309   OP2  81.2                                              
REMARK 620 3   U A3102   OP2  57.7  92.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A3340  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A A1971   OP1                                                    
REMARK 620 2   G A1941   OP2  93.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN 4 200  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 4  76   SG                                                     
REMARK 620 2 CYS 4  92   SG  133.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A3302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A A2866   OP1                                                    
REMARK 620 2   U A2864   OP2  87.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A3311  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A A2504   OP2                                                    
REMARK 620 2   A A2503   OP1  67.4                                              
REMARK 620 3   U A1950   OP2 111.7 110.9                                        
REMARK 620 4   U A1950   OP1  86.0 143.5  55.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A3307  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A A1815   OP2                                                    
REMARK 620 2   A A1814   OP1  84.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A3325  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A2989   OP2                                                    
REMARK 620 2   G A2724   OP2  78.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN 0 200  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS 0 123   SG                                                     
REMARK 620 2 CYS 0 113   SG   91.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A3353  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A A2935   OP2                                                    
REMARK 620 2   C A2985   OP2  72.1                                              
REMARK 620 3   G A2934   O3'  54.5 122.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A3348  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   U A2812   OP2                                                    
REMARK 620 2   U A2813   O4  100.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A3308  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   G A1776   O6                                                     
REMARK 620 2   A A1779   OP1  65.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A3341  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   A A1994   OP1                                                    
REMARK 620 2   G A3075   OP1  62.2                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A3323  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1   U A2660   OP2                                                    
REMARK 620 2   U A2660   O5'  51.5                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE A A 3301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3306                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3309                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3310                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3311                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3312                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3313                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3314                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3315                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3316                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3317                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3318                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3319                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3320                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3321                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3322                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3323                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3324                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3325                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3326                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3327                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3329                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3331                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3333                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3335                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3336                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3337                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3338                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3339                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3340                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3341                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3342                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3343                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3344                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3345                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3346                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3347                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3348                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3349                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3350                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3351                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3352                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3353                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3354                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3355                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3356                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3357                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3358                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3359                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3360                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3361                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3362                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3363                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3364                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3365                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 3366                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN 0 200                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN 4 200                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN r 200                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-2762   RELATED DB: EMDB                              
DBREF  3J7Y D    1   305  UNP    Q5T653   RM02_HUMAN       1    305             
DBREF  3J7Y E    1   348  UNP    P09001   RM03_HUMAN       1    348             
DBREF  3J7Y F    1   311  UNP    Q9BYD3   RM04_HUMAN       1    311             
DBREF  3J7Y H    1   267  UNP    Q9BYD2   RM09_HUMAN       1    267             
DBREF  3J7Y I    1   261  UNP    Q7Z7H8   RM10_HUMAN       1    261             
DBREF  3J7Y J    1   192  UNP    Q9Y3B7   RM11_HUMAN       1    192             
DBREF  3J7Y K    1   178  UNP    Q9BYD1   RM13_HUMAN       1    178             
DBREF  3J7Y L    1   145  UNP    Q6P1L8   RM14_HUMAN       1    145             
DBREF  3J7Y M    1   296  UNP    Q9P015   RM15_HUMAN       1    296             
DBREF  3J7Y N    1   251  UNP    Q9NX20   RM16_HUMAN       1    251             
DBREF  3J7Y O    1   175  UNP    Q9NRX2   RM17_HUMAN       1    175             
DBREF  3J7Y P    1   179  UNP    A8K9D2   A8K9D2_HUMAN     1    179             
DBREF  3J7Y Q    1   292  UNP    P49406   RM19_HUMAN       1    292             
DBREF  3J7Y R    1   149  UNP    Q9BYC9   RM20_HUMAN       1    149             
DBREF  3J7Y S    1   205  UNP    Q7Z2W9   RM21_HUMAN       1    205             
DBREF  3J7Y T    1   212  UNP    E7ESL0   E7ESL0_HUMAN     1    212             
DBREF  3J7Y U    1   153  UNP    Q16540   RM23_HUMAN       1    153             
DBREF  3J7Y V    1   216  UNP    Q96A35   RM24_HUMAN       1    216             
DBREF  3J7Y W    1   148  UNP    Q9P0M9   RM27_HUMAN       1    148             
DBREF  3J7Y X    1   256  UNP    Q4TT38   Q4TT38_HUMAN     1    256             
DBREF  3J7Y Y    1   250  UNP    Q9HD33   RM47_HUMAN       1    250             
DBREF  3J7Y Z    1   161  UNP    Q8TCC3   RM30_HUMAN       1    161             
DBREF  3J7Y 0    1   188  UNP    Q9BYC8   RM32_HUMAN       1    188             
DBREF  3J7Y 1    1    65  UNP    O75394   RM33_HUMAN       1     65             
DBREF  3J7Y 2    1    92  UNP    Q9BQ48   RM34_HUMAN       1     92             
DBREF  3J7Y 3    1   188  UNP    Q9NZE8   RM35_HUMAN       1    188             
DBREF  3J7Y 4    1   103  UNP    Q9P0J6   RM36_HUMAN       1    103             
DBREF  3J7Y 5    1   423  UNP    Q9BZE1   RM37_HUMAN       1    423             
DBREF  3J7Y 6    1   380  UNP    Q96DV4   RM38_HUMAN       1    380             
DBREF  3J7Y 7    1   338  UNP    Q9NYK5   RM39_HUMAN       1    338             
DBREF  3J7Y 8  -43   162  UNP    Q9NQ50   RM40_HUMAN       1    206             
DBREF  3J7Y 9    1   137  UNP    Q8IXM3   RM41_HUMAN       1    137             
DBREF  3J7Y a    1   142  UNP    Q9Y6G3   RM42_HUMAN       1    142             
DBREF  3J7Y b    1   155  UNP    Q8N983   RM43_HUMAN       1    155             
DBREF  3J7Y c    1   332  UNP    Q9H9J2   RM44_HUMAN       1    332             
DBREF  3J7Y d    1   306  UNP    Q9BRJ2   RM45_HUMAN       1    306             
DBREF  3J7Y e  -43   235  UNP    Q9H2W6   RM46_HUMAN       1    279             
DBREF  3J7Y f    1   259  UNP    Q96GC5   RM48_HUMAN       1    194             
DBREF  3J7Y g    1   166  UNP    Q13405   RM49_HUMAN       1    166             
DBREF  3J7Y h    1   158  UNP    Q8N5N7   RM50_HUMAN       1    158             
DBREF  3J7Y i    1   128  UNP    Q4U2R6   RM51_HUMAN       1    128             
DBREF  3J7Y j    1   123  UNP    A8K7J6   A8K7J6_HUMAN     1    123             
DBREF  3J7Y k    1   112  UNP    Q96EL3   RM53_HUMAN       1    112             
DBREF  3J7Y o    1   102  UNP    Q9BQC6   RT63_HUMAN       1    102             
DBREF  3J7Y p    0   206  UNP    Q14197   ICT1_HUMAN       1    206             
DBREF  3J7Y q    1   222  UNP    Q8TAE8   G45IP_HUMAN      1    222             
DBREF  3J7Y r    1   196  UNP    Q9NVS2   RT18A_HUMAN      1    196             
DBREF  3J7Y s    1   439  UNP    Q9NP92   RT30_HUMAN       1    439             
DBREF  3J7Y A 1671  3229  PDB    3J7Y     3J7Y          1671   3229             
DBREF  3J7Y B 1601  1673  PDB    3J7Y     3J7Y          1601   1673             
DBREF  3J7Y f    1   328  PDB    3J7Y     3J7Y             1    328             
DBREF  3J7Y t    1   414  PDB    3J7Y     3J7Y             1    414             
SEQRES   1 A 1559    G   C   U   A   A   A   C   C   U   A   G   C   C          
SEQRES   2 A 1559    C   C   A   A   A   C   C   C   A   C   U   C   C          
SEQRES   3 A 1559    A   C   C   U   U   A   C   U   A   C   C   A   G          
SEQRES   4 A 1559    A   C   A   A   C   C   U   U   A   G   C   C   A          
SEQRES   5 A 1559    A   A   C   C   A   U   U   U   A   C   C   C   A          
SEQRES   6 A 1559    A   A   U   A   A   A   G   U   A   U   A   G   G          
SEQRES   7 A 1559    C   G   A   U   A   G   A   A   A   U   U   G   A          
SEQRES   8 A 1559    A   A   C   C   U   G   G   C   G   C   A   A   U          
SEQRES   9 A 1559    A   G   A   U   A   U   A   G   U   A   C   C   G          
SEQRES  10 A 1559    C   A   A   G   G   G   A   A   A   G   A   U   G          
SEQRES  11 A 1559    A   A   A   A   A   U   U   A   U   A   A   C   C          
SEQRES  12 A 1559    A   A   G   C   A   U   A   A   U   A   U   A   G          
SEQRES  13 A 1559    C   A   A   G   G   A   C   U   A   A   C   C   C          
SEQRES  14 A 1559    C   U   A   U   A   C   C   U   U   C   U   G   C          
SEQRES  15 A 1559    A   U   A   A   U   G   A   A   U   U   A   A   C          
SEQRES  16 A 1559    U   A   G   A   A   A   U   A   A   C   U   U   U          
SEQRES  17 A 1559    G   C   A   A   G   G   A   G   A   G   C   C   A          
SEQRES  18 A 1559    A   A   G   C   U   A   A   G   A   C   C   C   C          
SEQRES  19 A 1559    C   G   A   A   A   C   C   A   G   A   C   G   A          
SEQRES  20 A 1559    G   C   U   A   C   C   U   A   A   G   A   A   C          
SEQRES  21 A 1559    A   G   C   U   A   A   A   A   G   A   G   C   A          
SEQRES  22 A 1559    C   A   C   C   C   G   U   C   U   A   U   G   U          
SEQRES  23 A 1559    A   G   C   A   A   A   A   U   A   G   U   G   G          
SEQRES  24 A 1559    G   A   A   G   A   U   U   U   A   U   A   G   G          
SEQRES  25 A 1559    U   A   G   A   G   G   C   G   A   C   A   A   A          
SEQRES  26 A 1559    C   C   U   A   C   C   G   A   G   C   C   U   G          
SEQRES  27 A 1559    G   U   G   A   U   A   G   C   U   G   G   U   U          
SEQRES  28 A 1559    G   U   C   C   A   A   G   A   U   A   G   A   A          
SEQRES  29 A 1559    U   C   U   U   A   G   U   U   C   A   A   C   U          
SEQRES  30 A 1559    U   U   A   A   A   U   U   U   G   C   C   C   A          
SEQRES  31 A 1559    C   A   G   A   A   C   C   C   U   C   U   A   A          
SEQRES  32 A 1559    A   U   C   C   C   C   U   U   G   U   A   A   A          
SEQRES  33 A 1559    U   U   U   A   A   C   U   G   U   U   A   G   U          
SEQRES  34 A 1559    C   C   A   A   A   G   A   G   G   A   A   C   A          
SEQRES  35 A 1559    G   C   U   C   U   U   U   G   G   A   C   A   C          
SEQRES  36 A 1559    U   A   G   G   A   A   A   A   A   A   C   C   U          
SEQRES  37 A 1559    U   G   U   A   G   A   G   A   G   A   G   U   A          
SEQRES  38 A 1559    A   A   A   A   A   U   U   U   A   A   C   A   C          
SEQRES  39 A 1559    C   C   A   U   A   G   U   A   G   G   C   C   U          
SEQRES  40 A 1559    A   A   A   A   G   C   A   G   C   C   A   C   C          
SEQRES  41 A 1559    A   A   U   U   A   A   G   A   A   A   G   C   G          
SEQRES  42 A 1559    U   U   C   A   A   G   C   U   C   A   A   C   A          
SEQRES  43 A 1559    C   C   C   A   C   U   A   C   C   U   A   A   A          
SEQRES  44 A 1559    A   A   A   U   C   C   C   A   A   A   C   A   U          
SEQRES  45 A 1559    A   U   A   A   C   U   G   A   A   C   U   C   C          
SEQRES  46 A 1559    U   C   A   C   A   C   C   C   A   A   U   U   G          
SEQRES  47 A 1559    G   A   C   C   A   A   U   C   U   A   U   C   A          
SEQRES  48 A 1559    C   C   C   U   A   U   A   G   A   A   G   A   A          
SEQRES  49 A 1559    C   U   A   A   U   G   U   U   A   G   U   A   U          
SEQRES  50 A 1559    A   A   G   U   A   A   C   A   U   G   A   A   A          
SEQRES  51 A 1559    A   C   A   U   U   C   U   C   C   U   C   C   G          
SEQRES  52 A 1559    C   A   U   A   A   G   C   C   U   G   C   G   U          
SEQRES  53 A 1559    C   A   G   A   U   U   A   A   A   A   C   A   C          
SEQRES  54 A 1559    U   G   A   A   C   U   G   A   C   A   A   U   U          
SEQRES  55 A 1559    A   A   C   A   G   C   C   C   A   A   U   A   U          
SEQRES  56 A 1559    C   U   A   C   A   A   U   C   A   A   C   C   A          
SEQRES  57 A 1559    A   C   A   A   G   U   C   A   U   U   A   U   U          
SEQRES  58 A 1559    A   C   C   C   U   C   A   C   U   G   U   C   A          
SEQRES  59 A 1559    A   C   C   C   A   A   C   A   C   A   G   G   C          
SEQRES  60 A 1559    A   U   G   C   U   C   A   U   A   A   G   G   A          
SEQRES  61 A 1559    A   A   G   G   U   U   A   A   A   A   A   A   A          
SEQRES  62 A 1559    G   U   A   A   A   A   G   G   A   A   C   U   C          
SEQRES  63 A 1559    G   G   C   A   A   A   U   C   U   U   A   C   C          
SEQRES  64 A 1559    C   C   G   C   C   U   G   U   U   U   A   C   C          
SEQRES  65 A 1559    A   A   A   A   A   C   A   U   C   A   C   C   U          
SEQRES  66 A 1559    C   U   A   G   C   A   U   C   A   C   C   A   G          
SEQRES  67 A 1559    U   A   U   U   A   G   A   G   G   C   A   C   C          
SEQRES  68 A 1559    G   C   C   U   G   C   C   C   A   G   U   G   A          
SEQRES  69 A 1559    C   A   C   A   U   G   U   U   U   A   A   C   G          
SEQRES  70 A 1559    G   C   C   G   C   G   G   U   A   C   C   C   U          
SEQRES  71 A 1559    A   A   C   C   G   U   G   C   A   A   A   G   G          
SEQRES  72 A 1559    U   A   G   C   A   U   A   A   U   C   A   C   U          
SEQRES  73 A 1559    U   G   U   U   C   C   U   U   A   A   A   U   A          
SEQRES  74 A 1559    G   G   G   A   C   C   U   G   U   A   U   G   A          
SEQRES  75 A 1559    A   U   G   G   C   U   C   C   A   C   G   A   G          
SEQRES  76 A 1559    G   G   U   U   C   A   G   C   U   G   U   C   U          
SEQRES  77 A 1559    C   U   U   A   C   U   U   U   U   A   A   C   C          
SEQRES  78 A 1559    A   G   U   G   A   A   A   U   U   G   A   C   C          
SEQRES  79 A 1559    U   G   C   C   C   G   U   G   A   A   G   A   G          
SEQRES  80 A 1559    G   C   G   G   G   C   A   U   A   A   C   A   C          
SEQRES  81 A 1559    A   G   C   A   A   G   A   C   G   A   G   A   A          
SEQRES  82 A 1559    G   A   C   C   C   U   A   U   G   G   A   G   C          
SEQRES  83 A 1559    U   U   U   A   A   U   U   U   A   U   U   A   A          
SEQRES  84 A 1559    U   G   C   A   A   A   C   A   G   U   A   C   C          
SEQRES  85 A 1559    U   A   A   C   A   A   A   C   C   C   A   C   A          
SEQRES  86 A 1559    G   G   U   C   C   U   A   A   A   C   U   A   C          
SEQRES  87 A 1559    C   A   A   A   C   C   U   G   C   A   U   U   A          
SEQRES  88 A 1559    A   A   A   A   U   U   U   C   G   G   U   U   G          
SEQRES  89 A 1559    G   G   G   C   G   A   C   C   U   C   G   G   A          
SEQRES  90 A 1559    G   C   A   G   A   A   C   C   C   A   A   C   C          
SEQRES  91 A 1559    U   C   C   G   A   G   C   A   G   U   A   C   A          
SEQRES  92 A 1559    U   G   C   U   A   A   G   A   C   U   U   C   A          
SEQRES  93 A 1559    C   C   A   G   U   C   A   A   A   G   C   G   A          
SEQRES  94 A 1559    A   C   U   A   C   U   A   U   A   C   U   C   A          
SEQRES  95 A 1559    A   U   U   G   A   U   C   C   A   A   U   A   A          
SEQRES  96 A 1559    C   U   U   G   A   C   C   A   A   C   G   G   A          
SEQRES  97 A 1559    A   C   A   A   G   U   U   A   C   C   C   U   A          
SEQRES  98 A 1559    G   G   G   A   U   A   A   C   A   G   C   G   C          
SEQRES  99 A 1559    A   A   U   C   C   U   A   U   U   C   U   A   G          
SEQRES 100 A 1559    A   G   U   C   C   A   U   A   U   C   A   A   C          
SEQRES 101 A 1559    A   A   U   A   G   G   G   U   U   U   A   C   G          
SEQRES 102 A 1559    A   C   C   U   C   G   A   U   G   U   U   G   G          
SEQRES 103 A 1559    A   U   C   A   G   G   A   C   A   U   C   C   C          
SEQRES 104 A 1559    G   A   U   G   G   U   G   C   A   G   C   C   G          
SEQRES 105 A 1559    C   U   A   U   U   A   A   A   G   G   U   U   C          
SEQRES 106 A 1559    G   U   U   U   G   U   U   C   A   A   C   G   A          
SEQRES 107 A 1559    U   U   A   A   A   G   U   C   C   U   A   C   G          
SEQRES 108 A 1559    U   G   A   U   C   U   G   A   G   U   U   C   A          
SEQRES 109 A 1559    G   A   C   C   G   G   A   G   U   A   A   U   C          
SEQRES 110 A 1559    C   A   G   G   U   C   G   G   U   U   U   C   U          
SEQRES 111 A 1559    A   U   C   U   A   C   U   U   U   C   A   A   A          
SEQRES 112 A 1559    U   U   C   C   U   C   C   C   U   G   U   A   C          
SEQRES 113 A 1559    G   A   A   A   G   G   A   C   A   A   G   A   G          
SEQRES 114 A 1559    A   A   A   U   A   A   G   G   C   C   U   A   C          
SEQRES 115 A 1559    U   U   C   A   C   A   A   A   G   C   G   C   C          
SEQRES 116 A 1559    U   U   C   C   C   C   C   G   U   A   A   A   U          
SEQRES 117 A 1559    G   A   U   A   U   C   A   U   C   U   C   A   A          
SEQRES 118 A 1559    C   U   U   A   G   U   A   U   U   A   U   A   C          
SEQRES 119 A 1559    C   C   A   C   A   C   C   C   A   C   C   C   A          
SEQRES 120 A 1559    A   G   A   A   C   A   G   G   G   U   U   U              
SEQRES   1 B   73    C   C   A   G   A   G   U   G   U   A   G   C   U          
SEQRES   2 B   73    U   A   A   C   A   C   A   A   A   G   C   A   C          
SEQRES   3 B   73    C   C   A   A   C   U   U   A   C   A   C   U   U          
SEQRES   4 B   73    A   G   G   A   G   A   U   U   U   C   A   A   C          
SEQRES   5 B   73    U   U   A   A   C   U   U   G   A   C   C   G   C          
SEQRES   6 B   73    U   C   U   G   A   C   C   A                              
SEQRES   1 D  305  MET ALA LEU CYS ALA LEU THR ARG ALA LEU ARG SER LEU          
SEQRES   2 D  305  ASN LEU ALA PRO PRO THR VAL ALA ALA PRO ALA PRO SER          
SEQRES   3 D  305  LEU PHE PRO ALA ALA GLN MET MET ASN ASN GLY LEU LEU          
SEQRES   4 D  305  GLN GLN PRO SER ALA LEU MET LEU LEU PRO CYS ARG PRO          
SEQRES   5 D  305  VAL LEU THR SER VAL ALA LEU ASN ALA ASN PHE VAL SER          
SEQRES   6 D  305  TRP LYS SER ARG THR LYS TYR THR ILE THR PRO VAL LYS          
SEQRES   7 D  305  MET ARG LYS SER GLY GLY ARG ASP HIS THR GLY ARG ILE          
SEQRES   8 D  305  ARG VAL HIS GLY ILE GLY GLY GLY HIS LYS GLN ARG TYR          
SEQRES   9 D  305  ARG MET ILE ASP PHE LEU ARG PHE ARG PRO GLU GLU THR          
SEQRES  10 D  305  LYS SER GLY PRO PHE GLU GLU LYS VAL ILE GLN VAL ARG          
SEQRES  11 D  305  TYR ASP PRO CYS ARG SER ALA ASP ILE ALA LEU VAL ALA          
SEQRES  12 D  305  GLY GLY SER ARG LYS ARG TRP ILE ILE ALA THR GLU ASN          
SEQRES  13 D  305  MET GLN ALA GLY ASP THR ILE LEU ASN SER ASN HIS ILE          
SEQRES  14 D  305  GLY ARG MET ALA VAL ALA ALA ARG GLU GLY ASP ALA HIS          
SEQRES  15 D  305  PRO LEU GLY ALA LEU PRO VAL GLY THR LEU ILE ASN ASN          
SEQRES  16 D  305  VAL GLU SER GLU PRO GLY ARG GLY ALA GLN TYR ILE ARG          
SEQRES  17 D  305  ALA ALA GLY THR CYS GLY VAL LEU LEU ARG LYS VAL ASN          
SEQRES  18 D  305  GLY THR ALA ILE ILE GLN LEU PRO SER LYS ARG GLN MET          
SEQRES  19 D  305  GLN VAL LEU GLU THR CYS VAL ALA THR VAL GLY ARG VAL          
SEQRES  20 D  305  SER ASN VAL ASP HIS ASN LYS ARG VAL ILE GLY LYS ALA          
SEQRES  21 D  305  GLY ARG ASN ARG TRP LEU GLY LYS ARG PRO ASN SER GLY          
SEQRES  22 D  305  ARG TRP HIS ARG LYS GLY GLY TRP ALA GLY ARG LYS ILE          
SEQRES  23 D  305  ARG PRO LEU PRO PRO MET LYS SER TYR VAL LYS LEU PRO          
SEQRES  24 D  305  SER ALA SER ALA GLN SER                                      
SEQRES   1 E  348  MET PRO GLY TRP ARG LEU LEU THR GLN VAL GLY ALA GLN          
SEQRES   2 E  348  VAL LEU GLY ARG LEU GLY ASP GLY LEU GLY ALA ALA LEU          
SEQRES   3 E  348  GLY PRO GLY ASN ARG THR HIS ILE TRP LEU PHE VAL ARG          
SEQRES   4 E  348  GLY LEU HIS GLY LYS SER GLY THR TRP TRP ASP GLU HIS          
SEQRES   5 E  348  LEU SER GLU GLU ASN VAL PRO PHE ILE LYS GLN LEU VAL          
SEQRES   6 E  348  SER ASP GLU ASP LYS ALA GLN LEU ALA SER LYS LEU CYS          
SEQRES   7 E  348  PRO LEU LYS ASP GLU PRO TRP PRO ILE HIS PRO TRP GLU          
SEQRES   8 E  348  PRO GLY SER PHE ARG VAL GLY LEU ILE ALA LEU LYS LEU          
SEQRES   9 E  348  GLY MET MET PRO LEU TRP THR LYS ASP GLY GLN LYS HIS          
SEQRES  10 E  348  VAL VAL THR LEU LEU GLN VAL GLN ASP CYS HIS VAL LEU          
SEQRES  11 E  348  LYS TYR THR SER LYS GLU ASN CYS ASN GLY LYS MET ALA          
SEQRES  12 E  348  THR LEU SER VAL GLY GLY LYS THR VAL SER ARG PHE ARG          
SEQRES  13 E  348  LYS ALA THR SER ILE LEU GLU PHE TYR ARG GLU LEU GLY          
SEQRES  14 E  348  LEU PRO PRO LYS GLN THR VAL LYS ILE PHE ASN ILE THR          
SEQRES  15 E  348  ASP ASN ALA ALA ILE LYS PRO GLY THR PRO LEU TYR ALA          
SEQRES  16 E  348  ALA HIS PHE ARG PRO GLY GLN TYR VAL ASP VAL THR ALA          
SEQRES  17 E  348  LYS THR ILE GLY LYS GLY PHE GLN GLY VAL MET LYS ARG          
SEQRES  18 E  348  TRP GLY PHE LYS GLY GLN PRO ALA THR HIS GLY GLN THR          
SEQRES  19 E  348  LYS THR HIS ARG ARG PRO GLY ALA VAL ALA THR GLY ASP          
SEQRES  20 E  348  ILE GLY ARG VAL TRP PRO GLY THR LYS MET PRO GLY LYS          
SEQRES  21 E  348  MET GLY ASN ILE TYR ARG THR GLU TYR GLY LEU LYS VAL          
SEQRES  22 E  348  TRP ARG ILE ASN THR LYS HIS ASN ILE ILE TYR VAL ASN          
SEQRES  23 E  348  GLY SER VAL PRO GLY HIS LYS ASN CYS LEU VAL LYS VAL          
SEQRES  24 E  348  LYS ASP SER LYS LEU PRO ALA TYR LYS ASP LEU GLY LYS          
SEQRES  25 E  348  ASN LEU PRO PHE PRO THR TYR PHE PRO ASP GLY ASP GLU          
SEQRES  26 E  348  GLU GLU LEU PRO GLU ASP LEU TYR ASP GLU ASN VAL CYS          
SEQRES  27 E  348  GLN PRO GLY ALA PRO SER ILE THR PHE ALA                      
SEQRES   1 F  311  MET LEU GLN PHE VAL ARG ALA GLY ALA ARG ALA TRP LEU          
SEQRES   2 F  311  ARG PRO THR GLY SER GLN GLY LEU SER SER LEU ALA GLU          
SEQRES   3 F  311  GLU ALA ALA ARG ALA THR GLU ASN PRO GLU GLN VAL ALA          
SEQRES   4 F  311  SER GLU GLY LEU PRO GLU PRO VAL LEU ARG LYS VAL GLU          
SEQRES   5 F  311  LEU PRO VAL PRO THR HIS ARG ARG PRO VAL GLN ALA TRP          
SEQRES   6 F  311  VAL GLU SER LEU ARG GLY PHE GLU GLN GLU ARG VAL GLY          
SEQRES   7 F  311  LEU ALA ASP LEU HIS PRO ASP VAL PHE ALA THR ALA PRO          
SEQRES   8 F  311  ARG LEU ASP ILE LEU HIS GLN VAL ALA MET TRP GLN LYS          
SEQRES   9 F  311  ASN PHE LYS ARG ILE SER TYR ALA LYS THR LYS THR ARG          
SEQRES  10 F  311  ALA GLU VAL ARG GLY GLY GLY ARG LYS PRO TRP PRO GLN          
SEQRES  11 F  311  LYS GLY THR GLY ARG ALA ARG HIS GLY SER ILE ARG SER          
SEQRES  12 F  311  PRO LEU TRP ARG GLY GLY GLY VAL ALA HIS GLY PRO ARG          
SEQRES  13 F  311  GLY PRO THR SER TYR TYR TYR MET LEU PRO MET LYS VAL          
SEQRES  14 F  311  ARG ALA LEU GLY LEU LYS VAL ALA LEU THR VAL LYS LEU          
SEQRES  15 F  311  ALA GLN ASP ASP LEU HIS ILE MET ASP SER LEU GLU LEU          
SEQRES  16 F  311  PRO THR GLY ASP PRO GLN TYR LEU THR GLU LEU ALA HIS          
SEQRES  17 F  311  TYR ARG ARG TRP GLY ASP SER VAL LEU LEU VAL ASP LEU          
SEQRES  18 F  311  THR HIS GLU GLU MET PRO GLN SER ILE VAL GLU ALA THR          
SEQRES  19 F  311  SER ARG LEU LYS THR PHE ASN LEU ILE PRO ALA VAL GLY          
SEQRES  20 F  311  LEU ASN VAL HIS SER MET LEU LYS HIS GLN THR LEU VAL          
SEQRES  21 F  311  LEU THR LEU PRO THR VAL ALA PHE LEU GLU ASP LYS LEU          
SEQRES  22 F  311  LEU TRP GLN ASP SER ARG TYR ARG PRO LEU TYR PRO PHE          
SEQRES  23 F  311  SER LEU PRO TYR SER ASP PHE PRO ARG PRO LEU PRO HIS          
SEQRES  24 F  311  ALA THR GLN GLY PRO ALA ALA THR PRO TYR HIS CYS              
SEQRES   1 H  267  MET ALA ALA PRO VAL VAL THR ALA PRO GLY ARG ALA LEU          
SEQRES   2 H  267  LEU ARG ALA GLY ALA GLY ARG LEU LEU ARG GLY GLY VAL          
SEQRES   3 H  267  GLN GLU LEU LEU ARG PRO ARG HIS GLU GLY ASN ALA PRO          
SEQRES   4 H  267  ASP LEU ALA CYS ASN PHE SER LEU SER GLN ASN ARG GLY          
SEQRES   5 H  267  THR VAL ILE VAL GLU ARG TRP TRP LYS VAL PRO LEU ALA          
SEQRES   6 H  267  GLY GLU GLY ARG LYS PRO ARG LEU HIS ARG ARG HIS ARG          
SEQRES   7 H  267  VAL TYR LYS LEU VAL GLU ASP THR LYS HIS ARG PRO LYS          
SEQRES   8 H  267  GLU ASN LEU GLU LEU ILE LEU THR GLN SER VAL GLU ASN          
SEQRES   9 H  267  VAL GLY VAL ARG GLY ASP LEU VAL SER VAL LYS LYS SER          
SEQRES  10 H  267  LEU GLY ARG ASN ARG LEU LEU PRO GLN GLY LEU ALA VAL          
SEQRES  11 H  267  TYR ALA SER PRO GLU ASN LYS LYS LEU PHE GLU GLU GLU          
SEQRES  12 H  267  LYS LEU LEU ARG GLN GLU GLY LYS LEU GLU LYS ILE GLN          
SEQRES  13 H  267  THR LYS ALA GLY GLU ALA THR VAL LYS PHE LEU LYS SER          
SEQRES  14 H  267  CYS ARG LEU GLU VAL GLY MET LYS ASN ASN VAL LYS TRP          
SEQRES  15 H  267  GLU LEU ASN PRO GLU ILE VAL ALA ARG HIS PHE PHE LYS          
SEQRES  16 H  267  ASN LEU GLY VAL VAL VAL ALA PRO HIS THR LEU LYS LEU          
SEQRES  17 H  267  PRO GLU GLU PRO ILE THR ARG TRP GLY GLU TYR TRP CYS          
SEQRES  18 H  267  GLU VAL THR VAL ASN GLY LEU ASP THR VAL ARG VAL PRO          
SEQRES  19 H  267  MET SER VAL VAL ASN PHE GLU LYS PRO LYS THR LYS ARG          
SEQRES  20 H  267  TYR LYS TYR TRP LEU ALA GLN GLN ALA ALA LYS ALA MET          
SEQRES  21 H  267  ALA PRO THR SER PRO GLN ILE                                  
SEQRES   1 I  261  MET ALA ALA ALA VAL ALA GLY MET LEU ARG GLY GLY LEU          
SEQRES   2 I  261  LEU PRO GLN ALA GLY ARG LEU PRO THR LEU GLN THR VAL          
SEQRES   3 I  261  ARG TYR GLY SER LYS ALA VAL THR ARG HIS ARG ARG VAL          
SEQRES   4 I  261  MET HIS PHE GLN ARG GLN LYS LEU MET ALA VAL THR GLU          
SEQRES   5 I  261  TYR ILE PRO PRO LYS PRO ALA ILE HIS PRO SER CYS LEU          
SEQRES   6 I  261  PRO SER PRO PRO SER PRO PRO GLN GLU GLU ILE GLY LEU          
SEQRES   7 I  261  ILE ARG LEU LEU ARG ARG GLU ILE ALA ALA VAL PHE GLN          
SEQRES   8 I  261  ASP ASN ARG MET ILE ALA VAL CYS GLN ASN VAL ALA LEU          
SEQRES   9 I  261  SER ALA GLU ASP LYS LEU LEU MET ARG HIS GLN LEU ARG          
SEQRES  10 I  261  LYS HIS LYS ILE LEU MET LYS VAL PHE PRO ASN GLN VAL          
SEQRES  11 I  261  LEU LYS PRO PHE LEU GLU ASP SER LYS TYR GLN ASN LEU          
SEQRES  12 I  261  LEU PRO LEU PHE VAL GLY HIS ASN MET LEU LEU VAL SER          
SEQRES  13 I  261  GLU GLU PRO LYS VAL LYS GLU MET VAL ARG ILE LEU ARG          
SEQRES  14 I  261  THR VAL PRO PHE LEU PRO LEU LEU GLY GLY CYS ILE ASP          
SEQRES  15 I  261  ASP THR ILE LEU SER ARG GLN GLY PHE ILE ASN TYR SER          
SEQRES  16 I  261  LYS LEU PRO SER LEU PRO LEU VAL GLN GLY GLU LEU VAL          
SEQRES  17 I  261  GLY GLY LEU THR CYS LEU THR ALA GLN THR HIS SER LEU          
SEQRES  18 I  261  LEU GLN HIS GLN PRO LEU GLN LEU THR THR LEU LEU ASP          
SEQRES  19 I  261  GLN TYR ILE ARG GLU GLN ARG GLU LYS ASP SER VAL MET          
SEQRES  20 I  261  SER ALA ASN GLY LYS PRO ASP PRO ASP THR VAL PRO ASP          
SEQRES  21 I  261  SER                                                          
SEQRES   1 J  192  MET SER LYS LEU GLY ARG ALA ALA ARG GLY LEU ARG LYS          
SEQRES   2 J  192  PRO GLU VAL GLY GLY VAL ILE ARG ALA ILE VAL ARG ALA          
SEQRES   3 J  192  GLY LEU ALA MET PRO GLY PRO PRO LEU GLY PRO VAL LEU          
SEQRES   4 J  192  GLY GLN ARG GLY VAL SER ILE ASN GLN PHE CYS LYS GLU          
SEQRES   5 J  192  PHE ASN GLU ARG THR LYS ASP ILE LYS GLU GLY ILE PRO          
SEQRES   6 J  192  LEU PRO THR LYS ILE LEU VAL LYS PRO ASP ARG THR PHE          
SEQRES   7 J  192  GLU ILE LYS ILE GLY GLN PRO THR VAL SER TYR PHE LEU          
SEQRES   8 J  192  LYS ALA ALA ALA GLY ILE GLU LYS GLY ALA ARG GLN THR          
SEQRES   9 J  192  GLY LYS GLU VAL ALA GLY LEU VAL THR LEU LYS HIS VAL          
SEQRES  10 J  192  TYR GLU ILE ALA ARG ILE LYS ALA GLN ASP GLU ALA PHE          
SEQRES  11 J  192  ALA LEU GLN ASP VAL PRO LEU SER SER VAL VAL ARG SER          
SEQRES  12 J  192  ILE ILE GLY SER ALA ARG SER LEU GLY ILE ARG VAL VAL          
SEQRES  13 J  192  LYS ASP LEU SER SER GLU GLU LEU ALA ALA PHE GLN LYS          
SEQRES  14 J  192  GLU ARG ALA ILE PHE LEU ALA ALA GLN LYS GLU ALA ASP          
SEQRES  15 J  192  LEU ALA ALA GLN GLU GLU ALA ALA LYS LYS                      
SEQRES   1 K  178  MET SER SER PHE SER ARG ALA PRO GLN GLN TRP ALA THR          
SEQRES   2 K  178  PHE ALA ARG ILE TRP TYR LEU LEU ASP GLY LYS MET GLN          
SEQRES   3 K  178  PRO PRO GLY LYS LEU ALA ALA MET ALA SER ILE ARG LEU          
SEQRES   4 K  178  GLN GLY LEU HIS LYS PRO VAL TYR HIS ALA LEU SER ASP          
SEQRES   5 K  178  CYS GLY ASP HIS VAL VAL ILE MET ASN THR ARG HIS ILE          
SEQRES   6 K  178  ALA PHE SER GLY ASN LYS TRP GLU GLN LYS VAL TYR SER          
SEQRES   7 K  178  SER HIS THR GLY TYR PRO GLY GLY PHE ARG GLN VAL THR          
SEQRES   8 K  178  ALA ALA GLN LEU HIS LEU ARG ASP PRO VAL ALA ILE VAL          
SEQRES   9 K  178  LYS LEU ALA ILE TYR GLY MET LEU PRO LYS ASN LEU HIS          
SEQRES  10 K  178  ARG ARG THR MET MET GLU ARG LEU HIS LEU PHE PRO ASP          
SEQRES  11 K  178  GLU TYR ILE PRO GLU ASP ILE LEU LYS ASN LEU VAL GLU          
SEQRES  12 K  178  GLU LEU PRO GLN PRO ARG LYS ILE PRO LYS ARG LEU ASP          
SEQRES  13 K  178  GLU TYR THR GLN GLU GLU ILE ASP ALA PHE PRO ARG LEU          
SEQRES  14 K  178  TRP THR PRO PRO GLU ASP TYR ARG LEU                          
SEQRES   1 L  145  MET ALA PHE PHE THR GLY LEU TRP GLY PRO PHE THR CYS          
SEQRES   2 L  145  VAL SER ARG VAL LEU SER HIS HIS CYS PHE SER THR THR          
SEQRES   3 L  145  GLY SER LEU SER ALA ILE GLN LYS MET THR ARG VAL ARG          
SEQRES   4 L  145  VAL VAL ASP ASN SER ALA LEU GLY ASN SER PRO TYR HIS          
SEQRES   5 L  145  ARG ALA PRO ARG CYS ILE HIS VAL TYR LYS LYS ASN GLY          
SEQRES   6 L  145  VAL GLY LYS VAL GLY ASP GLN ILE LEU LEU ALA ILE LYS          
SEQRES   7 L  145  GLY GLN LYS LYS LYS ALA LEU ILE VAL GLY HIS CYS MET          
SEQRES   8 L  145  PRO GLY PRO ARG MET THR PRO ARG PHE ASP SER ASN ASN          
SEQRES   9 L  145  VAL VAL LEU ILE GLU ASP ASN GLY ASN PRO VAL GLY THR          
SEQRES  10 L  145  ARG ILE LYS THR PRO ILE PRO THR SER LEU ARG LYS ARG          
SEQRES  11 L  145  GLU GLY GLU TYR SER LYS VAL LEU ALA ILE ALA GLN ASN          
SEQRES  12 L  145  PHE VAL                                                      
SEQRES   1 M  296  MET ALA GLY PRO LEU GLN GLY GLY GLY ALA ARG ALA LEU          
SEQRES   2 M  296  ASP LEU LEU ARG GLY LEU PRO ARG VAL SER LEU ALA ASN          
SEQRES   3 M  296  LEU LYS PRO ASN PRO GLY SER LYS LYS PRO GLU ARG ARG          
SEQRES   4 M  296  PRO ARG GLY ARG ARG ARG GLY ARG LYS CYS GLY ARG GLY          
SEQRES   5 M  296  HIS LYS GLY GLU ARG GLN ARG GLY THR ARG PRO ARG LEU          
SEQRES   6 M  296  GLY PHE GLU GLY GLY GLN THR PRO PHE TYR ILE ARG ILE          
SEQRES   7 M  296  PRO LYS TYR GLY PHE ASN GLU GLY HIS SER PHE ARG ARG          
SEQRES   8 M  296  GLN TYR LYS PRO LEU SER LEU ASN ARG LEU GLN TYR LEU          
SEQRES   9 M  296  ILE ASP LEU GLY ARG VAL ASP PRO SER GLN PRO ILE ASP          
SEQRES  10 M  296  LEU THR GLN LEU VAL ASN GLY ARG GLY VAL THR ILE GLN          
SEQRES  11 M  296  PRO LEU LYS ARG ASP TYR GLY VAL GLN LEU VAL GLU GLU          
SEQRES  12 M  296  GLY ALA ASP THR PHE THR ALA LYS VAL ASN ILE GLU VAL          
SEQRES  13 M  296  GLN LEU ALA SER GLU LEU ALA ILE ALA ALA ILE GLU LYS          
SEQRES  14 M  296  ASN GLY GLY VAL VAL THR THR ALA PHE TYR ASP PRO ARG          
SEQRES  15 M  296  SER LEU ASP ILE VAL CYS LYS PRO VAL PRO PHE PHE LEU          
SEQRES  16 M  296  ARG GLY GLN PRO ILE PRO LYS ARG MET LEU PRO PRO GLU          
SEQRES  17 M  296  GLU LEU VAL PRO TYR TYR THR ASP ALA LYS ASN ARG GLY          
SEQRES  18 M  296  TYR LEU ALA ASP PRO ALA LYS PHE PRO GLU ALA ARG LEU          
SEQRES  19 M  296  GLU LEU ALA ARG LYS TYR GLY TYR ILE LEU PRO ASP ILE          
SEQRES  20 M  296  THR LYS ASP GLU LEU PHE LYS MET LEU CYS THR ARG LYS          
SEQRES  21 M  296  ASP PRO ARG GLN ILE PHE PHE GLY LEU ALA PRO GLY TRP          
SEQRES  22 M  296  VAL VAL ASN MET ALA ASP LYS LYS ILE LEU LYS PRO THR          
SEQRES  23 M  296  ASP GLU ASN LEU LEU LYS TYR TYR THR SER                      
SEQRES   1 N  251  MET TRP ARG LEU LEU ALA ARG ALA SER ALA PRO LEU LEU          
SEQRES   2 N  251  ARG VAL PRO LEU SER ASP SER TRP ALA LEU LEU PRO ALA          
SEQRES   3 N  251  SER ALA GLY VAL LYS THR LEU LEU PRO VAL PRO SER PHE          
SEQRES   4 N  251  GLU ASP VAL SER ILE PRO GLU LYS PRO LYS LEU ARG PHE          
SEQRES   5 N  251  ILE GLU ARG ALA PRO LEU VAL PRO LYS VAL ARG ARG GLU          
SEQRES   6 N  251  PRO LYS ASN LEU SER ASP ILE ARG GLY PRO SER THR GLU          
SEQRES   7 N  251  ALA THR GLU PHE THR GLU GLY ASN PHE ALA ILE LEU ALA          
SEQRES   8 N  251  LEU GLY GLY GLY TYR LEU HIS TRP GLY HIS PHE GLU MET          
SEQRES   9 N  251  MET ARG LEU THR ILE ASN ARG SER MET ASP PRO LYS ASN          
SEQRES  10 N  251  MET PHE ALA ILE TRP ARG VAL PRO ALA PRO PHE LYS PRO          
SEQRES  11 N  251  ILE THR ARG LYS SER VAL GLY HIS ARG MET GLY GLY GLY          
SEQRES  12 N  251  LYS GLY ALA ILE ASP HIS TYR VAL THR PRO VAL LYS ALA          
SEQRES  13 N  251  GLY ARG LEU VAL VAL GLU MET GLY GLY ARG CYS GLU PHE          
SEQRES  14 N  251  GLU GLU VAL GLN GLY PHE LEU ASP GLN VAL ALA HIS LYS          
SEQRES  15 N  251  LEU PRO PHE ALA ALA LYS ALA VAL SER ARG GLY THR LEU          
SEQRES  16 N  251  GLU LYS MET ARG LYS ASP GLN GLU GLU ARG GLU ARG ASN          
SEQRES  17 N  251  ASN GLN ASN PRO TRP THR PHE GLU ARG ILE ALA THR ALA          
SEQRES  18 N  251  ASN MET LEU GLY ILE ARG LYS VAL LEU SER PRO TYR ASP          
SEQRES  19 N  251  LEU THR HIS LYS GLY LYS TYR TRP GLY LYS PHE TYR MET          
SEQRES  20 N  251  PRO LYS ARG VAL                                              
SEQRES   1 O  175  MET ARG LEU SER VAL ALA ALA ALA ILE SER HIS GLY ARG          
SEQRES   2 O  175  VAL PHE ARG ARG MET GLY LEU GLY PRO GLU SER ARG ILE          
SEQRES   3 O  175  HIS LEU LEU ARG ASN LEU LEU THR GLY LEU VAL ARG HIS          
SEQRES   4 O  175  GLU ARG ILE GLU ALA PRO TRP ALA ARG VAL ASP GLU MET          
SEQRES   5 O  175  ARG GLY TYR ALA GLU LYS LEU ILE ASP TYR GLY LYS LEU          
SEQRES   6 O  175  GLY ASP THR ASN GLU ARG ALA MET ARG MET ALA ASP PHE          
SEQRES   7 O  175  TRP LEU THR GLU LYS ASP LEU ILE PRO LYS LEU PHE GLN          
SEQRES   8 O  175  VAL LEU ALA PRO ARG TYR LYS ASP GLN THR GLY GLY TYR          
SEQRES   9 O  175  THR ARG MET LEU GLN ILE PRO ASN ARG SER LEU ASP ARG          
SEQRES  10 O  175  ALA LYS MET ALA VAL ILE GLU TYR LYS GLY ASN CYS LEU          
SEQRES  11 O  175  PRO PRO LEU PRO LEU PRO ARG ARG ASP SER HIS LEU THR          
SEQRES  12 O  175  LEU LEU ASN GLN LEU LEU GLN GLY LEU ARG GLN ASP LEU          
SEQRES  13 O  175  ARG GLN SER GLN GLU ALA SER ASN HIS SER SER HIS THR          
SEQRES  14 O  175  ALA GLN THR PRO GLY ILE                                      
SEQRES   1 P  179  MET ALA LEU ARG SER GLN PHE TRP GLY PHE SER VAL CYS          
SEQRES   2 P  179  ARG ASN PRO GLY CYS ARG PHE ALA ALA LEU SER THR SER          
SEQRES   3 P  179  SER GLU PRO ALA ALA LYS PRO GLU VAL ASP PRO VAL GLU          
SEQRES   4 P  179  ASN GLU ALA VAL ALA PRO GLU PHE THR ASN ARG ASN PRO          
SEQRES   5 P  179  ARG ASN LEU GLU LEU LEU SER VAL ALA ARG LYS GLU ARG          
SEQRES   6 P  179  GLY TRP ARG THR VAL PHE PRO SER ARG GLU PHE TRP HIS          
SEQRES   7 P  179  ARG LEU ARG VAL ILE ARG THR GLN HIS HIS VAL GLU ALA          
SEQRES   8 P  179  LEU VAL GLU HIS GLN ASN GLY LYS VAL VAL VAL SER ALA          
SEQRES   9 P  179  SER THR ARG GLU TRP ALA ILE LYS LYS HIS LEU TYR SER          
SEQRES  10 P  179  THR ARG ASN VAL VAL ALA CYS GLU SER ILE GLY ARG VAL          
SEQRES  11 P  179  LEU ALA GLN ARG CYS LEU GLU ALA GLY ILE ASN PHE MET          
SEQRES  12 P  179  VAL TYR GLN PRO THR PRO TRP GLU ALA ALA SER ASP SER          
SEQRES  13 P  179  MET LYS ARG LEU GLN SER ALA MET THR GLU GLY GLY VAL          
SEQRES  14 P  179  VAL LEU ARG GLU PRO GLN ARG ILE TYR GLU                      
SEQRES   1 Q  292  MET ALA ALA CYS ILE ALA ALA GLY HIS TRP ALA ALA MET          
SEQRES   2 Q  292  GLY LEU GLY ARG SER PHE GLN ALA ALA ARG THR LEU LEU          
SEQRES   3 Q  292  PRO PRO PRO ALA SER ILE ALA CYS ARG VAL HIS ALA GLY          
SEQRES   4 Q  292  PRO VAL ARG GLN GLN SER THR GLY PRO SER GLU PRO GLY          
SEQRES   5 Q  292  ALA PHE GLN PRO PRO PRO LYS PRO VAL ILE VAL ASP LYS          
SEQRES   6 Q  292  HIS ARG PRO VAL GLU PRO GLU ARG ARG PHE LEU SER PRO          
SEQRES   7 Q  292  GLU PHE ILE PRO ARG ARG GLY ARG THR ASP PRO LEU LYS          
SEQRES   8 Q  292  PHE GLN ILE GLU ARG LYS ASP MET LEU GLU ARG ARG LYS          
SEQRES   9 Q  292  VAL LEU HIS ILE PRO GLU PHE TYR VAL GLY SER ILE LEU          
SEQRES  10 Q  292  ARG VAL THR THR ALA ASP PRO TYR ALA SER GLY LYS ILE          
SEQRES  11 Q  292  SER GLN PHE LEU GLY ILE CYS ILE GLN ARG SER GLY ARG          
SEQRES  12 Q  292  GLY LEU GLY ALA THR PHE ILE LEU ARG ASN VAL ILE GLU          
SEQRES  13 Q  292  GLY GLN GLY VAL GLU ILE CYS PHE GLU LEU TYR ASN PRO          
SEQRES  14 Q  292  ARG VAL GLN GLU ILE GLN VAL VAL LYS LEU GLU LYS ARG          
SEQRES  15 Q  292  LEU ASP ASP SER LEU LEU TYR LEU ARG ASP ALA LEU PRO          
SEQRES  16 Q  292  GLU TYR SER THR PHE ASP VAL ASN MET LYS PRO VAL VAL          
SEQRES  17 Q  292  GLN GLU PRO ASN GLN LYS VAL PRO VAL ASN GLU LEU LYS          
SEQRES  18 Q  292  VAL LYS MET LYS PRO LYS PRO TRP SER LYS ARG TRP GLU          
SEQRES  19 Q  292  ARG PRO ASN PHE ASN ILE LYS GLY ILE ARG PHE ASP LEU          
SEQRES  20 Q  292  CYS LEU THR GLU GLN GLN MET LYS GLU ALA GLN LYS TRP          
SEQRES  21 Q  292  ASN GLN PRO TRP LEU GLU PHE ASP MET MET ARG GLU TYR          
SEQRES  22 Q  292  ASP THR SER LYS ILE GLU ALA ALA ILE TRP LYS GLU ILE          
SEQRES  23 Q  292  GLU ALA SER LYS ARG SER                                      
SEQRES   1 R  149  MET VAL PHE LEU THR ALA GLN LEU TRP LEU ARG ASN ARG          
SEQRES   2 R  149  VAL THR ASP ARG TYR PHE ARG ILE GLN GLU VAL LEU LYS          
SEQRES   3 R  149  HIS ALA ARG HIS PHE ARG GLY ARG LYS ASN ARG CYS TYR          
SEQRES   4 R  149  ARG LEU ALA VAL ARG THR VAL ILE ARG ALA PHE VAL LYS          
SEQRES   5 R  149  CYS THR LYS ALA ARG TYR LEU LYS LYS LYS ASN MET ARG          
SEQRES   6 R  149  THR LEU TRP ILE ASN ARG ILE THR ALA ALA SER GLN GLU          
SEQRES   7 R  149  HIS GLY LEU LYS TYR PRO ALA LEU ILE GLY ASN LEU VAL          
SEQRES   8 R  149  LYS CYS GLN VAL GLU LEU ASN ARG LYS VAL LEU ALA ASP          
SEQRES   9 R  149  LEU ALA ILE TYR GLU PRO LYS THR PHE LYS SER LEU ALA          
SEQRES  10 R  149  ALA LEU ALA SER ARG ARG ARG HIS GLU GLY PHE ALA ALA          
SEQRES  11 R  149  ALA LEU GLY ASP GLY LYS GLU PRO GLU GLY ILE PHE SER          
SEQRES  12 R  149  ARG VAL VAL GLN TYR HIS                                      
SEQRES   1 S  205  MET ALA ALA SER SER LEU THR VAL THR LEU GLY ARG LEU          
SEQRES   2 S  205  ALA SER ALA CYS SER HIS SER ILE LEU ARG PRO SER GLY          
SEQRES   3 S  205  PRO GLY ALA ALA SER LEU TRP SER ALA SER ARG ARG PHE          
SEQRES   4 S  205  ASN SER GLN SER THR SER TYR LEU PRO GLY TYR VAL PRO          
SEQRES   5 S  205  LYS THR SER LEU SER SER PRO PRO TRP PRO GLU VAL VAL          
SEQRES   6 S  205  LEU PRO ASP PRO VAL GLU GLU THR ARG HIS HIS ALA GLU          
SEQRES   7 S  205  VAL VAL LYS LYS VAL ASN GLU MET ILE VAL THR GLY GLN          
SEQRES   8 S  205  TYR GLY ARG LEU PHE ALA VAL VAL HIS PHE ALA SER ARG          
SEQRES   9 S  205  GLN TRP LYS VAL THR SER GLU ASP LEU ILE LEU ILE GLY          
SEQRES  10 S  205  ASN GLU LEU ASP LEU ALA CYS GLY GLU ARG ILE ARG LEU          
SEQRES  11 S  205  GLU LYS VAL LEU LEU VAL GLY ALA ASP ASN PHE THR LEU          
SEQRES  12 S  205  LEU GLY LYS PRO LEU LEU GLY LYS ASP LEU VAL ARG VAL          
SEQRES  13 S  205  GLU ALA THR VAL ILE GLU LYS THR GLU SER TRP PRO ARG          
SEQRES  14 S  205  ILE ILE MET ARG PHE ARG LYS ARG LYS ASN PHE LYS LYS          
SEQRES  15 S  205  LYS ARG ILE VAL THR THR PRO GLN THR VAL LEU ARG ILE          
SEQRES  16 S  205  ASN SER ILE GLU ILE ALA PRO CYS LEU LEU                      
SEQRES   1 T  212  MET ALA ALA ALA VAL LEU GLY GLN LEU GLY ALA LEU TRP          
SEQRES   2 T  212  ILE HIS ASN LEU ARG SER ARG GLY LYS LEU ALA LEU GLY          
SEQRES   3 T  212  LEU LEU SER PHE HIS SER VAL LEU PRO GLN SER TYR ILE          
SEQRES   4 T  212  HIS THR SER ALA SER LEU ASP ILE SER ARG LYS TRP GLU          
SEQRES   5 T  212  LYS LYS ASN LYS ILE VAL TYR PRO PRO GLN LEU PRO GLY          
SEQRES   6 T  212  GLU PRO ARG ARG PRO ALA GLU ILE TYR HIS CYS ARG ARG          
SEQRES   7 T  212  GLN ILE LYS TYR SER LYS ASP LYS MET TRP TYR LEU ALA          
SEQRES   8 T  212  LYS LEU ILE ARG GLY MET SER ILE ASP GLN ALA LEU ALA          
SEQRES   9 T  212  GLN LEU GLU PHE ASN ASP LYS LYS GLY ALA LYS ILE ILE          
SEQRES  10 T  212  LYS GLU VAL LEU LEU GLU ALA GLN ASP MET ALA VAL ARG          
SEQRES  11 T  212  ASP HIS ASN VAL GLU PHE ARG SER ASN LEU TYR ILE ALA          
SEQRES  12 T  212  GLU SER THR SER GLY ARG GLY GLN CYS LEU LYS ARG ILE          
SEQRES  13 T  212  ARG TYR HIS GLY ARG GLY ARG PHE GLY ILE MET GLU LYS          
SEQRES  14 T  212  VAL TYR CYS HIS TYR PHE VAL LYS LEU VAL GLU GLY PRO          
SEQRES  15 T  212  PRO PRO PRO PRO GLU PRO PRO LYS THR ALA VAL ALA HIS          
SEQRES  16 T  212  ALA LYS GLU TYR ILE GLN GLN LEU ARG SER ARG THR ILE          
SEQRES  17 T  212  VAL HIS THR LEU                                              
SEQRES   1 U  153  MET ALA ARG ASN VAL VAL TYR PRO LEU TYR ARG LEU GLY          
SEQRES   2 U  153  GLY PRO GLN LEU ARG VAL PHE ARG THR ASN PHE PHE ILE          
SEQRES   3 U  153  GLN LEU VAL ARG PRO GLY VAL ALA GLN PRO GLU ASP THR          
SEQRES   4 U  153  VAL GLN PHE ARG ILE PRO MET GLU MET THR ARG VAL ASP          
SEQRES   5 U  153  LEU ARG ASN TYR LEU GLU GLY ILE TYR ASN VAL PRO VAL          
SEQRES   6 U  153  ALA ALA VAL ARG THR ARG VAL GLN HIS GLY SER ASN LYS          
SEQRES   7 U  153  ARG ARG ASP HIS ARG ASN VAL ARG ILE LYS LYS PRO ASP          
SEQRES   8 U  153  TYR LYS VAL ALA TYR VAL GLN LEU ALA HIS GLY GLN THR          
SEQRES   9 U  153  PHE THR PHE PRO ASP LEU PHE PRO GLU LYS ASP GLU SER          
SEQRES  10 U  153  PRO GLU GLY SER ALA ALA ASP ASP LEU TYR SER MET LEU          
SEQRES  11 U  153  GLU GLU GLU ARG GLN GLN ARG GLN SER SER ASP PRO ARG          
SEQRES  12 U  153  ARG GLY GLY VAL PRO SER TRP PHE GLY LEU                      
SEQRES   1 V  216  MET ARG LEU SER ALA LEU LEU ALA LEU ALA SER LYS VAL          
SEQRES   2 V  216  THR LEU PRO PRO HIS TYR ARG TYR GLY MET SER PRO PRO          
SEQRES   3 V  216  GLY SER VAL ALA ASP LYS ARG LYS ASN PRO PRO TRP ILE          
SEQRES   4 V  216  ARG ARG ARG PRO VAL VAL VAL GLU PRO ILE SER ASP GLU          
SEQRES   5 V  216  ASP TRP TYR LEU PHE CYS GLY ASP THR VAL GLU ILE LEU          
SEQRES   6 V  216  GLU GLY LYS ASP ALA GLY LYS GLN GLY LYS VAL VAL GLN          
SEQRES   7 V  216  VAL ILE ARG GLN ARG ASN TRP VAL VAL VAL GLY GLY LEU          
SEQRES   8 V  216  ASN THR HIS TYR ARG TYR ILE GLY LYS THR MET ASP TYR          
SEQRES   9 V  216  ARG GLY THR MET ILE PRO SER GLU ALA PRO LEU LEU HIS          
SEQRES  10 V  216  ARG GLN VAL LYS LEU VAL ASP PRO MET ASP ARG LYS PRO          
SEQRES  11 V  216  THR GLU ILE GLU TRP ARG PHE THR GLU ALA GLY GLU ARG          
SEQRES  12 V  216  VAL ARG VAL SER THR ARG SER GLY ARG ILE ILE PRO LYS          
SEQRES  13 V  216  PRO GLU PHE PRO ARG ALA ASP GLY ILE VAL PRO GLU THR          
SEQRES  14 V  216  TRP ILE ASP GLY PRO LYS ASP THR SER VAL GLU ASP ALA          
SEQRES  15 V  216  LEU GLU ARG THR TYR VAL PRO CYS LEU LYS THR LEU GLN          
SEQRES  16 V  216  GLU GLU VAL MET GLU ALA MET GLY ILE LYS GLU THR ARG          
SEQRES  17 V  216  LYS TYR LYS LYS VAL TYR TRP TYR                              
SEQRES   1 W  148  MET ALA SER VAL VAL LEU ALA LEU ARG THR ARG THR ALA          
SEQRES   2 W  148  VAL THR SER LEU LEU SER PRO THR PRO ALA THR ALA LEU          
SEQRES   3 W  148  ALA VAL ARG TYR ALA SER LYS LYS SER GLY GLY SER SER          
SEQRES   4 W  148  LYS ASN LEU GLY GLY LYS SER SER GLY ARG ARG GLN GLY          
SEQRES   5 W  148  ILE LYS LYS MET GLU GLY HIS TYR VAL HIS ALA GLY ASN          
SEQRES   6 W  148  ILE ILE ALA THR GLN ARG HIS PHE ARG TRP HIS PRO GLY          
SEQRES   7 W  148  ALA HIS VAL GLY VAL GLY LYS ASN LYS CYS LEU TYR ALA          
SEQRES   8 W  148  LEU GLU GLU GLY ILE VAL ARG TYR THR LYS GLU VAL TYR          
SEQRES   9 W  148  VAL PRO HIS PRO ARG ASN THR GLU ALA VAL ASP LEU ILE          
SEQRES  10 W  148  THR ARG LEU PRO LYS GLY ALA VAL LEU TYR LYS THR PHE          
SEQRES  11 W  148  VAL HIS VAL VAL PRO ALA LYS PRO GLU GLY THR PHE LYS          
SEQRES  12 W  148  LEU VAL ALA MET LEU                                          
SEQRES   1 X  256  MET PRO LEU HIS LYS TYR PRO VAL TRP LEU TRP LYS ARG          
SEQRES   2 X  256  LEU GLN LEU ARG GLU GLY ILE CYS SER ARG LEU PRO GLY          
SEQRES   3 X  256  HIS TYR LEU ARG SER LEU GLU GLU GLU ARG THR PRO THR          
SEQRES   4 X  256  PRO VAL HIS TYR ARG PRO HIS GLY ALA LYS PHE LYS ILE          
SEQRES   5 X  256  ASN PRO LYS ASN GLY GLN ARG GLU ARG VAL GLU ASP VAL          
SEQRES   6 X  256  PRO ILE PRO ILE TYR PHE PRO PRO GLU SER GLN ARG GLY          
SEQRES   7 X  256  LEU TRP GLY GLY GLU GLY TRP ILE LEU GLY GLN ILE TYR          
SEQRES   8 X  256  ALA ASN ASN ASP LYS LEU SER LYS ARG LEU LYS LYS VAL          
SEQRES   9 X  256  TRP LYS PRO GLN LEU PHE GLU ARG GLU PHE TYR SER GLU          
SEQRES  10 X  256  ILE LEU ASP LYS LYS PHE THR VAL THR VAL THR MET ARG          
SEQRES  11 X  256  THR LEU ASP LEU ILE ASP GLU ALA TYR GLY LEU ASP PHE          
SEQRES  12 X  256  TYR ILE LEU LYS ALA SER GLY GLU ASP LEU CYS SER LYS          
SEQRES  13 X  256  PHE GLY MET ASP LEU LYS ARG GLY MET LEU LEU ARG LEU          
SEQRES  14 X  256  ALA ARG GLN ASP PRO GLN LEU HIS PRO GLU ASP PRO GLU          
SEQRES  15 X  256  ARG ARG ALA ALA ILE TYR ASP LYS TYR LYS GLU PHE ALA          
SEQRES  16 X  256  ILE PRO GLU GLU GLU ALA GLU TRP VAL GLY LEU THR LEU          
SEQRES  17 X  256  GLU GLU ALA ILE GLU LYS GLN ARG LEU LEU GLU GLU LYS          
SEQRES  18 X  256  ASP PRO VAL PRO LEU PHE LYS ILE TYR VAL ALA GLU LEU          
SEQRES  19 X  256  ILE GLN GLN LEU GLN GLN GLN ALA LEU SER GLU PRO ALA          
SEQRES  20 X  256  VAL VAL GLN LYS ARG ALA SER GLY GLN                          
SEQRES   1 Y  250  MET ALA ALA ALA GLY LEU ALA LEU LEU CYS ARG ARG VAL          
SEQRES   2 Y  250  SER SER ALA LEU LYS SER SER ARG SER LEU ILE THR PRO          
SEQRES   3 Y  250  GLN VAL PRO ALA CYS THR GLY PHE PHE LEU SER LEU LEU          
SEQRES   4 Y  250  PRO LYS SER THR PRO ASN VAL THR SER PHE HIS GLN TYR          
SEQRES   5 Y  250  ARG LEU LEU HIS THR THR LEU SER ARG LYS GLY LEU GLU          
SEQRES   6 Y  250  GLU PHE PHE ASP ASP PRO LYS ASN TRP GLY GLN GLU LYS          
SEQRES   7 Y  250  VAL LYS SER GLY ALA ALA TRP THR CYS GLN GLN LEU ARG          
SEQRES   8 Y  250  ASN LYS SER ASN GLU ASP LEU HIS LYS LEU TRP TYR VAL          
SEQRES   9 Y  250  LEU LEU LYS GLU ARG ASN MET LEU LEU THR LEU GLU GLN          
SEQRES  10 Y  250  GLU ALA LYS ARG GLN ARG LEU PRO MET PRO SER PRO GLU          
SEQRES  11 Y  250  ARG LEU ASP LYS VAL VAL ASP SER MET ASP ALA LEU ASP          
SEQRES  12 Y  250  LYS VAL VAL GLN GLU ARG GLU ASP ALA LEU ARG LEU LEU          
SEQRES  13 Y  250  GLN THR GLY GLN GLU ARG ALA ARG PRO GLY ALA TRP ARG          
SEQRES  14 Y  250  ARG ASP ILE PHE GLY ARG ILE ILE TRP HIS LYS PHE LYS          
SEQRES  15 Y  250  GLN TRP VAL ILE PRO TRP HIS LEU ASN LYS ARG TYR ASN          
SEQRES  16 Y  250  ARG LYS ARG PHE PHE ALA LEU PRO TYR VAL ASP HIS PHE          
SEQRES  17 Y  250  LEU ARG LEU GLU ARG GLU LYS ARG ALA ARG ILE LYS ALA          
SEQRES  18 Y  250  ARG LYS GLU ASN LEU GLU ARG LYS LYS ALA LYS ILE LEU          
SEQRES  19 Y  250  LEU LYS LYS PHE PRO HIS LEU ALA GLU ALA GLN LYS SER          
SEQRES  20 Y  250  SER LEU VAL                                                  
SEQRES   1 Z  161  MET ALA GLY ILE LEU ARG LEU VAL VAL GLN TRP PRO PRO          
SEQRES   2 Z  161  GLY ARG LEU GLN THR VAL THR LYS GLY VAL GLU SER LEU          
SEQRES   3 Z  161  ILE CYS THR ASP TRP ILE ARG HIS LYS PHE THR ARG SER          
SEQRES   4 Z  161  ARG ILE PRO GLU LYS VAL PHE GLN ALA SER PRO GLU ASP          
SEQRES   5 Z  161  HIS GLU LYS TYR GLY GLY ASP PRO GLN ASN PRO HIS LYS          
SEQRES   6 Z  161  LEU HIS ILE VAL THR ARG ILE LYS SER THR ARG ARG ARG          
SEQRES   7 Z  161  PRO TYR TRP GLU LYS ASP ILE ILE LYS MET LEU GLY LEU          
SEQRES   8 Z  161  GLU LYS ALA HIS THR PRO GLN VAL HIS LYS ASN ILE PRO          
SEQRES   9 Z  161  SER VAL ASN ALA LYS LEU LYS VAL VAL LYS HIS LEU ILE          
SEQRES  10 Z  161  ARG ILE LYS PRO LEU LYS LEU PRO GLN GLY LEU PRO ALA          
SEQRES  11 Z  161  GLU GLU ASN MET SER ASN THR CYS LEU LYS SER THR GLY          
SEQRES  12 Z  161  GLU LEU VAL VAL GLN TRP HIS LEU LYS PRO VAL GLU GLN          
SEQRES  13 Z  161  LYS ALA HIS GLU SER                                          
SEQRES   1 0  188  MET ALA LEU ALA MET LEU VAL LEU VAL VAL SER PRO TRP          
SEQRES   2 0  188  SER ALA ALA ARG GLY VAL LEU ARG ASN TYR TRP GLU ARG          
SEQRES   3 0  188  LEU LEU ARG LYS LEU PRO GLN SER ARG PRO GLY PHE PRO          
SEQRES   4 0  188  SER PRO PRO TRP GLY PRO ALA LEU ALA VAL GLN GLY PRO          
SEQRES   5 0  188  ALA MET PHE THR GLU PRO ALA ASN ASP THR SER GLY SER          
SEQRES   6 0  188  LYS GLU ASN SER SER LEU LEU ASP SER ILE PHE TRP MET          
SEQRES   7 0  188  ALA ALA PRO LYS ASN ARG ARG THR ILE GLU VAL ASN ARG          
SEQRES   8 0  188  CYS ARG ARG ARG ASN PRO GLN LYS LEU ILE LYS VAL LYS          
SEQRES   9 0  188  ASN ASN ILE ASP VAL CYS PRO GLU CYS GLY HIS LEU LYS          
SEQRES  10 0  188  GLN LYS HIS VAL LEU CYS ALA TYR CYS TYR GLU LYS VAL          
SEQRES  11 0  188  CYS LYS GLU THR ALA GLU ILE ARG ARG GLN ILE GLY LYS          
SEQRES  12 0  188  GLN GLU GLY GLY PRO PHE LYS ALA PRO THR ILE GLU THR          
SEQRES  13 0  188  VAL VAL LEU TYR THR GLY GLU THR PRO SER GLU GLN ASP          
SEQRES  14 0  188  GLN GLY LYS ARG ILE ILE GLU ARG ASP ARG LYS ARG PRO          
SEQRES  15 0  188  SER TRP PHE THR GLN ASN                                      
SEQRES   1 1   65  MET PHE LEU SER ALA VAL PHE PHE ALA LYS SER LYS SER          
SEQRES   2 1   65  LYS ASN ILE LEU VAL ARG MET VAL SER GLU ALA GLY THR          
SEQRES   3 1   65  GLY PHE CYS PHE ASN THR LYS ARG ASN ARG LEU ARG GLU          
SEQRES   4 1   65  LYS LEU THR LEU LEU HIS TYR ASP PRO VAL VAL LYS GLN          
SEQRES   5 1   65  ARG VAL LEU PHE VAL GLU LYS LYS LYS ILE ARG SER LEU          
SEQRES   1 2   92  MET ALA VAL LEU ALA GLY SER LEU LEU GLY PRO THR SER          
SEQRES   2 2   92  ARG SER ALA ALA LEU LEU GLY GLY ARG TRP LEU GLN PRO          
SEQRES   3 2   92  ARG ALA TRP LEU GLY PHE PRO ASP ALA TRP GLY LEU PRO          
SEQRES   4 2   92  THR PRO GLN GLN ALA ARG GLY LYS ALA ARG GLY ASN GLU          
SEQRES   5 2   92  TYR GLN PRO SER ASN ILE LYS ARG LYS ASN LYS HIS GLY          
SEQRES   6 2   92  TRP VAL ARG ARG LEU SER THR PRO ALA GLY VAL GLN VAL          
SEQRES   7 2   92  ILE LEU ARG ARG MET LEU LYS GLY ARG LYS SER LEU SER          
SEQRES   8 2   92  HIS                                                          
SEQRES   1 3  188  MET ALA ALA SER ALA PHE ALA GLY ALA VAL ARG ALA ALA          
SEQRES   2 3  188  SER GLY ILE LEU ARG PRO LEU ASN ILE LEU ALA SER SER          
SEQRES   3 3  188  THR TYR ARG ASN CYS VAL LYS ASN ALA SER LEU ILE SER          
SEQRES   4 3  188  ALA LEU SER THR GLY ARG PHE SER HIS ILE GLN THR PRO          
SEQRES   5 3  188  VAL VAL SER SER THR PRO ARG LEU THR THR SER GLU ARG          
SEQRES   6 3  188  ASN LEU THR CYS GLY HIS THR SER VAL ILE LEU ASN ARG          
SEQRES   7 3  188  MET ALA PRO VAL LEU PRO SER VAL LEU LYS LEU PRO VAL          
SEQRES   8 3  188  ARG SER LEU THR TYR PHE SER ALA ARG LYS GLY LYS ARG          
SEQRES   9 3  188  LYS THR VAL LYS ALA VAL ILE ASP ARG PHE LEU ARG LEU          
SEQRES  10 3  188  HIS CYS GLY LEU TRP VAL ARG ARG LYS ALA GLY TYR LYS          
SEQRES  11 3  188  LYS LYS LEU TRP LYS LYS THR PRO ALA ARG LYS LYS ARG          
SEQRES  12 3  188  LEU ARG GLU PHE VAL PHE CYS ASN LYS THR GLN SER LYS          
SEQRES  13 3  188  LEU LEU ASP LYS MET THR THR SER PHE TRP LYS ARG ARG          
SEQRES  14 3  188  ASN TRP TYR VAL ASP ASP PRO TYR GLN LYS TYR HIS ASP          
SEQRES  15 3  188  ARG THR ASN LEU LYS VAL                                      
SEQRES   1 4  103  MET ALA ASN LEU PHE ILE ARG LYS MET VAL ASN PRO LEU          
SEQRES   2 4  103  LEU TYR LEU SER ARG HIS THR VAL LYS PRO ARG ALA LEU          
SEQRES   3 4  103  SER THR PHE LEU PHE GLY SER ILE ARG GLY ALA ALA PRO          
SEQRES   4 4  103  VAL ALA VAL GLU PRO GLY ALA ALA VAL ARG SER LEU LEU          
SEQRES   5 4  103  SER PRO GLY LEU LEU PRO HIS LEU LEU PRO ALA LEU GLY          
SEQRES   6 4  103  PHE LYS ASN LYS THR VAL LEU LYS LYS ARG CYS LYS ASP          
SEQRES   7 4  103  CYS TYR LEU VAL LYS ARG ARG GLY ARG TRP TYR VAL TYR          
SEQRES   8 4  103  CYS LYS THR HIS PRO ARG HIS LYS GLN ARG GLN MET              
SEQRES   1 5  423  MET ALA LEU ALA SER GLY PRO ALA ARG ARG ALA LEU ALA          
SEQRES   2 5  423  GLY SER GLY GLN LEU GLY LEU GLY GLY PHE GLY ALA PRO          
SEQRES   3 5  423  ARG ARG GLY ALA TYR GLU TRP GLY VAL ARG SER THR ARG          
SEQRES   4 5  423  LYS SER GLU PRO PRO PRO LEU ASP ARG VAL TYR GLU ILE          
SEQRES   5 5  423  PRO GLY LEU GLU PRO ILE THR PHE ALA GLY LYS MET HIS          
SEQRES   6 5  423  PHE VAL PRO TRP LEU ALA ARG PRO ILE PHE PRO PRO TRP          
SEQRES   7 5  423  ASP ARG GLY TYR LYS ASP PRO ARG PHE TYR ARG SER PRO          
SEQRES   8 5  423  PRO LEU HIS GLU HIS PRO LEU TYR LYS ASP GLN ALA CYS          
SEQRES   9 5  423  TYR ILE PHE HIS HIS ARG CYS ARG LEU LEU GLU GLY VAL          
SEQRES  10 5  423  LYS GLN ALA LEU TRP LEU THR LYS THR LYS LEU ILE GLU          
SEQRES  11 5  423  GLY LEU PRO GLU LYS VAL LEU SER LEU VAL ASP ASP PRO          
SEQRES  12 5  423  ARG ASN HIS ILE GLU ASN GLN ASP GLU CYS VAL LEU ASN          
SEQRES  13 5  423  VAL ILE SER HIS ALA ARG LEU TRP GLN THR THR GLU GLU          
SEQRES  14 5  423  ILE PRO LYS ARG GLU THR TYR CYS PRO VAL ILE VAL ASP          
SEQRES  15 5  423  ASN LEU ILE GLN LEU CYS LYS SER GLN ILE LEU LYS HIS          
SEQRES  16 5  423  PRO SER LEU ALA ARG ARG ILE CYS VAL GLN ASN SER THR          
SEQRES  17 5  423  PHE SER ALA THR TRP ASN ARG GLU SER LEU LEU LEU GLN          
SEQRES  18 5  423  VAL ARG GLY SER GLY GLY ALA ARG LEU SER THR LYS ASP          
SEQRES  19 5  423  PRO LEU PRO THR ILE ALA SER ARG GLU GLU ILE GLU ALA          
SEQRES  20 5  423  THR LYS ASN HIS VAL LEU GLU THR PHE TYR PRO ILE SER          
SEQRES  21 5  423  PRO ILE ILE ASP LEU HIS GLU CYS ASN ILE TYR ASP VAL          
SEQRES  22 5  423  LYS ASN ASP THR GLY PHE GLN GLU GLY TYR PRO TYR PRO          
SEQRES  23 5  423  TYR PRO HIS THR LEU TYR LEU LEU ASP LYS ALA ASN LEU          
SEQRES  24 5  423  ARG PRO HIS ARG LEU GLN PRO ASP GLN LEU ARG ALA LYS          
SEQRES  25 5  423  MET ILE LEU PHE ALA PHE GLY SER ALA LEU ALA GLN ALA          
SEQRES  26 5  423  ARG LEU LEU TYR GLY ASN ASP ALA LYS VAL LEU GLU GLN          
SEQRES  27 5  423  PRO VAL VAL VAL GLN SER VAL GLY THR ASP GLY ARG VAL          
SEQRES  28 5  423  PHE HIS PHE LEU VAL PHE GLN LEU ASN THR THR ASP LEU          
SEQRES  29 5  423  ASP CYS ASN GLU GLY VAL LYS ASN LEU ALA TRP VAL ASP          
SEQRES  30 5  423  SER ASP GLN LEU LEU TYR GLN HIS PHE TRP CYS LEU PRO          
SEQRES  31 5  423  VAL ILE LYS LYS ARG VAL VAL VAL GLU PRO VAL GLY PRO          
SEQRES  32 5  423  VAL GLY PHE LYS PRO GLU THR PHE ARG LYS PHE LEU ALA          
SEQRES  33 5  423  LEU TYR LEU HIS GLY ALA ALA                                  
SEQRES   1 6  380  MET ALA ALA PRO TRP TRP ARG ALA ALA LEU CYS GLU CYS          
SEQRES   2 6  380  ARG ARG TRP ARG GLY PHE SER THR SER ALA VAL LEU GLY          
SEQRES   3 6  380  ARG ARG THR PRO PRO LEU GLY PRO MET PRO ASN SER ASP          
SEQRES   4 6  380  ILE ASP LEU SER ASN LEU GLU ARG LEU GLU LYS TYR ARG          
SEQRES   5 6  380  SER PHE ASP ARG TYR ARG ARG ARG ALA GLU GLN GLU ALA          
SEQRES   6 6  380  GLN ALA PRO HIS TRP TRP ARG THR TYR ARG GLU TYR PHE          
SEQRES   7 6  380  GLY GLU LYS THR ASP PRO LYS GLU LYS ILE ASP ILE GLY          
SEQRES   8 6  380  LEU PRO PRO PRO LYS VAL SER ARG THR GLN GLN LEU LEU          
SEQRES   9 6  380  GLU ARG LYS GLN ALA ILE GLN GLU LEU ARG ALA ASN VAL          
SEQRES  10 6  380  GLU GLU GLU ARG ALA ALA ARG LEU ARG THR ALA SER VAL          
SEQRES  11 6  380  PRO LEU ASP ALA VAL ARG ALA GLU TRP GLU ARG THR CYS          
SEQRES  12 6  380  GLY PRO TYR HIS LYS GLN ARG LEU ALA GLU TYR TYR GLY          
SEQRES  13 6  380  LEU TYR ARG ASP LEU PHE HIS GLY ALA THR PHE VAL PRO          
SEQRES  14 6  380  ARG VAL PRO LEU HIS VAL ALA TYR ALA VAL GLY GLU ASP          
SEQRES  15 6  380  ASP LEU MET PRO VAL TYR CYS GLY ASN GLU VAL THR PRO          
SEQRES  16 6  380  THR GLU ALA ALA GLN ALA PRO GLU VAL THR TYR GLU ALA          
SEQRES  17 6  380  GLU GLU GLY SER LEU TRP THR LEU LEU LEU THR SER LEU          
SEQRES  18 6  380  ASP GLY HIS LEU LEU GLU PRO ASP ALA GLU TYR LEU HIS          
SEQRES  19 6  380  TRP LEU LEU THR ASN ILE PRO GLY ASN ARG VAL ALA GLU          
SEQRES  20 6  380  GLY GLN VAL THR CYS PRO TYR LEU PRO PRO PHE PRO ALA          
SEQRES  21 6  380  ARG GLY SER GLY ILE HIS ARG LEU ALA PHE LEU LEU PHE          
SEQRES  22 6  380  LYS GLN ASP GLN PRO ILE ASP PHE SER GLU ASP ALA ARG          
SEQRES  23 6  380  PRO SER PRO CYS TYR GLN LEU ALA GLN ARG THR PHE ARG          
SEQRES  24 6  380  THR PHE ASP PHE TYR LYS LYS HIS GLN GLU THR MET THR          
SEQRES  25 6  380  PRO ALA GLY LEU SER PHE PHE GLN CYS ARG TRP ASP ASP          
SEQRES  26 6  380  SER VAL THR TYR ILE PHE HIS GLN LEU LEU ASP MET ARG          
SEQRES  27 6  380  GLU PRO VAL PHE GLU PHE VAL ARG PRO PRO PRO TYR HIS          
SEQRES  28 6  380  PRO LYS GLN LYS ARG PHE PRO HIS ARG GLN PRO LEU ARG          
SEQRES  29 6  380  TYR LEU ASP ARG TYR ARG ASP SER HIS GLU PRO THR TYR          
SEQRES  30 6  380  GLY ILE TYR                                                  
SEQRES   1 7  338  MET GLU ALA LEU ALA MET GLY SER ARG ALA LEU ARG LEU          
SEQRES   2 7  338  TRP LEU VAL ALA PRO GLY GLY GLY ILE LYS TRP ARG PHE          
SEQRES   3 7  338  ILE ALA THR SER SER ALA SER GLN LEU SER PRO THR GLU          
SEQRES   4 7  338  LEU THR GLU MET ARG ASN ASP LEU PHE ASN LYS GLU LYS          
SEQRES   5 7  338  ALA ARG GLN LEU SER LEU THR PRO ARG THR GLU LYS ILE          
SEQRES   6 7  338  GLU VAL LYS HIS VAL GLY LYS THR ASP PRO GLY THR VAL          
SEQRES   7 7  338  PHE VAL MET ASN LYS ASN ILE SER THR PRO TYR SER CYS          
SEQRES   8 7  338  ALA MET HIS LEU SER GLU TRP TYR CYS ARG LYS SER ILE          
SEQRES   9 7  338  LEU ALA LEU VAL ASP GLY GLN PRO TRP ASP MET TYR LYS          
SEQRES  10 7  338  PRO LEU THR LYS SER CYS GLU ILE LYS PHE LEU THR PHE          
SEQRES  11 7  338  LYS ASP CYS ASP PRO GLY GLU VAL ASN LYS ALA TYR TRP          
SEQRES  12 7  338  ARG SER CYS ALA MET MET MET GLY CYS VAL ILE GLU ARG          
SEQRES  13 7  338  ALA PHE LYS ASP GLU TYR MET VAL ASN LEU VAL ARG ALA          
SEQRES  14 7  338  PRO GLU VAL PRO VAL ILE SER GLY ALA PHE CYS TYR ASP          
SEQRES  15 7  338  VAL VAL LEU ASP SER LYS LEU ASP GLU TRP MET PRO THR          
SEQRES  16 7  338  LYS GLU ASN LEU ARG SER PHE THR LYS ASP ALA HIS ALA          
SEQRES  17 7  338  LEU ILE TYR LYS ASP LEU PRO PHE GLU THR LEU GLU VAL          
SEQRES  18 7  338  GLU ALA LYS VAL ALA LEU GLU ILE PHE GLN HIS SER LYS          
SEQRES  19 7  338  TYR LYS VAL ASP PHE ILE GLU GLU LYS ALA SER GLN ASN          
SEQRES  20 7  338  PRO GLU ARG ILE VAL LYS LEU HIS ARG ILE GLY ASP PHE          
SEQRES  21 7  338  ILE ASP VAL SER GLU GLY PRO LEU ILE PRO ARG THR SER          
SEQRES  22 7  338  ILE CYS PHE GLN TYR GLU VAL SER ALA VAL HIS ASN LEU          
SEQRES  23 7  338  GLN PRO THR GLN PRO SER LEU ILE ARG ARG PHE GLN GLY          
SEQRES  24 7  338  VAL SER LEU PRO VAL HIS LEU ARG ALA HIS PHE THR ILE          
SEQRES  25 7  338  TRP ASP LYS LEU LEU GLU ARG SER ARG LYS MET VAL THR          
SEQRES  26 7  338  GLU ASP GLN SER LYS ALA THR GLU GLU CYS THR SER THR          
SEQRES   1 8  206  MET THR ALA SER VAL LEU ARG SER ILE SER LEU ALA LEU          
SEQRES   2 8  206  ARG PRO THR SER GLY LEU LEU GLY THR TRP GLN THR GLN          
SEQRES   3 8  206  LEU ARG GLU THR HIS GLN ARG ALA SER LEU LEU SER PHE          
SEQRES   4 8  206  TRP GLU LEU ILE PRO MET ARG SER GLU PRO LEU ARG LYS          
SEQRES   5 8  206  LYS LYS LYS VAL ASP PRO LYS LYS ASP GLN GLU ALA LYS          
SEQRES   6 8  206  GLU ARG LEU LYS ARG LYS ILE ARG LYS LEU GLU LYS ALA          
SEQRES   7 8  206  THR GLN GLU LEU ILE PRO ILE GLU ASP PHE ILE THR PRO          
SEQRES   8 8  206  LEU LYS PHE LEU ASP LYS ALA ARG GLU ARG PRO GLN VAL          
SEQRES   9 8  206  GLU LEU THR PHE GLU GLU THR GLU ARG ARG ALA LEU LEU          
SEQRES  10 8  206  LEU LYS LYS TRP SER LEU TYR LYS GLN GLN GLU ARG LYS          
SEQRES  11 8  206  MET GLU ARG ASP THR ILE ARG ALA MET LEU GLU ALA GLN          
SEQRES  12 8  206  GLN GLU ALA LEU GLU GLU LEU GLN LEU GLU SER PRO LYS          
SEQRES  13 8  206  LEU HIS ALA GLU ALA ILE LYS ARG ASP PRO ASN LEU PHE          
SEQRES  14 8  206  PRO PHE GLU LYS GLU GLY PRO HIS TYR THR PRO PRO ILE          
SEQRES  15 8  206  PRO ASN TYR GLN PRO PRO GLU GLY ARG TYR ASN ASP ILE          
SEQRES  16 8  206  THR LYS VAL TYR THR GLN VAL GLU PHE LYS ARG                  
SEQRES   1 9  137  MET GLY VAL LEU ALA ALA ALA ALA ARG CYS LEU VAL ARG          
SEQRES   2 9  137  GLY ALA ASP ARG MET SER LYS TRP THR SER LYS ARG GLY          
SEQRES   3 9  137  PRO ARG SER PHE ARG GLY ARG LYS GLY ARG GLY ALA LYS          
SEQRES   4 9  137  GLY ILE GLY PHE LEU THR SER GLY TRP ARG PHE VAL GLN          
SEQRES   5 9  137  ILE LYS GLU MET VAL PRO GLU PHE VAL VAL PRO ASP LEU          
SEQRES   6 9  137  THR GLY PHE LYS LEU LYS PRO TYR VAL SER TYR LEU ALA          
SEQRES   7 9  137  PRO GLU SER GLU GLU THR PRO LEU THR ALA ALA GLN LEU          
SEQRES   8 9  137  PHE SER GLU ALA VAL ALA PRO ALA ILE GLU LYS ASP PHE          
SEQRES   9 9  137  LYS ASP GLY THR PHE ASP PRO ASP ASN LEU GLU LYS TYR          
SEQRES  10 9  137  GLY PHE GLU PRO THR GLN GLU GLY LYS LEU PHE GLN LEU          
SEQRES  11 9  137  TYR PRO ARG ASN PHE LEU ARG                                  
SEQRES   1 a  142  MET ALA VAL ALA ALA VAL LYS TRP VAL MET SER LYS ARG          
SEQRES   2 a  142  THR ILE LEU LYS HIS LEU PHE PRO VAL GLN ASN GLY ALA          
SEQRES   3 a  142  LEU TYR CYS VAL CYS HIS LYS SER THR TYR SER PRO LEU          
SEQRES   4 a  142  PRO ASP ASP TYR ASN CYS ASN VAL GLU LEU ALA LEU THR          
SEQRES   5 a  142  SER ASP GLY ARG THR ILE VAL CYS TYR HIS PRO SER VAL          
SEQRES   6 a  142  ASP ILE PRO TYR GLU HIS THR LYS PRO ILE PRO ARG PRO          
SEQRES   7 a  142  ASP PRO VAL HIS ASN ASN GLU GLU THR HIS ASP GLN VAL          
SEQRES   8 a  142  LEU LYS THR ARG LEU GLU GLU LYS VAL GLU HIS LEU GLU          
SEQRES   9 a  142  GLU GLY PRO MET ILE GLU GLN LEU SER LYS MET PHE PHE          
SEQRES  10 a  142  THR THR LYS HIS ARG TRP TYR PRO HIS GLY ARG TYR HIS          
SEQRES  11 a  142  ARG CYS ARG LYS ASN LEU ASN PRO PRO LYS ASP ARG              
SEQRES   1 b  155  MET THR ALA ARG GLY THR PRO SER ARG PHE LEU ALA SER          
SEQRES   2 b  155  VAL LEU HIS ASN GLY LEU GLY ARG TYR VAL GLN GLN LEU          
SEQRES   3 b  155  GLN ARG LEU SER PHE SER VAL SER ARG ASP GLY ALA SER          
SEQRES   4 b  155  SER ARG GLY ALA ARG GLU PHE VAL GLU ARG GLU VAL ILE          
SEQRES   5 b  155  ASP PHE ALA ARG ARG ASN PRO GLY VAL VAL ILE TYR VAL          
SEQRES   6 b  155  ASN SER ARG PRO CYS CYS VAL PRO ARG VAL VAL ALA GLU          
SEQRES   7 b  155  TYR LEU ASN GLY ALA VAL ARG GLU GLU SER ILE HIS CYS          
SEQRES   8 b  155  LYS SER VAL GLU GLU ILE SER THR LEU VAL GLN LYS LEU          
SEQRES   9 b  155  ALA ASP GLN SER GLY LEU ASP VAL ILE ARG ILE ARG LYS          
SEQRES  10 b  155  PRO PHE HIS THR ASP ASN PRO SER ILE GLN GLY GLN TRP          
SEQRES  11 b  155  HIS PRO PHE THR ASN LYS PRO THR THR PHE ARG GLY LEU          
SEQRES  12 b  155  ARG PRO ARG GLU VAL GLN ASP PRO ALA PRO ALA GLN              
SEQRES   1 c  332  MET ALA SER GLY LEU VAL ARG LEU LEU GLN GLN GLY HIS          
SEQRES   2 c  332  ARG CYS LEU LEU ALA PRO VAL ALA PRO LYS LEU VAL PRO          
SEQRES   3 c  332  PRO VAL ARG GLY VAL LYS LYS GLY PHE ARG ALA ALA PHE          
SEQRES   4 c  332  ARG PHE GLN LYS GLU LEU GLU ARG GLN ARG LEU LEU ARG          
SEQRES   5 c  332  CYS PRO PRO PRO PRO VAL ARG ARG SER GLU LYS PRO ASN          
SEQRES   6 c  332  TRP ASP TYR HIS ALA GLU ILE GLN ALA PHE GLY HIS ARG          
SEQRES   7 c  332  LEU GLN GLU ASN PHE SER LEU ASP LEU LEU LYS THR ALA          
SEQRES   8 c  332  PHE VAL ASN SER CYS TYR ILE LYS SER GLU GLU ALA LYS          
SEQRES   9 c  332  ARG GLN GLN LEU GLY ILE GLU LYS GLU ALA VAL LEU LEU          
SEQRES  10 c  332  ASN LEU LYS SER ASN GLN GLU LEU SER GLU GLN GLY THR          
SEQRES  11 c  332  SER PHE SER GLN THR CYS LEU THR GLN PHE LEU GLU ASP          
SEQRES  12 c  332  GLU TYR PRO ASP MET PRO THR GLU GLY ILE LYS ASN LEU          
SEQRES  13 c  332  VAL ASP PHE LEU THR GLY GLU GLU VAL VAL CYS HIS VAL          
SEQRES  14 c  332  ALA ARG ASN LEU ALA VAL GLU GLN LEU THR LEU SER GLU          
SEQRES  15 c  332  GLU PHE PRO VAL PRO PRO ALA VAL LEU GLN GLN THR PHE          
SEQRES  16 c  332  PHE ALA VAL ILE GLY ALA LEU LEU GLN SER SER GLY PRO          
SEQRES  17 c  332  GLU ARG THR ALA LEU PHE ILE ARG ASP PHE LEU ILE THR          
SEQRES  18 c  332  GLN MET THR GLY LYS GLU LEU PHE GLU MET TRP LYS ILE          
SEQRES  19 c  332  ILE ASN PRO MET GLY LEU LEU VAL GLU GLU LEU LYS LYS          
SEQRES  20 c  332  ARG ASN VAL SER ALA PRO GLU SER ARG LEU THR ARG GLN          
SEQRES  21 c  332  SER GLY GLY THR THR ALA LEU PRO LEU TYR PHE VAL GLY          
SEQRES  22 c  332  LEU TYR CYS ASP LYS LYS LEU ILE ALA GLU GLY PRO GLY          
SEQRES  23 c  332  GLU THR VAL LEU VAL ALA GLU GLU GLU ALA ALA ARG VAL          
SEQRES  24 c  332  ALA LEU ARG LYS LEU TYR GLY PHE THR GLU ASN ARG ARG          
SEQRES  25 c  332  PRO TRP ASN TYR SER LYS PRO LYS GLU THR LEU ARG ALA          
SEQRES  26 c  332  GLU LYS SER ILE THR ALA SER                                  
SEQRES   1 d  306  MET ALA ALA PRO ILE PRO GLN GLY PHE SER CYS LEU SER          
SEQRES   2 d  306  ARG PHE LEU GLY TRP TRP PHE ARG GLN PRO VAL LEU VAL          
SEQRES   3 d  306  THR GLN SER ALA ALA ILE VAL PRO VAL ARG THR LYS LYS          
SEQRES   4 d  306  ARG PHE THR PRO PRO ILE TYR GLN PRO LYS PHE LYS THR          
SEQRES   5 d  306  GLU LYS GLU PHE MET GLN HIS ALA ARG LYS ALA GLY LEU          
SEQRES   6 d  306  VAL ILE PRO PRO GLU LYS SER ASP ARG SER ILE HIS LEU          
SEQRES   7 d  306  ALA CYS THR ALA GLY ILE PHE ASP ALA TYR VAL PRO PRO          
SEQRES   8 d  306  GLU GLY ASP ALA ARG ILE SER SER LEU SER LYS GLU GLY          
SEQRES   9 d  306  LEU ILE GLU ARG THR GLU ARG MET LYS LYS THR MET ALA          
SEQRES  10 d  306  SER GLN VAL SER ILE ARG ARG ILE LYS ASP TYR ASP ALA          
SEQRES  11 d  306  ASN PHE LYS ILE LYS ASP PHE PRO GLU LYS ALA LYS ASP          
SEQRES  12 d  306  ILE PHE ILE GLU ALA HIS LEU CYS LEU ASN ASN SER ASP          
SEQRES  13 d  306  HIS ASP ARG LEU HIS THR LEU VAL THR GLU HIS CYS PHE          
SEQRES  14 d  306  PRO ASP MET THR TRP ASP ILE LYS TYR LYS THR VAL ARG          
SEQRES  15 d  306  TRP SER PHE VAL GLU SER LEU GLU PRO SER HIS VAL VAL          
SEQRES  16 d  306  GLN VAL ARG CYS SER SER MET MET ASN GLN GLY ASN VAL          
SEQRES  17 d  306  TYR GLY GLN ILE THR VAL ARG MET HIS THR ARG GLN THR          
SEQRES  18 d  306  LEU ALA ILE TYR ASP ARG PHE GLY ARG LEU MET TYR GLY          
SEQRES  19 d  306  GLN GLU ASP VAL PRO LYS ASP VAL LEU GLU TYR VAL VAL          
SEQRES  20 d  306  PHE GLU LYS GLN LEU THR ASN PRO TYR GLY SER TRP ARG          
SEQRES  21 d  306  MET HIS THR LYS ILE VAL PRO PRO TRP ALA PRO PRO LYS          
SEQRES  22 d  306  GLN PRO ILE LEU LYS THR VAL MET ILE PRO GLY PRO GLN          
SEQRES  23 d  306  LEU LYS PRO GLU GLU GLU TYR GLU GLU ALA GLN GLY GLU          
SEQRES  24 d  306  ALA GLN LYS PRO GLN LEU ALA                                  
SEQRES   1 e  279  MET ALA ALA PRO VAL ARG ARG THR LEU LEU GLY VAL ALA          
SEQRES   2 e  279  GLY GLY TRP ARG ARG PHE GLU ARG LEU TRP ALA GLY SER          
SEQRES   3 e  279  LEU SER SER ARG SER LEU ALA LEU ALA ALA ALA PRO SER          
SEQRES   4 e  279  SER ASN GLY SER PRO TRP ARG LEU LEU GLY ALA LEU CYS          
SEQRES   5 e  279  LEU GLN ARG PRO PRO VAL VAL SER LYS PRO LEU THR PRO          
SEQRES   6 e  279  LEU GLN GLU GLU MET ALA SER LEU LEU GLN GLN ILE GLU          
SEQRES   7 e  279  ILE GLU ARG SER LEU TYR SER ASP HIS GLU LEU ARG ALA          
SEQRES   8 e  279  LEU ASP GLU ASN GLN ARG LEU ALA LYS LYS LYS ALA ASP          
SEQRES   9 e  279  LEU HIS ASP GLU GLU ASP GLU GLN ASP ILE LEU LEU ALA          
SEQRES  10 e  279  GLN ASP LEU GLU ASP MET TRP GLU GLN LYS PHE LEU GLN          
SEQRES  11 e  279  PHE LYS LEU GLY ALA ARG ILE THR GLU ALA ASP GLU LYS          
SEQRES  12 e  279  ASN ASP ARG THR SER LEU ASN ARG LYS LEU ASP ARG ASN          
SEQRES  13 e  279  LEU VAL LEU LEU VAL ARG GLU LYS PHE GLY ASP GLN ASP          
SEQRES  14 e  279  VAL TRP ILE LEU PRO GLN ALA GLU TRP GLN PRO GLY GLU          
SEQRES  15 e  279  THR LEU ARG GLY THR ALA GLU ARG THR LEU ALA THR LEU          
SEQRES  16 e  279  SER GLU ASN ASN MET GLU ALA LYS PHE LEU GLY ASN ALA          
SEQRES  17 e  279  PRO CYS GLY HIS TYR THR PHE LYS PHE PRO GLN ALA MET          
SEQRES  18 e  279  ARG THR GLU SER ASN LEU GLY ALA LYS VAL PHE PHE PHE          
SEQRES  19 e  279  LYS ALA LEU LEU LEU THR GLY ASP PHE SER GLN ALA GLY          
SEQRES  20 e  279  ASN LYS GLY HIS HIS VAL TRP VAL THR LYS ASP GLU LEU          
SEQRES  21 e  279  GLY ASP TYR LEU LYS PRO LYS TYR LEU ALA GLN VAL ARG          
SEQRES  22 e  279  ARG PHE VAL SER ASP LEU                                      
SEQRES   1 f  211  MET SER GLY THR LEU GLU LYS VAL LEU CYS LEU ARG ASN          
SEQRES   2 f  211  ASN THR ILE PHE LYS GLN ALA PHE SER LEU LEU ARG PHE          
SEQRES   3 f  211  ARG THR SER GLY GLU LYS PRO ILE TYR SER VAL GLY GLY          
SEQRES   4 f  211  ILE LEU LEU SER ILE SER ARG PRO TYR LYS THR LYS PRO          
SEQRES   5 f  211  THR HIS GLY ILE GLY LYS TYR LYS HIS LEU ILE LYS ALA          
SEQRES   6 f  211  GLU GLU PRO LYS LYS LYS LYS GLY LYS VAL GLU VAL ARG          
SEQRES   7 f  211  ALA ILE ASN LEU GLY THR ASP TYR GLU TYR GLY VAL LEU          
SEQRES   8 f  211  ASN ILE HIS LEU THR ALA TYR ASP MET THR LEU ALA GLU          
SEQRES   9 f  211  SER TYR ALA GLN TYR VAL HIS ASN LEU CYS ASN SER LEU          
SEQRES  10 f  211  SER ILE LYS VAL GLU GLU SER TYR ALA MET PRO THR LYS          
SEQRES  11 f  211  THR ILE GLU VAL LEU GLN LEU GLN ASP GLN GLY SER LYS          
SEQRES  12 f  211  MET LEU LEU ASP SER VAL LEU THR THR HIS GLU ARG VAL          
SEQRES  13 f  211  VAL GLN ILE SER GLY LEU SER ALA THR PHE ALA GLU ILE          
SEQRES  14 f  211  PHE LEU GLU ILE ILE GLN SER SER LEU PRO GLU GLY VAL          
SEQRES  15 f  211  ARG LEU SER VAL LYS GLU HIS THR GLU GLU ASP PHE UNK          
SEQRES  16 f  211  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES  17 f  211  UNK UNK UNK                                                  
SEQRES   1 g  166  MET ALA ALA THR MET PHE ARG ALA THR LEU ARG GLY TRP          
SEQRES   2 g  166  ARG THR GLY VAL GLN ARG GLY CYS GLY LEU ARG LEU LEU          
SEQRES   3 g  166  SER GLN THR GLN GLY PRO PRO ASP TYR PRO ARG PHE VAL          
SEQRES   4 g  166  GLU SER VAL ASP GLU TYR GLN PHE VAL GLU ARG LEU LEU          
SEQRES   5 g  166  PRO ALA THR ARG ILE PRO ASP PRO PRO LYS HIS GLU HIS          
SEQRES   6 g  166  TYR PRO THR PRO SER GLY TRP GLN PRO PRO ARG ASP PRO          
SEQRES   7 g  166  PRO PRO ASN LEU PRO TYR PHE VAL ARG ARG SER ARG MET          
SEQRES   8 g  166  HIS ASN ILE PRO VAL TYR LYS ASP ILE THR HIS GLY ASN          
SEQRES   9 g  166  ARG GLN MET THR VAL ILE ARG LYS VAL GLU GLY ASP ILE          
SEQRES  10 g  166  TRP ALA LEU GLN LYS ASP VAL GLU ASP PHE LEU SER PRO          
SEQRES  11 g  166  LEU LEU GLY LYS THR PRO VAL THR GLN VAL ASN GLU VAL          
SEQRES  12 g  166  THR GLY THR LEU ARG ILE LYS GLY TYR PHE ASP GLN GLU          
SEQRES  13 g  166  LEU LYS ALA TRP LEU LEU GLU LYS GLY PHE                      
SEQRES   1 h  158  MET ALA ALA ARG SER VAL SER GLY ILE THR ARG ARG VAL          
SEQRES   2 h  158  PHE MET TRP THR VAL SER GLY THR PRO CYS ARG GLU PHE          
SEQRES   3 h  158  TRP SER ARG PHE ARG LYS GLU LYS GLU PRO VAL VAL VAL          
SEQRES   4 h  158  GLU THR VAL GLU GLU LYS LYS GLU PRO ILE LEU VAL CYS          
SEQRES   5 h  158  PRO PRO LEU ARG SER ARG ALA TYR THR PRO PRO GLU ASP          
SEQRES   6 h  158  LEU GLN SER ARG LEU GLU SER TYR VAL LYS GLU VAL PHE          
SEQRES   7 h  158  GLY SER SER LEU PRO SER ASN TRP GLN ASP ILE SER LEU          
SEQRES   8 h  158  GLU ASP SER ARG LEU LYS PHE ASN LEU LEU ALA HIS LEU          
SEQRES   9 h  158  ALA ASP ASP LEU GLY HIS VAL VAL PRO ASN SER ARG LEU          
SEQRES  10 h  158  HIS GLN MET CYS ARG VAL ARG ASP VAL LEU ASP PHE TYR          
SEQRES  11 h  158  ASN VAL PRO ILE GLN ASP ARG SER LYS PHE ASP GLU LEU          
SEQRES  12 h  158  SER ALA SER ASN LEU PRO PRO ASN LEU LYS ILE THR TRP          
SEQRES  13 h  158  SER TYR                                                      
SEQRES   1 i  128  MET ALA GLY ASN LEU LEU SER GLY ALA GLY ARG ARG LEU          
SEQRES   2 i  128  TRP ASP TRP VAL PRO LEU ALA CYS ARG SER PHE SER LEU          
SEQRES   3 i  128  GLY VAL PRO ARG LEU ILE GLY ILE ARG LEU THR LEU PRO          
SEQRES   4 i  128  PRO PRO LYS VAL VAL ASP ARG TRP ASN GLU LYS ARG ALA          
SEQRES   5 i  128  MET PHE GLY VAL TYR ASP ASN ILE GLY ILE LEU GLY ASN          
SEQRES   6 i  128  PHE GLU LYS HIS PRO LYS GLU LEU ILE ARG GLY PRO ILE          
SEQRES   7 i  128  TRP LEU ARG GLY TRP LYS GLY ASN GLU LEU GLN ARG CYS          
SEQRES   8 i  128  ILE ARG LYS ARG LYS MET VAL GLY SER ARG MET PHE ALA          
SEQRES   9 i  128  ASP ASP LEU HIS ASN LEU ASN LYS ARG ILE ARG TYR LEU          
SEQRES  10 i  128  TYR LYS HIS PHE ASN ARG HIS GLY LYS PHE ARG                  
SEQRES   1 j  123  MET ALA ALA LEU VAL THR VAL LEU PHE THR GLY VAL ARG          
SEQRES   2 j  123  ARG LEU HIS CYS SER ALA ALA ALA TRP ALA GLY GLY GLN          
SEQRES   3 j  123  TRP ARG LEU GLN GLN GLY LEU ALA ALA ASN PRO SER GLY          
SEQRES   4 j  123  TYR GLY PRO LEU THR GLU LEU PRO ASP TRP SER TYR ALA          
SEQRES   5 j  123  ASP GLY ARG PRO ALA PRO PRO MET LYS GLY GLN LEU ARG          
SEQRES   6 j  123  ARG LYS ALA GLU ARG GLU THR PHE ALA ARG ARG VAL VAL          
SEQRES   7 j  123  LEU LEU SER GLN GLU MET ASP ALA GLY LEU GLN ALA TRP          
SEQRES   8 j  123  GLN LEU ARG GLN GLN LYS LEU GLN GLU GLU GLN ARG LYS          
SEQRES   9 j  123  GLN GLU ASN ALA LEU LYS PRO LYS GLY ALA SER LEU LYS          
SEQRES  10 j  123  SER PRO LEU PRO SER GLN                                      
SEQRES   1 k  112  MET ALA ALA ALA LEU ALA ARG LEU GLY LEU ARG PRO VAL          
SEQRES   2 k  112  LYS GLN VAL ARG VAL GLN PHE CYS PRO PHE GLU LYS ASN          
SEQRES   3 k  112  VAL GLU SER THR ARG THR PHE LEU GLN THR VAL SER SER          
SEQRES   4 k  112  GLU LYS VAL ARG SER THR ASN LEU ASN CYS SER VAL ILE          
SEQRES   5 k  112  ALA ASP VAL ARG HIS ASP GLY SER GLU PRO CYS VAL ASP          
SEQRES   6 k  112  VAL LEU PHE GLY ASP GLY HIS ARG LEU ILE MET ARG GLY          
SEQRES   7 k  112  ALA HIS LEU THR ALA LEU GLU MET LEU THR ALA PHE ALA          
SEQRES   8 k  112  SER HIS ILE ARG ALA ARG ASP ALA ALA GLY SER GLY ASP          
SEQRES   9 k  112  LYS PRO GLY ALA ASP THR GLY ARG                              
SEQRES   1 o  102  MET PHE LEU THR ALA LEU LEU TRP ARG GLY ARG ILE PRO          
SEQRES   2 o  102  GLY ARG GLN TRP ILE GLY LYS HIS ARG ARG PRO ARG PHE          
SEQRES   3 o  102  VAL SER LEU ARG ALA LYS GLN ASN MET ILE ARG ARG LEU          
SEQRES   4 o  102  GLU ILE GLU ALA GLU ASN HIS TYR TRP LEU SER MET PRO          
SEQRES   5 o  102  TYR MET THR ARG GLU GLN GLU ARG GLY HIS ALA ALA VAL          
SEQRES   6 o  102  ARG ARG ARG GLU ALA PHE GLU ALA ILE LYS ALA ALA ALA          
SEQRES   7 o  102  THR SER LYS PHE PRO PRO HIS ARG PHE ILE ALA ASP GLN          
SEQRES   8 o  102  LEU ASP HIS LEU ASN VAL THR LYS LYS TRP SER                  
SEQRES   1 p  206  MET ALA ALA THR ARG CYS LEU ARG TRP GLY LEU SER ARG          
SEQRES   2 p  206  ALA GLY VAL TRP LEU LEU PRO PRO PRO ALA ARG CYS PRO          
SEQRES   3 p  206  ARG ARG ALA LEU HIS LYS GLN LYS ASP GLY THR GLU PHE          
SEQRES   4 p  206  LYS SER ILE TYR SER LEU ASP LYS LEU TYR PRO GLU SER          
SEQRES   5 p  206  GLN GLY SER ASP THR ALA TRP ARG VAL PRO ASN GLY ALA          
SEQRES   6 p  206  LYS GLN ALA ASP SER ASP ILE PRO LEU ASP ARG LEU THR          
SEQRES   7 p  206  ILE SER TYR CYS ARG SER SER GLY PRO GLY GLY GLN ASN          
SEQRES   8 p  206  VAL ASN LYS VAL ASN SER LYS ALA GLU VAL ARG PHE HIS          
SEQRES   9 p  206  LEU ALA THR ALA GLU TRP ILE ALA GLU PRO VAL ARG GLN          
SEQRES  10 p  206  LYS ILE ALA ILE THR HIS LYS ASN LYS ILE ASN ARG LEU          
SEQRES  11 p  206  GLY GLU LEU ILE LEU THR SER GLU SER SER ARG TYR GLN          
SEQRES  12 p  206  PHE ARG ASN LEU ALA ASP CYS LEU GLN LYS ILE ARG ASP          
SEQRES  13 p  206  MET ILE THR GLU ALA SER GLN THR PRO LYS GLU PRO THR          
SEQRES  14 p  206  LYS GLU ASP VAL LYS LEU HIS ARG ILE ARG ILE GLU ASN          
SEQRES  15 p  206  MET ASN ARG GLU ARG LEU ARG GLN LYS ARG ILE HIS SER          
SEQRES  16 p  206  ALA VAL LYS THR SER ARG ARG VAL ASP MET ASP                  
SEQRES   1 q  222  MET ALA ALA SER VAL ARG GLN ALA ARG SER LEU LEU GLY          
SEQRES   2 q  222  VAL ALA ALA THR LEU ALA PRO GLY SER ARG GLY TYR ARG          
SEQRES   3 q  222  ALA ARG PRO PRO PRO ARG ARG ARG PRO GLY PRO ARG TRP          
SEQRES   4 q  222  PRO ASP PRO GLU ASP LEU LEU THR PRO ARG TRP GLN LEU          
SEQRES   5 q  222  GLY PRO ARG TYR ALA ALA LYS GLN PHE ALA ARG TYR GLY          
SEQRES   6 q  222  ALA ALA SER GLY VAL VAL PRO GLY SER LEU TRP PRO SER          
SEQRES   7 q  222  PRO GLU GLN LEU ARG GLU LEU GLU ALA GLU GLU ARG GLU          
SEQRES   8 q  222  TRP TYR PRO SER LEU ALA THR MET GLN GLU SER LEU ARG          
SEQRES   9 q  222  VAL LYS GLN LEU ALA GLU GLU GLN LYS ARG ARG GLU ARG          
SEQRES  10 q  222  GLU GLN HIS ILE ALA GLU CYS MET ALA LYS MET PRO GLN          
SEQRES  11 q  222  MET ILE VAL ASN TRP GLN GLN GLN GLN ARG GLU ASN TRP          
SEQRES  12 q  222  GLU LYS ALA GLN ALA ASP LYS GLU ARG ARG ALA ARG LEU          
SEQRES  13 q  222  GLN ALA GLU ALA GLN GLU LEU LEU GLY TYR GLN VAL ASP          
SEQRES  14 q  222  PRO ARG SER ALA ARG PHE GLN GLU LEU LEU GLN ASP LEU          
SEQRES  15 q  222  GLU LYS LYS GLU ARG LYS ARG LEU LYS GLU GLU LYS GLN          
SEQRES  16 q  222  LYS ARG LYS LYS GLU ALA ARG ALA ALA ALA LEU ALA ALA          
SEQRES  17 q  222  ALA VAL ALA GLN ASP PRO ALA ALA SER GLY ALA PRO SER          
SEQRES  18 q  222  SER                                                          
SEQRES   1 r  196  MET ALA ALA LEU LYS ALA LEU VAL SER GLY CYS GLY ARG          
SEQRES   2 r  196  LEU LEU ARG GLY LEU LEU ALA GLY PRO ALA ALA THR SER          
SEQRES   3 r  196  TRP SER ARG LEU PRO ALA ARG GLY PHE ARG GLU VAL VAL          
SEQRES   4 r  196  GLU THR GLN GLU GLY LYS THR THR ILE ILE GLU GLY ARG          
SEQRES   5 r  196  ILE THR ALA THR PRO LYS GLU SER PRO ASN PRO PRO ASN          
SEQRES   6 r  196  PRO SER GLY GLN CYS PRO ILE CYS ARG TRP ASN LEU LYS          
SEQRES   7 r  196  HIS LYS TYR ASN TYR ASP ASP VAL LEU LEU LEU SER GLN          
SEQRES   8 r  196  PHE ILE ARG PRO HIS GLY GLY MET LEU PRO ARG LYS ILE          
SEQRES   9 r  196  THR GLY LEU CYS GLN GLU GLU HIS ARG LYS ILE GLU GLU          
SEQRES  10 r  196  CYS VAL LYS MET ALA HIS ARG ALA GLY LEU LEU PRO ASN          
SEQRES  11 r  196  HIS ARG PRO ARG LEU PRO GLU GLY VAL VAL PRO LYS SER          
SEQRES  12 r  196  LYS PRO GLN LEU ASN ARG TYR LEU THR ARG TRP ALA PRO          
SEQRES  13 r  196  GLY SER VAL LYS PRO ILE TYR LYS LYS GLY PRO ARG TRP          
SEQRES  14 r  196  ASN ARG VAL ARG MET PRO VAL GLY SER PRO LEU LEU ARG          
SEQRES  15 r  196  ASP ASN VAL CYS TYR SER ARG THR PRO TRP LYS LEU TYR          
SEQRES  16 r  196  HIS                                                          
SEQRES   1 s  439  MET ALA ALA ALA ARG CYS TRP ARG PRO LEU LEU ARG GLY          
SEQRES   2 s  439  PRO ARG LEU SER LEU HIS THR ALA ALA ASN ALA ALA ALA          
SEQRES   3 s  439  THR ALA THR GLU THR THR CYS GLN ASP VAL ALA ALA THR          
SEQRES   4 s  439  PRO VAL ALA ARG TYR PRO PRO ILE VAL ALA SER MET THR          
SEQRES   5 s  439  ALA ASP SER LYS ALA ALA ARG LEU ARG ARG ILE GLU ARG          
SEQRES   6 s  439  TRP GLN ALA THR VAL HIS ALA ALA GLU SER VAL ASP GLU          
SEQRES   7 s  439  LYS LEU ARG ILE LEU THR LYS MET GLN PHE MET LYS TYR          
SEQRES   8 s  439  MET VAL TYR PRO GLN THR PHE ALA LEU ASN ALA ASP ARG          
SEQRES   9 s  439  TRP TYR GLN TYR PHE THR LYS THR VAL PHE LEU SER GLY          
SEQRES  10 s  439  LEU PRO PRO PRO PRO ALA GLU PRO GLU PRO GLU PRO GLU          
SEQRES  11 s  439  PRO GLU PRO GLU PRO ALA LEU ASP LEU ALA ALA LEU ARG          
SEQRES  12 s  439  ALA VAL ALA CYS ASP CYS LEU LEU GLN GLU HIS PHE TYR          
SEQRES  13 s  439  LEU ARG ARG ARG ARG ARG VAL HIS ARG TYR GLU GLU SER          
SEQRES  14 s  439  GLU VAL ILE SER LEU PRO PHE LEU ASP GLN LEU VAL SER          
SEQRES  15 s  439  THR LEU VAL GLY LEU LEU SER PRO HIS ASN PRO ALA LEU          
SEQRES  16 s  439  ALA ALA ALA ALA LEU ASP TYR ARG CYS PRO VAL HIS PHE          
SEQRES  17 s  439  TYR TRP VAL ARG GLY GLU GLU ILE ILE PRO ARG GLY HIS          
SEQRES  18 s  439  ARG ARG GLY ARG ILE ASP ASP LEU ARG TYR GLN ILE ASP          
SEQRES  19 s  439  ASP LYS PRO ASN ASN GLN ILE ARG ILE SER LYS GLN LEU          
SEQRES  20 s  439  ALA GLU PHE VAL PRO LEU ASP TYR SER VAL PRO ILE GLU          
SEQRES  21 s  439  ILE PRO THR ILE LYS CYS LYS PRO ASP LYS LEU PRO LEU          
SEQRES  22 s  439  PHE LYS ARG GLN TYR GLU ASN HIS ILE PHE VAL GLY SER          
SEQRES  23 s  439  LYS THR ALA ASP PRO CYS CYS TYR GLY HIS THR GLN PHE          
SEQRES  24 s  439  HIS LEU LEU PRO ASP LYS LEU ARG ARG GLU ARG LEU LEU          
SEQRES  25 s  439  ARG GLN ASN CYS ALA ASP GLN ILE GLU VAL VAL PHE ARG          
SEQRES  26 s  439  ALA ASN ALA ILE ALA SER LEU PHE ALA TRP THR GLY ALA          
SEQRES  27 s  439  GLN ALA MET TYR GLN GLY PHE TRP SER GLU ALA ASP VAL          
SEQRES  28 s  439  THR ARG PRO PHE VAL SER GLN ALA VAL ILE THR ASP GLY          
SEQRES  29 s  439  LYS TYR PHE SER PHE PHE CYS TYR GLN LEU ASN THR LEU          
SEQRES  30 s  439  ALA LEU THR THR GLN ALA ASP GLN ASN ASN PRO ARG LYS          
SEQRES  31 s  439  ASN ILE CYS TRP GLY THR GLN SER LYS PRO LEU TYR GLU          
SEQRES  32 s  439  THR ILE GLU ASP ASN ASP VAL LYS GLY PHE ASN ASP ASP          
SEQRES  33 s  439  VAL LEU LEU GLN ILE VAL HIS PHE LEU LEU ASN ARG PRO          
SEQRES  34 s  439  LYS GLU GLU LYS SER GLN LEU LEU GLU ASN                      
SEQRES   1 t  127  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   2 t  127  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   3 t  127  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   4 t  127  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   5 t  127  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   6 t  127  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   7 t  127  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   8 t  127  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   9 t  127  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES  10 t  127  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK                      
HET      A  A3301      22                                                       
HET     MG  A3302       1                                                       
HET     MG  A3303       1                                                       
HET     MG  A3304       1                                                       
HET     MG  A3305       1                                                       
HET     MG  A3306       1                                                       
HET     MG  A3307       1                                                       
HET     MG  A3308       1                                                       
HET     MG  A3309       1                                                       
HET     MG  A3310       1                                                       
HET     MG  A3311       1                                                       
HET     MG  A3312       1                                                       
HET     MG  A3313       1                                                       
HET     MG  A3314       1                                                       
HET     MG  A3315       1                                                       
HET     MG  A3316       1                                                       
HET     MG  A3317       1                                                       
HET     MG  A3318       1                                                       
HET     MG  A3319       1                                                       
HET     MG  A3320       1                                                       
HET     MG  A3321       1                                                       
HET     MG  A3322       1                                                       
HET     MG  A3323       1                                                       
HET     MG  A3324       1                                                       
HET     MG  A3325       1                                                       
HET     MG  A3326       1                                                       
HET     MG  A3327       1                                                       
HET     MG  A3328       1                                                       
HET     MG  A3329       1                                                       
HET     MG  A3330       1                                                       
HET     MG  A3331       1                                                       
HET     MG  A3332       1                                                       
HET     MG  A3333       1                                                       
HET     MG  A3334       1                                                       
HET     MG  A3335       1                                                       
HET     MG  A3336       1                                                       
HET     MG  A3337       1                                                       
HET     MG  A3338       1                                                       
HET     MG  A3339       1                                                       
HET     MG  A3340       1                                                       
HET     MG  A3341       1                                                       
HET     MG  A3342       1                                                       
HET     MG  A3343       1                                                       
HET     MG  A3344       1                                                       
HET     MG  A3345       1                                                       
HET     MG  A3346       1                                                       
HET     MG  A3347       1                                                       
HET     MG  A3348       1                                                       
HET     MG  A3349       1                                                       
HET     MG  A3350       1                                                       
HET     MG  A3351       1                                                       
HET     MG  A3352       1                                                       
HET     MG  A3353       1                                                       
HET     MG  A3354       1                                                       
HET     MG  A3355       1                                                       
HET     MG  A3356       1                                                       
HET     MG  A3357       1                                                       
HET     MG  A3358       1                                                       
HET     MG  A3359       1                                                       
HET     MG  A3360       1                                                       
HET     MG  A3361       1                                                       
HET     MG  A3362       1                                                       
HET     MG  A3363       1                                                       
HET     MG  A3364       1                                                       
HET     MG  A3365       1                                                       
HET     MG  A3366       1                                                       
HET     MG  E 401       1                                                       
HET     ZN  0 200       1                                                       
HET     ZN  4 200       1                                                       
HET     ZN  r 200       1                                                       
HETNAM       A ADENOSINE-5'-MONOPHOSPHATE                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      ZN ZINC ION                                                         
FORMUL  52    A    C10 H14 N5 O7 P                                              
FORMUL  53   MG    66(MG 2+)                                                    
FORMUL  19   ZN    3(ZN 2+)                                                     
HELIX    1   1 GLY D  185  LEU D  187  5                                   3    
HELIX    2   2 ASP D  251  ARG D  255  5                                   5    
HELIX    3   3 LYS D  259  LEU D  266  1                                   8    
HELIX    4   4 GLU E   56  LYS E   76  1                                  21    
HELIX    5   5 CYS E   78  GLU E   83  1                                   6    
HELIX    6   6 SER E  153  LYS E  157  5                                   5    
HELIX    7   7 ALA E  158  LEU E  168  1                                  11    
HELIX    8   8 TYR E  194  PHE E  198  5                                   5    
HELIX    9   9 GLY E  217  TRP E  222  1                                   6    
HELIX   10  10 LEU E  304  LYS E  308  5                                   5    
HELIX   11  11 HIS F   83  THR F   89  1                                   7    
HELIX   12  12 ARG F   92  LYS F  107  1                                  16    
HELIX   13  13 PRO F  166  GLN F  184  1                                  19    
HELIX   14  14 ASP F  199  ARG F  211  1                                  13    
HELIX   15  15 PRO F  227  LEU F  237  1                                  11    
HELIX   16  16 PRO F  244  LEU F  248  5                                   5    
HELIX   17  17 ASN F  249  HIS F  256  1                                   8    
HELIX   18  18 LEU F  263  TRP F  275  1                                  13    
HELIX   19  19 LYS H  116  ARG H  122  1                                   7    
HELIX   20  20 LEU H  123  GLY H  127  5                                   5    
HELIX   21  21 SER H  133  ARG H  147  1                                  15    
HELIX   22  22 HIS I   41  THR I   51  1                                  11    
HELIX   23  23 LEU I   78  ASN I   93  1                                  16    
HELIX   24  24 SER I  105  HIS I  119  1                                  15    
HELIX   25  25 PRO I  127  LYS I  139  1                                  13    
HELIX   26  26 LYS I  160  VAL I  171  1                                  12    
HELIX   27  27 SER I  187  LEU I  197  1                                  11    
HELIX   28  28 LEU J   35  GLY J   40  1                                   6    
HELIX   29  29 ILE J   46  ILE J   60  1                                  15    
HELIX   30  30 THR J   86  ALA J   95  1                                  10    
HELIX   31  31 THR J  113  GLN J  126  1                                  14    
HELIX   32  32 PRO J  136  LEU J  151  1                                  16    
HELIX   33  33 SER K    5  PHE K   14  1                                  10    
HELIX   34  34 GLY K   29  GLY K   41  1                                  13    
HELIX   35  35 ASN K   61  HIS K   64  5                                   4    
HELIX   36  36 ASN K   70  LYS K   75  1                                   6    
HELIX   37  37 ALA K   92  ASP K   99  1                                   8    
HELIX   38  38 VAL K  101  LEU K  112  1                                  12    
HELIX   39  39 LEU K  116  ARG K  124  1                                   9    
HELIX   40  40 PRO K  134  LEU K  141  1                                   8    
HELIX   41  41 THR K  159  PHE K  166  1                                   8    
HELIX   42  42 SER L   44  SER L   49  1                                   6    
HELIX   43  43 PRO L  124  ARG L  130  5                                   7    
HELIX   44  44 TYR L  134  ILE L  140  1                                   7    
HELIX   45  45 ARG M   11  LEU M   16  1                                   6    
HELIX   46  46 PRO M   73  ILE M   78  1                                   6    
HELIX   47  47 GLY M   86  ARG M   90  5                                   5    
HELIX   48  48 LEU M   98  GLY M  108  1                                  11    
HELIX   49  49 ASP M  117  ARG M  125  1                                   9    
HELIX   50  50 SER M  160  ASN M  170  1                                  11    
HELIX   51  51 ASP M  180  LYS M  189  1                                  10    
HELIX   52  52 LYS M  189  GLY M  197  1                                   9    
HELIX   53  53 LEU M  210  THR M  215  1                                   6    
HELIX   54  54 ASP M  216  ARG M  220  5                                   5    
HELIX   55  55 LYS M  228  GLY M  241  1                                  14    
HELIX   56  56 LEU M  252  CYS M  257  1                                   6    
HELIX   57  57 ASP M  287  SER M  296  1                                  10    
HELIX   58  58 ASN N   68  ILE N   72  5                                   5    
HELIX   59  59 HIS N   98  SER N  112  1                                  15    
HELIX   60  60 GLU N  168  LEU N  183  1                                  16    
HELIX   61  61 ARG N  192  ASN N  209  1                                  18    
HELIX   62  62 THR N  214  ALA N  221  1                                   8    
HELIX   63  63 GLY N  225  VAL N  229  5                                   5    
HELIX   64  64 GLY O   21  GLU O   40  1                                  20    
HELIX   65  65 TRP O   46  LEU O   65  1                                  20    
HELIX   66  66 ASN O   69  LEU O   80  1                                  12    
HELIX   67  67 ASP O   84  VAL O   92  1                                   9    
HELIX   68  68 VAL O   92  TYR O   97  1                                   6    
HELIX   69  69 THR O  143  GLN O  160  1                                  18    
HELIX   70  70 ARG P   53  LEU P   58  1                                   6    
HELIX   71  71 SER P  105  TRP P  109  5                                   5    
HELIX   72  72 VAL P  121  GLY P  139  1                                  19    
HELIX   73  73 THR P  148  SER P  154  1                                   7    
HELIX   74  74 SER P  154  GLY P  168  1                                  15    
HELIX   75  75 ASP Q   88  LEU Q  106  1                                  19    
HELIX   76  76 ARG Q  143  GLY Q  146  5                                   4    
HELIX   77  77 LEU Q  187  ALA Q  193  5                                   7    
HELIX   78  78 ARG Q  244  LEU Q  249  1                                   6    
HELIX   79  79 THR Q  250  LYS Q  259  1                                  10    
HELIX   80  80 THR Q  275  SER Q  292  1                                  18    
HELIX   81  81 ASP R   16  ARG R   29  1                                  14    
HELIX   82  82 ARG R   32  ARG R   37  5                                   6    
HELIX   83  83 CYS R   38  GLU R   78  1                                  41    
HELIX   84  84 LYS R   82  GLN R   94  1                                  13    
HELIX   85  85 ASN R   98  GLU R  109  1                                  12    
HELIX   86  86 GLU R  109  GLY R  133  1                                  25    
HELIX   87  87 ASP S   68  GLY S   90  1                                  23    
HELIX   88  88 ARG T   49  ASN T   55  1                                   7    
HELIX   89  89 SER T   83  ARG T   95  1                                  13    
HELIX   90  90 SER T   98  ASN T  109  1                                  12    
HELIX   91  91 LYS T  111  ASP T  131  1                                  21    
HELIX   92  92 PHE T  136  SER T  138  5                                   3    
HELIX   93  93 THR T  191  ARG T  206  1                                  16    
HELIX   94  94 THR U   49  TYR U   61  1                                  13    
HELIX   95  95 SER V   28  ASN V   35  1                                   8    
HELIX   96  96 SER V  178  LEU V  183  1                                   6    
HELIX   97  97 LYS V  192  GLY V  203  1                                  12    
HELIX   98  98 ASN W  110  LEU W  120  1                                  11    
HELIX   99  99 PRO X    7  TRP X    9  5                                   3    
HELIX  100 100 LEU X   10  GLY X   19  1                                  10    
HELIX  101 101 GLY X   19  LEU X   24  1                                   6    
HELIX  102 102 PRO X   25  GLU X   35  1                                  11    
HELIX  103 103 THR X  128  ALA X  138  1                                  11    
HELIX  104 104 GLY X  140  ALA X  148  1                                   9    
HELIX  105 105 SER X  149  CYS X  154  1                                   6    
HELIX  106 106 SER X  155  GLN X  172  1                                  18    
HELIX  107 107 ASP X  180  TYR X  191  1                                  12    
HELIX  108 108 PRO X  197  VAL X  204  1                                   8    
HELIX  109 109 THR X  207  GLU X  219  1                                  13    
HELIX  110 110 PRO X  225  SER X  244  1                                  20    
HELIX  111 111 GLY Y   63  PHE Y   68  5                                   6    
HELIX  112 112 ASP Y   70  TRP Y   74  5                                   5    
HELIX  113 113 THR Y   86  LYS Y   93  1                                   8    
HELIX  114 114 SER Y   94  ARG Y  123  1                                  30    
HELIX  115 115 PRO Y  129  THR Y  158  1                                  30    
HELIX  116 116 PRO Y  187  LEU Y  190  5                                   4    
HELIX  117 117 ASN Y  191  ARG Y  196  1                                   6    
HELIX  118 118 PRO Y  203  PHE Y  238  1                                  36    
HELIX  119 119 SER Z   49  TYR Z   56  1                                   8    
HELIX  120 120 PRO Z   79  GLY Z   90  1                                  12    
HELIX  121 121 ILE Z  103  VAL Z  113  1                                  11    
HELIX  122 122 ALA Z  130  MET Z  134  5                                   5    
HELIX  123 123 THR 0   86  ARG 0   95  1                                  10    
HELIX  124 124 CYS 0  123  GLU 0  145  1                                  23    
HELIX  125 125 SER 2   56  GLY 2   65  1                                  10    
HELIX  126 126 GLY 2   65  THR 2   72  1                                   8    
HELIX  127 127 THR 2   72  GLY 2   86  1                                  15    
HELIX  128 128 VAL 3  107  ARG 3  113  1                                   7    
HELIX  129 129 THR 3  137  ARG 3  145  1                                   9    
HELIX  130 130 ASN 3  151  THR 3  162  1                                  12    
HELIX  131 131 THR 3  163  ARG 3  168  5                                   6    
HELIX  132 132 TYR 3  177  HIS 3  181  5                                   5    
HELIX  133 133 HIS 4   95  LYS 4   99  5                                   5    
HELIX  134 134 ASP 5   47  ILE 5   52  5                                   6    
HELIX  135 135 ASP 5   84  TYR 5   88  5                                   5    
HELIX  136 136 GLY 5  116  LYS 5  125  1                                  10    
HELIX  137 137 PRO 5  133  LEU 5  139  1                                   7    
HELIX  138 138 ASP 5  151  LEU 5  163  1                                  13    
HELIX  139 139 LYS 5  172  SER 5  190  1                                  19    
HELIX  140 140 GLN 5  191  LEU 5  193  5                                   3    
HELIX  141 141 HIS 5  195  ALA 5  199  5                                   5    
HELIX  142 142 SER 5  241  LYS 5  249  1                                   9    
HELIX  143 143 GLN 5  305  TYR 5  329  1                                  25    
HELIX  144 144 LYS 5  407  HIS 5  420  1                                  14    
HELIX  145 145 PHE 6   54  ALA 6   67  1                                  14    
HELIX  146 146 THR 6   73  PHE 6   78  1                                   6    
HELIX  147 147 THR 6  100  GLU 6  118  1                                  19    
HELIX  148 148 PRO 6  131  THR 6  142  1                                  12    
HELIX  149 149 CYS 6  143  GLY 6  156  1                                  14    
HELIX  150 150 GLY 6  156  LEU 6  161  1                                   6    
HELIX  151 151 GLN 6  292  THR 6  297  1                                   6    
HELIX  152 152 ARG 6  299  LYS 6  306  1                                   8    
HELIX  153 153 ASP 6  324  LEU 6  334  1                                  11    
HELIX  154 154 PRO 6  362  TYR 6  369  5                                   8    
HELIX  155 155 PRO 7   37  LEU 7   58  1                                  22    
HELIX  156 156 THR 7   87  SER 7   96  1                                  10    
HELIX  157 157 GLU 7   97  SER 7  103  1                                   7    
HELIX  158 158 PRO 7  135  PHE 7  158  1                                  24    
HELIX  159 159 THR 7  195  ASP 7  213  1                                  19    
HELIX  160 160 GLU 7  222  GLN 7  231  1                                  10    
HELIX  161 161 SER 7  233  ASN 7  247  1                                  15    
HELIX  162 162 ARG 7  271  SER 7  273  5                                   3    
HELIX  163 163 HIS 7  309  LYS 7  322  1                                  14    
HELIX  164 164 PHE 8   64  SER 8  110  1                                  47    
HELIX  165 165 SER 8  110  LYS 8  119  1                                  10    
HELIX  166 166 PRO 9   27  LYS 9   34  1                                   8    
HELIX  167 167 THR 9   87  GLU 9   94  1                                   8    
HELIX  168 168 VAL 9   96  ASP 9  103  1                                   8    
HELIX  169 169 GLU a  105  PHE a  117  1                                  13    
HELIX  170 170 THR a  119  TRP a  123  5                                   5    
HELIX  171 171 GLY a  127  LYS a  134  1                                   8    
HELIX  172 172 GLY b   37  SER b   40  5                                   4    
HELIX  173 173 ARG b   41  ASN b   58  1                                  18    
HELIX  174 174 SER b   93  GLN b  107  1                                  15    
HELIX  175 175 THR b  139  LEU b  143  5                                   5    
HELIX  176 176 PHE c   35  CYS c   53  1                                  19    
HELIX  177 177 ASP c   67  LEU c   79  1                                  13    
HELIX  178 178 SER c   84  VAL c   93  1                                  10    
HELIX  179 179 ASN c   94  GLN c  107  1                                  14    
HELIX  180 180 ASN c  122  TYR c  145  1                                  24    
HELIX  181 181 PRO c  149  GLY c  162  1                                  14    
HELIX  182 182 GLU c  164  ALA c  174  1                                  11    
HELIX  183 183 ALA c  174  THR c  179  1                                   6    
HELIX  184 184 PRO c  187  SER c  206  1                                  20    
HELIX  185 185 GLY c  207  LEU c  219  1                                  13    
HELIX  186 186 ILE c  220  MET c  223  5                                   4    
HELIX  187 187 ASN c  236  ASN c  249  1                                  14    
HELIX  188 188 THR c  288  TYR c  305  1                                  18    
HELIX  189 189 SER d  118  ALA d  130  1                                  13    
HELIX  190 190 ASP d  136  SER d  155  1                                  20    
HELIX  191 191 ASP d  156  HIS d  161  1                                   6    
HELIX  192 192 HIS d  167  TRP d  174  1                                   8    
HELIX  193 193 THR e  139  GLU e  153  1                                  15    
HELIX  194 194 LEU e  225  ASP e  234  1                                  10    
HELIX  195 195 MET f  100  SER f  118  1                                  19    
HELIX  196 196 SER f  163  SER f  176  1                                  14    
HELIX  197 197 GLU g   44  LEU g   52  1                                   9    
HELIX  198 198 ASP g  116  GLY g  133  1                                  18    
HELIX  199 199 PHE g  153  GLY g  165  1                                  13    
HELIX  200 200 LEU h   66  PHE h   78  1                                  13    
HELIX  201 201 ASP h   93  GLY h  109  1                                  17    
HELIX  202 202 ARG h  122  VAL h  132  1                                  11    
HELIX  203 203 SER h  138  SER h  146  1                                   9    
HELIX  204 204 ASN i   48  MET i   53  1                                   6    
HELIX  205 205 HIS i   69  LEU i   73  5                                   5    
HELIX  206 206 PRO i   77  ARG i   81  5                                   5    
HELIX  207 207 ASN i   86  VAL i   98  1                                  13    
HELIX  208 208 GLY i   99  MET i  102  5                                   4    
HELIX  209 209 PHE i  103  ARG i  123  1                                  21    
HELIX  210 210 GLN j   26  GLN j   31  1                                   6    
HELIX  211 211 MET j   60  ASN j  107  1                                  48    
HELIX  212 212 VAL k   27  THR k   36  1                                  10    
HELIX  213 213 LYS k   41  ASN k   46  1                                   6    
HELIX  214 214 THR k   82  ALA k   96  1                                  15    
HELIX  215 215 SER o   28  SER o   50  1                                  23    
HELIX  216 216 ARG o   56  ARG o   60  5                                   5    
HELIX  217 217 ALA o   63  SER o   80  1                                  18    
HELIX  218 218 PHE o   87  LEU o   95  1                                   9    
HELIX  219 219 ASN o   96  LYS o   99  5                                   4    
HELIX  220 220 ALA p  112  HIS p  123  1                                  12    
HELIX  221 221 TYR p  142  GLN p  163  1                                  22    
HELIX  222 222 PRO q   48  GLY q   53  1                                   6    
HELIX  223 223 GLY q   53  TYR q   64  1                                  12    
HELIX  224 224 VAL q   71  LEU q   75  5                                   5    
HELIX  225 225 SER q   78  TYR q   93  1                                  16    
HELIX  226 226 SER q   95  ARG q  152  1                                  58    
HELIX  227 227 CYS r   70  ASN r   76  1                                   7    
HELIX  228 228 ASP r   85  SER r   90  1                                   6    
HELIX  229 229 GLN r   91  ILE r   93  5                                   3    
HELIX  230 230 PRO r  101  GLY r  106  1                                   6    
HELIX  231 231 CYS r  108  GLY r  126  1                                  19    
HELIX  232 232 PRO r  167  ARG r  171  5                                   5    
HELIX  233 233 SER s   55  ALA s   73  1                                  19    
HELIX  234 234 SER s   75  LYS s   85  1                                  11    
HELIX  235 235 ASN s  101  LYS s  111  1                                  11    
HELIX  236 236 ALA s  141  PHE s  155  1                                  15    
HELIX  237 237 GLU s  167  ILE s  172  1                                   6    
HELIX  238 238 ILE s  172  SER s  189  1                                  18    
HELIX  239 239 PRO s  193  ALA s  198  1                                   6    
HELIX  240 240 LYS s  267  LEU s  271  5                                   5    
HELIX  241 241 ARG s  307  GLN s  314  1                                   8    
HELIX  242 242 ASP s  318  GLN s  343  1                                  26    
HELIX  243 243 THR s  380  GLN s  385  1                                   6    
HELIX  244 244 ASN s  414  ASN s  427  1                                  14    
HELIX  245 245 UNK t  101  UNK t  127  1                                  27    
HELIX  246 246 UNK t  201  UNK t  217  1                                  17    
HELIX  247 247 UNK t  306  UNK t  311  1                                   6    
HELIX  248 248 UNK t  401  UNK t  414  1                                  14    
SHEET    1   A 2 VAL D  77  LYS D  78  0                                        
SHEET    2   A 2 ARG D 103  TYR D 104 -1  O  TYR D 104   N  VAL D  77           
SHEET    1   B 4 ARG D 147  ILE D 152  0                                        
SHEET    2   B 4 ILE D 139  GLY D 144 -1  N  ALA D 140   O  ILE D 151           
SHEET    3   B 4 PHE D 122  ARG D 130 -1  N  ILE D 127   O  LEU D 141           
SHEET    4   B 4 THR D 162  ASN D 165 -1  O  ILE D 163   N  GLU D 124           
SHEET    1   C 7 ALA D 181  PRO D 183  0                                        
SHEET    2   C 7 VAL D 241  VAL D 244 -1  O  ALA D 242   N  HIS D 182           
SHEET    3   C 7 LEU D 192  ASN D 194 -1  N  ASN D 194   O  THR D 243           
SHEET    4   C 7 GLY D 214  VAL D 220 -1  O  GLY D 214   N  ILE D 193           
SHEET    5   C 7 THR D 223  GLN D 227 -1  O  ILE D 225   N  ARG D 218           
SHEET    6   C 7 GLN D 233  LEU D 237 -1  O  VAL D 236   N  ALA D 224           
SHEET    7   C 7 LYS D 293  SER D 294  1  O  LYS D 293   N  GLN D 235           
SHEET    1   D 2 VAL D 196  GLU D 197  0                                        
SHEET    2   D 2 ALA D 204  TYR D 206 -1  O  TYR D 206   N  VAL D 196           
SHEET    1   E 8 LEU E 332  TYR E 333  0                                        
SHEET    2   E 8 TYR E 265  ASN E 277 -1  N  ILE E 276   O  LEU E 332           
SHEET    3   E 8 ILE E 282  ASN E 286 -1  O  TYR E 284   N  ARG E 275           
SHEET    4   E 8 LYS E 116  GLN E 123 -1  N  THR E 120   O  VAL E 285           
SHEET    5   E 8 LEU E  99  TRP E 110 -1  N  LEU E 104   O  LEU E 121           
SHEET    6   E 8 LEU E 296  ASP E 301 -1  O  VAL E 297   N  ALA E 101           
SHEET    7   E 8 TYR E 203  LYS E 209 -1  N  ASP E 205   O  LYS E 300           
SHEET    8   E 8 TYR E 265  ASN E 277 -1  O  GLU E 268   N  VAL E 206           
SHEET    1   F 3 VAL E 129  THR E 133  0                                        
SHEET    2   F 3 ALA E 143  VAL E 147 -1  O  THR E 144   N  THR E 133           
SHEET    3   F 3 LYS E 177  ILE E 181 -1  O  ILE E 181   N  ALA E 143           
SHEET    1   G 2 PHE E 215  GLN E 216  0                                        
SHEET    2   G 2 GLY E 259  LYS E 260 -1  O  GLY E 259   N  GLN E 216           
SHEET    1   H 7 LEU F  48  ARG F  49  0                                        
SHEET    2   H 7 LEU F  79  ASP F  81  1  O  ASP F  81   N  ARG F  49           
SHEET    3   H 7 GLN F  63  GLU F  67 -1  N  ALA F  64   O  ALA F  80           
SHEET    4   H 7 LEU F 187  MET F 190  1  O  ILE F 189   N  GLU F  67           
SHEET    5   H 7 THR F 258  THR F 262  1  O  LEU F 261   N  MET F 190           
SHEET    6   H 7 VAL F 216  VAL F 219  1  N  VAL F 219   O  VAL F 260           
SHEET    7   H 7 ASN F 241  ILE F 243  1  O  ASN F 241   N  LEU F 218           
SHEET    1   I 2 ILE F 109  SER F 110  0                                        
SHEET    2   I 2 THR F 159  SER F 160 -1  O  THR F 159   N  SER F 110           
SHEET    1   J 2 VAL H  54  ARG H  58  0                                        
SHEET    2   J 2 TYR H  80  ASP H  85 -1  O  LYS H  81   N  GLU H  57           
SHEET    1   K 3 LEU H 111  LYS H 115  0                                        
SHEET    2   K 3 ASN H  93  LEU H  98 -1  N  LEU H  94   O  VAL H 114           
SHEET    3   K 3 ALA H 129  TYR H 131 -1  O  VAL H 130   N  ILE H  97           
SHEET    1   L 4 ILE I 121  LYS I 124  0                                        
SHEET    2   L 4 MET I 152  SER I 156 -1  O  LEU I 153   N  LYS I 124           
SHEET    3   L 4 MET I  95  CYS I  99 -1  N  ALA I  97   O  LEU I 154           
SHEET    4   L 4 CYS I 180  ILE I 181 -1  O  CYS I 180   N  ILE I  96           
SHEET    1   M 2 LEU J  71  VAL J  72  0                                        
SHEET    2   M 2 PHE J  78  GLU J  79 -1  O  GLU J  79   N  LEU J  71           
SHEET    1   N 3 TRP K  18  ASP K  22  0                                        
SHEET    2   N 3 HIS K  56  MET K  60  1  O  VAL K  58   N  TYR K  19           
SHEET    3   N 3 LEU K 125  LEU K 127  1  O  HIS K 126   N  ILE K  59           
SHEET    1   O 2 ALA K  66  SER K  68  0                                        
SHEET    2   O 2 ASN r 148  TYR r 150  1  O  ASN r 148   N  PHE K  67           
SHEET    1   P 2 VAL K  76  HIS K  80  0                                        
SHEET    2   P 2 PHE K  87  THR K  91 -1  O  VAL K  90   N  TYR K  77           
SHEET    1   Q 5 ARG L  39  VAL L  40  0                                        
SHEET    2   Q 5 ASN L 104  ILE L 108  1  O  VAL L 105   N  ARG L  39           
SHEET    3   Q 5 GLN L  80  ILE L  86 -1  N  LEU L  85   O  VAL L 106           
SHEET    4   Q 5 GLN L  72  ILE L  77 -1  N  ILE L  77   O  GLN L  80           
SHEET    5   Q 5 ARG L  56  VAL L  60 -1  N  ARG L  56   O  ALA L  76           
SHEET    1   R 6 PRO L  98  PHE L 100  0                                        
SHEET    2   R 6 GLN Q 158  GLU Q 165 -1  O  GLU Q 161   N  ARG L  99           
SHEET    3   R 6 THR Q 148  ILE Q 155 -1  N  ILE Q 155   O  GLN Q 158           
SHEET    4   R 6 ILE Q 130  SER Q 141 -1  N  ILE Q 136   O  ARG Q 152           
SHEET    5   R 6 ILE Q 116  ALA Q 122 -1  N  THR Q 121   O  SER Q 131           
SHEET    6   R 6 GLU Q 173  LYS Q 178 -1  O  GLN Q 175   N  ARG Q 118           
SHEET    1   S 2 ILE L 119  ILE L 123  0                                        
SHEET    2   S 2 ALA L 141  PHE L 144  1  O  GLN L 142   N  ILE L 119           
SHEET    1   T 3 GLN M  92  SER M  97  0                                        
SHEET    2   T 3 ASP M 135  VAL M 141  1  O  GLN M 139   N  LEU M  96           
SHEET    3   T 3 LEU M 158  ALA M 159  1  O  LEU M 158   N  LEU M 140           
SHEET    1   U 2 ASN M 153  VAL M 156  0                                        
SHEET    2   U 2 VAL M 173  THR M 176  1  O  THR M 175   N  ILE M 154           
SHEET    1   V 3 VAL M 274  ASN M 276  0                                        
SHEET    2   V 3 LYS M 281  LEU M 283 -1  O  LEU M 283   N  VAL M 274           
SHEET    3   V 3 SER g  41  VAL g  42 -1  O  VAL g  42   N  ILE M 282           
SHEET    1   W 4 MET N 118  TRP N 122  0                                        
SHEET    2   W 4 LEU N 159  GLY N 165 -1  O  GLU N 162   N  ILE N 121           
SHEET    3   W 4 PHE N  87  ALA N  91 -1  N  PHE N  87   O  MET N 163           
SHEET    4   W 4 ALA N 187  SER N 191 -1  O  LYS N 188   N  LEU N  90           
SHEET    1   X 3 GLY N  95  LEU N  97  0                                        
SHEET    2   X 3 ALA N 146  VAL N 154 -1  O  THR N 152   N  LEU N  97           
SHEET    3   X 3 LYS N 129  ARG N 133 -1  N  ILE N 131   O  HIS N 149           
SHEET    1   Y 3 GLU O  43  PRO O  45  0                                        
SHEET    2   Y 3 MET O 120  GLU O 124 -1  O  ALA O 121   N  ALA O  44           
SHEET    3   Y 3 ARG O 106  ILE O 110 -1  N  LEU O 108   O  VAL O 122           
SHEET    1   Z 3 VAL P  82  ARG P  84  0                                        
SHEET    2   Z 3 VAL P  89  GLU P  94 -1  O  GLU P  90   N  ILE P  83           
SHEET    3   Z 3 VAL P 100  ALA P 104 -1  O  VAL P 101   N  VAL P  93           
SHEET    1  AA 6 ARG S 104  THR S 109  0                                        
SHEET    2  AA 6 PHE S  96  PHE S 101 -1  N  ALA S  97   O  VAL S 108           
SHEET    3  AA 6 VAL S 133  GLY S 137 -1  O  GLY S 137   N  PHE S  96           
SHEET    4  AA 6 ASN S 140  LEU S 144 -1  O  LEU S 143   N  VAL S 136           
SHEET    5  AA 6 UNK t  24  UNK t  30 -1  O  UNK t  28   N  ASN S 140           
SHEET    6  AA 6 UNK t  11  UNK t  16 -1  N  UNK t  16   O  UNK t  25           
SHEET    1  AB 6 PHE b 119  HIS b 120  0                                        
SHEET    2  AB 6 LEU S 113  ILE S 116 -1  N  LEU S 113   O  HIS b 120           
SHEET    3  AB 6 PRO S 189  ILE S 200 -1  O  LEU S 193   N  ILE S 114           
SHEET    4  AB 6 VAL S 154  GLU S 165 -1  N  THR S 159   O  ARG S 194           
SHEET    5  AB 6 ARG S 127  LEU S 130 -1  N  LEU S 130   O  VAL S 156           
SHEET    6  AB 6 TRP j  49  TYR j  51 -1  O  SER j  50   N  ARG S 129           
SHEET    1  AC 2 ARG S 169  ARG S 175  0                                        
SHEET    2  AC 2 PHE S 180  VAL S 186 -1  O  ARG S 184   N  ILE S 171           
SHEET    1  AD 3 GLU T  72  ILE T  80  0                                        
SHEET    2  AD 3 CYS T 172  GLU T 180 -1  O  LEU T 178   N  ILE T  73           
SHEET    3  AD 3 LEU T 140  ARG T 149 -1  N  THR T 146   O  PHE T 175           
SHEET    1  AE 2 LEU T 153  ILE T 156  0                                        
SHEET    2  AE 2 ILE T 166  LYS T 169 -1  O  LYS T 169   N  LEU T 153           
SHEET    1  AF 2 ARG U  18  VAL U  19  0                                        
SHEET    2  AF 2 GLU 9  59  PHE 9  60  1  O  GLU 9  59   N  VAL U  19           
SHEET    1  AG 4 GLN U  27  VAL U  29  0                                        
SHEET    2  AG 4 THR U  39  ILE U  44 -1  O  GLN U  41   N  VAL U  29           
SHEET    3  AG 4 TYR U  92  LEU U  99 -1  O  LYS U  93   N  ILE U  44           
SHEET    4  AG 4 VAL U  65  GLN U  73 -1  N  GLN U  73   O  TYR U  92           
SHEET    1  AH 6 LEU V 115  LEU V 116  0                                        
SHEET    2  AH 6 TRP V  85  VAL V  88 -1  N  VAL V  86   O  LEU V 115           
SHEET    3  AH 6 GLN V  73  ILE V  80 -1  N  GLN V  78   O  VAL V  87           
SHEET    4  AH 6 THR V  61  ILE V  64 -1  N  VAL V  62   O  GLY V  74           
SHEET    5  AH 6 VAL V 120  VAL V 123 -1  O  LYS V 121   N  GLU V  63           
SHEET    6  AH 6 PRO V 130  THR V 131 -1  O  THR V 131   N  LEU V 122           
SHEET    1  AI 2 THR V  93  ILE V  98  0                                        
SHEET    2  AI 2 THR V 107  GLU V 112 -1  O  THR V 107   N  ILE V  98           
SHEET    1  AJ 3 ILE V 133  PHE V 137  0                                        
SHEET    2  AJ 3 ARG V 143  SER V 147 -1  O  VAL V 146   N  GLU V 134           
SHEET    3  AJ 3 ILE V 153  ILE V 154 -1  O  ILE V 154   N  ARG V 145           
SHEET    1  AK 4 GLY W  52  ILE W  53  0                                        
SHEET    2  AK 4 ILE W  66  THR W  69 -1  O  THR W  69   N  GLY W  52           
SHEET    3  AK 4 LEU W  89  ALA W  91 -1  O  LEU W  89   N  ALA W  68           
SHEET    4  AK 4 VAL W  81  VAL W  83 -1  N  GLY W  82   O  TYR W  90           
SHEET    1  AL 4 TYR W  60  VAL W  61  0                                        
SHEET    2  AL 4 GLY W  95  GLU W 102 -1  O  GLY W  95   N  VAL W  61           
SHEET    3  AL 4 LYS W 128  PRO W 135 -1  O  HIS W 132   N  ARG W  98           
SHEET    4  AL 4 HIS W  76  PRO W  77  1  N  HIS W  76   O  VAL W 131           
SHEET    1  AM 2 LEU W 144  LEU W 148  0                                        
SHEET    2  AM 2 GLU 6 339  PHE 6 342 -1  O  GLU 6 339   N  LEU W 148           
SHEET    1  AN 2 ILE X  86  TYR X  91  0                                        
SHEET    2  AN 2 ARG X 100  TRP X 105 -1  O  LEU X 101   N  ILE X  90           
SHEET    1  AO 2 ARG X 112  SER X 116  0                                        
SHEET    2  AO 2 LYS X 121  VAL X 125 -1  O  PHE X 123   N  PHE X 114           
SHEET    1  AP 2 ARG Y 169  ARG Y 170  0                                        
SHEET    2  AP 2 ILE Y 176  ILE Y 177 -1  O  ILE Y 177   N  ARG Y 169           
SHEET    1  AQ 3 PRO Z  97  LYS Z 101  0                                        
SHEET    2  AQ 3 LEU Z  66  ARG Z  71 -1  N  VAL Z  69   O  GLN Z  98           
SHEET    3  AQ 3 ILE Z 117  PRO Z 121 -1  O  LYS Z 120   N  ILE Z  68           
SHEET    1  AR 2 ILE 0 107  ASP 0 108  0                                        
SHEET    2  AR 2 LYS 0 117  GLN 0 118 -1  O  LYS 0 117   N  ASP 0 108           
SHEET    1  AS 2 VAL 0 157  LEU 0 159  0                                        
SHEET    2  AS 2 ILE 0 174  GLU 0 176  1  O  ILE 0 175   N  LEU 0 159           
SHEET    1  AT 4 CYS 1  29  ASN 1  35  0                                        
SHEET    2  AT 4 ASN 1  15  SER 1  22 -1  N  ILE 1  16   O  ARG 1  34           
SHEET    3  AT 4 GLN 1  52  SER 1  64 -1  O  VAL 1  57   N  VAL 1  21           
SHEET    4  AT 4 THR 1  42  ASP 1  47 -1  N  LEU 1  43   O  PHE 1  56           
SHEET    1  AU 3 PHE 3 114  ARG 3 116  0                                        
SHEET    2  AU 3 TRP 3 122  ARG 3 125 -1  O  VAL 3 123   N  LEU 3 115           
SHEET    3  AU 3 PHE 3 147  PHE 3 149 -1  O  VAL 3 148   N  ARG 3 124           
SHEET    1  AV 2 TYR 4  80  ARG 4  84  0                                        
SHEET    2  AV 2 ARG 4  87  TYR 4  91 -1  O  TYR 4  89   N  VAL 4  82           
SHEET    1  AW 4 ALA 5 211  TRP 5 213  0                                        
SHEET    2  AW 4 LEU 5 220  VAL 5 222 -1  O  LEU 5 220   N  TRP 5 213           
SHEET    3  AW 4 CYS 5 104  PHE 5 107  1  N  TYR 5 105   O  GLN 5 221           
SHEET    4  AW 4 HIS 5 266  CYS 5 268 -1  O  CYS 5 268   N  CYS 5 104           
SHEET    1  AX 7 THR 5 126  ILE 5 129  0                                        
SHEET    2  AX 7 ASN 5 372  ASP 5 377  1  O  VAL 5 376   N  ILE 5 129           
SHEET    3  AX 7 PHE 5 354  PHE 5 357 -1  N  VAL 5 356   O  TRP 5 375           
SHEET    4  AX 7 VAL 5 342  VAL 5 345 -1  N  VAL 5 342   O  PHE 5 357           
SHEET    5  AX 7 TYR 5 287  TYR 5 292  1  N  HIS 5 289   O  GLN 5 343           
SHEET    6  AX 7 ALA 5 228  THR 5 232 -1  N  LEU 5 230   O  THR 5 290           
SHEET    7  AX 7 ARG 5 201  VAL 5 204 -1  N  ILE 5 202   O  SER 5 231           
SHEET    1  AY 3 MET 6 185  PRO 6 186  0                                        
SHEET    2  AY 3 HIS 6 174  TYR 6 177 -1  N  TYR 6 177   O  MET 6 185           
SHEET    3  AY 3 GLU 6 203  THR 6 205 -1  O  GLU 6 203   N  ALA 6 176           
SHEET    1  AZ 6 ASN 6 191  GLU 6 192  0                                        
SHEET    2  AZ 6 MET 6 311  CYS 6 321  1  O  GLN 6 320   N  ASN 6 191           
SHEET    3  AZ 6 HIS 6 266  GLN 6 275 -1  N  PHE 6 270   O  SER 6 317           
SHEET    4  AZ 6 TRP 6 214  SER 6 220 -1  N  THR 6 219   O  ALA 6 269           
SHEET    5  AZ 6 TYR 6 232  THR 6 238 -1  O  HIS 6 234   N  LEU 6 218           
SHEET    6  AZ 6 GLN 6 249  VAL 6 250 -1  O  GLN 6 249   N  THR 6 238           
SHEET    1  BA 6 PRO 7 112  ASP 7 114  0                                        
SHEET    2  BA 6 LEU 7 105  VAL 7 108 -1  N  ALA 7 106   O  TRP 7 113           
SHEET    3  BA 6 GLU 7 124  LEU 7 128 -1  O  LEU 7 128   N  LEU 7 105           
SHEET    4  BA 6 LYS 7  64  HIS 7  69  1  N  LYS 7  68   O  ILE 7 125           
SHEET    5  BA 6 VAL 7  78  ASN 7  82 -1  O  PHE 7  79   N  VAL 7  67           
SHEET    6  BA 6 VAL d 280  ILE d 282 -1  O  VAL d 280   N  VAL 7  80           
SHEET    1  BB 4 LEU 7 166  ARG 7 168  0                                        
SHEET    2  BB 4 PHE 7 179  VAL 7 183 -1  O  ASP 7 182   N  ARG 7 168           
SHEET    3  BB 4 ARG 7 295  PRO 7 303 -1  O  GLY 7 299   N  PHE 7 179           
SHEET    4  BB 4 CYS 7 275  GLU 7 279 -1  N  GLN 7 277   O  LEU 7 302           
SHEET    1  BC 4 LEU 7 166  ARG 7 168  0                                        
SHEET    2  BC 4 PHE 7 179  VAL 7 183 -1  O  ASP 7 182   N  ARG 7 168           
SHEET    3  BC 4 ARG 7 295  PRO 7 303 -1  O  GLY 7 299   N  PHE 7 179           
SHEET    4  BC 4 VAL 7 283  HIS 7 284 -1  N  HIS 7 284   O  ARG 7 296           
SHEET    1  BD 3 GLU 7 217  VAL 7 221  0                                        
SHEET    2  BD 3 VAL 7 252  ILE 7 257 -1  O  VAL 7 252   N  VAL 7 221           
SHEET    3  BD 3 PHE 7 260  VAL 7 263 -1  O  ASP 7 262   N  HIS 7 255           
SHEET    1  BE 2 GLY 9  42  THR 9  45  0                                        
SHEET    2  BE 2 ARG 9  49  GLN 9  52 -1  O  VAL 9  51   N  PHE 9  43           
SHEET    1  BF 5 VAL b  84  SER b  88  0                                        
SHEET    2  BF 5 ARG b  74  TYR b  79 -1  N  VAL b  75   O  GLU b  87           
SHEET    3  BF 5 LEU b  26  SER b  32 -1  N  SER b  32   O  ARG b  74           
SHEET    4  BF 5 TYR b  64  VAL b  65  1  O  TYR b  64   N  PHE b  31           
SHEET    5  BF 5 LYS h 153  ILE h 154  1  O  LYS h 153   N  VAL b  65           
SHEET    1  BG 3 LEU c 257  SER c 261  0                                        
SHEET    2  BG 3 LEU c 269  TYR c 275 -1  O  PHE c 271   N  ARG c 259           
SHEET    3  BG 3 LEU c 280  GLY c 286 -1  O  GLY c 284   N  VAL c 272           
SHEET    1  BH 2 THR d 180  VAL d 181  0                                        
SHEET    2  BH 2 ILE d 224  TYR d 225 -1  O  TYR d 225   N  THR d 180           
SHEET    1  BI 3 SER d 184  SER d 188  0                                        
SHEET    2  BI 3 TYR d 209  THR d 221 -1  O  THR d 221   N  SER d 184           
SHEET    3  BI 3 HIS d 193  ARG d 198 -1  N  ARG d 198   O  GLN d 211           
SHEET    1  BJ 4 SER d 184  SER d 188  0                                        
SHEET    2  BJ 4 TYR d 209  THR d 221 -1  O  THR d 221   N  SER d 184           
SHEET    3  BJ 4 LYS d 240  GLN d 251 -1  O  VAL d 242   N  THR d 218           
SHEET    4  BJ 4 ARG d 260  LYS d 264 -1  O  HIS d 262   N  VAL d 247           
SHEET    1  BK 2 ARG e 102  SER e 104  0                                        
SHEET    2  BK 2 LYS e 186  PHE e 188  1  O  PHE e 188   N  THR e 103           
SHEET    1  BL 5 GLU e 157  PHE e 160  0                                        
SHEET    2  BL 5 LYS e 191  LEU e 193 -1  O  LEU e 193   N  GLU e 157           
SHEET    3  BL 5 ARG e 107  ASP e 110  1  N  LEU e 109   O  ALA e 192           
SHEET    4  BL 5 LEU e 113  VAL e 117 -1  O  LEU e 115   N  LYS e 108           
SHEET    5  BL 5 HIS e 208  VAL e 211 -1  O  VAL e 211   N  VAL e 114           
SHEET    1  BM 2 LYS f 120  VAL f 121  0                                        
SHEET    2  BM 2 ILE f 159  SER f 160 -1  O  SER f 160   N  LYS f 120           
SHEET    1  BN 2 ALA f 126  MET f 127  0                                        
SHEET    2  BN 2 GLU f 154  ARG f 155 -1  O  GLU f 154   N  MET f 127           
SHEET    1  BO 2 ARG f 183  LEU f 184  0                                        
SHEET    2  BO 2 UNK f 264  UNK f 265 -1  O  UNK f 264   N  LEU f 184           
SHEET    1  BP 2 TYR g  84  VAL g  86  0                                        
SHEET    2  BP 2 VAL g 113  GLY g 115 -1  O  GLU g 114   N  PHE g  85           
SHEET    1  BQ 4 VAL g  96  ILE g 100  0                                        
SHEET    2  BQ 4 GLN g 106  ILE g 110 -1  O  MET g 107   N  ASP g  99           
SHEET    3  BQ 4 THR g 146  LYS g 150 -1  O  ILE g 149   N  THR g 108           
SHEET    4  BQ 4 THR g 138  ASN g 141 -1  N  GLN g 139   O  ARG g 148           
SHEET    1  BR 4 ASP k  65  VAL k  66  0                                        
SHEET    2  BR 4 LEU k  74  MET k  76 -1  O  LEU k  74   N  VAL k  66           
SHEET    3  BR 4 ILE r  48  ILE r  53  1  O  ILE r  49   N  ILE k  75           
SHEET    4  BR 4 ARG r  36  GLU r  40 -1  N  VAL r  39   O  GLU r  50           
SHEET    1  BS 3 THR p  77  CYS p  81  0                                        
SHEET    2  BS 3 LYS p  98  PHE p 103 -1  O  ARG p 102   N  THR p  77           
SHEET    3  BS 3 LEU p 133  ILE p 134 -1  O  LEU p 133   N  PHE p 103           
SHEET    1  BT 4 VAL s 206  ILE s 216  0                                        
SHEET    2  BT 4 ILE s 226  ASP s 235 -1  O  TYR s 231   N  TRP s 210           
SHEET    3  BT 4 LYS s  90  VAL s  93  1  N  TYR s  91   O  ARG s 230           
SHEET    4  BT 4 PHE s 274  ARG s 276 -1  O  PHE s 274   N  MET s  92           
SHEET    1  BU 7 THR s 112  SER s 116  0                                        
SHEET    2  BU 7 ASN s 391  GLY s 395  1  O  CYS s 393   N  VAL s 113           
SHEET    3  BU 7 TYR s 366  LEU s 374 -1  N  GLN s 373   O  ILE s 392           
SHEET    4  BU 7 PHE s 355  THR s 362 -1  N  SER s 357   O  TYR s 372           
SHEET    5  BU 7 TYR s 294  PHE s 299  1  N  GLN s 298   O  VAL s 360           
SHEET    6  BU 7 ASN s 239  ILE s 243 -1  N  ASN s 239   O  PHE s 299           
SHEET    7  BU 7 ALA s 199  TYR s 202 -1  N  ASP s 201   O  GLN s 240           
SHEET    1  BV 4 THR s 112  SER s 116  0                                        
SHEET    2  BV 4 ASN s 391  GLY s 395  1  O  CYS s 393   N  VAL s 113           
SHEET    3  BV 4 TYR s 366  LEU s 374 -1  N  GLN s 373   O  ILE s 392           
SHEET    4  BV 4 LYS s 399  PRO s 400 -1  O  LYS s 399   N  PHE s 367           
LINK         OP2   U A2115                MG    MG A3365     1555   1555  1.79  
LINK         OP1   U A3037                MG    MG A3342     1555   1555  1.86  
LINK         OP2   C A1726                MG    MG A3305     1555   1555  1.90  
LINK         OP1   G A3063                MG    MG A3339     1555   1555  1.94  
LINK         OP2   G A1918                MG    MG A3310     1555   1555  1.95  
LINK         OP1   C A2603                MG    MG A3335     1555   1555  1.97  
LINK         OP1   U A2115                MG    MG A3366     1555   1555  1.97  
LINK         OP1   A A1961                MG    MG A3317     1555   1555  1.97  
LINK         OP2   A A2250                MG    MG A3316     1555   1555  1.97  
LINK         OP1   C A2986                MG    MG A3351     1555   1555  1.97  
LINK         OP1   C A2114                MG    MG A3365     1555   1555  1.98  
LINK         OP2   G A2733                MG    MG A3349     1555   1555  1.99  
LINK         OP2   A A2452                MG    MG A3320     1555   1555  1.99  
LINK         OP1   A A2935                MG    MG A3351     1555   1555  2.01  
LINK         OP2   A A2313                MG    MG A3324     1555   1555  2.01  
LINK         OP2   A A2298                MG    MG A3326     1555   1555  2.03  
LINK         OP2   A A3005                MG    MG A3354     1555   1555  2.04  
LINK         OP2   G A2917                MG    MG A3363     1555   1555  2.08  
LINK         SG  CYS r  70                ZN    ZN r 200     1555   1555  2.08  
LINK         OP2   A A2958                MG    MG A3352     1555   1555  2.10  
LINK         OP2   G A2719                MG    MG A3347     1555   1555  2.11  
LINK         OP2   A A1994                MG    MG A3313     1555   1555  2.11  
LINK         OP2   C A1942                MG    MG A3309     1555   1555  2.12  
LINK         OP1   C A1922                MG    MG A3361     1555   1555  2.13  
LINK         OP2   A A2027                MG    MG A3314     1555   1555  2.13  
LINK         OP1   A A2430                MG    MG A3317     1555   1555  2.13  
LINK         OP2   U A2253                MG    MG A3315     1555   1555  2.14  
LINK         OP1   A A2468                MG    MG A3337     1555   1555  2.16  
LINK         OP2   A A2451                MG    MG A3320     1555   1555  2.17  
LINK         OP2   A A1757                MG    MG A3304     1555   1555  2.17  
LINK         OP1   U A3102                MG    MG A3356     1555   1555  2.17  
LINK         OP2   A A2604                MG    MG A3335     1555   1555  2.18  
LINK         OP2   C A2474                MG    MG A3342     1555   1555  2.19  
LINK         OP1   A A2509                MG    MG A3343     1555   1555  2.19  
LINK         OP1   A A1971                MG    MG A3340     1555   1555  2.19  
LINK         SG  CYS 4  76                ZN    ZN 4 200     1555   1555  2.20  
LINK         OP1   C A1951                MG    MG A3360     1555   1555  2.20  
LINK         OP1   C A1725                MG    MG A3305     1555   1555  2.21  
LINK         OP1   A A2866                MG    MG A3302     1555   1555  2.21  
LINK         OP1   A A2725                MG    MG A3344     1555   1555  2.21  
LINK         OP2   A A2720                MG    MG A3347     1555   1555  2.22  
LINK         OP1   A A3076                MG    MG A3313     1555   1555  2.22  
LINK         OP1   C A2423                MG    MG A3318     1555   1555  2.22  
LINK         OP2   A A2918                MG    MG A3363     1555   1555  2.22  
LINK         OP2   A A2504                MG    MG A3311     1555   1555  2.22  
LINK         OP2   A A1815                MG    MG A3307     1555   1555  2.23  
LINK         OP1   G A2040                MG    MG A3362     1555   1555  2.23  
LINK         OP2   G A2989                MG    MG A3325     1555   1555  2.26  
LINK         OP2   A A2480                MG    MG A3359     1555   1555  2.27  
LINK         OP2   U A2864                MG    MG A3302     1555   1555  2.28  
LINK         OP1   C A2100                MG    MG A3365     1555   1555  2.28  
LINK         OP2   G A3075                MG    MG A3331     1555   1555  2.28  
LINK         OP1   C A2494                MG    MG A3319     1555   1555  2.28  
LINK         OP1   C A2252                MG    MG A3315     1555   1555  2.29  
LINK         OP2   A A2473                MG    MG A3342     1555   1555  2.29  
LINK         OP2   G A2496                MG    MG A3333     1555   1555  2.29  
LINK         O6    G A1851                MG    MG A3351     1555   1555  2.30  
LINK         OP2   A A2469                MG    MG A3337     1555   1555  2.32  
LINK         OP1   C A3066                MG    MG A3355     1555   1555  2.35  
LINK         SG  CYS 0 123                ZN    ZN 0 200     1555   1555  2.36  
LINK         OP1   A A2462                MG    MG E 401     1555   1555  2.36  
LINK         OP1   U A1848                MG    MG A3303     1555   1555  2.36  
LINK         OP2   A A1971                MG    MG A3309     1555   1555  2.41  
LINK         OP1   A A2668                MG    MG A3324     1555   1555  2.42  
LINK         OP2   A A2935                MG    MG A3353     1555   1555  2.42  
LINK         O4    U A1758                MG    MG A3304     1555   1555  2.43  
LINK         O4    U A2475                MG    MG A3342     1555   1555  2.43  
LINK         OP2   U A2812                MG    MG A3348     1555   1555  2.43  
LINK         OP2   A A2468                MG    MG A3346     1555   1555  2.43  
LINK         OP1   A A3064                MG    MG A3339     1555   1555  2.44  
LINK         OP1   U A3038                MG    MG A3358     1555   1555  2.48  
LINK         OP2   A A2309                MG    MG A3356     1555   1555  2.49  
LINK         OP1   G A2733                MG    MG A3329     1555   1555  2.50  
LINK         OP2   G A2011                MG    MG A3312     1555   1555  2.51  
LINK         OP1   U A2141                MG    MG A3315     1555   1555  2.51  
LINK         OP2   G A2724                MG    MG A3325     1555   1555  2.52  
LINK         OP2   G A1941                MG    MG A3340     1555   1555  2.54  
LINK         OP2   A A1907                MG    MG A3364     1555   1555  2.55  
LINK         O6    G A1776                MG    MG A3308     1555   1555  2.56  
LINK         OP1   A A2503                MG    MG A3311     1555   1555  2.57  
LINK         SG  CYS 4  92                ZN    ZN 4 200     1555   1555  2.57  
LINK         OP1   A A1994                MG    MG A3341     1555   1555  2.59  
LINK         OP1   A A2633                MG    MG A3345     1555   1555  2.60  
LINK         OP2   G A1776                MG    MG A3306     1555   1555  2.62  
LINK         O4    U A2813                MG    MG A3348     1555   1555  2.63  
LINK         OP1   A A1779                MG    MG A3308     1555   1555  2.63  
LINK         OP2   G A2732                MG    MG A3349     1555   1555  2.69  
LINK         OP2   U A1950                MG    MG A3311     1555   1555  2.71  
LINK         OP1   G A3075                MG    MG A3341     1555   1555  2.72  
LINK         OP2   A A2875                MG    MG A3357     1555   1555  2.75  
LINK         OP2   C A2985                MG    MG A3353     1555   1555  2.76  
LINK         OP1   U A1950                MG    MG A3311     1555   1555  2.84  
LINK         OP2   U A2660                MG    MG A3323     1555   1555  2.85  
LINK         OP1   A A1814                MG    MG A3307     1555   1555  2.89  
LINK         O3'   G A2934                MG    MG A3353     1555   1555  2.93  
LINK         OP2   A A1993                MG    MG A3313     1555   1555  2.94  
LINK         O5'   U A2660                MG    MG A3323     1555   1555  2.94  
LINK         O6    G A2448                MG    MG A3338     1555   1555  2.95  
LINK         SG  CYS r 108                ZN    ZN r 200     1555   1555  2.95  
LINK         OP2   U A3102                MG    MG A3356     1555   1555  2.95  
LINK         SG  CYS 0 113                ZN    ZN 0 200     1555   1555  2.96  
LINK         O5'   G A2732                MG    MG A3349     1555   1555  2.97  
CISPEP   1 HIS E  231    GLY E  232          0       -17.27                     
CISPEP   2 GLY E  323    ASP E  324          0         4.61                     
CISPEP   3 THR J  104    GLY J  105          0         0.71                     
CISPEP   4 GLY L  112    ASN L  113          0        -9.13                     
CISPEP   5 PHE P   71    PRO P   72          0       -10.37                     
CISPEP   6 LYS R  136    GLU R  137          0        -2.56                     
CISPEP   7 LYS S  146    PRO S  147          0       -11.55                     
CISPEP   8 GLY V  141    GLU V  142          0         4.45                     
CISPEP   9 PRO 5   53    GLY 5   54          0        -0.95                     
CISPEP  10 GLU 5  115    GLY 5  116          0        23.44                     
CISPEP  11 GLU 5  216    SER 5  217          0         8.85                     
CISPEP  12 TYR 5  257    PRO 5  258          0         3.21                     
CISPEP  13 PRO 5  261    ILE 5  262          0        17.44                     
CISPEP  14 ARG 6   72    THR 6   73          0        27.82                     
CISPEP  15 ASP 6  182    ASP 6  183          0         0.78                     
CISPEP  16 ASP 6  371    SER 6  372          0        -5.74                     
CISPEP  17 PRO 7   75    GLY 7   76          0       -11.90                     
CISPEP  18 PHE c  184    PRO c  185          0        -5.97                     
CISPEP  19 ASP d  129    ALA d  130          0        12.30                     
CISPEP  20 PRO d  267    PRO d  268          0         5.66                     
CISPEP  21 TYR g   66    PRO g   67          0        -2.81                     
CISPEP  22 ASP g   77    PRO g   78          0        -4.02                     
CISPEP  23 PRO h   63    GLU h   64          0        17.59                     
CISPEP  24 ARG k   77    GLY k   78          0       -14.88                     
CISPEP  25 UNK t   20    UNK t   21          0       -10.80                     
SITE     1 AC1  5   U A2898    C A2899    G A2909    A A2910                    
SITE     2 AC1  5   A A2919                                                     
SITE     1 AC2  2   U A2864    A A2866                                          
SITE     1 AC3  3   U A1848    U A2020  GLN M  58                               
SITE     1 AC4  2   A A1757    U A1758                                          
SITE     1 AC5  3   A A1723    C A1725    C A1726                               
SITE     1 AC6  2   G A1776    U A1778                                          
SITE     1 AC7  3   A A1814    A A1815    G A1816                               
SITE     1 AC8  2   G A1776    A A1779                                          
SITE     1 AC9  2   C A1942    A A1971                                          
SITE     1 BC1  2   A A1917    G A1918                                          
SITE     1 BC2  3   U A1950    A A2503    A A2504                               
SITE     1 BC3  3   G A2009    U A2010    G A2011                               
SITE     1 BC4  3   A A1993    A A1994    A A3076                               
SITE     1 BC5  1   A A2027                                                     
SITE     1 BC6  3   U A2141    C A2252    U A2253                               
SITE     1 BC7  3   U A2150    A A2250  ARG R  65                               
SITE     1 BC8  3   A A1960    A A1961    A A2430                               
SITE     1 BC9  1   C A2423                                                     
SITE     1 CC1  1   C A2494                                                     
SITE     1 CC2  2   A A2451    A A2452                                          
SITE     1 CC3  1   C A2508                                                     
SITE     1 CC4  1   G A2453                                                     
SITE     1 CC5  1   U A2660                                                     
SITE     1 CC6  2   A A2313    A A2668                                          
SITE     1 CC7  2   G A2724    G A2989                                          
SITE     1 CC8  2   A A2298    G A2300                                          
SITE     1 CC9  1   G A2989                                                     
SITE     1 DC1  2   C A1721    G A2733                                          
SITE     1 DC2  3   A A2926    A A3074    G A3075                               
SITE     1 DC3  1   G A2496                                                     
SITE     1 DC4  2   C A2603    A A2604                                          
SITE     1 DC5  1   G A2673                                                     
SITE     1 DC6  2   A A2468    A A2469                                          
SITE     1 DC7  1   G A2448                                                     
SITE     1 DC8  3   U A3062    G A3063    A A3064                               
SITE     1 DC9  4   A A1940    G A1941    A A1971    A A1972                    
SITE     1 EC1  2   A A1994    G A3075                                          
SITE     1 EC2  4   A A2473    C A2474    U A2475    U A3037                    
SITE     1 EC3  2   A A2509  GLY D 273                                          
SITE     1 EC4  4   A A2725    U A2930    A A2931  LYS F 131                    
SITE     1 EC5  2   A A2564    A A2633                                          
SITE     1 EC6  2   A A2468    G A2655                                          
SITE     1 EC7  2   G A2719    A A2720                                          
SITE     1 EC8  2   U A2812    U A2813                                          
SITE     1 EC9  2   G A2732    G A2733                                          
SITE     1 FC1  1   G A2815                                                     
SITE     1 FC2  4   G A1851    A A2935    C A2986    U A2987                    
SITE     1 FC3  1   A A2958                                                     
SITE     1 FC4  4   G A2934    A A2935    C A2985    C A2986                    
SITE     1 FC5  1   A A3005                                                     
SITE     1 FC6  2   C A3066    U A3098                                          
SITE     1 FC7  2   A A2309    U A3102                                          
SITE     1 FC8  1   A A2875                                                     
SITE     1 FC9  1   U A3038                                                     
SITE     1 GC1  1   A A2480                                                     
SITE     1 GC2  2   U A1950    C A1951                                          
SITE     1 GC3  1   C A1922                                                     
SITE     1 GC4  1   G A2040                                                     
SITE     1 GC5  3   C A2036    G A2917    A A2918                               
SITE     1 GC6  1   A A1907                                                     
SITE     1 GC7  3   C A2100    C A2114    U A2115                               
SITE     1 GC8  1   U A2115                                                     
SITE     1 GC9  5   A A1953    U A1954    A A2462  THR E 234                    
SITE     2 GC9  5 HIS E 237                                                     
SITE     1 HC1  5 CYS 0 110  GLU 0 112  CYS 0 113  CYS 0 123                    
SITE     2 HC1  5 CYS 0 126                                                     
SITE     1 HC2  4 CYS 4  76  CYS 4  79  CYS 4  92  HIS 4  98                    
SITE     1 HC3  3 CYS r  70  CYS r  73  CYS r 108                               
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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