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Database: PDB
Entry: 5XTD
LinkDB: 5XTD
Original site: 5XTD 
HEADER    OXIDOREDUCTASE/ELECTRON TRANSPORT       19-JUN-17   5XTD              
TITLE     CRYO-EM STRUCTURE OF HUMAN RESPIRATORY COMPLEX I                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN 1,            
COMPND   3 MITOCHONDRIAL;                                                       
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: COMPLEX I-51KD,CI-51KD,NADH DEHYDROGENASE FLAVOPROTEIN 1,   
COMPND   6 NADH-UBIQUINONE OXIDOREDUCTASE 51 KDA SUBUNIT;                       
COMPND   7 EC: 1.6.5.3,1.6.99.3;                                                
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 8,     
COMPND  10 MITOCHONDRIAL;                                                       
COMPND  11 CHAIN: B;                                                            
COMPND  12 SYNONYM: COMPLEX I-23KD,CI-23KD,NADH-UBIQUINONE OXIDOREDUCTASE 23 KDA
COMPND  13 SUBUNIT,TYKY SUBUNIT;                                                
COMPND  14 EC: 1.6.5.3,1.6.99.3;                                                
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 7,     
COMPND  17 MITOCHONDRIAL;                                                       
COMPND  18 CHAIN: C;                                                            
COMPND  19 SYNONYM: COMPLEX I-20KD,CI-20KD,NADH-UBIQUINONE OXIDOREDUCTASE 20 KDA
COMPND  20 SUBUNIT,PSST SUBUNIT;                                                
COMPND  21 EC: 1.6.5.3,1.6.99.3;                                                
COMPND  22 MOL_ID: 4;                                                           
COMPND  23 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 
COMPND  24 6;                                                                   
COMPND  25 CHAIN: E;                                                            
COMPND  26 SYNONYM: COMPLEX I-B14,CI-B14,LYR MOTIF-CONTAINING PROTEIN 6,NADH-   
COMPND  27 UBIQUINONE OXIDOREDUCTASE B14 SUBUNIT;                               
COMPND  28 MOL_ID: 5;                                                           
COMPND  29 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 
COMPND  30 2;                                                                   
COMPND  31 CHAIN: F;                                                            
COMPND  32 SYNONYM: COMPLEX I-B8,CI-B8,NADH-UBIQUINONE OXIDOREDUCTASE B8        
COMPND  33 SUBUNIT;                                                             
COMPND  34 MOL_ID: 6;                                                           
COMPND  35 MOLECULE: ACYL CARRIER PROTEIN, MITOCHONDRIAL;                       
COMPND  36 CHAIN: G, X;                                                         
COMPND  37 SYNONYM: ACP,CI-SDAP,NADH-UBIQUINONE OXIDOREDUCTASE 9.6 KDA SUBUNIT; 
COMPND  38 MOL_ID: 7;                                                           
COMPND  39 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 
COMPND  40 5;                                                                   
COMPND  41 CHAIN: H;                                                            
COMPND  42 SYNONYM: COMPLEX I SUBUNIT B13,COMPLEX I-13KD-B,CI-13KD-B,NADH-      
COMPND  43 UBIQUINONE OXIDOREDUCTASE 13 KDA-B SUBUNIT;                          
COMPND  44 MOL_ID: 8;                                                           
COMPND  45 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 
COMPND  46 7;                                                                   
COMPND  47 CHAIN: I;                                                            
COMPND  48 SYNONYM: COMPLEX I-B14.5A,CI-B14.5A,NADH-UBIQUINONE OXIDOREDUCTASE   
COMPND  49 SUBUNIT B14.5A;                                                      
COMPND  50 MOL_ID: 9;                                                           
COMPND  51 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 
COMPND  52 9, MITOCHONDRIAL;                                                    
COMPND  53 CHAIN: J;                                                            
COMPND  54 SYNONYM: COMPLEX I-39KD,CI-39KD,NADH-UBIQUINONE OXIDOREDUCTASE 39 KDA
COMPND  55 SUBUNIT;                                                             
COMPND  56 MOL_ID: 10;                                                          
COMPND  57 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN 3,            
COMPND  58 MITOCHONDRIAL;                                                       
COMPND  59 CHAIN: K;                                                            
COMPND  60 SYNONYM: COMPLEX I-9KD,CI-9KD,NADH-UBIQUINONE OXIDOREDUCTASE 9 KDA   
COMPND  61 SUBUNIT,RENAL CARCINOMA ANTIGEN NY-REN-4;                            
COMPND  62 MOL_ID: 11;                                                          
COMPND  63 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 4,     
COMPND  64 MITOCHONDRIAL;                                                       
COMPND  65 CHAIN: L;                                                            
COMPND  66 SYNONYM: COMPLEX I-18 KDA,CI-18 KDA,COMPLEX I-AQDQ,CI-AQDQ,NADH-     
COMPND  67 UBIQUINONE OXIDOREDUCTASE 18 KDA SUBUNIT;                            
COMPND  68 MOL_ID: 12;                                                          
COMPND  69 MOLECULE: NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT,             
COMPND  70 MITOCHONDRIAL;                                                       
COMPND  71 CHAIN: M;                                                            
COMPND  72 SYNONYM: COMPLEX I-75KD,CI-75KD;                                     
COMPND  73 EC: 1.6.5.3,1.6.99.3;                                                
COMPND  74 MOL_ID: 13;                                                          
COMPND  75 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 
COMPND  76 12;                                                                  
COMPND  77 CHAIN: N;                                                            
COMPND  78 SYNONYM: 13 KDA DIFFERENTIATION-ASSOCIATED PROTEIN,COMPLEX I-B17.2,  
COMPND  79 CIB17.2,NADH-UBIQUINONE OXIDOREDUCTASE SUBUNIT B17.2;                
COMPND  80 MOL_ID: 14;                                                          
COMPND  81 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN 2,            
COMPND  82 MITOCHONDRIAL;                                                       
COMPND  83 CHAIN: O;                                                            
COMPND  84 SYNONYM: NADH-UBIQUINONE OXIDOREDUCTASE 24 KDA SUBUNIT;              
COMPND  85 EC: 1.6.5.3,1.6.99.3;                                                
COMPND  86 MOL_ID: 15;                                                          
COMPND  87 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 3,     
COMPND  88 MITOCHONDRIAL;                                                       
COMPND  89 CHAIN: P;                                                            
COMPND  90 SYNONYM: COMPLEX I-30KD,CI-30KD,NADH-UBIQUINONE OXIDOREDUCTASE 30 KDA
COMPND  91 SUBUNIT;                                                             
COMPND  92 EC: 1.6.5.3,1.6.99.3;                                                
COMPND  93 MOL_ID: 16;                                                          
COMPND  94 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 2,     
COMPND  95 MITOCHONDRIAL;                                                       
COMPND  96 CHAIN: Q;                                                            
COMPND  97 SYNONYM: COMPLEX I-49KD,CI-49KD,NADH-UBIQUINONE OXIDOREDUCTASE 49 KDA
COMPND  98 SUBUNIT;                                                             
COMPND  99 EC: 1.6.5.3,1.6.99.3;                                                
COMPND 100 MOL_ID: 17;                                                          
COMPND 101 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 
COMPND 102 1;                                                                   
COMPND 103 CHAIN: S;                                                            
COMPND 104 SYNONYM: COMPLEX I-MWFE,CI-MWFE,NADH-UBIQUINONE OXIDOREDUCTASE MWFE  
COMPND 105 SUBUNIT;                                                             
COMPND 106 MOL_ID: 18;                                                          
COMPND 107 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 6,     
COMPND 108 MITOCHONDRIAL;                                                       
COMPND 109 CHAIN: T;                                                            
COMPND 110 SYNONYM: COMPLEX I-13KD-A,CI-13KD-A,NADH-UBIQUINONE OXIDOREDUCTASE 13
COMPND 111 KDA-A SUBUNIT;                                                       
COMPND 112 MOL_ID: 19;                                                          
COMPND 113 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 
COMPND 114 3;                                                                   
COMPND 115 CHAIN: U;                                                            
COMPND 116 SYNONYM: COMPLEX I-B9,CI-B9,NADH-UBIQUINONE OXIDOREDUCTASE B9        
COMPND 117 SUBUNIT;                                                             
COMPND 118 MOL_ID: 20;                                                          
COMPND 119 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 
COMPND 120 11;                                                                  
COMPND 121 CHAIN: V;                                                            
COMPND 122 SYNONYM: COMPLEX I-B14.7,CI-B14.7,NADH-UBIQUINONE OXIDOREDUCTASE     
COMPND 123 SUBUNIT B14.7;                                                       
COMPND 124 MOL_ID: 21;                                                          
COMPND 125 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 
COMPND 126 13;                                                                  
COMPND 127 CHAIN: W;                                                            
COMPND 128 SYNONYM: CELL DEATH REGULATORY PROTEIN GRIM-19,COMPLEX I-B16.6,CI-   
COMPND 129 B16.6,GENE ASSOCIATED WITH RETINOIC AND INTERFERON-INDUCED MORTALITY 
COMPND 130 19 PROTEIN,GENE ASSOCIATED WITH RETINOIC AND IFN-INDUCED MORTALITY 19
COMPND 131 PROTEIN,NADH-UBIQUINONE OXIDOREDUCTASE B16.6 SUBUNIT;                
COMPND 132 MOL_ID: 22;                                                          
COMPND 133 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 BETA SUBCOMPLEX SUBUNIT  
COMPND 134 2, MITOCHONDRIAL;                                                    
COMPND 135 CHAIN: Y;                                                            
COMPND 136 SYNONYM: COMPLEX I-AGGG,CI-AGGG,NADH-UBIQUINONE OXIDOREDUCTASE AGGG  
COMPND 137 SUBUNIT;                                                             
COMPND 138 MOL_ID: 23;                                                          
COMPND 139 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 BETA SUBCOMPLEX SUBUNIT  
COMPND 140 3;                                                                   
COMPND 141 CHAIN: Z;                                                            
COMPND 142 SYNONYM: COMPLEX I-B12,CI-B12,NADH-UBIQUINONE OXIDOREDUCTASE B12     
COMPND 143 SUBUNIT;                                                             
COMPND 144 MOL_ID: 24;                                                          
COMPND 145 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 BETA SUBCOMPLEX SUBUNIT  
COMPND 146 5, MITOCHONDRIAL;                                                    
COMPND 147 CHAIN: a;                                                            
COMPND 148 SYNONYM: COMPLEX I-SGDH,CI-SGDH,NADH-UBIQUINONE OXIDOREDUCTASE SGDH  
COMPND 149 SUBUNIT;                                                             
COMPND 150 MOL_ID: 25;                                                          
COMPND 151 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 BETA SUBCOMPLEX SUBUNIT  
COMPND 152 6;                                                                   
COMPND 153 CHAIN: b;                                                            
COMPND 154 SYNONYM: COMPLEX I-B17,CI-B17,NADH-UBIQUINONE OXIDOREDUCTASE B17     
COMPND 155 SUBUNIT;                                                             
COMPND 156 MOL_ID: 26;                                                          
COMPND 157 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 BETA SUBCOMPLEX SUBUNIT  
COMPND 158 8, MITOCHONDRIAL;                                                    
COMPND 159 CHAIN: c;                                                            
COMPND 160 SYNONYM: COMPLEX I-ASHI,CI-ASHI,NADH-UBIQUINONE OXIDOREDUCTASE ASHI  
COMPND 161 SUBUNIT;                                                             
COMPND 162 MOL_ID: 27;                                                          
COMPND 163 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 BETA SUBCOMPLEX SUBUNIT  
COMPND 164 10;                                                                  
COMPND 165 CHAIN: d;                                                            
COMPND 166 SYNONYM: COMPLEX I-PDSW,CI-PDSW,NADH-UBIQUINONE OXIDOREDUCTASE PDSW  
COMPND 167 SUBUNIT;                                                             
COMPND 168 MOL_ID: 28;                                                          
COMPND 169 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 BETA SUBCOMPLEX SUBUNIT  
COMPND 170 11, MITOCHONDRIAL;                                                   
COMPND 171 CHAIN: e;                                                            
COMPND 172 SYNONYM: COMPLEX I-ESSS,CI-ESSS,NADH-UBIQUINONE OXIDOREDUCTASE ESSS  
COMPND 173 SUBUNIT,NEURONAL PROTEIN 17.3,P17.3;                                 
COMPND 174 MOL_ID: 29;                                                          
COMPND 175 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 SUBUNIT C1,              
COMPND 176 MITOCHONDRIAL;                                                       
COMPND 177 CHAIN: f;                                                            
COMPND 178 SYNONYM: COMPLEX I-KFYI,CI-KFYI,NADH-UBIQUINONE OXIDOREDUCTASE KFYI  
COMPND 179 SUBUNIT;                                                             
COMPND 180 MOL_ID: 30;                                                          
COMPND 181 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 SUBUNIT C2;              
COMPND 182 CHAIN: g;                                                            
COMPND 183 SYNONYM: COMPLEX I-B14.5B,CI-B14.5B,HUMAN LUNG CANCER ONCOGENE 1     
COMPND 184 PROTEIN,HLC-1,NADH-UBIQUINONE OXIDOREDUCTASE SUBUNIT B14.5B;         
COMPND 185 MOL_ID: 31;                                                          
COMPND 186 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 5;     
COMPND 187 CHAIN: h;                                                            
COMPND 188 SYNONYM: COMPLEX I-15 KDA,CI-15 KDA,NADH-UBIQUINONE OXIDOREDUCTASE 15
COMPND 189 KDA SUBUNIT;                                                         
COMPND 190 MOL_ID: 32;                                                          
COMPND 191 MOLECULE: NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 2;                    
COMPND 192 CHAIN: i;                                                            
COMPND 193 EC: 1.6.5.3;                                                         
COMPND 194 MOL_ID: 33;                                                          
COMPND 195 MOLECULE: NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 3;                    
COMPND 196 CHAIN: j;                                                            
COMPND 197 EC: 1.6.5.3;                                                         
COMPND 198 MOL_ID: 34;                                                          
COMPND 199 MOLECULE: NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 4L;                   
COMPND 200 CHAIN: k;                                                            
COMPND 201 EC: 1.6.5.3;                                                         
COMPND 202 MOL_ID: 35;                                                          
COMPND 203 MOLECULE: NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 5;                    
COMPND 204 CHAIN: l;                                                            
COMPND 205 EC: 1.6.5.3;                                                         
COMPND 206 MOL_ID: 36;                                                          
COMPND 207 MOLECULE: NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 6;                    
COMPND 208 CHAIN: m;                                                            
COMPND 209 EC: 1.6.5.3;                                                         
COMPND 210 MOL_ID: 37;                                                          
COMPND 211 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 BETA SUBCOMPLEX SUBUNIT  
COMPND 212 1;                                                                   
COMPND 213 CHAIN: n;                                                            
COMPND 214 SYNONYM: COMPLEX I-MNLL,CI-MNLL,NADH-UBIQUINONE OXIDOREDUCTASE MNLL  
COMPND 215 SUBUNIT;                                                             
COMPND 216 MOL_ID: 38;                                                          
COMPND 217 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 BETA SUBCOMPLEX SUBUNIT  
COMPND 218 4;                                                                   
COMPND 219 CHAIN: o;                                                            
COMPND 220 SYNONYM: COMPLEX I-B15,CI-B15,NADH-UBIQUINONE OXIDOREDUCTASE B15     
COMPND 221 SUBUNIT;                                                             
COMPND 222 MOL_ID: 39;                                                          
COMPND 223 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 BETA SUBCOMPLEX SUBUNIT  
COMPND 224 9;                                                                   
COMPND 225 CHAIN: p;                                                            
COMPND 226 SYNONYM: COMPLEX I-B22,CI-B22,LYR MOTIF-CONTAINING PROTEIN 3,NADH-   
COMPND 227 UBIQUINONE OXIDOREDUCTASE B22 SUBUNIT;                               
COMPND 228 MOL_ID: 40;                                                          
COMPND 229 MOLECULE: NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 4;                    
COMPND 230 CHAIN: r;                                                            
COMPND 231 EC: 1.6.5.3;                                                         
COMPND 232 MOL_ID: 41;                                                          
COMPND 233 MOLECULE: NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 1;                    
COMPND 234 CHAIN: s;                                                            
COMPND 235 EC: 1.6.5.3;                                                         
COMPND 236 MOL_ID: 42;                                                          
COMPND 237 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 
COMPND 238 8;                                                                   
COMPND 239 CHAIN: u;                                                            
COMPND 240 SYNONYM: COMPLEX I-19KD,CI-19KD,COMPLEX I-PGIV,CI-PGIV,NADH-         
COMPND 241 UBIQUINONE OXIDOREDUCTASE 19 KDA SUBUNIT;                            
COMPND 242 MOL_ID: 43;                                                          
COMPND 243 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 BETA SUBCOMPLEX SUBUNIT  
COMPND 244 7;                                                                   
COMPND 245 CHAIN: v;                                                            
COMPND 246 SYNONYM: CELL ADHESION PROTEIN SQM1,COMPLEX I-B18,CI-B18,NADH-       
COMPND 247 UBIQUINONE OXIDOREDUCTASE B18 SUBUNIT;                               
COMPND 248 MOL_ID: 44;                                                          
COMPND 249 MOLECULE: NADH DEHYDROGENASE [UBIQUINONE] 1 ALPHA SUBCOMPLEX SUBUNIT 
COMPND 250 10, MITOCHONDRIAL;                                                   
COMPND 251 CHAIN: w;                                                            
COMPND 252 SYNONYM: COMPLEX I-42KD,CI-42KD,NADH-UBIQUINONE OXIDOREDUCTASE 42 KDA
COMPND 253 SUBUNIT                                                              
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   7 ORGANISM_COMMON: HUMAN;                                              
SOURCE   8 ORGANISM_TAXID: 9606;                                                
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 MOL_ID: 4;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_COMMON: HUMAN;                                              
SOURCE  16 ORGANISM_TAXID: 9606;                                                
SOURCE  17 MOL_ID: 5;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  19 ORGANISM_COMMON: HUMAN;                                              
SOURCE  20 ORGANISM_TAXID: 9606;                                                
SOURCE  21 MOL_ID: 6;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606;                                                
SOURCE  25 MOL_ID: 7;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  27 ORGANISM_COMMON: HUMAN;                                              
SOURCE  28 ORGANISM_TAXID: 9606;                                                
SOURCE  29 MOL_ID: 8;                                                           
SOURCE  30 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  31 ORGANISM_COMMON: HUMAN;                                              
SOURCE  32 ORGANISM_TAXID: 9606;                                                
SOURCE  33 MOL_ID: 9;                                                           
SOURCE  34 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  35 ORGANISM_COMMON: HUMAN;                                              
SOURCE  36 ORGANISM_TAXID: 9606;                                                
SOURCE  37 MOL_ID: 10;                                                          
SOURCE  38 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  39 ORGANISM_COMMON: HUMAN;                                              
SOURCE  40 ORGANISM_TAXID: 9606;                                                
SOURCE  41 MOL_ID: 11;                                                          
SOURCE  42 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  43 ORGANISM_COMMON: HUMAN;                                              
SOURCE  44 ORGANISM_TAXID: 9606;                                                
SOURCE  45 MOL_ID: 12;                                                          
SOURCE  46 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  47 ORGANISM_COMMON: HUMAN;                                              
SOURCE  48 ORGANISM_TAXID: 9606;                                                
SOURCE  49 MOL_ID: 13;                                                          
SOURCE  50 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  51 ORGANISM_COMMON: HUMAN;                                              
SOURCE  52 ORGANISM_TAXID: 9606;                                                
SOURCE  53 MOL_ID: 14;                                                          
SOURCE  54 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  55 ORGANISM_COMMON: HUMAN;                                              
SOURCE  56 ORGANISM_TAXID: 9606;                                                
SOURCE  57 MOL_ID: 15;                                                          
SOURCE  58 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  59 ORGANISM_COMMON: HUMAN;                                              
SOURCE  60 ORGANISM_TAXID: 9606;                                                
SOURCE  61 MOL_ID: 16;                                                          
SOURCE  62 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  63 ORGANISM_COMMON: HUMAN;                                              
SOURCE  64 ORGANISM_TAXID: 9606;                                                
SOURCE  65 MOL_ID: 17;                                                          
SOURCE  66 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  67 ORGANISM_COMMON: HUMAN;                                              
SOURCE  68 ORGANISM_TAXID: 9606;                                                
SOURCE  69 MOL_ID: 18;                                                          
SOURCE  70 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  71 ORGANISM_COMMON: HUMAN;                                              
SOURCE  72 ORGANISM_TAXID: 9606;                                                
SOURCE  73 MOL_ID: 19;                                                          
SOURCE  74 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  75 ORGANISM_COMMON: HUMAN;                                              
SOURCE  76 ORGANISM_TAXID: 9606;                                                
SOURCE  77 MOL_ID: 20;                                                          
SOURCE  78 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  79 ORGANISM_COMMON: HUMAN;                                              
SOURCE  80 ORGANISM_TAXID: 9606;                                                
SOURCE  81 MOL_ID: 21;                                                          
SOURCE  82 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  83 ORGANISM_COMMON: HUMAN;                                              
SOURCE  84 ORGANISM_TAXID: 9606;                                                
SOURCE  85 MOL_ID: 22;                                                          
SOURCE  86 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  87 ORGANISM_COMMON: HUMAN;                                              
SOURCE  88 ORGANISM_TAXID: 9606;                                                
SOURCE  89 MOL_ID: 23;                                                          
SOURCE  90 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  91 ORGANISM_COMMON: HUMAN;                                              
SOURCE  92 ORGANISM_TAXID: 9606;                                                
SOURCE  93 MOL_ID: 24;                                                          
SOURCE  94 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  95 ORGANISM_COMMON: HUMAN;                                              
SOURCE  96 ORGANISM_TAXID: 9606;                                                
SOURCE  97 MOL_ID: 25;                                                          
SOURCE  98 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  99 ORGANISM_COMMON: HUMAN;                                              
SOURCE 100 ORGANISM_TAXID: 9606;                                                
SOURCE 101 MOL_ID: 26;                                                          
SOURCE 102 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 103 ORGANISM_COMMON: HUMAN;                                              
SOURCE 104 ORGANISM_TAXID: 9606;                                                
SOURCE 105 MOL_ID: 27;                                                          
SOURCE 106 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 107 ORGANISM_COMMON: HUMAN;                                              
SOURCE 108 ORGANISM_TAXID: 9606;                                                
SOURCE 109 MOL_ID: 28;                                                          
SOURCE 110 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 111 ORGANISM_COMMON: HUMAN;                                              
SOURCE 112 ORGANISM_TAXID: 9606;                                                
SOURCE 113 MOL_ID: 29;                                                          
SOURCE 114 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 115 ORGANISM_COMMON: HUMAN;                                              
SOURCE 116 ORGANISM_TAXID: 9606;                                                
SOURCE 117 MOL_ID: 30;                                                          
SOURCE 118 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 119 ORGANISM_COMMON: HUMAN;                                              
SOURCE 120 ORGANISM_TAXID: 9606;                                                
SOURCE 121 MOL_ID: 31;                                                          
SOURCE 122 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 123 ORGANISM_COMMON: HUMAN;                                              
SOURCE 124 ORGANISM_TAXID: 9606;                                                
SOURCE 125 MOL_ID: 32;                                                          
SOURCE 126 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 127 ORGANISM_COMMON: HUMAN;                                              
SOURCE 128 ORGANISM_TAXID: 9606;                                                
SOURCE 129 MOL_ID: 33;                                                          
SOURCE 130 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 131 ORGANISM_COMMON: HUMAN;                                              
SOURCE 132 ORGANISM_TAXID: 9606;                                                
SOURCE 133 MOL_ID: 34;                                                          
SOURCE 134 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 135 ORGANISM_COMMON: HUMAN;                                              
SOURCE 136 ORGANISM_TAXID: 9606;                                                
SOURCE 137 MOL_ID: 35;                                                          
SOURCE 138 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 139 ORGANISM_COMMON: HUMAN;                                              
SOURCE 140 ORGANISM_TAXID: 9606;                                                
SOURCE 141 MOL_ID: 36;                                                          
SOURCE 142 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 143 ORGANISM_COMMON: HUMAN;                                              
SOURCE 144 ORGANISM_TAXID: 9606;                                                
SOURCE 145 MOL_ID: 37;                                                          
SOURCE 146 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 147 ORGANISM_COMMON: HUMAN;                                              
SOURCE 148 ORGANISM_TAXID: 9606;                                                
SOURCE 149 MOL_ID: 38;                                                          
SOURCE 150 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 151 ORGANISM_COMMON: HUMAN;                                              
SOURCE 152 ORGANISM_TAXID: 9606;                                                
SOURCE 153 MOL_ID: 39;                                                          
SOURCE 154 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 155 ORGANISM_COMMON: HUMAN;                                              
SOURCE 156 ORGANISM_TAXID: 9606;                                                
SOURCE 157 MOL_ID: 40;                                                          
SOURCE 158 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 159 ORGANISM_COMMON: HUMAN;                                              
SOURCE 160 ORGANISM_TAXID: 9606;                                                
SOURCE 161 MOL_ID: 41;                                                          
SOURCE 162 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 163 ORGANISM_COMMON: HUMAN;                                              
SOURCE 164 ORGANISM_TAXID: 9606;                                                
SOURCE 165 MOL_ID: 42;                                                          
SOURCE 166 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 167 ORGANISM_COMMON: HUMAN;                                              
SOURCE 168 ORGANISM_TAXID: 9606;                                                
SOURCE 169 MOL_ID: 43;                                                          
SOURCE 170 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 171 ORGANISM_COMMON: HUMAN;                                              
SOURCE 172 ORGANISM_TAXID: 9606;                                                
SOURCE 173 MOL_ID: 44;                                                          
SOURCE 174 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE 175 ORGANISM_COMMON: HUMAN;                                              
SOURCE 176 ORGANISM_TAXID: 9606                                                 
KEYWDS    HOMO SAPIENS, OXIDOREDUCTASE, RESPIRATORY, OXIDOREDUCTASE-ELECTRON    
KEYWDS   2 TRANSPORT COMPLEX                                                    
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    J.GU,M.WU,M.YANG                                                      
REVDAT   3   06-DEC-17 5XTD    1       JRNL   REMARK                            
REVDAT   2   06-SEP-17 5XTD    1       JRNL                                     
REVDAT   1   30-AUG-17 5XTD    0                                                
JRNL        AUTH   R.GUO,S.ZONG,M.WU,J.GU,M.YANG                                
JRNL        TITL   ARCHITECTURE OF HUMAN MITOCHONDRIAL RESPIRATORY MEGACOMPLEX  
JRNL        TITL 2 I2III2IV2.                                                   
JRNL        REF    CELL                          V. 170  1247 2017              
JRNL        REFN                   ISSN 1097-4172                               
JRNL        PMID   28844695                                                     
JRNL        DOI    10.1016/J.CELL.2017.07.050                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : EMAN, AUTOEMATION, CTFFIND, COOT,         
REMARK   3                            RELION, RELION, RELION, PHENIX            
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)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 3.700                          
REMARK   3   NUMBER OF PARTICLES               : 167761                         
REMARK   3   CTF CORRECTION METHOD             : NONE                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 5XTD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-JUL-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300004147.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : NULL                              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : HUMAN RESPIRATORY COMPLEX I       
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.40                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : FEI FALCON II (4K X 4K)        
REMARK 245   MINIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MAXIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : NULL                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 1.25                           
REMARK 245   ILLUMINATION MODE                 : OTHER                          
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 45-MERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, E, F, G, H, I, J, K,         
REMARK 350                    AND CHAINS: L, M, N, O, P, Q, S, T, U,            
REMARK 350                    AND CHAINS: V, W, X, Y, Z, a, b, c, d, e,         
REMARK 350                    AND CHAINS: f, g, h, i, j, k, l, m, n,            
REMARK 350                    AND CHAINS: o, p, r, s, u, v, w                   
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA I    75                                                      
REMARK 465     LEU I    76                                                      
REMARK 465     VAL I    77                                                      
REMARK 465     SER I    78                                                      
REMARK 465     GLY I    79                                                      
REMARK 465     LYS I    80                                                      
REMARK 465     PRO I    81                                                      
REMARK 465     ALA I    82                                                      
REMARK 465     GLU I    83                                                      
REMARK 465     SER I    84                                                      
REMARK 465     SER I    85                                                      
REMARK 465     ALA I    86                                                      
REMARK 465     VAL I    87                                                      
REMARK 465     ALA I    88                                                      
REMARK 465     ALA I    89                                                      
REMARK 465     MET b     1                                                      
REMARK 465     THR b     2                                                      
REMARK 465     HIS b   127                                                      
REMARK 465     HIS b   128                                                      
REMARK 465     MET v     1                                                      
REMARK 465     GLY v     2                                                      
REMARK 465     THR v    24                                                      
REMARK 465     PHE v    25                                                      
REMARK 465     PRO v    26                                                      
REMARK 465     PRO v    27                                                      
REMARK 465     ASP v    28                                                      
REMARK 465     TYR v    29                                                      
REMARK 465     GLY v    30                                                      
REMARK 465     PHE v    31                                                      
REMARK 465     PRO v    32                                                      
REMARK 465     GLU v    33                                                      
REMARK 465     ARG v    34                                                      
REMARK 465     GLY v   125                                                      
REMARK 465     GLN v   126                                                      
REMARK 465     GLY v   127                                                      
REMARK 465     PRO v   128                                                      
REMARK 465     GLY v   129                                                      
REMARK 465     GLU v   130                                                      
REMARK 465     VAL v   131                                                      
REMARK 465     ASP v   132                                                      
REMARK 465     PRO v   133                                                      
REMARK 465     LYS v   134                                                      
REMARK 465     VAL v   135                                                      
REMARK 465     ALA v   136                                                      
REMARK 465     LEU v   137                                                      
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     SER G 112    CB   OG                                             
REMARK 470     ASP G 150    CG   OD1  OD2                                       
REMARK 470     LYS G 151    CG   CD   CE   NZ                                   
REMARK 470     LYS G 152    CG   CD   CE   NZ                                   
REMARK 470     ASP G 153    CG   OD1  OD2                                       
REMARK 470     CYS M 131    SG                                                  
REMARK 470     SER X 112    CB   OG                                             
REMARK 470     TRP Z  51    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP Z  51    CZ3  CH2                                            
REMARK 470     LYS c 159    CG   CD   CE   NZ                                   
REMARK 470     GLN c 160    CG   CD   OE1  NE2                                  
REMARK 470     LYS c 176    CG   CD   CE   NZ                                   
REMARK 470     GLU c 177    CG   CD   OE1  OE2                                  
REMARK 470     PRO c 178    CG   CD                                             
REMARK 470     GLU c 179    CG   CD   OE1  OE2                                  
REMARK 470     ARG c 180    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL c 181    CG1  CG2                                            
REMARK 470     VAL c 182    CG1  CG2                                            
REMARK 470     HIS c 183    CG   ND1  CD2  CE1  NE2                             
REMARK 470     TYR c 184    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU c 185    CG   CD   OE1  OE2                                  
REMARK 470     ILE c 186    CG1  CG2  CD1                                       
REMARK 470     MET d   1    CG   SD   CE                                        
REMARK 470     PRO d   2    CG   CD                                             
REMARK 470     ASP d   3    CG   OD1  OD2                                       
REMARK 470     SER d   4    OG                                                  
REMARK 470     TRP d   5    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP d   5    CZ3  CH2                                            
REMARK 470     ASP d   6    CG   OD1  OD2                                       
REMARK 470     LYS d   7    CG   CD   CE   NZ                                   
REMARK 470     ASP d   8    CG   OD1  OD2                                       
REMARK 470     THR d 171    OG1  CG2                                            
REMARK 470     GLU j 115    CG   CD   OE1  OE2                                  
REMARK 470     THR l 573    OG1  CG2                                            
REMARK 470     LEU v  10    CG   CD1  CD2                                       
REMARK 470     ASP v  12    CG   OD1  OD2                                       
REMARK 470     SER v  14    OG                                                  
REMARK 470     VAL v  15    CG1  CG2                                            
REMARK 470     GLU v  16    CG   CD   OE1  OE2                                  
REMARK 470     PRO v  17    CG   CD                                             
REMARK 470     ASP v  18    CG   OD1  OD2                                       
REMARK 470     PRO v  19    CG   CD                                             
REMARK 470     LEU v  20    CG   CD1  CD2                                       
REMARK 470     GLN v  21    CG   CD   OE1  NE2                                  
REMARK 470     MET v  22    CG   SD   CE                                        
REMARK 470     PRO v  23    CG   CD                                             
REMARK 470     LEU w  36    CG   CD1  CD2                                       
REMARK 470     ARG w  37    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET w  40    CG   SD   CE                                        
REMARK 470     TRP w  41    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP w  41    CZ3  CH2                                            
REMARK 470     LEU w  44    CG   CD1  CD2                                       
REMARK 470     LEU w  45    CG   CD1  CD2                                       
REMARK 470     ASP w  47    CG   OD1  OD2                                       
REMARK 470     LYS w  48    CG   CD   CE   NZ                                   
REMARK 470     ARG w 261    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU w 262    CG   CD   OE1  OE2                                  
REMARK 470     GLN w 264    CG   CD   OE1  NE2                                  
REMARK 470     ASP w 265    CG   OD1  OD2                                       
REMARK 470     SER w 266    OG                                                  
REMARK 470     LYS w 267    CG   CD   CE   NZ                                   
REMARK 470     LYS w 268    CG   CD   CE   NZ                                   
REMARK 470     VAL w 269    CG1  CG2                                            
REMARK 470     VAL w 270    CG1  CG2                                            
REMARK 470     GLU w 271    CG   CD   OE1  OE2                                  
REMARK 470     ASP w 272    CG   OD1  OD2                                       
REMARK 470     ILE w 273    CG1  CG2  CD1                                       
REMARK 470     GLU w 274    CG   CD   OE1  OE2                                  
REMARK 470     TYR w 275    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU w 276    CG   CD1  CD2                                       
REMARK 470     LYS w 277    CG   CD   CE   NZ                                   
REMARK 470     PHE w 278    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP w 279    CG   OD1  OD2                                       
REMARK 470     LYS w 280    CG   CD   CE   NZ                                   
REMARK 470     PRO w 282    CG   CD                                             
REMARK 470     TRP w 283    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP w 283    CZ3  CH2                                            
REMARK 470     LEU w 284    CG   CD1  CD2                                       
REMARK 470     LYS w 285    CG   CD   CE   NZ                                   
REMARK 470     GLN w 286    CG   CD   OE1  NE2                                  
REMARK 470     THR w 345    OG1  CG2                                            
REMARK 470     GLU w 346    CG   CD   OE1  OE2                                  
REMARK 470     VAL w 347    CG1  CG2                                            
REMARK 470     ASP w 349    CG   OD1  OD2                                       
REMARK 470     LYS w 350    CG   CD   CE   NZ                                   
REMARK 470     LEU w 354    CG   CD1  CD2                                       
REMARK 470     LYS w 355    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD2  ASP b   108     CG1  VAL d    19              1.05            
REMARK 500   SG   CYS M   176    FE4   SF4 M   802              1.38            
REMARK 500   SG   CYS M   176     S2   SF4 M   802              1.54            
REMARK 500   O    ILE J   206     OD2  ASP J   211              1.61            
REMARK 500   CD1  ILE l   571     O5   PEE l   701              1.64            
REMARK 500   NH1  ARG Y    72     OH   TYR l   390              1.76            
REMARK 500   CE2  PHE a    55     CE2  TYR p   118              1.82            
REMARK 500   O    LEU l   227     ND1  HIS l   230              1.88            
REMARK 500   OE2  GLU Y    96     O    GLU c   185              1.89            
REMARK 500   NZ   LYS d   105     OD2  ASP l   197              1.91            
REMARK 500   CE2  PHE a    55     CD2  TYR p   118              1.91            
REMARK 500   O    ASN J   171     CD2  LEU J   181              1.92            
REMARK 500   OD1  ASN E    70     O4   8Q1 E   201              1.95            
REMARK 500   OG   SER l   193     ND2  ASN l   205              1.95            
REMARK 500   N    GLY b   107     OE1  GLU b   115              1.96            
REMARK 500   OE2  GLU C   204     NH1  ARG C   206              1.98            
REMARK 500   OG1  THR c   122     NH1  ARG o    12              1.99            
REMARK 500   O    ASP Q    70     OD1  ASP Q    74              2.00            
REMARK 500   OD2  ASP Q   140     OG   SER Q   143              2.02            
REMARK 500   OE1  GLU C   143     OH   TYR J    89              2.03            
REMARK 500   CE   LYS d   105     OD2  ASP l   197              2.04            
REMARK 500   CG   ASP b   108     CG1  VAL d    19              2.04            
REMARK 500   NH1  ARG H    45     OE2  GLU H    49              2.04            
REMARK 500   CE1  TYR l    84     CE   MET l    88              2.05            
REMARK 500   O    MET r    78     NH1  ARG r   432              2.05            
REMARK 500   OE2  GLU c   169     NH2  ARG v    56              2.05            
REMARK 500   CA   SER X   112     O2   8Q1 p   201              2.06            
REMARK 500   O    LEU Q    82     CG1  VAL Q    98              2.06            
REMARK 500   CE1  PHE l    54     OD1  ASP l    58              2.06            
REMARK 500   OG   SER P   134     OG   SER P   139              2.07            
REMARK 500   O    ILE Q   450     OG1  THR Q   453              2.07            
REMARK 500   CZ   PHE l    54     OD1  ASP l    58              2.07            
REMARK 500   O    TYR i   298     OG1  THR i   303              2.08            
REMARK 500   O    ALA i   180     OG   SER i   183              2.08            
REMARK 500   O    THR B    81     NH2  ARG N    58              2.09            
REMARK 500   N    ASN A   244     O2P  FMN A   502              2.09            
REMARK 500   OH   TYR o    23     OE1  GLU p    68              2.09            
REMARK 500   OE2  GLU d   111     N    CYS d   119              2.09            
REMARK 500   O    LEU s   265     OG   SER s   268              2.10            
REMARK 500   O    ASN E    70     O40  8Q1 E   201              2.10            
REMARK 500   O    ASN r   144     OG1  THR r   147              2.10            
REMARK 500   OE2  GLU i    54     NZ   LYS i    58              2.10            
REMARK 500   O    PRO V    84     ND2  ASN V    89              2.10            
REMARK 500   O    ASP M   194     OG1  THR M   208              2.10            
REMARK 500   OG   SER X    99     OG   SER X   102              2.11            
REMARK 500   O    ARG Q   294     N    GLY Q   321              2.11            
REMARK 500   OH   TYR c   163     O    THR v    42              2.11            
REMARK 500   OD2  ASP w    63     OH   TYR w   241              2.11            
REMARK 500   OD1  ASP O    54     OH   TYR O    60              2.11            
REMARK 500   OE1  GLU a   143     ND2  ASN r   175              2.11            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     113 CLOSE CONTACTS                                
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    PRO E  19   C   -  N   -  CA  ANGL. DEV. =   9.9 DEGREES          
REMARK 500    PRO I  39   C   -  N   -  CA  ANGL. DEV. =  11.4 DEGREES          
REMARK 500    PRO Q 366   C   -  N   -  CA  ANGL. DEV. =  10.6 DEGREES          
REMARK 500    PRO W  11   C   -  N   -  CA  ANGL. DEV. = -10.1 DEGREES          
REMARK 500    PRO Y  87   C   -  N   -  CD  ANGL. DEV. =  18.6 DEGREES          
REMARK 500    PRO Y  87   CA  -  N   -  CD  ANGL. DEV. =  -9.2 DEGREES          
REMARK 500    TRP Y  92   N   -  CA  -  C   ANGL. DEV. = -18.9 DEGREES          
REMARK 500    PRO b  37   C   -  N   -  CD  ANGL. DEV. =  13.1 DEGREES          
REMARK 500    PRO d   2   N   -  CA  -  CB  ANGL. DEV. =   8.1 DEGREES          
REMARK 500    PRO i 324   C   -  N   -  CA  ANGL. DEV. =  20.4 DEGREES          
REMARK 500    PRO i 324   C   -  N   -  CD  ANGL. DEV. = -16.2 DEGREES          
REMARK 500    PRO s  90   C   -  N   -  CA  ANGL. DEV. =   9.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  35      117.00   -173.06                                   
REMARK 500    ASP A  50      106.26     63.05                                   
REMARK 500    TYR A  63     -101.66     13.26                                   
REMARK 500    PRO A  73     -100.53    -59.16                                   
REMARK 500    ASP A  74      -88.48     52.20                                   
REMARK 500    PRO A  94      103.64    -50.67                                   
REMARK 500    MET A 102       41.93   -105.19                                   
REMARK 500    ASP A 134       57.04   -159.39                                   
REMARK 500    ILE A 182     -155.66   -117.30                                   
REMARK 500    ASN A 185      -39.19     62.51                                   
REMARK 500    ALA A 186      100.29     60.69                                   
REMARK 500    SER A 189      -28.40     71.57                                   
REMARK 500    ARG A 256      -79.47   -103.16                                   
REMARK 500    ASN A 270       48.16   -100.79                                   
REMARK 500    HIS A 281       97.83    -63.71                                   
REMARK 500    LYS A 302      -84.43   -117.67                                   
REMARK 500    SER A 323      -46.67   -133.68                                   
REMARK 500    ALA A 352       29.00     49.59                                   
REMARK 500    SER A 378       17.99   -159.07                                   
REMARK 500    CYS A 379      -84.62     36.28                                   
REMARK 500    GLN A 381      -76.80    -79.60                                   
REMARK 500    GLU A 420      -75.33    -55.58                                   
REMARK 500    ASN B  40     -115.83     54.35                                   
REMARK 500    MET B  41      -32.47     62.14                                   
REMARK 500    LEU B  59      -72.10    -99.17                                   
REMARK 500    TRP B  61      -34.52     72.97                                   
REMARK 500    THR B  62      -81.79     40.50                                   
REMARK 500    CYS B 121      103.55    -39.09                                   
REMARK 500    ALA B 164      -78.68    -73.41                                   
REMARK 500    PHE B 171      -30.55   -139.28                                   
REMARK 500    PHE B 173       40.24   -163.61                                   
REMARK 500    SER C  78       68.27   -157.56                                   
REMARK 500    PHE C  84       13.37   -173.25                                   
REMARK 500    ALA C  87     -149.74   -163.71                                   
REMARK 500    TYR C 101      -61.45   -108.91                                   
REMARK 500    ASP C 102       93.84     62.14                                   
REMARK 500    SER C 113      151.58     71.71                                   
REMARK 500    ARG C 115      -54.11   -126.09                                   
REMARK 500    ASP C 118      -74.39   -109.22                                   
REMARK 500    SER C 165      -83.05    -57.92                                   
REMARK 500    VAL C 167       58.48   -100.87                                   
REMARK 500    ARG C 168     -126.22     40.98                                   
REMARK 500    ILE E  20      -81.58    -56.31                                   
REMARK 500    PHE E  21      -71.73   -121.99                                   
REMARK 500    ASP E  24      160.20     67.15                                   
REMARK 500    THR E  74      -24.00   -140.03                                   
REMARK 500    TRP E  97     -158.64    -85.46                                   
REMARK 500    LYS E  98     -161.07     54.72                                   
REMARK 500    VAL E 124      -70.79    -72.03                                   
REMARK 500    ASP E 127     -167.90     57.84                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     556 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 LYS w  338     TYR w  339                 -142.74                    
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     CDL V  201                                                       
REMARK 610     CDL i  401                                                       
REMARK 610     PEE l  701                                                       
REMARK 610     CDL l  703                                                       
REMARK 610     CDL l  704                                                       
REMARK 610     CDL n  101                                                       
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                             SF4 A 501  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 381   NE2                                                    
REMARK 620 2 SF4 A 501   S2  112.5                                              
REMARK 620 3 SF4 A 501   S3   67.7  89.9                                        
REMARK 620 4 SF4 A 501   S4  147.0  90.0  89.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 301  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 114   N                                                      
REMARK 620 2 SF4 B 301   S1  116.1                                              
REMARK 620 3 SF4 B 301   S3   90.0  90.5                                        
REMARK 620 4 SF4 B 301   S4  154.8  89.1  90.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 B 302  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY B 154   N                                                      
REMARK 620 2 SF4 B 302   S1  103.0                                              
REMARK 620 3 SF4 B 302   S2   96.5  89.4                                        
REMARK 620 4 SF4 B 302   S3  164.1  91.5  90.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C 301  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  89   SG                                                     
REMARK 620 2 SF4 C 301   S1   86.5                                              
REMARK 620 3 SF4 C 301   S3   86.3  88.7                                        
REMARK 620 4 SF4 C 301   S4  176.4  90.6  91.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 M 801  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS M 124   NE2                                                    
REMARK 620 2 SF4 M 801   S1  117.5                                              
REMARK 620 3 SF4 M 801   S2  141.1  89.7                                        
REMARK 620 4 SF4 M 801   S4  113.7  91.8  90.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 M 801  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS M 137   SG                                                     
REMARK 620 2 SF4 M 801   S1  121.8                                              
REMARK 620 3 SF4 M 801   S2  101.5  89.7                                        
REMARK 620 4 SF4 M 801   S3  148.1  87.8  89.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 M 802  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS M 176   SG                                                     
REMARK 620 2 SF4 M 802   S2   40.8                                              
REMARK 620 3 SF4 M 802   S3   58.0  90.1                                        
REMARK 620 4 SF4 M 802   S4  112.2  89.6  90.2                                  
REMARK 620 5 CYS M 179   O   121.1  88.5 178.5  89.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FES O 301  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS O 176   SG                                                     
REMARK 620 2 FES O 301   S1  102.4                                              
REMARK 620 3 FES O 301   S2   81.2  90.5                                        
REMARK 620 4 CYS O 180   SG   81.2 162.8  73.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FMN A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PLX B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8Q1 E 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NDP J 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 M 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SF4 M 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FES M 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FES O 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PLX U 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CDL V 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEE V 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PLX V 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEE W 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PLX b 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PLX g 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PLX g 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PLX g 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CDL i 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEE l 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEE l 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CDL l 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CDL l 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CDL n 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8Q1 p 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PLX r 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PLX r 502                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-6773   RELATED DB: EMDB                              
DBREF  5XTD A   27   457  UNP    P49821   NDUV1_HUMAN     27    457             
DBREF  5XTD B   35   210  UNP    O00217   NDUS8_HUMAN     35    210             
DBREF  5XTD C   58   213  UNP    O75251   NDUS7_HUMAN     58    213             
DBREF  5XTD E   16   128  UNP    P56556   NDUA6_HUMAN     42    154             
DBREF  5XTD F   14    96  UNP    O43678   NDUA2_HUMAN     14     96             
DBREF  5XTD G   72   156  UNP    O14561   ACPM_HUMAN      72    156             
DBREF  5XTD H    5   116  UNP    Q16718   NDUA5_HUMAN      5    116             
DBREF  5XTD I    4   113  UNP    O95182   NDUA7_HUMAN      4    113             
DBREF  5XTD J   40   376  UNP    Q16795   NDUA9_HUMAN     40    376             
DBREF  5XTD K   74   106  UNP    P56181   NDUV3_HUMAN     74    106             
DBREF  5XTD L   58   175  UNP    O43181   NDUS4_HUMAN     58    175             
DBREF  5XTD M   30   716  UNP    P28331   NDUS1_HUMAN     30    716             
DBREF  5XTD N    2   144  UNP    Q9UI09   NDUAC_HUMAN      2    144             
DBREF  5XTD O   36   247  UNP    P19404   NDUV2_HUMAN     36    247             
DBREF  5XTD P   43   250  UNP    O75489   NDUS3_HUMAN     43    250             
DBREF  5XTD Q   34   430  UNP    O75306   NDUS2_HUMAN     34    463             
DBREF  5XTD S    1    70  UNP    O15239   NDUA1_HUMAN      1     70             
DBREF  5XTD T   29   123  UNP    O75380   NDUS6_HUMAN     29    123             
DBREF  5XTD U    2    84  UNP    O95167   NDUA3_HUMAN      2     84             
DBREF  5XTD V    2   141  UNP    Q86Y39   NDUAB_HUMAN      2    141             
DBREF  5XTD W    7   144  UNP    Q9P0J0   NDUAD_HUMAN      7    144             
DBREF  5XTD X   72   156  UNP    O14561   ACPM_HUMAN      72    156             
DBREF  5XTD Y   39    97  UNP    O95178   NDUB2_HUMAN     39     97             
DBREF  5XTD Z   10    89  UNP    O43676   NDUB3_HUMAN     10     89             
DBREF  5XTD a   52   189  UNP    O43674   NDUB5_HUMAN     52    189             
DBREF  5XTD b    1   128  UNP    O95139   NDUB6_HUMAN      1    128             
DBREF  5XTD c   34   186  UNP    O95169   NDUB8_HUMAN     34    186             
DBREF  5XTD d    1   171  UNP    O96000   NDUBA_HUMAN      1    171             
DBREF  5XTD e   54   150  UNP    Q9NX14   NDUBB_HUMAN     54    150             
DBREF  5XTD f   28    74  UNP    O43677   NDUC1_HUMAN     28     74             
DBREF  5XTD g    1   119  UNP    O95298   NDUC2_HUMAN      1    119             
DBREF  5XTD h    2   105  UNP    O43920   NDUS5_HUMAN      2    105             
DBREF  5XTD i    1   347  UNP    Q4GRX1   Q4GRX1_HUMAN     1    347             
DBREF  5XTD j    1   115  UNP    B9EE38   B9EE38_HUMAN     1    115             
DBREF  5XTD k    1    97  UNP    V9JN72   V9JN72_HUMAN     1     97             
DBREF  5XTD l    1   603  UNP    X5BVZ3   X5BVZ3_HUMAN     1    603             
DBREF  5XTD m    1   174  UNP    Q8HAX7   Q8HAX7_HUMAN     1    174             
DBREF  5XTD n    3    58  UNP    O75438   NDUB1_HUMAN      3     58             
DBREF  5XTD o    2   129  UNP    O95168   NDUB4_HUMAN      2    129             
DBREF  5XTD p    8   179  UNP    Q9Y6M9   NDUB9_HUMAN      8    179             
DBREF  5XTD r    1   459  UNP    B2XJG5   B2XJG5_HUMAN     1    459             
DBREF  5XTD s    1   318  UNP    H9PGF0   H9PGF0_HUMAN     1    318             
DBREF  5XTD u    4   172  UNP    P51970   NDUA8_HUMAN      4    172             
DBREF  5XTD v    1   137  UNP    P17568   NDUB7_HUMAN      1    137             
DBREF  5XTD w   36   355  UNP    O95299   NDUAA_HUMAN     36    355             
SEQRES   1 A  431  PRO LYS LYS THR SER PHE GLY SER LEU LYS ASP GLU ASP          
SEQRES   2 A  431  ARG ILE PHE THR ASN LEU TYR GLY ARG HIS ASP TRP ARG          
SEQRES   3 A  431  LEU LYS GLY SER LEU SER ARG GLY ASP TRP TYR LYS THR          
SEQRES   4 A  431  LYS GLU ILE LEU LEU LYS GLY PRO ASP TRP ILE LEU GLY          
SEQRES   5 A  431  GLU ILE LYS THR SER GLY LEU ARG GLY ARG GLY GLY ALA          
SEQRES   6 A  431  GLY PHE PRO THR GLY LEU LYS TRP SER PHE MET ASN LYS          
SEQRES   7 A  431  PRO SER ASP GLY ARG PRO LYS TYR LEU VAL VAL ASN ALA          
SEQRES   8 A  431  ASP GLU GLY GLU PRO GLY THR CYS LYS ASP ARG GLU ILE          
SEQRES   9 A  431  LEU ARG HIS ASP PRO HIS LYS LEU LEU GLU GLY CYS LEU          
SEQRES  10 A  431  VAL GLY GLY ARG ALA MET GLY ALA ARG ALA ALA TYR ILE          
SEQRES  11 A  431  TYR ILE ARG GLY GLU PHE TYR ASN GLU ALA SER ASN LEU          
SEQRES  12 A  431  GLN VAL ALA ILE ARG GLU ALA TYR GLU ALA GLY LEU ILE          
SEQRES  13 A  431  GLY LYS ASN ALA CYS GLY SER GLY TYR ASP PHE ASP VAL          
SEQRES  14 A  431  PHE VAL VAL ARG GLY ALA GLY ALA TYR ILE CYS GLY GLU          
SEQRES  15 A  431  GLU THR ALA LEU ILE GLU SER ILE GLU GLY LYS GLN GLY          
SEQRES  16 A  431  LYS PRO ARG LEU LYS PRO PRO PHE PRO ALA ASP VAL GLY          
SEQRES  17 A  431  VAL PHE GLY CYS PRO THR THR VAL ALA ASN VAL GLU THR          
SEQRES  18 A  431  VAL ALA VAL SER PRO THR ILE CYS ARG ARG GLY GLY THR          
SEQRES  19 A  431  TRP PHE ALA GLY PHE GLY ARG GLU ARG ASN SER GLY THR          
SEQRES  20 A  431  LYS LEU PHE ASN ILE SER GLY HIS VAL ASN HIS PRO CYS          
SEQRES  21 A  431  THR VAL GLU GLU GLU MET SER VAL PRO LEU LYS GLU LEU          
SEQRES  22 A  431  ILE GLU LYS HIS ALA GLY GLY VAL THR GLY GLY TRP ASP          
SEQRES  23 A  431  ASN LEU LEU ALA VAL ILE PRO GLY GLY SER SER THR PRO          
SEQRES  24 A  431  LEU ILE PRO LYS SER VAL CYS GLU THR VAL LEU MET ASP          
SEQRES  25 A  431  PHE ASP ALA LEU VAL GLN ALA GLN THR GLY LEU GLY THR          
SEQRES  26 A  431  ALA ALA VAL ILE VAL MET ASP ARG SER THR ASP ILE VAL          
SEQRES  27 A  431  LYS ALA ILE ALA ARG LEU ILE GLU PHE TYR LYS HIS GLU          
SEQRES  28 A  431  SER CYS GLY GLN CYS THR PRO CYS ARG GLU GLY VAL ASP          
SEQRES  29 A  431  TRP MET ASN LYS VAL MET ALA ARG PHE VAL ARG GLY ASP          
SEQRES  30 A  431  ALA ARG PRO ALA GLU ILE ASP SER LEU TRP GLU ILE SER          
SEQRES  31 A  431  LYS GLN ILE GLU GLY HIS THR ILE CYS ALA LEU GLY ASP          
SEQRES  32 A  431  GLY ALA ALA TRP PRO VAL GLN GLY LEU ILE ARG HIS PHE          
SEQRES  33 A  431  ARG PRO GLU LEU GLU GLU ARG MET GLN ARG PHE ALA GLN          
SEQRES  34 A  431  GLN HIS                                                      
SEQRES   1 B  176  THR TYR LYS TYR VAL ASN MET GLN ASP PRO GLU MET ASP          
SEQRES   2 B  176  MET LYS SER VAL THR ASP ARG ALA ALA ARG THR LEU LEU          
SEQRES   3 B  176  TRP THR GLU LEU PHE ARG GLY LEU GLY MET THR LEU SER          
SEQRES   4 B  176  TYR LEU PHE ARG GLU PRO ALA THR ILE ASN TYR PRO PHE          
SEQRES   5 B  176  GLU LYS GLY PRO LEU SER PRO ARG PHE ARG GLY GLU HIS          
SEQRES   6 B  176  ALA LEU ARG ARG TYR PRO SER GLY GLU GLU ARG CYS ILE          
SEQRES   7 B  176  ALA CYS LYS LEU CYS GLU ALA ILE CYS PRO ALA GLN ALA          
SEQRES   8 B  176  ILE THR ILE GLU ALA GLU PRO ARG ALA ASP GLY SER ARG          
SEQRES   9 B  176  ARG THR THR ARG TYR ASP ILE ASP MET THR LYS CYS ILE          
SEQRES  10 B  176  TYR CYS GLY PHE CYS GLN GLU ALA CYS PRO VAL ASP ALA          
SEQRES  11 B  176  ILE VAL GLU GLY PRO ASN PHE GLU PHE SER THR GLU THR          
SEQRES  12 B  176  HIS GLU GLU LEU LEU TYR ASN LYS GLU LYS LEU LEU ASN          
SEQRES  13 B  176  ASN GLY ASP LYS TRP GLU ALA GLU ILE ALA ALA ASN ILE          
SEQRES  14 B  176  GLN ALA ASP TYR LEU TYR ARG                                  
SEQRES   1 C  156  SER ARG GLY GLU TYR VAL VAL ALA LYS LEU ASP ASP LEU          
SEQRES   2 C  156  VAL ASN TRP ALA ARG ARG SER SER LEU TRP PRO MET THR          
SEQRES   3 C  156  PHE GLY LEU ALA CYS CYS ALA VAL GLU MET MET HIS MET          
SEQRES   4 C  156  ALA ALA PRO ARG TYR ASP MET ASP ARG PHE GLY VAL VAL          
SEQRES   5 C  156  PHE ARG ALA SER PRO ARG GLN SER ASP VAL MET ILE VAL          
SEQRES   6 C  156  ALA GLY THR LEU THR ASN LYS MET ALA PRO ALA LEU ARG          
SEQRES   7 C  156  LYS VAL TYR ASP GLN MET PRO GLU PRO ARG TYR VAL VAL          
SEQRES   8 C  156  SER MET GLY SER CYS ALA ASN GLY GLY GLY TYR TYR HIS          
SEQRES   9 C  156  TYR SER TYR SER VAL VAL ARG GLY CYS ASP ARG ILE VAL          
SEQRES  10 C  156  PRO VAL ASP ILE TYR ILE PRO GLY CYS PRO PRO THR ALA          
SEQRES  11 C  156  GLU ALA LEU LEU TYR GLY ILE LEU GLN LEU GLN ARG LYS          
SEQRES  12 C  156  ILE LYS ARG GLU ARG ARG LEU GLN ILE TRP TYR ARG ARG          
SEQRES   1 E  113  PHE VAL LYS PRO ILE PHE SER ARG ASP MET ASN GLU ALA          
SEQRES   2 E  113  LYS ARG ARG VAL ARG GLU LEU TYR ARG ALA TRP TYR ARG          
SEQRES   3 E  113  GLU VAL PRO ASN THR VAL HIS GLN PHE GLN LEU ASP ILE          
SEQRES   4 E  113  THR VAL LYS MET GLY ARG ASP LYS VAL ARG GLU MET PHE          
SEQRES   5 E  113  MET LYS ASN ALA HIS VAL THR ASP PRO ARG VAL VAL ASP          
SEQRES   6 E  113  LEU LEU VAL ILE LYS GLY LYS ILE GLU LEU GLU GLU THR          
SEQRES   7 E  113  ILE LYS VAL TRP LYS GLN ARG THR HIS VAL MET ARG PHE          
SEQRES   8 E  113  PHE HIS GLU THR GLU ALA PRO ARG PRO LYS ASP PHE LEU          
SEQRES   9 E  113  SER LYS PHE TYR VAL GLY HIS ASP PRO                          
SEQRES   1 F   83  LEU GLY LEU ARG GLU ILE ARG ILE HIS LEU CYS GLN ARG          
SEQRES   2 F   83  SER PRO GLY SER GLN GLY VAL ARG ASP PHE ILE GLU LYS          
SEQRES   3 F   83  ARG TYR VAL GLU LEU LYS LYS ALA ASN PRO ASP LEU PRO          
SEQRES   4 F   83  ILE LEU ILE ARG GLU CYS SER ASP VAL GLN PRO LYS LEU          
SEQRES   5 F   83  TRP ALA ARG TYR ALA PHE GLY GLN GLU THR ASN VAL PRO          
SEQRES   6 F   83  LEU ASN ASN PHE SER ALA ASP GLN VAL THR ARG ALA LEU          
SEQRES   7 F   83  GLU ASN VAL LEU SER                                          
SEQRES   1 G   85  PRO PRO LEU THR LEU GLU GLY ILE GLN ASP ARG VAL LEU          
SEQRES   2 G   85  TYR VAL LEU LYS LEU TYR ASP LYS ILE ASP PRO GLU LYS          
SEQRES   3 G   85  LEU SER VAL ASN SER HIS PHE MET LYS ASP LEU GLY LEU          
SEQRES   4 G   85  ASP SER LEU ASP GLN VAL GLU ILE ILE MET ALA MET GLU          
SEQRES   5 G   85  ASP GLU PHE GLY PHE GLU ILE PRO ASP ILE ASP ALA GLU          
SEQRES   6 G   85  LYS LEU MET CYS PRO GLN GLU ILE VAL ASP TYR ILE ALA          
SEQRES   7 G   85  ASP LYS LYS ASP VAL TYR GLU                                  
SEQRES   1 H  112  LEU LYS LYS THR THR GLY LEU VAL GLY LEU ALA VAL CYS          
SEQRES   2 H  112  ASN THR PRO HIS GLU ARG LEU ARG ILE LEU TYR THR LYS          
SEQRES   3 H  112  ILE LEU ASP VAL LEU GLU GLU ILE PRO LYS ASN ALA ALA          
SEQRES   4 H  112  TYR ARG LYS TYR THR GLU GLN ILE THR ASN GLU LYS LEU          
SEQRES   5 H  112  ALA MET VAL LYS ALA GLU PRO ASP VAL LYS LYS LEU GLU          
SEQRES   6 H  112  ASP GLN LEU GLN GLY GLY GLN LEU GLU GLU VAL ILE LEU          
SEQRES   7 H  112  GLN ALA GLU HIS GLU LEU ASN LEU ALA ARG LYS MET ARG          
SEQRES   8 H  112  GLU TRP LYS LEU TRP GLU PRO LEU VAL GLU GLU PRO PRO          
SEQRES   9 H  112  ALA ASP GLN TRP LYS TRP PRO ILE                              
SEQRES   1 I  110  ALA THR ARG LEU ILE GLN ARG LEU ARG ASN TRP ALA SER          
SEQRES   2 I  110  GLY HIS ASP LEU GLN GLY LYS LEU GLN LEU ARG TYR GLN          
SEQRES   3 I  110  GLU ILE SER LYS ARG THR GLN PRO PRO PRO LYS LEU PRO          
SEQRES   4 I  110  VAL GLY PRO SER HIS LYS LEU SER ASN ASN TYR TYR CYS          
SEQRES   5 I  110  THR ARG ASP GLY ARG ARG GLU SER VAL PRO PRO SER ILE          
SEQRES   6 I  110  ILE MET SER SER GLN LYS ALA LEU VAL SER GLY LYS PRO          
SEQRES   7 I  110  ALA GLU SER SER ALA VAL ALA ALA THR GLU LYS LYS ALA          
SEQRES   8 I  110  VAL THR PRO ALA PRO PRO ILE LYS ARG TRP GLU LEU SER          
SEQRES   9 I  110  SER ASP GLN PRO TYR LEU                                      
SEQRES   1 J  337  LEU MET PRO HIS GLY LYS GLY GLY ARG SER SER VAL SER          
SEQRES   2 J  337  GLY ILE VAL ALA THR VAL PHE GLY ALA THR GLY PHE LEU          
SEQRES   3 J  337  GLY ARG TYR VAL VAL ASN HIS LEU GLY ARG MET GLY SER          
SEQRES   4 J  337  GLN VAL ILE ILE PRO TYR ARG CYS ASP LYS TYR ASP ILE          
SEQRES   5 J  337  MET HIS LEU ARG PRO MET GLY ASP LEU GLY GLN LEU LEU          
SEQRES   6 J  337  PHE LEU GLU TRP ASP ALA ARG ASP LYS ASP SER ILE ARG          
SEQRES   7 J  337  ARG VAL VAL GLN HIS SER ASN VAL VAL ILE ASN LEU ILE          
SEQRES   8 J  337  GLY ARG ASP TRP GLU THR LYS ASN PHE ASP PHE GLU ASP          
SEQRES   9 J  337  VAL PHE VAL LYS ILE PRO GLN ALA ILE ALA GLN LEU SER          
SEQRES  10 J  337  LYS GLU ALA GLY VAL GLU LYS PHE ILE HIS VAL SER HIS          
SEQRES  11 J  337  LEU ASN ALA ASN ILE LYS SER SER SER ARG TYR LEU ARG          
SEQRES  12 J  337  ASN LYS ALA VAL GLY GLU LYS VAL VAL ARG ASP ALA PHE          
SEQRES  13 J  337  PRO GLU ALA ILE ILE VAL LYS PRO SER ASP ILE PHE GLY          
SEQRES  14 J  337  ARG GLU ASP ARG PHE LEU ASN SER PHE ALA SER MET HIS          
SEQRES  15 J  337  ARG PHE GLY PRO ILE PRO LEU GLY SER LEU GLY TRP LYS          
SEQRES  16 J  337  THR VAL LYS GLN PRO VAL TYR VAL VAL ASP VAL SER LYS          
SEQRES  17 J  337  GLY ILE VAL ASN ALA VAL LYS ASP PRO ASP ALA ASN GLY          
SEQRES  18 J  337  LYS SER PHE ALA PHE VAL GLY PRO SER ARG TYR LEU LEU          
SEQRES  19 J  337  PHE HIS LEU VAL LYS TYR ILE PHE ALA VAL ALA HIS ARG          
SEQRES  20 J  337  LEU PHE LEU PRO PHE PRO LEU PRO LEU PHE ALA TYR ARG          
SEQRES  21 J  337  TRP VAL ALA ARG VAL PHE GLU ILE SER PRO PHE GLU PRO          
SEQRES  22 J  337  TRP ILE THR ARG ASP LYS VAL GLU ARG MET HIS ILE THR          
SEQRES  23 J  337  ASP MET LYS LEU PRO HIS LEU PRO GLY LEU GLU ASP LEU          
SEQRES  24 J  337  GLY ILE GLN ALA THR PRO LEU GLU LEU LYS ALA ILE GLU          
SEQRES  25 J  337  VAL LEU ARG ARG HIS ARG THR TYR ARG TRP LEU SER ALA          
SEQRES  26 J  337  GLU ILE GLU ASP VAL LYS PRO ALA LYS THR VAL ASN              
SEQRES   1 K   33  LEU GLN HIS HIS ASP TYR SER THR TYR THR PHE LEU ASP          
SEQRES   2 K   33  LEU ASN LEU GLU LEU SER LYS PHE ARG MET PRO GLN PRO          
SEQRES   3 K   33  SER SER GLY ARG GLU SER PRO                                  
SEQRES   1 L  118  LYS LEU ASP ILE THR THR LEU THR GLY VAL PRO GLU GLU          
SEQRES   2 L  118  HIS ILE LYS THR ARG LYS VAL ARG ILE PHE VAL PRO ALA          
SEQRES   3 L  118  ARG ASN ASN MET GLN SER GLY VAL ASN ASN THR LYS LYS          
SEQRES   4 L  118  TRP LYS MET GLU PHE ASP THR ARG GLU ARG TRP GLU ASN          
SEQRES   5 L  118  PRO LEU MET GLY TRP ALA SER THR ALA ASP PRO LEU SER          
SEQRES   6 L  118  ASN MET VAL LEU THR PHE SER THR LYS GLU ASP ALA VAL          
SEQRES   7 L  118  SER PHE ALA GLU LYS ASN GLY TRP SER TYR ASP ILE GLU          
SEQRES   8 L  118  GLU ARG LYS VAL PRO LYS PRO LYS SER LYS SER TYR GLY          
SEQRES   9 L  118  ALA ASN PHE SER TRP ASN LYS ARG THR ARG VAL SER THR          
SEQRES  10 L  118  LYS                                                          
SEQRES   1 M  687  ASN LEU ILE GLU VAL PHE VAL ASP GLY GLN SER VAL MET          
SEQRES   2 M  687  VAL GLU PRO GLY THR THR VAL LEU GLN ALA CYS GLU LYS          
SEQRES   3 M  687  VAL GLY MET GLN ILE PRO ARG PHE CYS TYR HIS GLU ARG          
SEQRES   4 M  687  LEU SER VAL ALA GLY ASN CYS ARG MET CYS LEU VAL GLU          
SEQRES   5 M  687  ILE GLU LYS ALA PRO LYS VAL VAL ALA ALA CYS ALA MET          
SEQRES   6 M  687  PRO VAL MET LYS GLY TRP ASN ILE LEU THR ASN SER GLU          
SEQRES   7 M  687  LYS SER LYS LYS ALA ARG GLU GLY VAL MET GLU PHE LEU          
SEQRES   8 M  687  LEU ALA ASN HIS PRO LEU ASP CYS PRO ILE CYS ASP GLN          
SEQRES   9 M  687  GLY GLY GLU CYS ASP LEU GLN ASP GLN SER MET MET PHE          
SEQRES  10 M  687  GLY ASN ASP ARG SER ARG PHE LEU GLU GLY LYS ARG ALA          
SEQRES  11 M  687  VAL GLU ASP LYS ASN ILE GLY PRO LEU VAL LYS THR ILE          
SEQRES  12 M  687  MET THR ARG CYS ILE GLN CYS THR ARG CYS ILE ARG PHE          
SEQRES  13 M  687  ALA SER GLU ILE ALA GLY VAL ASP ASP LEU GLY THR THR          
SEQRES  14 M  687  GLY ARG GLY ASN ASP MET GLN VAL GLY THR TYR ILE GLU          
SEQRES  15 M  687  LYS MET PHE MET SER GLU LEU SER GLY ASN ILE ILE ASP          
SEQRES  16 M  687  ILE CYS PRO VAL GLY ALA LEU THR SER LYS PRO TYR ALA          
SEQRES  17 M  687  PHE THR ALA ARG PRO TRP GLU THR ARG LYS THR GLU SER          
SEQRES  18 M  687  ILE ASP VAL MET ASP ALA VAL GLY SER ASN ILE VAL VAL          
SEQRES  19 M  687  SER THR ARG THR GLY GLU VAL MET ARG ILE LEU PRO ARG          
SEQRES  20 M  687  MET HIS GLU ASP ILE ASN GLU GLU TRP ILE SER ASP LYS          
SEQRES  21 M  687  THR ARG PHE ALA TYR ASP GLY LEU LYS ARG GLN ARG LEU          
SEQRES  22 M  687  THR GLU PRO MET VAL ARG ASN GLU LYS GLY LEU LEU THR          
SEQRES  23 M  687  TYR THR SER TRP GLU ASP ALA LEU SER ARG VAL ALA GLY          
SEQRES  24 M  687  MET LEU GLN SER PHE GLN GLY LYS ASP VAL ALA ALA ILE          
SEQRES  25 M  687  ALA GLY GLY LEU VAL ASP ALA GLU ALA LEU VAL ALA LEU          
SEQRES  26 M  687  LYS ASP LEU LEU ASN ARG VAL ASP SER ASP THR LEU CYS          
SEQRES  27 M  687  THR GLU GLU VAL PHE PRO THR ALA GLY ALA GLY THR ASP          
SEQRES  28 M  687  LEU ARG SER ASN TYR LEU LEU ASN THR THR ILE ALA GLY          
SEQRES  29 M  687  VAL GLU GLU ALA ASP VAL VAL LEU LEU VAL GLY THR ASN          
SEQRES  30 M  687  PRO ARG PHE GLU ALA PRO LEU PHE ASN ALA ARG ILE ARG          
SEQRES  31 M  687  LYS SER TRP LEU HIS ASN ASP LEU LYS VAL ALA LEU ILE          
SEQRES  32 M  687  GLY SER PRO VAL ASP LEU THR TYR THR TYR ASP HIS LEU          
SEQRES  33 M  687  GLY ASP SER PRO LYS ILE LEU GLN ASP ILE ALA SER GLY          
SEQRES  34 M  687  SER HIS PRO PHE SER GLN VAL LEU LYS GLU ALA LYS LYS          
SEQRES  35 M  687  PRO MET VAL VAL LEU GLY SER SER ALA LEU GLN ARG ASN          
SEQRES  36 M  687  ASP GLY ALA ALA ILE LEU ALA ALA VAL SER SER ILE ALA          
SEQRES  37 M  687  GLN LYS ILE ARG MET THR SER GLY VAL THR GLY ASP TRP          
SEQRES  38 M  687  LYS VAL MET ASN ILE LEU HIS ARG ILE ALA SER GLN VAL          
SEQRES  39 M  687  ALA ALA LEU ASP LEU GLY TYR LYS PRO GLY VAL GLU ALA          
SEQRES  40 M  687  ILE ARG LYS ASN PRO PRO LYS VAL LEU PHE LEU LEU GLY          
SEQRES  41 M  687  ALA ASP GLY GLY CYS ILE THR ARG GLN ASP LEU PRO LYS          
SEQRES  42 M  687  ASP CYS PHE ILE ILE TYR GLN GLY HIS HIS GLY ASP VAL          
SEQRES  43 M  687  GLY ALA PRO ILE ALA ASP VAL ILE LEU PRO GLY ALA ALA          
SEQRES  44 M  687  TYR THR GLU LYS SER ALA THR TYR VAL ASN THR GLU GLY          
SEQRES  45 M  687  ARG ALA GLN GLN THR LYS VAL ALA VAL THR PRO PRO GLY          
SEQRES  46 M  687  LEU ALA ARG GLU ASP TRP LYS ILE ILE ARG ALA LEU SER          
SEQRES  47 M  687  GLU ILE ALA GLY MET THR LEU PRO TYR ASP THR LEU ASP          
SEQRES  48 M  687  GLN VAL ARG ASN ARG LEU GLU GLU VAL SER PRO ASN LEU          
SEQRES  49 M  687  VAL ARG TYR ASP ASP ILE GLU GLY ALA ASN TYR PHE GLN          
SEQRES  50 M  687  GLN ALA ASN GLU LEU SER LYS LEU VAL ASN GLN GLN LEU          
SEQRES  51 M  687  LEU ALA ASP PRO LEU VAL PRO PRO GLN LEU THR ILE LYS          
SEQRES  52 M  687  ASP PHE TYR MET THR ASP SER ILE SER ARG ALA SER GLN          
SEQRES  53 M  687  THR MET ALA LYS CYS VAL LYS ALA VAL THR GLU                  
SEQRES   1 N  143  GLU LEU VAL GLN VAL LEU LYS ARG GLY LEU GLN GLN ILE          
SEQRES   2 N  143  THR GLY HIS GLY GLY LEU ARG GLY TYR LEU ARG VAL PHE          
SEQRES   3 N  143  PHE ARG THR ASN ASP ALA LYS VAL GLY THR LEU VAL GLY          
SEQRES   4 N  143  GLU ASP LYS TYR GLY ASN LYS TYR TYR GLU ASP ASN LYS          
SEQRES   5 N  143  GLN PHE PHE GLY ARG HIS ARG TRP VAL VAL TYR THR THR          
SEQRES   6 N  143  GLU MET ASN GLY LYS ASN THR PHE TRP ASP VAL ASP GLY          
SEQRES   7 N  143  SER MET VAL PRO PRO GLU TRP HIS ARG TRP LEU HIS SER          
SEQRES   8 N  143  MET THR ASP ASP PRO PRO THR THR LYS PRO LEU THR ALA          
SEQRES   9 N  143  ARG LYS PHE ILE TRP THR ASN HIS LYS PHE ASN VAL THR          
SEQRES  10 N  143  GLY THR PRO GLU GLN TYR VAL PRO TYR SER THR THR ARG          
SEQRES  11 N  143  LYS LYS ILE GLN GLU TRP ILE PRO PRO SER THR PRO TYR          
SEQRES   1 O  212  GLY ALA LEU PHE VAL HIS ARG ASP THR PRO GLU ASN ASN          
SEQRES   2 O  212  PRO ASP THR PRO PHE ASP PHE THR PRO GLU ASN TYR LYS          
SEQRES   3 O  212  ARG ILE GLU ALA ILE VAL LYS ASN TYR PRO GLU GLY HIS          
SEQRES   4 O  212  LYS ALA ALA ALA VAL LEU PRO VAL LEU ASP LEU ALA GLN          
SEQRES   5 O  212  ARG GLN ASN GLY TRP LEU PRO ILE SER ALA MET ASN LYS          
SEQRES   6 O  212  VAL ALA GLU VAL LEU GLN VAL PRO PRO MET ARG VAL TYR          
SEQRES   7 O  212  GLU VAL ALA THR PHE TYR THR MET TYR ASN ARG LYS PRO          
SEQRES   8 O  212  VAL GLY LYS TYR HIS ILE GLN VAL CYS THR THR THR PRO          
SEQRES   9 O  212  CYS MET LEU ARG ASN SER ASP SER ILE LEU GLU ALA ILE          
SEQRES  10 O  212  GLN LYS LYS LEU GLY ILE LYS VAL GLY GLU THR THR PRO          
SEQRES  11 O  212  ASP LYS LEU PHE THR LEU ILE GLU VAL GLU CYS LEU GLY          
SEQRES  12 O  212  ALA CYS VAL ASN ALA PRO MET VAL GLN ILE ASN ASP ASN          
SEQRES  13 O  212  TYR TYR GLU ASP LEU THR ALA LYS ASP ILE GLU GLU ILE          
SEQRES  14 O  212  ILE ASP GLU LEU LYS ALA GLY LYS ILE PRO LYS PRO GLY          
SEQRES  15 O  212  PRO ARG SER GLY ARG PHE SER CYS GLU PRO ALA GLY GLY          
SEQRES  16 O  212  LEU THR SER LEU THR GLU PRO PRO LYS GLY PRO GLY PHE          
SEQRES  17 O  212  GLY VAL GLN ALA                                              
SEQRES   1 P  208  THR ARG PRO THR VAL ARG PRO ARG ASN ASP VAL ALA HIS          
SEQRES   2 P  208  LYS GLN LEU SER ALA PHE GLY GLU TYR VAL ALA GLU ILE          
SEQRES   3 P  208  LEU PRO LYS TYR VAL GLN GLN VAL GLN VAL SER CYS PHE          
SEQRES   4 P  208  ASN GLU LEU GLU VAL CYS ILE HIS PRO ASP GLY VAL ILE          
SEQRES   5 P  208  PRO VAL LEU THR PHE LEU ARG ASP HIS THR ASN ALA GLN          
SEQRES   6 P  208  PHE LYS SER LEU VAL ASP LEU THR ALA VAL ASP VAL PRO          
SEQRES   7 P  208  THR ARG GLN ASN ARG PHE GLU ILE VAL TYR ASN LEU LEU          
SEQRES   8 P  208  SER LEU ARG PHE ASN SER ARG ILE ARG VAL LYS THR TYR          
SEQRES   9 P  208  THR ASP GLU LEU THR PRO ILE GLU SER ALA VAL SER VAL          
SEQRES  10 P  208  PHE LYS ALA ALA ASN TRP TYR GLU ARG GLU ILE TRP ASP          
SEQRES  11 P  208  MET PHE GLY VAL PHE PHE ALA ASN HIS PRO ASP LEU ARG          
SEQRES  12 P  208  ARG ILE LEU THR ASP TYR GLY PHE GLU GLY HIS PRO PHE          
SEQRES  13 P  208  ARG LYS ASP PHE PRO LEU SER GLY TYR VAL GLU LEU ARG          
SEQRES  14 P  208  TYR ASP ASP GLU VAL LYS ARG VAL VAL ALA GLU PRO VAL          
SEQRES  15 P  208  GLU LEU ALA GLN GLU PHE ARG LYS PHE ASP LEU ASN SER          
SEQRES  16 P  208  PRO TRP GLU ALA PHE PRO VAL TYR ARG GLN PRO PRO GLU          
SEQRES   1 Q  430  VAL ARG GLN TRP GLN PRO ASP VAL GLU TRP ALA GLN GLN          
SEQRES   2 Q  430  PHE GLY GLY ALA VAL MET TYR PRO SER LYS GLU THR ALA          
SEQRES   3 Q  430  HIS TRP LYS PRO PRO PRO TRP ASN ASP VAL ASP PRO PRO          
SEQRES   4 Q  430  LYS ASP THR ILE VAL LYS ASN ILE THR LEU ASN PHE GLY          
SEQRES   5 Q  430  PRO GLN HIS PRO ALA ALA HIS GLY VAL LEU ARG LEU VAL          
SEQRES   6 Q  430  MET GLU LEU SER GLY GLU MET VAL ARG LYS CYS ASP PRO          
SEQRES   7 Q  430  HIS ILE GLY LEU LEU HIS ARG GLY THR GLU LYS LEU ILE          
SEQRES   8 Q  430  GLU TYR LYS THR TYR LEU GLN ALA LEU PRO TYR PHE ASP          
SEQRES   9 Q  430  ARG LEU ASP TYR VAL SER MET MET CYS ASN GLU GLN ALA          
SEQRES  10 Q  430  TYR SER LEU ALA VAL GLU LYS LEU LEU ASN ILE ARG PRO          
SEQRES  11 Q  430  PRO PRO ARG ALA GLN TRP ILE ARG VAL LEU PHE GLY GLU          
SEQRES  12 Q  430  ILE THR ARG LEU LEU ASN HIS ILE MET ALA VAL THR THR          
SEQRES  13 Q  430  HIS ALA LEU ASP LEU GLY ALA MET THR PRO PHE PHE TRP          
SEQRES  14 Q  430  LEU PHE GLU GLU ARG GLU LYS MET PHE GLU PHE TYR GLU          
SEQRES  15 Q  430  ARG VAL SER GLY ALA ARG MET HIS ALA ALA TYR ILE ARG          
SEQRES  16 Q  430  PRO GLY GLY VAL HIS GLN ASP LEU PRO LEU GLY LEU MET          
SEQRES  17 Q  430  ASP ASP ILE TYR GLN PHE SER LYS ASN PHE SER LEU ARG          
SEQRES  18 Q  430  LEU ASP GLU LEU GLU GLU LEU LEU THR ASN ASN ARG ILE          
SEQRES  19 Q  430  TRP ARG ASN ARG THR ILE ASP ILE GLY VAL VAL THR ALA          
SEQRES  20 Q  430  GLU GLU ALA LEU ASN TYR GLY PHE SER GLY VAL MET LEU          
SEQRES  21 Q  430  ARG GLY SER GLY ILE GLN TRP ASP LEU ARG LYS THR GLN          
SEQRES  22 Q  430  PRO TYR ASP VAL TYR ASP GLN VAL GLU PHE ASP VAL PRO          
SEQRES  23 Q  430  VAL GLY SER ARG GLY ASP CYS TYR ASP ARG TYR LEU CYS          
SEQRES  24 Q  430  ARG VAL GLU GLU MET ARG GLN SER LEU ARG ILE ILE ALA          
SEQRES  25 Q  430  GLN CYS LEU ASN LYS MET PRO PRO GLY GLU ILE LYS VAL          
SEQRES  26 Q  430  ASP ASP ALA LYS VAL SER PRO PRO LYS ARG ALA GLU MET          
SEQRES  27 Q  430  LYS THR SER MET GLU SER LEU ILE HIS HIS PHE LYS LEU          
SEQRES  28 Q  430  TYR THR GLU GLY TYR GLN VAL PRO PRO GLY ALA THR TYR          
SEQRES  29 Q  430  THR ALA ILE GLU ALA PRO LYS GLY GLU PHE GLY VAL TYR          
SEQRES  30 Q  430  LEU VAL SER ASP GLY SER SER ARG PRO TYR ARG CYS LYS          
SEQRES  31 Q  430  ILE LYS ALA PRO GLY PHE ALA HIS LEU ALA GLY LEU ASP          
SEQRES  32 Q  430  LYS MET SER LYS GLY HIS MET LEU ALA ASP VAL VAL ALA          
SEQRES  33 Q  430  ILE ILE GLY THR GLN ASP ILE VAL PHE GLY GLU VAL ASP          
SEQRES  34 Q  430  ARG                                                          
SEQRES   1 S   70  MET TRP PHE GLU ILE LEU PRO GLY LEU SER VAL MET GLY          
SEQRES   2 S   70  VAL CYS LEU LEU ILE PRO GLY LEU ALA THR ALA TYR ILE          
SEQRES   3 S   70  HIS ARG PHE THR ASN GLY GLY LYS GLU LYS ARG VAL ALA          
SEQRES   4 S   70  HIS PHE GLY TYR HIS TRP SER LEU MET GLU ARG ASP ARG          
SEQRES   5 S   70  ARG ILE SER GLY VAL ASP ARG TYR TYR VAL SER LYS GLY          
SEQRES   6 S   70  LEU GLU ASN ILE ASP                                          
SEQRES   1 T   95  GLY VAL ARG VAL SER PRO THR GLY GLU LYS VAL THR HIS          
SEQRES   2 T   95  THR GLY GLN VAL TYR ASP ASP LYS ASP TYR ARG ARG ILE          
SEQRES   3 T   95  ARG PHE VAL GLY ARG GLN LYS GLU VAL ASN GLU ASN PHE          
SEQRES   4 T   95  ALA ILE ASP LEU ILE ALA GLU GLN PRO VAL SER GLU VAL          
SEQRES   5 T   95  GLU THR ARG VAL ILE ALA CYS ASP GLY GLY GLY GLY ALA          
SEQRES   6 T   95  LEU GLY HIS PRO LYS VAL TYR ILE ASN LEU ASP LYS GLU          
SEQRES   7 T   95  THR LYS THR GLY THR CYS GLY TYR CYS GLY LEU GLN PHE          
SEQRES   8 T   95  ARG GLN HIS HIS                                              
SEQRES   1 U   83  ALA ALA ARG VAL GLY ALA PHE LEU LYS ASN ALA TRP ASP          
SEQRES   2 U   83  LYS GLU PRO VAL LEU VAL VAL SER PHE VAL VAL GLY GLY          
SEQRES   3 U   83  LEU ALA VAL ILE LEU PRO PRO LEU SER PRO TYR PHE LYS          
SEQRES   4 U   83  TYR SER VAL MET ILE ASN LYS ALA THR PRO TYR ASN TYR          
SEQRES   5 U   83  PRO VAL PRO VAL ARG ASP ASP GLY ASN MET PRO ASP VAL          
SEQRES   6 U   83  PRO SER HIS PRO GLN ASP PRO GLN GLY PRO SER LEU GLU          
SEQRES   7 U   83  TRP LEU LYS LYS LEU                                          
SEQRES   1 V  140  ALA PRO LYS VAL PHE ARG GLN TYR TRP ASP ILE PRO ASP          
SEQRES   2 V  140  GLY THR ASP CYS HIS ARG LYS ALA TYR SER THR THR SER          
SEQRES   3 V  140  ILE ALA SER VAL ALA GLY LEU THR ALA ALA ALA TYR ARG          
SEQRES   4 V  140  VAL THR LEU ASN PRO PRO GLY THR PHE LEU GLU GLY VAL          
SEQRES   5 V  140  ALA LYS VAL GLY GLN TYR THR PHE THR ALA ALA ALA VAL          
SEQRES   6 V  140  GLY ALA VAL PHE GLY LEU THR THR CYS ILE SER ALA HIS          
SEQRES   7 V  140  VAL ARG GLU LYS PRO ASP ASP PRO LEU ASN TYR PHE LEU          
SEQRES   8 V  140  GLY GLY CYS ALA GLY GLY LEU THR LEU GLY ALA ARG THR          
SEQRES   9 V  140  HIS ASN TYR GLY ILE GLY ALA ALA ALA CYS VAL TYR PHE          
SEQRES  10 V  140  GLY ILE ALA ALA SER LEU VAL LYS MET GLY ARG LEU GLU          
SEQRES  11 V  140  GLY TRP GLU VAL PHE ALA LYS PRO LYS VAL                      
SEQRES   1 W  138  LYS GLN ASP MET PRO PRO PRO GLY GLY TYR GLY PRO ILE          
SEQRES   2 W  138  ASP TYR LYS ARG ASN LEU PRO ARG ARG GLY LEU SER GLY          
SEQRES   3 W  138  TYR SER MET LEU ALA ILE GLY ILE GLY THR LEU ILE TYR          
SEQRES   4 W  138  GLY HIS TRP SER ILE MET LYS TRP ASN ARG GLU ARG ARG          
SEQRES   5 W  138  ARG LEU GLN ILE GLU ASP PHE GLU ALA ARG ILE ALA LEU          
SEQRES   6 W  138  LEU PRO LEU LEU GLN ALA GLU THR ASP ARG ARG THR LEU          
SEQRES   7 W  138  GLN MET LEU ARG GLU ASN LEU GLU GLU GLU ALA ILE ILE          
SEQRES   8 W  138  MET LYS ASP VAL PRO ASP TRP LYS VAL GLY GLU SER VAL          
SEQRES   9 W  138  PHE HIS THR THR ARG TRP VAL PRO PRO LEU ILE GLY GLU          
SEQRES  10 W  138  LEU TYR GLY LEU ARG THR THR GLU GLU ALA LEU HIS ALA          
SEQRES  11 W  138  SER HIS GLY PHE MET TRP TYR THR                              
SEQRES   1 X   85  PRO PRO LEU THR LEU GLU GLY ILE GLN ASP ARG VAL LEU          
SEQRES   2 X   85  TYR VAL LEU LYS LEU TYR ASP LYS ILE ASP PRO GLU LYS          
SEQRES   3 X   85  LEU SER VAL ASN SER HIS PHE MET LYS ASP LEU GLY LEU          
SEQRES   4 X   85  ASP SER LEU ASP GLN VAL GLU ILE ILE MET ALA MET GLU          
SEQRES   5 X   85  ASP GLU PHE GLY PHE GLU ILE PRO ASP ILE ASP ALA GLU          
SEQRES   6 X   85  LYS LEU MET CYS PRO GLN GLU ILE VAL ASP TYR ILE ALA          
SEQRES   7 X   85  ASP LYS LYS ASP VAL TYR GLU                                  
SEQRES   1 Y   59  HIS ILE GLU PRO ARG TYR ARG GLN PHE PRO GLN LEU THR          
SEQRES   2 Y   59  ARG SER GLN VAL PHE GLN SER GLU PHE PHE SER GLY LEU          
SEQRES   3 Y   59  MET TRP PHE TRP ILE LEU TRP ARG PHE TRP HIS ASP SER          
SEQRES   4 Y   59  GLU GLU VAL LEU GLY HIS PHE PRO TYR PRO ASP PRO SER          
SEQRES   5 Y   59  GLN TRP THR ASP GLU GLU LEU                                  
SEQRES   1 Z   80  GLY HIS HIS LYS MET GLU LEU PRO ASP TYR ARG GLN TRP          
SEQRES   2 Z   80  LYS ILE GLU GLY THR PRO LEU GLU THR ILE GLN LYS LYS          
SEQRES   3 Z   80  LEU ALA ALA LYS GLY LEU ARG ASP PRO TRP GLY ARG ASN          
SEQRES   4 Z   80  GLU ALA TRP ARG TYR MET GLY GLY PHE ALA LYS SER VAL          
SEQRES   5 Z   80  SER PHE SER ASP VAL PHE PHE LYS GLY PHE LYS TRP GLY          
SEQRES   6 Z   80  PHE ALA ALA PHE VAL VAL ALA VAL GLY ALA GLU TYR TYR          
SEQRES   7 Z   80  LEU GLU                                                      
SEQRES   1 a  138  LYS ARG LEU PHE VAL ILE ARG PRO SER ARG PHE TYR ASP          
SEQRES   2 a  138  ARG ARG PHE LEU LYS LEU LEU ARG PHE TYR ILE ALA LEU          
SEQRES   3 a  138  THR GLY ILE PRO VAL ALA ILE PHE ILE THR LEU VAL ASN          
SEQRES   4 a  138  VAL PHE ILE GLY GLN ALA GLU LEU ALA GLU ILE PRO GLU          
SEQRES   5 a  138  GLY TYR VAL PRO GLU HIS TRP GLU TYR TYR LYS HIS PRO          
SEQRES   6 a  138  ILE SER ARG TRP ILE ALA ARG ASN PHE TYR ASP SER PRO          
SEQRES   7 a  138  GLU LYS ILE TYR GLU ARG THR MET ALA VAL LEU GLN ILE          
SEQRES   8 a  138  GLU ALA GLU LYS ALA GLU LEU ARG VAL LYS GLU LEU GLU          
SEQRES   9 a  138  VAL ARG LYS LEU MET HIS VAL ARG GLY ASP GLY PRO TRP          
SEQRES  10 a  138  TYR TYR TYR GLU THR ILE ASP LYS GLU LEU ILE ASP HIS          
SEQRES  11 a  138  SER PRO LYS ALA THR PRO ASP ASN                              
SEQRES   1 b  128  MET THR GLY TYR THR PRO ASP GLU LYS LEU ARG LEU GLN          
SEQRES   2 b  128  GLN LEU ARG GLU LEU ARG ARG ARG TRP LEU LYS ASP GLN          
SEQRES   3 b  128  GLU LEU SER PRO ARG GLU PRO VAL LEU PRO PRO GLN LYS          
SEQRES   4 b  128  MET GLY PRO MET GLU LYS PHE TRP ASN LYS PHE LEU GLU          
SEQRES   5 b  128  ASN LYS SER PRO TRP ARG LYS MET VAL HIS GLY VAL TYR          
SEQRES   6 b  128  LYS LYS SER ILE PHE VAL PHE THR HIS VAL LEU VAL PRO          
SEQRES   7 b  128  VAL TRP ILE ILE HIS TYR TYR MET LYS TYR HIS VAL SER          
SEQRES   8 b  128  GLU LYS PRO TYR GLY ILE VAL GLU LYS LYS SER ARG ILE          
SEQRES   9 b  128  PHE PRO GLY ASP THR ILE LEU GLU THR GLY GLU VAL ILE          
SEQRES  10 b  128  PRO PRO MET LYS GLU PHE PRO ASP GLN HIS HIS                  
SEQRES   1 c  153  LYS ASP MET PHE PRO GLY PRO TYR PRO ARG THR PRO GLU          
SEQRES   2 c  153  GLU ARG ALA ALA ALA ALA LYS LYS TYR ASN MET ARG VAL          
SEQRES   3 c  153  GLU ASP TYR GLU PRO TYR PRO ASP ASP GLY MET GLY TYR          
SEQRES   4 c  153  GLY ASP TYR PRO LYS LEU PRO ASP ARG SER GLN HIS GLU          
SEQRES   5 c  153  ARG ASP PRO TRP TYR SER TRP ASP GLN PRO GLY LEU ARG          
SEQRES   6 c  153  LEU ASN TRP GLY GLU PRO MET HIS TRP HIS LEU ASP MET          
SEQRES   7 c  153  TYR ASN ARG ASN ARG VAL ASP THR SER PRO THR PRO VAL          
SEQRES   8 c  153  SER TRP HIS VAL MET CYS MET GLN LEU PHE GLY PHE LEU          
SEQRES   9 c  153  ALA PHE MET ILE PHE MET CYS TRP VAL GLY ASP VAL TYR          
SEQRES  10 c  153  PRO VAL TYR GLN PRO VAL GLY PRO LYS GLN TYR PRO TYR          
SEQRES  11 c  153  ASN ASN LEU TYR LEU GLU ARG GLY GLY ASP PRO SER LYS          
SEQRES  12 c  153  GLU PRO GLU ARG VAL VAL HIS TYR GLU ILE                      
SEQRES   1 d  171  MET PRO ASP SER TRP ASP LYS ASP VAL TYR PRO GLU PRO          
SEQRES   2 d  171  PRO ARG ARG THR PRO VAL GLN PRO ASN PRO ILE VAL TYR          
SEQRES   3 d  171  MET MET LYS ALA PHE ASP LEU ILE VAL ASP ARG PRO VAL          
SEQRES   4 d  171  THR LEU VAL ARG GLU PHE ILE GLU ARG GLN HIS ALA LYS          
SEQRES   5 d  171  ASN ARG TYR TYR TYR TYR HIS ARG GLN TYR ARG ARG VAL          
SEQRES   6 d  171  PRO ASP ILE THR GLU CYS LYS GLU GLU ASP ILE MET CYS          
SEQRES   7 d  171  MET TYR GLU ALA GLU MET GLN TRP LYS ARG ASP TYR LYS          
SEQRES   8 d  171  VAL ASP GLN GLU ILE ILE ASN ILE MET GLN ASP ARG LEU          
SEQRES   9 d  171  LYS ALA CYS GLN GLN ARG GLU GLY GLN ASN TYR GLN GLN          
SEQRES  10 d  171  ASN CYS ILE LYS GLU VAL GLU GLN PHE THR GLN VAL ALA          
SEQRES  11 d  171  LYS ALA TYR GLN ASP ARG TYR GLN ASP LEU GLY ALA TYR          
SEQRES  12 d  171  SER SER ALA ARG LYS CYS LEU ALA LYS GLN ARG GLN ARG          
SEQRES  13 d  171  MET LEU GLN GLU ARG LYS ALA ALA LYS GLU ALA ALA ALA          
SEQRES  14 d  171  ALA THR                                                      
SEQRES   1 e   97  PRO TRP GLN GLU ASP PRO GLU PRO GLU ASP GLU ASN LEU          
SEQRES   2 e   97  TYR GLU LYS ASN PRO ASP SER HIS GLY TYR ASP LYS ASP          
SEQRES   3 e   97  PRO VAL LEU ASP VAL TRP ASN MET ARG LEU VAL PHE PHE          
SEQRES   4 e   97  PHE GLY VAL SER ILE ILE LEU VAL LEU GLY SER THR PHE          
SEQRES   5 e   97  VAL ALA TYR LEU PRO ASP TYR ARG MET LYS GLU TRP SER          
SEQRES   6 e   97  ARG ARG GLU ALA GLU ARG LEU VAL LYS TYR ARG GLU ALA          
SEQRES   7 e   97  ASN GLY LEU PRO ILE MET GLU SER ASN CYS PHE ASP PRO          
SEQRES   8 e   97  SER LYS ILE GLN LEU PRO                                      
SEQRES   1 f   47  LYS PHE TYR VAL ARG GLU PRO PRO ASN ALA LYS PRO ASP          
SEQRES   2 f   47  TRP LEU LYS VAL GLY PHE THR LEU GLY THR THR VAL PHE          
SEQRES   3 f   47  LEU TRP ILE TYR LEU ILE LYS GLN HIS ASN GLU ASP ILE          
SEQRES   4 f   47  LEU GLU TYR LYS ARG ARG ASN GLY                              
SEQRES   1 g  119  MET ILE ALA ARG ARG ASN PRO GLU PRO LEU ARG PHE LEU          
SEQRES   2 g  119  PRO ASP GLU ALA ARG SER LEU PRO PRO PRO LYS LEU THR          
SEQRES   3 g  119  ASP PRO ARG LEU LEU TYR ILE GLY PHE LEU GLY TYR CYS          
SEQRES   4 g  119  SER GLY LEU ILE ASP ASN LEU ILE ARG ARG ARG PRO ILE          
SEQRES   5 g  119  ALA THR ALA GLY LEU HIS ARG GLN LEU LEU TYR ILE THR          
SEQRES   6 g  119  ALA PHE PHE PHE ALA GLY TYR TYR LEU VAL LYS ARG GLU          
SEQRES   7 g  119  ASP TYR LEU TYR ALA VAL ARG ASP ARG GLU MET PHE GLY          
SEQRES   8 g  119  TYR MET LYS LEU HIS PRO GLU ASP PHE PRO GLU GLU ASP          
SEQRES   9 g  119  LYS LYS THR TYR GLY GLU ILE PHE GLU LYS PHE HIS PRO          
SEQRES  10 g  119  ILE ARG                                                      
SEQRES   1 h  104  PRO PHE LEU ASP ILE GLN LYS ARG PHE GLY LEU ASN ILE          
SEQRES   2 h  104  ASP ARG TRP LEU THR ILE GLN SER GLY GLU GLN PRO TYR          
SEQRES   3 h  104  LYS MET ALA GLY ARG CYS HIS ALA PHE GLU LYS GLU TRP          
SEQRES   4 h  104  ILE GLU CYS ALA HIS GLY ILE GLY TYR THR ARG ALA GLU          
SEQRES   5 h  104  LYS GLU CYS LYS ILE GLU TYR ASP ASP PHE VAL GLU CYS          
SEQRES   6 h  104  LEU LEU ARG GLN LYS THR MET ARG ARG ALA GLY THR ILE          
SEQRES   7 h  104  ARG LYS GLN ARG ASP LYS LEU ILE LYS GLU GLY LYS TYR          
SEQRES   8 h  104  THR PRO PRO PRO HIS HIS ILE GLY LYS GLY GLU PRO ARG          
SEQRES   1 i  347  MET ASN PRO LEU ALA GLN PRO VAL ILE TYR SER THR ILE          
SEQRES   2 i  347  PHE ALA GLY THR LEU ILE THR ALA LEU SER SER HIS TRP          
SEQRES   3 i  347  PHE PHE THR TRP VAL GLY LEU GLU MET ASN MET LEU ALA          
SEQRES   4 i  347  PHE ILE PRO VAL LEU THR LYS LYS MET ASN PRO ARG SER          
SEQRES   5 i  347  THR GLU ALA ALA ILE LYS TYR PHE LEU THR GLN ALA THR          
SEQRES   6 i  347  ALA SER MET ILE LEU LEU MET ALA ILE LEU PHE ASN ASN          
SEQRES   7 i  347  MET LEU SER GLY GLN TRP THR MET THR ASN THR THR ASN          
SEQRES   8 i  347  GLN TYR SER SER LEU MET ILE MET MET ALA MET ALA MET          
SEQRES   9 i  347  LYS LEU GLY MET ALA PRO PHE HIS PHE TRP VAL PRO GLU          
SEQRES  10 i  347  VAL THR GLN GLY THR PRO LEU THR SER GLY LEU LEU LEU          
SEQRES  11 i  347  LEU THR TRP GLN LYS LEU ALA PRO ILE SER ILE MET TYR          
SEQRES  12 i  347  GLN ILE SER PRO SER LEU ASN VAL ASN LEU LEU LEU THR          
SEQRES  13 i  347  LEU SER ILE LEU SER ILE MET ALA GLY SER TRP GLY GLY          
SEQRES  14 i  347  LEU ASN GLN THR GLN LEU ARG LYS ILE LEU ALA TYR SER          
SEQRES  15 i  347  SER ILE THR HIS MET GLY TRP MET MET ALA VAL LEU PRO          
SEQRES  16 i  347  TYR ASN PRO ASN MET THR ILE LEU ASN LEU THR ILE TYR          
SEQRES  17 i  347  ILE ILE LEU THR THR THR ALA PHE LEU LEU LEU ASN LEU          
SEQRES  18 i  347  ASN SER SER THR THR THR LEU LEU LEU SER ARG THR TRP          
SEQRES  19 i  347  ASN LYS LEU THR TRP LEU THR PRO LEU ILE PRO SER THR          
SEQRES  20 i  347  LEU LEU SER LEU GLY GLY LEU PRO PRO LEU THR GLY PHE          
SEQRES  21 i  347  LEU PRO LYS TRP ALA ILE ILE GLU GLU PHE THR LYS ASN          
SEQRES  22 i  347  ASN SER LEU ILE ILE PRO THR ILE MET ALA THR ILE THR          
SEQRES  23 i  347  LEU LEU ASN LEU TYR PHE TYR LEU ARG LEU ILE TYR SER          
SEQRES  24 i  347  THR SER ILE THR LEU LEU PRO MET SER ASN ASN VAL LYS          
SEQRES  25 i  347  MET LYS TRP GLN PHE GLU HIS THR LYS PRO THR PRO PHE          
SEQRES  26 i  347  LEU PRO THR LEU ILE ALA LEU THR THR LEU LEU LEU PRO          
SEQRES  27 i  347  ILE SER PRO PHE MET LEU MET ILE LEU                          
SEQRES   1 j  115  MET ASN PHE ALA LEU ILE LEU MET THR ASN THR LEU LEU          
SEQRES   2 j  115  ALA LEU LEU LEU MET ILE ILE THR PHE TRP LEU PRO GLN          
SEQRES   3 j  115  LEU ASN GLY TYR MET GLU LYS SER THR PRO TYR GLU CYS          
SEQRES   4 j  115  GLY PHE ASP PRO MET SER PRO ALA ARG VAL PRO PHE SER          
SEQRES   5 j  115  MET LYS PHE PHE LEU VAL ALA ILE THR PHE LEU LEU PHE          
SEQRES   6 j  115  ASP LEU GLU ILE ALA LEU LEU LEU PRO LEU PRO TRP ALA          
SEQRES   7 j  115  LEU GLN THR THR ASN LEU PRO LEU MET VAL MET SER SER          
SEQRES   8 j  115  LEU LEU LEU ILE ILE ILE LEU ALA LEU SER LEU ALA TYR          
SEQRES   9 j  115  GLU TRP LEU GLN LYS GLY LEU ASP TRP ALA GLU                  
SEQRES   1 k   97  MET PRO LEU ILE TYR MET ASN ILE MET LEU ALA PHE THR          
SEQRES   2 k   97  ILE SER LEU LEU GLY MET LEU VAL TYR ARG SER HIS LEU          
SEQRES   3 k   97  MET SER SER LEU LEU CYS LEU GLU GLY MET MET LEU SER          
SEQRES   4 k   97  LEU PHE ILE MET ALA THR LEU MET THR LEU ASN THR HIS          
SEQRES   5 k   97  SER LEU LEU ALA ASN ILE MET PRO ILE VAL MET LEU VAL          
SEQRES   6 k   97  PHE ALA ALA CYS GLU ALA ALA VAL GLY LEU ALA LEU LEU          
SEQRES   7 k   97  VAL SER ILE SER ASN THR TYR GLY LEU ASP TYR VAL HIS          
SEQRES   8 k   97  ASN LEU ASN LEU LEU GLN                                      
SEQRES   1 l  603  MET THR MET HIS THR THR MET ALA THR LEU THR LEU THR          
SEQRES   2 l  603  SER LEU ILE PRO PRO ILE LEU THR THR LEU VAL ASN PRO          
SEQRES   3 l  603  ASN LYS LYS ASN SER TYR PRO HIS TYR VAL LYS SER ILE          
SEQRES   4 l  603  VAL ALA SER THR PHE ILE ILE SER LEU PHE PRO THR THR          
SEQRES   5 l  603  MET PHE MET CYS LEU ASP GLN GLU VAL ILE ILE SER ASN          
SEQRES   6 l  603  TRP HIS TRP ALA THR THR GLN THR THR GLN LEU SER LEU          
SEQRES   7 l  603  SER PHE LYS LEU ASP TYR PHE SER MET MET PHE ILE PRO          
SEQRES   8 l  603  VAL ALA LEU PHE VAL THR TRP SER ILE MET GLU PHE SER          
SEQRES   9 l  603  LEU TRP TYR MET ASN SER ASP PRO ASN ILE ASN GLN PHE          
SEQRES  10 l  603  PHE LYS TYR LEU LEU ILE PHE LEU ILE THR MET LEU ILE          
SEQRES  11 l  603  LEU VAL THR ALA ASN ASN LEU PHE GLN LEU PHE ILE GLY          
SEQRES  12 l  603  TRP GLU GLY VAL GLY ILE MET SER PHE LEU LEU ILE SER          
SEQRES  13 l  603  TRP TRP TYR ALA ARG ALA ASP ALA ASN THR ALA ALA ILE          
SEQRES  14 l  603  GLN ALA ILE LEU TYR ASN ARG ILE GLY ASP ILE GLY PHE          
SEQRES  15 l  603  ILE LEU ALA LEU ALA TRP PHE ILE LEU HIS SER ASN SER          
SEQRES  16 l  603  TRP ASP PRO GLN GLN MET ALA LEU LEU ASN ALA ASN PRO          
SEQRES  17 l  603  SER LEU THR PRO LEU LEU GLY LEU LEU LEU ALA ALA ALA          
SEQRES  18 l  603  GLY LYS SER ALA GLN LEU GLY LEU HIS PRO TRP LEU PRO          
SEQRES  19 l  603  SER ALA MET GLU GLY PRO THR PRO VAL SER ALA LEU LEU          
SEQRES  20 l  603  HIS SER SER THR MET VAL VAL ALA GLY ILE PHE LEU LEU          
SEQRES  21 l  603  ILE ARG PHE HIS PRO LEU ALA GLU ASN ASN PRO LEU ILE          
SEQRES  22 l  603  GLN THR LEU THR LEU CYS LEU GLY ALA ILE THR THR LEU          
SEQRES  23 l  603  PHE ALA ALA VAL CYS ALA LEU THR GLN ASN ASP ILE LYS          
SEQRES  24 l  603  LYS ILE VAL ALA PHE SER THR SER SER GLN LEU GLY LEU          
SEQRES  25 l  603  MET MET VAL THR ILE GLY ILE ASN GLN PRO HIS LEU ALA          
SEQRES  26 l  603  PHE LEU HIS ILE CYS THR HIS ALA PHE PHE LYS ALA MET          
SEQRES  27 l  603  LEU PHE MET CYS SER GLY SER ILE ILE HIS ASN LEU ASN          
SEQRES  28 l  603  ASN GLU GLN ASP ILE ARG LYS MET GLY GLY LEU LEU LYS          
SEQRES  29 l  603  THR MET PRO LEU THR SER THR SER LEU THR ILE GLY SER          
SEQRES  30 l  603  LEU ALA LEU ALA GLY MET PRO PHE LEU THR GLY PHE TYR          
SEQRES  31 l  603  SER LYS ASP HIS ILE ILE GLU THR ALA ASN MET SER TYR          
SEQRES  32 l  603  THR ASN ALA TRP ALA LEU SER ILE THR LEU ILE ALA THR          
SEQRES  33 l  603  SER LEU THR SER ALA TYR SER THR ARG MET ILE LEU LEU          
SEQRES  34 l  603  THR LEU THR GLY GLN PRO ARG PHE PRO THR LEU THR ASN          
SEQRES  35 l  603  ILE ASN GLU ASN ASN PRO THR LEU LEU ASN PRO ILE LYS          
SEQRES  36 l  603  ARG LEU ALA ALA GLY SER LEU PHE ALA GLY PHE LEU ILE          
SEQRES  37 l  603  THR ASN ASN ILE SER PRO ALA SER PRO PHE GLN THR THR          
SEQRES  38 l  603  ILE PRO LEU TYR LEU LYS LEU THR ALA LEU ALA VAL THR          
SEQRES  39 l  603  PHE LEU GLY LEU LEU THR ALA LEU ASP LEU ASN TYR LEU          
SEQRES  40 l  603  THR ASN LYS LEU LYS MET LYS SER PRO LEU CYS THR PHE          
SEQRES  41 l  603  TYR PHE SER ASN MET LEU GLY PHE TYR PRO SER ILE MET          
SEQRES  42 l  603  HIS ARG THR ILE PRO TYR LEU GLY LEU LEU THR SER GLN          
SEQRES  43 l  603  ASN LEU PRO LEU LEU LEU LEU ASP LEU THR TRP LEU GLU          
SEQRES  44 l  603  LYS LEU LEU PRO LYS THR ILE SER GLN HIS GLN ILE SER          
SEQRES  45 l  603  THR SER ILE ILE THR SER THR GLN LYS GLY MET ILE LYS          
SEQRES  46 l  603  LEU TYR PHE LEU SER PHE PHE PHE PRO LEU ILE LEU THR          
SEQRES  47 l  603  LEU LEU LEU ILE THR                                          
SEQRES   1 m  174  MET MET TYR ALA LEU PHE LEU LEU SER VAL GLY LEU VAL          
SEQRES   2 m  174  MET GLY PHE VAL GLY PHE SER SER LYS PRO SER PRO ILE          
SEQRES   3 m  174  TYR GLY GLY LEU VAL LEU ILE VAL SER GLY VAL VAL GLY          
SEQRES   4 m  174  CYS VAL ILE ILE LEU ASN PHE GLY GLY GLY TYR MET GLY          
SEQRES   5 m  174  LEU MET VAL PHE LEU ILE TYR LEU GLY GLY MET MET VAL          
SEQRES   6 m  174  VAL PHE GLY TYR THR THR ALA MET ALA ILE GLU GLU TYR          
SEQRES   7 m  174  PRO GLU ALA TRP GLY SER GLY VAL GLU VAL LEU VAL SER          
SEQRES   8 m  174  VAL LEU VAL GLY LEU ALA MET GLU VAL GLY LEU VAL LEU          
SEQRES   9 m  174  TRP VAL LYS GLU TYR ASP GLY VAL VAL VAL VAL VAL ASN          
SEQRES  10 m  174  PHE ASN SER VAL GLY SER TRP MET ILE TYR GLU GLY GLU          
SEQRES  11 m  174  GLY SER GLY PHE ILE ARG GLU ASP PRO ILE GLY ALA GLY          
SEQRES  12 m  174  ALA LEU TYR ASP TYR GLY ARG TRP LEU VAL VAL VAL THR          
SEQRES  13 m  174  GLY TRP THR LEU PHE VAL GLY VAL TYR ILE VAL ILE GLU          
SEQRES  14 m  174  ILE ALA ARG GLY ASN                                          
SEQRES   1 n   56  ASN LEU LEU GLN ILE VAL ARG ASP HIS TRP VAL HIS VAL          
SEQRES   2 n   56  LEU VAL PRO MET GLY PHE VAL ILE GLY CYS TYR LEU ASP          
SEQRES   3 n   56  ARG LYS SER ASP GLU ARG LEU THR ALA PHE ARG ASN LYS          
SEQRES   4 n   56  SER MET LEU PHE LYS ARG GLU LEU GLN PRO SER GLU GLU          
SEQRES   5 n   56  VAL THR TRP LYS                                              
SEQRES   1 o  128  SER PHE PRO LYS TYR LYS PRO SER SER LEU ARG THR LEU          
SEQRES   2 o  128  PRO GLU THR LEU ASP PRO ALA GLU TYR ASN ILE SER PRO          
SEQRES   3 o  128  GLU THR ARG ARG ALA GLN ALA GLU ARG LEU ALA ILE ARG          
SEQRES   4 o  128  ALA GLN LEU LYS ARG GLU TYR LEU LEU GLN TYR ASN ASP          
SEQRES   5 o  128  PRO ASN ARG ARG GLY LEU ILE GLU ASN PRO ALA LEU LEU          
SEQRES   6 o  128  ARG TRP ALA TYR ALA ARG THR ILE ASN VAL TYR PRO ASN          
SEQRES   7 o  128  PHE ARG PRO THR PRO LYS ASN SER LEU MET GLY ALA LEU          
SEQRES   8 o  128  CYS GLY PHE GLY PRO LEU ILE PHE ILE TYR TYR ILE ILE          
SEQRES   9 o  128  LYS THR GLU ARG ASP ARG LYS GLU LYS LEU ILE GLN GLU          
SEQRES  10 o  128  GLY LYS LEU ASP ARG THR PHE HIS LEU SER TYR                  
SEQRES   1 p  172  PRO TYR LEU THR HIS GLN GLN LYS VAL LEU ARG LEU TYR          
SEQRES   2 p  172  LYS ARG ALA LEU ARG HIS LEU GLU SER TRP CYS VAL GLN          
SEQRES   3 p  172  ARG ASP LYS TYR ARG TYR PHE ALA CYS LEU MET ARG ALA          
SEQRES   4 p  172  ARG PHE GLU GLU HIS LYS ASN GLU LYS ASP MET ALA LYS          
SEQRES   5 p  172  ALA THR GLN LEU LEU LYS GLU ALA GLU GLU GLU PHE TRP          
SEQRES   6 p  172  TYR ARG GLN HIS PRO GLN PRO TYR ILE PHE PRO ASP SER          
SEQRES   7 p  172  PRO GLY GLY THR SER TYR GLU ARG TYR ASP CYS TYR LYS          
SEQRES   8 p  172  VAL PRO GLU TRP CYS LEU ASP ASP TRP HIS PRO SER GLU          
SEQRES   9 p  172  LYS ALA MET TYR PRO ASP TYR PHE ALA LYS ARG GLU GLN          
SEQRES  10 p  172  TRP LYS LYS LEU ARG ARG GLU SER TRP GLU ARG GLU VAL          
SEQRES  11 p  172  LYS GLN LEU GLN GLU GLU THR PRO PRO GLY GLY PRO LEU          
SEQRES  12 p  172  THR GLU ALA LEU PRO PRO ALA ARG LYS GLU GLY ASP LEU          
SEQRES  13 p  172  PRO PRO LEU TRP TRP TYR ILE VAL THR ARG PRO ARG GLU          
SEQRES  14 p  172  ARG PRO MET                                                  
SEQRES   1 r  459  MET LEU LYS LEU ILE VAL PRO THR ILE MET LEU LEU PRO          
SEQRES   2 r  459  LEU THR TRP LEU SER LYS LYS HIS MET ILE TRP ILE ASN          
SEQRES   3 r  459  THR THR THR HIS SER LEU ILE ILE SER ILE ILE PRO LEU          
SEQRES   4 r  459  LEU PHE PHE ASN GLN ILE ASN ASN ASN LEU PHE SER CYS          
SEQRES   5 r  459  SER LEU THR PHE SER SER ASP PRO LEU THR THR PRO LEU          
SEQRES   6 r  459  LEU MET LEU THR THR TRP LEU LEU PRO LEU THR ILE MET          
SEQRES   7 r  459  ALA SER GLN ARG HIS LEU SER SER GLU PRO LEU SER ARG          
SEQRES   8 r  459  LYS LYS LEU TYR LEU SER MET LEU ILE PHE LEU GLN ILE          
SEQRES   9 r  459  SER LEU ILE MET THR PHE THR ALA THR GLU LEU ILE MET          
SEQRES  10 r  459  PHE TYR ILE PHE PHE GLU THR THR LEU ILE PRO THR LEU          
SEQRES  11 r  459  ALA ILE ILE THR ARG TRP GLY ASN GLN PRO GLU ARG LEU          
SEQRES  12 r  459  ASN ALA GLY THR TYR PHE LEU PHE TYR THR LEU VAL GLY          
SEQRES  13 r  459  SER LEU PRO LEU LEU ILE ALA LEU ILE TYR THR HIS ASN          
SEQRES  14 r  459  THR LEU GLY SER LEU ASN ILE LEU LEU LEU THR LEU THR          
SEQRES  15 r  459  ALA GLN GLU LEU SER ASN SER TRP ALA ASN ASN LEU MET          
SEQRES  16 r  459  TRP LEU ALA TYR THR MET ALA PHE MET VAL LYS MET PRO          
SEQRES  17 r  459  LEU TYR GLY LEU HIS LEU TRP LEU PRO LYS ALA HIS VAL          
SEQRES  18 r  459  GLU ALA PRO ILE ALA GLY SER MET VAL LEU ALA ALA VAL          
SEQRES  19 r  459  LEU LEU LYS LEU GLY GLY TYR GLY MET MET ARG LEU THR          
SEQRES  20 r  459  LEU ILE LEU ASN PRO LEU THR LYS HIS MET ALA TYR PRO          
SEQRES  21 r  459  PHE LEU VAL LEU SER LEU TRP GLY MET ILE MET THR SER          
SEQRES  22 r  459  SER ILE CYS LEU ARG GLN THR ASP LEU LYS SER LEU ILE          
SEQRES  23 r  459  ALA TYR SER SER ILE SER HIS MET ALA LEU VAL VAL THR          
SEQRES  24 r  459  ALA ILE LEU ILE GLN THR PRO TRP SER PHE THR GLY ALA          
SEQRES  25 r  459  VAL ILE LEU MET ILE ALA HIS GLY LEU THR SER SER LEU          
SEQRES  26 r  459  LEU PHE CYS LEU ALA ASN SER ASN TYR GLU ARG THR HIS          
SEQRES  27 r  459  SER ARG ILE MET ILE LEU SER GLN GLY LEU GLN THR LEU          
SEQRES  28 r  459  LEU PRO LEU MET ALA PHE TRP TRP LEU LEU ALA SER LEU          
SEQRES  29 r  459  ALA ASN LEU ALA LEU PRO PRO THR ILE ASN LEU LEU GLY          
SEQRES  30 r  459  GLU LEU SER VAL LEU VAL THR THR PHE SER TRP SER ASN          
SEQRES  31 r  459  ILE THR LEU LEU LEU THR GLY LEU ASN MET LEU VAL THR          
SEQRES  32 r  459  ALA LEU TYR SER LEU TYR MET PHE THR THR THR GLN TRP          
SEQRES  33 r  459  GLY SER LEU THR HIS HIS ILE ASN ASN MET LYS PRO SER          
SEQRES  34 r  459  PHE THR ARG GLU ASN THR LEU MET PHE MET HIS LEU SER          
SEQRES  35 r  459  PRO ILE LEU LEU LEU SER LEU ASN PRO ASP ILE ILE THR          
SEQRES  36 r  459  GLY PHE SER SER                                              
SEQRES   1 s  318  MET PRO MET ALA ASN LEU LEU LEU LEU ILE VAL PRO ILE          
SEQRES   2 s  318  LEU ILE ALA MET ALA PHE LEU MET LEU THR GLU ARG LYS          
SEQRES   3 s  318  ILE LEU GLY TYR MET GLN LEU ARG LYS GLY PRO ASN VAL          
SEQRES   4 s  318  VAL GLY PRO TYR GLY LEU LEU GLN PRO PHE ALA ASP ALA          
SEQRES   5 s  318  MET LYS LEU PHE THR LYS GLU PRO LEU LYS PRO ALA THR          
SEQRES   6 s  318  SER THR ILE THR LEU TYR ILE THR ALA PRO THR LEU ALA          
SEQRES   7 s  318  LEU THR ILE ALA LEU LEU LEU TRP THR PRO LEU PRO MET          
SEQRES   8 s  318  PRO ASN PRO LEU VAL ASN LEU ASN LEU GLY LEU LEU PHE          
SEQRES   9 s  318  ILE LEU ALA THR SER SER LEU ALA VAL TYR SER ILE LEU          
SEQRES  10 s  318  TRP SER GLY TRP ALA SER ASN SER ASN TYR ALA LEU ILE          
SEQRES  11 s  318  GLY ALA LEU ARG ALA VAL ALA GLN THR ILE SER TYR GLU          
SEQRES  12 s  318  VAL THR LEU ALA ILE ILE LEU LEU SER THR LEU LEU MET          
SEQRES  13 s  318  SER GLY SER PHE ASN LEU SER THR LEU ILE THR THR GLN          
SEQRES  14 s  318  GLU HIS LEU TRP LEU LEU LEU PRO SER TRP PRO LEU ALA          
SEQRES  15 s  318  MET MET TRP PHE ILE SER THR LEU ALA GLU THR ASN ARG          
SEQRES  16 s  318  ALA PRO PHE ASP LEU ALA GLU GLY GLU SER GLU LEU VAL          
SEQRES  17 s  318  SER GLY PHE ASN ILE GLU TYR ALA ALA GLY PRO PHE ALA          
SEQRES  18 s  318  LEU PHE PHE MET ALA GLU TYR THR ASN ILE ILE MET MET          
SEQRES  19 s  318  ASN THR LEU THR THR THR ILE PHE LEU GLY THR THR TYR          
SEQRES  20 s  318  ASP ALA LEU SER PRO GLU LEU TYR THR THR TYR PHE VAL          
SEQRES  21 s  318  THR LYS THR LEU LEU LEU THR SER LEU PHE LEU TRP ILE          
SEQRES  22 s  318  ARG THR ALA TYR PRO ARG PHE ARG TYR ASP GLN LEU MET          
SEQRES  23 s  318  HIS LEU LEU TRP LYS ASN PHE LEU PRO LEU THR LEU ALA          
SEQRES  24 s  318  LEU LEU MET TRP HIS VAL SER MET PRO ILE THR ILE SER          
SEQRES  25 s  318  SER ILE PRO PRO GLN THR                                      
SEQRES   1 u  169  ILE VAL GLU LEU PRO THR LEU GLU GLU LEU LYS VAL ASP          
SEQRES   2 u  169  GLU VAL LYS ILE SER SER ALA VAL LEU LYS ALA ALA ALA          
SEQRES   3 u  169  HIS HIS TYR GLY ALA GLN CYS ASP LYS PRO ASN LYS GLU          
SEQRES   4 u  169  PHE MET LEU CYS ARG TRP GLU GLU LYS ASP PRO ARG ARG          
SEQRES   5 u  169  CYS LEU GLU GLU GLY LYS LEU VAL ASN LYS CYS ALA LEU          
SEQRES   6 u  169  ASP PHE PHE ARG GLN ILE LYS ARG HIS CYS ALA GLU PRO          
SEQRES   7 u  169  PHE THR GLU TYR TRP THR CYS ILE ASP TYR THR GLY GLN          
SEQRES   8 u  169  GLN LEU PHE ARG HIS CYS ARG LYS GLN GLN ALA LYS PHE          
SEQRES   9 u  169  ASP GLU CYS VAL LEU ASP LYS LEU GLY TRP VAL ARG PRO          
SEQRES  10 u  169  ASP LEU GLY GLU LEU SER LYS VAL THR LYS VAL LYS THR          
SEQRES  11 u  169  ASP ARG PRO LEU PRO GLU ASN PRO TYR HIS SER ARG PRO          
SEQRES  12 u  169  ARG PRO ASP PRO SER PRO GLU ILE GLU GLY ASP LEU GLN          
SEQRES  13 u  169  PRO ALA THR HIS GLY SER ARG PHE TYR PHE TRP THR LYS          
SEQRES   1 v  137  MET GLY ALA HIS LEU VAL ARG ARG TYR LEU GLY ASP ALA          
SEQRES   2 v  137  SER VAL GLU PRO ASP PRO LEU GLN MET PRO THR PHE PRO          
SEQRES   3 v  137  PRO ASP TYR GLY PHE PRO GLU ARG LYS GLU ARG GLU MET          
SEQRES   4 v  137  VAL ALA THR GLN GLN GLU MET MET ASP ALA GLN LEU ARG          
SEQRES   5 v  137  LEU GLN LEU ARG ASP TYR CYS ALA HIS HIS LEU ILE ARG          
SEQRES   6 v  137  LEU LEU LYS CYS LYS ARG ASP SER PHE PRO ASN PHE LEU          
SEQRES   7 v  137  ALA CYS LYS GLN GLU ARG HIS ASP TRP ASP TYR CYS GLU          
SEQRES   8 v  137  HIS ARG ASP TYR VAL MET ARG MET LYS GLU PHE GLU ARG          
SEQRES   9 v  137  GLU ARG ARG LEU LEU GLN ARG LYS LYS ARG ARG GLU LYS          
SEQRES  10 v  137  LYS ALA ALA GLU LEU ALA LYS GLY GLN GLY PRO GLY GLU          
SEQRES  11 v  137  VAL ASP PRO LYS VAL ALA LEU                                  
SEQRES   1 w  320  LEU ARG TYR GLY MET TRP HIS PHE LEU LEU GLY ASP LYS          
SEQRES   2 w  320  ALA SER LYS ARG LEU THR GLU ARG SER ARG VAL ILE THR          
SEQRES   3 w  320  VAL ASP GLY ASN ILE CYS THR GLY LYS GLY LYS LEU ALA          
SEQRES   4 w  320  LYS GLU ILE ALA GLU LYS LEU GLY PHE LYS HIS PHE PRO          
SEQRES   5 w  320  GLU ALA GLY ILE HIS TYR PRO ASP SER THR THR GLY ASP          
SEQRES   6 w  320  GLY LYS PRO LEU ALA THR ASP TYR ASN GLY ASN CYS SER          
SEQRES   7 w  320  LEU GLU LYS PHE TYR ASP ASP PRO ARG SER ASN ASP GLY          
SEQRES   8 w  320  ASN SER TYR ARG LEU GLN SER TRP LEU TYR SER SER ARG          
SEQRES   9 w  320  LEU LEU GLN TYR SER ASP ALA LEU GLU HIS LEU LEU THR          
SEQRES  10 w  320  THR GLY GLN GLY VAL VAL LEU GLU ARG SER ILE PHE SER          
SEQRES  11 w  320  ASP PHE VAL PHE LEU GLU ALA MET TYR ASN GLN GLY PHE          
SEQRES  12 w  320  ILE ARG LYS GLN CYS VAL ASP HIS TYR ASN GLU VAL LYS          
SEQRES  13 w  320  SER VAL THR ILE CYS ASP TYR LEU PRO PRO HIS LEU VAL          
SEQRES  14 w  320  ILE TYR ILE ASP VAL PRO VAL PRO GLU VAL GLN ARG ARG          
SEQRES  15 w  320  ILE GLN LYS LYS GLY ASP PRO HIS GLU MET LYS ILE THR          
SEQRES  16 w  320  SER ALA TYR LEU GLN ASP ILE GLU ASN ALA TYR LYS LYS          
SEQRES  17 w  320  THR PHE LEU PRO GLU MET SER GLU LYS CYS GLU VAL LEU          
SEQRES  18 w  320  GLN TYR SER ALA ARG GLU ALA GLN ASP SER LYS LYS VAL          
SEQRES  19 w  320  VAL GLU ASP ILE GLU TYR LEU LYS PHE ASP LYS GLY PRO          
SEQRES  20 w  320  TRP LEU LYS GLN ASP ASN ARG THR LEU TYR HIS LEU ARG          
SEQRES  21 w  320  LEU LEU VAL GLN ASP LYS PHE GLU VAL LEU ASN TYR THR          
SEQRES  22 w  320  SER ILE PRO ILE PHE LEU PRO GLU VAL THR ILE GLY ALA          
SEQRES  23 w  320  HIS GLN THR ASP ARG VAL LEU HIS GLN PHE ARG GLU LEU          
SEQRES  24 w  320  PRO GLY ARG LYS TYR SER PRO GLY TYR ASN THR GLU VAL          
SEQRES  25 w  320  GLY ASP LYS TRP ILE TRP LEU LYS                              
HET    SF4  A 501       8                                                       
HET    FMN  A 502      31                                                       
HET    SF4  B 301       8                                                       
HET    SF4  B 302       8                                                       
HET    PLX  B 303      52                                                       
HET    SF4  C 301       8                                                       
HET    8Q1  E 201      35                                                       
HET    NDP  J 401      48                                                       
HET    SF4  M 801       8                                                       
HET    SF4  M 802       8                                                       
HET    FES  M 803       4                                                       
HET    FES  O 301       4                                                       
HET    PLX  U 101      52                                                       
HET    CDL  V 201      63                                                       
HET    PEE  V 202      51                                                       
HET    PLX  V 203      52                                                       
HET    PEE  W 201      51                                                       
HET    PLX  b 201      52                                                       
HET    PLX  g 201      52                                                       
HET    PLX  g 202      52                                                       
HET    PLX  g 203      52                                                       
HET    CDL  i 401      64                                                       
HET    PEE  l 701      49                                                       
HET    PEE  l 702      51                                                       
HET    CDL  l 703      64                                                       
HET    CDL  l 704      64                                                       
HET    CDL  n 101      64                                                       
HET    8Q1  p 201      35                                                       
HET    PLX  r 501      52                                                       
HET    PLX  r 502      52                                                       
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     FMN FLAVIN MONONUCLEOTIDE                                            
HETNAM     PLX (9R,11S)-9-({[(1S)-1-HYDROXYHEXADECYL]OXY}METHYL)-2,2-           
HETNAM   2 PLX  DIMETHYL-5,7,10-TRIOXA-2LAMBDA~5~-AZA-6LAMBDA~5~-               
HETNAM   3 PLX  PHOSPHAOCTACOSANE-6,6,11-TRIOL                                  
HETNAM     8Q1 S-[2-({N-[(2R)-2-HYDROXY-3,3-DIMETHYL-4-(PHOSPHONOOXY)           
HETNAM   2 8Q1  BUTANOYL]-BETA-ALANYL}AMINO)ETHYL] DODECANETHIOATE              
HETNAM     NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE                  
HETNAM   2 NDP  PHOSPHATE                                                       
HETNAM     FES FE2/S2 (INORGANIC) CLUSTER                                       
HETNAM     CDL CARDIOLIPIN                                                      
HETNAM     PEE 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE                    
HETSYN     FMN RIBOFLAVIN MONOPHOSPHATE                                         
HETSYN     8Q1 S-DODECANOYL-4'-PHOSPHOPANTETHEINE                               
HETSYN     CDL DIPHOSPHATIDYL GLYCEROL; BIS-(1,2-DIACYL-SN-GLYCERO-3-           
HETSYN   2 CDL  PHOSPHO)-1',3'-SN-GLYCEROL                                      
HETSYN     PEE DOPE                                                             
FORMUL  46  SF4    6(FE4 S4)                                                    
FORMUL  47  FMN    C17 H21 N4 O9 P                                              
FORMUL  50  PLX    9(C42 H89 N O8 P 1+)                                         
FORMUL  52  8Q1    2(C23 H45 N2 O8 P S)                                         
FORMUL  53  NDP    C21 H30 N7 O17 P3                                            
FORMUL  56  FES    2(FE2 S2)                                                    
FORMUL  59  CDL    5(C81 H156 O17 P2 2-)                                        
FORMUL  60  PEE    4(C41 H83 N O8 P 1+)                                         
HELIX    1 AA1 ARG A   52  ARG A   59  1                                   8    
HELIX    2 AA2 ASP A   74  THR A   82  1                                   9    
HELIX    3 AA3 PRO A   94  PHE A  101  1                                   8    
HELIX    4 AA4 MET A  102  LYS A  104  5                                   3    
HELIX    5 AA5 CYS A  125  ASP A  134  1                                  10    
HELIX    6 AA6 ASP A  134  GLY A  150  1                                  17    
HELIX    7 AA7 TYR A  163  ALA A  179  1                                  17    
HELIX    8 AA8 ALA A  203  GLY A  207  5                                   5    
HELIX    9 AA9 GLU A  208  GLU A  217  1                                  10    
HELIX   10 AB1 GLY A  234  CYS A  238  5                                   5    
HELIX   11 AB2 VAL A  245  ARG A  257  1                                  13    
HELIX   12 AB3 GLY A  258  GLY A  264  1                                   7    
HELIX   13 AB4 PRO A  295  LYS A  302  1                                   8    
HELIX   14 AB5 GLY A  310  ASP A  312  5                                   3    
HELIX   15 AB6 LYS A  329  GLU A  333  1                                   5    
HELIX   16 AB7 ASP A  338  ALA A  345  1                                   8    
HELIX   17 AB8 LEU A  349  THR A  351  5                                   3    
HELIX   18 AB9 ILE A  363  GLU A  377  1                                  15    
HELIX   19 AC1 CYS A  382  GLY A  402  1                                  21    
HELIX   20 AC2 ALA A  407  GLU A  420  1                                  14    
HELIX   21 AC3 ALA A  426  GLN A  455  1                                  30    
HELIX   22 AC4 ASP B   47  TRP B   61  1                                  15    
HELIX   23 AC5 THR B   62  ARG B   77  1                                  16    
HELIX   24 AC6 LEU B  116  CYS B  121  1                                   6    
HELIX   25 AC7 GLY B  154  CYS B  160  1                                   7    
HELIX   26 AC8 THR B  177  GLU B  180  5                                   4    
HELIX   27 AC9 LYS B  185  TRP B  195  1                                  11    
HELIX   28 AD1 TRP B  195  TYR B  207  1                                  13    
HELIX   29 AD2 LEU B  208  ARG B  210  5                                   3    
HELIX   30 AD3 ARG C   59  SER C   77  1                                  19    
HELIX   31 AD4 CYS C   89  ALA C   97  1                                   9    
HELIX   32 AD5 ASP C  102  GLY C  107  5                                   6    
HELIX   33 AD6 MET C  130  MET C  141  1                                  12    
HELIX   34 AD7 MET C  150  GLY C  157  1                                   8    
HELIX   35 AD8 GLY C  158  HIS C  161  5                                   4    
HELIX   36 AD9 GLY C  169  ILE C  173  5                                   5    
HELIX   37 AE1 THR C  186  ARG C  203  1                                  18    
HELIX   38 AE2 ARG C  205  ARG C  212  1                                   8    
HELIX   39 AE3 ASP E   24  ARG E   41  1                                  18    
HELIX   40 AE4 GLU E   42  PHE E   50  1                                   9    
HELIX   41 AE5 THR E   55  PHE E   67  1                                  13    
HELIX   42 AE6 ASP E   75  LYS E   95  1                                  21    
HELIX   43 AE7 GLN E   99  ARG E  105  1                                   7    
HELIX   44 AE8 ASP E  117  GLY E  125  1                                   9    
HELIX   45 AE9 SER F   27  LYS F   39  1                                  13    
HELIX   46 AF1 ARG F   40  ASN F   48  1                                   9    
HELIX   47 AF2 ALA F   70  GLY F   72  5                                   3    
HELIX   48 AF3 SER F   83  VAL F   94  1                                  12    
HELIX   49 AF4 THR G   75  TYR G   90  1                                  16    
HELIX   50 AF5 ASP G  111  GLY G  127  1                                  17    
HELIX   51 AF6 ASP G  132  LEU G  138  1                                   7    
HELIX   52 AF7 CYS G  140  LYS G  152  1                                  13    
HELIX   53 AF8 THR H   19  GLU H   36  1                                  18    
HELIX   54 AF9 ALA H   42  GLU H   62  1                                  21    
HELIX   55 AG1 ASP H   64  LEU H   72  1                                   9    
HELIX   56 AG2 GLU H   79  ARG H   95  1                                  17    
HELIX   57 AG3 GLU H   96  LYS H   98  5                                   3    
HELIX   58 AG4 THR I    5  GLY I   17  1                                  13    
HELIX   59 AG5 TYR I   53  ASP I   58  1                                   6    
HELIX   60 AG6 GLY I   59  SER I   63  5                                   5    
HELIX   61 AG7 GLY J   63  MET J   76  1                                  14    
HELIX   62 AG8 LYS J   88  GLY J   98  5                                  11    
HELIX   63 AG9 ASP J   99  GLY J  101  5                                   3    
HELIX   64 AH1 LYS J  113  VAL J  120  1                                   8    
HELIX   65 AH2 ASP J  140  PHE J  145  1                                   6    
HELIX   66 AH3 VAL J  146  GLY J  160  1                                  15    
HELIX   67 AH4 SER J  178  PHE J  195  1                                  18    
HELIX   68 AH5 ASP J  211  GLY J  224  1                                  14    
HELIX   69 AH6 TYR J  241  ASP J  255  1                                  15    
HELIX   70 AH7 LEU J  272  HIS J  285  1                                  14    
HELIX   71 AH8 PRO J  294  GLU J  306  1                                  13    
HELIX   72 AH9 THR J  315  ILE J  324  1                                  10    
HELIX   73 AI1 GLY J  334  LEU J  338  5                                   5    
HELIX   74 AI2 PRO J  344  LEU J  347  5                                   4    
HELIX   75 AI3 LYS J  348  ARG J  354  1                                   7    
HELIX   76 AI4 THR J  358  SER J  363  1                                   6    
HELIX   77 AI5 ILE J  366  LYS J  370  5                                   5    
HELIX   78 AI6 TYR K   82  LEU K   91  1                                  10    
HELIX   79 AI7 SER K   92  ARG K   95  5                                   4    
HELIX   80 AI8 PRO L   68  ARG L   75  1                                   8    
HELIX   81 AI9 ASP L  119  ASN L  123  5                                   5    
HELIX   82 AJ1 THR L  130  GLY L  142  1                                  13    
HELIX   83 AJ2 TYR L  160  PHE L  164  5                                   5    
HELIX   84 AJ3 THR M   48  GLY M   57  1                                  10    
HELIX   85 AJ4 SER M  106  LEU M  121  1                                  16    
HELIX   86 AJ5 CYS M  137  PHE M  146  1                                  10    
HELIX   87 AJ6 THR M  180  SER M  187  1                                   8    
HELIX   88 AJ7 GLY M  220  CYS M  226  1                                   7    
HELIX   89 AJ8 ARG M  241  THR M  245  5                                   5    
HELIX   90 AJ9 SER M  287  PHE M  292  1                                   6    
HELIX   91 AK1 ALA M  293  ARG M  299  5                                   7    
HELIX   92 AK2 SER M  318  GLN M  331  1                                  14    
HELIX   93 AK3 ASP M  347  VAL M  361  1                                  15    
HELIX   94 AK4 GLY M  393  ALA M  397  5                                   5    
HELIX   95 AK5 ASN M  406  GLU M  410  5                                   5    
HELIX   96 AK6 ALA M  411  HIS M  424  1                                  14    
HELIX   97 AK7 ASP M  447  GLY M  458  1                                  12    
HELIX   98 AK8 HIS M  460  ALA M  469  1                                  10    
HELIX   99 AK9 GLY M  477  GLN M  482  5                                   6    
HELIX  100 AL1 ASP M  485  SER M  504  1                                  20    
HELIX  101 AL2 SER M  521  LEU M  528  1                                   8    
HELIX  102 AL3 VAL M  534  ARG M  538  5                                   5    
HELIX  103 AL4 VAL M  575  ALA M  580  1                                   6    
HELIX  104 AL5 GLU M  618  ALA M  630  1                                  13    
HELIX  105 AL6 THR M  638  GLU M  648  1                                  11    
HELIX  106 AL7 PRO M  651  ARG M  655  5                                   5    
HELIX  107 AL8 PHE M  665  LEU M  674  1                                  10    
HELIX  108 AL9 THR M  690  MET M  696  5                                   7    
HELIX  109 AM1 ASP M  698  SER M  704  1                                   7    
HELIX  110 AM2 SER M  704  GLU M  716  1                                  13    
HELIX  111 AM3 LEU N    3  GLY N   16  1                                  14    
HELIX  112 AM4 LEU N   20  THR N   30  1                                  11    
HELIX  113 AM5 GLU N   67  LYS N   71  5                                   5    
HELIX  114 AM6 PRO N   83  HIS N   91  1                                   9    
HELIX  115 AM7 THR O   56  TYR O   70  1                                  15    
HELIX  116 AM8 HIS O   74  ALA O   77  5                                   4    
HELIX  117 AM9 ALA O   78  GLN O   89  1                                  12    
HELIX  118 AN1 PRO O   94  LEU O  105  1                                  12    
HELIX  119 AN2 PRO O  108  TYR O  119  1                                  12    
HELIX  120 AN3 THR O  137  LEU O  142  1                                   6    
HELIX  121 AN4 ASN O  144  GLY O  157  1                                  14    
HELIX  122 AN5 THR O  197  LYS O  209  1                                  13    
HELIX  123 AN6 ASN P   51  LEU P   69  1                                  19    
HELIX  124 AN7 HIS P   89  ASP P   91  5                                   3    
HELIX  125 AN8 GLY P   92  ASP P  102  1                                  11    
HELIX  126 AN9 LYS P  161  ALA P  163  5                                   3    
HELIX  127 AO1 ASN P  164  MET P  173  1                                  10    
HELIX  128 AO2 ASP Q   40  GLY Q   49  1                                  10    
HELIX  129 AO3 VAL Q   69  THR Q   75  1                                   7    
HELIX  130 AO4 GLY Q  119  TYR Q  126  1                                   8    
HELIX  131 AO5 THR Q  128  LEU Q  133  1                                   6    
HELIX  132 AO6 LEU Q  133  ARG Q  138  1                                   6    
HELIX  133 AO7 MET Q  144  LEU Q  159  1                                  16    
HELIX  134 AO8 PRO Q  164  LEU Q  194  1                                  31    
HELIX  135 AO9 MET Q  197  GLY Q  219  1                                  23    
HELIX  136 AP1 GLY Q  239  ASN Q  250  1                                  12    
HELIX  137 AP2 ASN Q  250  GLU Q  260  1                                  11    
HELIX  138 AP3 ASN Q  265  ILE Q  273  1                                   9    
HELIX  139 AP4 THR Q  279  GLY Q  287  1                                   9    
HELIX  140 AP5 GLY Q  290  GLY Q  295  1                                   6    
HELIX  141 AP6 ASP Q  309  GLN Q  313  5                                   5    
HELIX  142 AP7 ASP Q  325  LYS Q  350  1                                  26    
HELIX  143 AP8 LYS Q  367  LYS Q  372  1                                   6    
HELIX  144 AP9 SER Q  374  TYR Q  385  1                                  12    
HELIX  145 AQ1 ALA Q  426  LYS Q  440  1                                  15    
HELIX  146 AQ2 MET Q  443  GLN Q  454  1                                  12    
HELIX  147 AQ3 VAL Q  457  ASP Q  462  1                                   6    
HELIX  148 AQ4 MET S    1  PHE S    3  5                                   3    
HELIX  149 AQ5 GLU S    4  LEU S   16  1                                  13    
HELIX  150 AQ6 LEU S   16  ASN S   31  1                                  16    
HELIX  151 AQ7 PHE S   41  GLY S   56  1                                  16    
HELIX  152 AQ8 GLY S   65  ASP S   70  5                                   6    
HELIX  153 AQ9 ASP T   50  VAL T   57  5                                   8    
HELIX  154 AR1 PHE T   67  GLN T   75  1                                   9    
HELIX  155 AR2 ALA U    3  TRP U   13  1                                  11    
HELIX  156 AR3 GLU U   16  SER U   36  1                                  21    
HELIX  157 AR4 TYR U   38  THR U   49  1                                  12    
HELIX  158 AR5 LEU U   78  LEU U   84  1                                   7    
HELIX  159 AR6 PRO V    3  ASP V   11  1                                   9    
HELIX  160 AR7 ASP V   17  ASN V   44  1                                  28    
HELIX  161 AR8 THR V   48  GLU V   82  1                                  35    
HELIX  162 AR9 PRO V   87  HIS V  106  1                                  20    
HELIX  163 AS1 ASN V  107  GLY V  132  1                                  26    
HELIX  164 AS2 SER W   34  ALA W   70  1                                  37    
HELIX  165 AS3 LEU W   71  LYS W   99  1                                  29    
HELIX  166 AS4 LEU W  120  TYR W  125  1                                   6    
HELIX  167 AS5 THR W  129  GLY W  139  1                                  11    
HELIX  168 AS6 THR X   75  TYR X   90  1                                  16    
HELIX  169 AS7 LEU X  110  GLY X  127  1                                  18    
HELIX  170 AS8 PRO X  131  GLU X  136  1                                   6    
HELIX  171 AS9 CYS X  140  LYS X  152  1                                  13    
HELIX  172 AT1 THR Y   51  ASP Y   76  1                                  26    
HELIX  173 AT2 ASP Z   18  TRP Z   22  5                                   5    
HELIX  174 AT3 THR Z   27  LYS Z   39  1                                  13    
HELIX  175 AT4 TRP Z   45  MET Z   54  1                                  10    
HELIX  176 AT5 SER Z   62  PHE Z   68  1                                   7    
HELIX  177 AT6 GLY Z   70  GLU Z   89  1                                  20    
HELIX  178 AT7 ARG a   61  THR a   78  1                                  18    
HELIX  179 AT8 GLY a   79  PHE a   92  1                                  14    
HELIX  180 AT9 GLU a  108  TYR a  113  5                                   6    
HELIX  181 AU1 HIS a  115  PHE a  125  1                                  11    
HELIX  182 AU2 SER a  128  GLY a  164  1                                  37    
HELIX  183 AU3 ASP a  175  ILE a  179  5                                   5    
HELIX  184 AU4 THR b    5  GLN b   26  1                                  22    
HELIX  185 AU5 MET b   40  ASN b   48  1                                   9    
HELIX  186 AU6 ASN b   48  ASN b   53  1                                   6    
HELIX  187 AU7 SER b   55  VAL b   75  1                                  21    
HELIX  188 AU8 VAL b   75  LYS b   93  1                                  19    
HELIX  189 AU9 THR c   44  TYR c   55  1                                  12    
HELIX  190 AV1 SER c   82  ARG c   86  5                                   5    
HELIX  191 AV2 LEU c  109  ASN c  113  5                                   5    
HELIX  192 AV3 SER c  125  TYR c  150  1                                  26    
HELIX  193 AV4 TYR c  161  TYR c  167  1                                   7    
HELIX  194 AV5 LEU c  168  ARG c  170  5                                   3    
HELIX  195 AV6 PRO d    2  LYS d    7  5                                   6    
HELIX  196 AV7 PRO d   21  VAL d   35  1                                  15    
HELIX  197 AV8 VAL d   35  ASN d   53  1                                  19    
HELIX  198 AV9 ASP d   67  CYS d   71  5                                   5    
HELIX  199 AW1 ILE d   76  GLU d  111  1                                  36    
HELIX  200 AW2 TYR d  115  TYR d  137  1                                  23    
HELIX  201 AW3 SER d  145  THR d  171  1                                  27    
HELIX  202 AW4 ASN e   65  ASN e   70  1                                   6    
HELIX  203 AW5 ASP e   79  GLY e   94  1                                  16    
HELIX  204 AW6 ILE e   97  TYR e  108  1                                  12    
HELIX  205 AW7 MET e  114  GLY e  133  1                                  20    
HELIX  206 AW8 GLU f   33  ALA f   37  5                                   5    
HELIX  207 AW9 TRP f   41  ASN f   73  1                                  33    
HELIX  208 AX1 PRO g   14  LEU g   20  5                                   7    
HELIX  209 AX2 ASP g   27  ARG g   48  1                                  22    
HELIX  210 AX3 GLY g   56  HIS g   96  1                                  41    
HELIX  211 AX4 PRO g   97  PHE g  100  5                                   4    
HELIX  212 AX5 ASP h    5  PHE h   10  1                                   6    
HELIX  213 AX6 ASP h   15  THR h   19  5                                   5    
HELIX  214 AX7 GLN h   25  MET h   29  5                                   5    
HELIX  215 AX8 HIS h   34  ALA h   44  1                                  11    
HELIX  216 AX9 ARG h   51  CYS h   56  1                                   6    
HELIX  217 AY1 CYS h   56  ARG h   69  1                                  14    
HELIX  218 AY2 ARG h   69  LYS h   85  1                                  17    
HELIX  219 AY3 ALA i    5  SER i   23  1                                  19    
HELIX  220 AY4 HIS i   25  THR i   45  1                                  21    
HELIX  221 AY5 ASN i   49  SER i   81  1                                  33    
HELIX  222 AY6 GLN i   92  LEU i  106  1                                  15    
HELIX  223 AY7 PHE i  111  PHE i  113  5                                   3    
HELIX  224 AY8 TRP i  114  THR i  122  1                                   9    
HELIX  225 AY9 PRO i  123  THR i  132  1                                  10    
HELIX  226 AZ1 LYS i  135  ILE i  145  1                                  11    
HELIX  227 AZ2 SER i  146  LEU i  149  5                                   4    
HELIX  228 AZ3 ASN i  150  LEU i  170  1                                  21    
HELIX  229 AZ4 GLN i  174  LEU i  194  1                                  21    
HELIX  230 AZ5 PRO i  198  SER i  223  1                                  26    
HELIX  231 AZ6 THR i  226  SER i  231  1                                   6    
HELIX  232 AZ7 ARG i  232  ASN i  235  5                                   4    
HELIX  233 AZ8 LEU i  237  THR i  241  5                                   5    
HELIX  234 AZ9 PRO i  242  GLY i  252  1                                  11    
HELIX  235 BA1 GLY i  259  LYS i  272  1                                  14    
HELIX  236 BA2 LEU i  276  SER i  299  1                                  24    
HELIX  237 BA3 ASN i  310  TRP i  315  5                                   6    
HELIX  238 BA4 PHE i  325  THR i  334  1                                  10    
HELIX  239 BA5 LEU i  336  PRO i  338  5                                   3    
HELIX  240 BA6 ILE i  339  LEU i  347  1                                   9    
HELIX  241 BA7 ASN j    2  TRP j   23  1                                  22    
HELIX  242 BA8 MET j   53  LEU j   73  1                                  21    
HELIX  243 BA9 PRO j   74  LEU j   79  1                                   6    
HELIX  244 BB1 ASN j   83  GLN j  108  1                                  26    
HELIX  245 BB2 PRO k    2  TYR k   22  1                                  21    
HELIX  246 BB3 LEU k   26  THR k   51  1                                  26    
HELIX  247 BB4 LEU k   54  ALA k   56  5                                   3    
HELIX  248 BB5 ASN k   57  TYR k   85  1                                  29    
HELIX  249 BB6 THR l    2  SER l   14  1                                  13    
HELIX  250 BB7 ILE l   16  ASN l   25  1                                  10    
HELIX  251 BB8 ASN l   30  LEU l   57  1                                  28    
HELIX  252 BB9 ASP l   83  MET l  108  1                                  26    
HELIX  253 BC1 ASN l  113  ALA l  134  1                                  22    
HELIX  254 BC2 ASN l  136  SER l  156  1                                  21    
HELIX  255 BC3 ARG l  161  ASN l  194  1                                  34    
HELIX  256 BC4 ASP l  197  ASN l  205  1                                   9    
HELIX  257 BC5 SER l  209  SER l  224  1                                  16    
HELIX  258 BC6 GLN l  226  HIS l  230  5                                   5    
HELIX  259 BC7 LEU l  233  MET l  237  5                                   5    
HELIX  260 BC8 PRO l  240  HIS l  248  1                                   9    
HELIX  261 BC9 VAL l  254  PHE l  263  1                                  10    
HELIX  262 BD1 PHE l  263  GLU l  268  1                                   6    
HELIX  263 BD2 ASN l  270  LEU l  293  1                                  24    
HELIX  264 BD3 ASP l  297  ILE l  319  1                                  23    
HELIX  265 BD4 GLN l  321  LEU l  350  1                                  30    
HELIX  266 BD5 ASP l  355  MET l  359  5                                   5    
HELIX  267 BD6 MET l  366  GLY l  382  1                                  17    
HELIX  268 BD7 SER l  391  SER l  402  1                                  12    
HELIX  269 BD8 ALA l  406  LEU l  431  1                                  26    
HELIX  270 BD9 LEU l  451  ILE l  472  1                                  22    
HELIX  271 BE1 PRO l  483  ASN l  509  1                                  27    
HELIX  272 BE2 LEU l  517  MET l  525  1                                   9    
HELIX  273 BE3 PHE l  528  ASN l  547  1                                  20    
HELIX  274 BE4 THR l  556  LEU l  562  1                                   7    
HELIX  275 BE5 PRO l  563  THR l  577  1                                  15    
HELIX  276 BE6 MET l  583  LEU l  600  1                                  18    
HELIX  277 BE7 TYR m    3  SER m   20  1                                  18    
HELIX  278 BE8 SER m   24  ASN m   45  1                                  22    
HELIX  279 BE9 GLY m   48  TYR m   59  1                                  12    
HELIX  280 BF1 GLY m   62  ALA m   72  1                                  11    
HELIX  281 BF2 MET m   73  ILE m   75  5                                   3    
HELIX  282 BF3 GLY m   85  ASP m  110  1                                  26    
HELIX  283 BF4 GLY m  111  VAL m  113  5                                   3    
HELIX  284 BF5 ARG m  136  ALA m  144  1                                   9    
HELIX  285 BF6 GLY m  149  ARG m  172  1                                  24    
HELIX  286 BF7 LEU n    4  VAL n    8  1                                   5    
HELIX  287 BF8 ARG n    9  HIS n   14  5                                   6    
HELIX  288 BF9 VAL n   15  LEU n   35  1                                  21    
HELIX  289 BG1 THR n   36  ARG n   39  5                                   4    
HELIX  290 BG2 PRO o   15  TYR o   23  5                                   9    
HELIX  291 BG3 SER o   26  ASP o   53  1                                  28    
HELIX  292 BG4 ASN o   62  ARG o   72  1                                  11    
HELIX  293 BG5 ASN o   75  PHE o   80  1                                   6    
HELIX  294 BG6 THR o   83  GLU o  118  1                                  36    
HELIX  295 BG7 THR p   11  VAL p   32  1                                  22    
HELIX  296 BG8 GLN p   33  GLU p   50  1                                  18    
HELIX  297 BG9 MET p   57  ARG p   74  1                                  18    
HELIX  298 BH1 PRO p  100  TRP p  107  5                                   8    
HELIX  299 BH2 HIS p  108  ALA p  113  1                                   6    
HELIX  300 BH3 TYR p  115  THR p  144  1                                  30    
HELIX  301 BH4 TRP p  167  THR p  172  1                                   6    
HELIX  302 BH5 LEU r    2  SER r   18  1                                  17    
HELIX  303 BH6 MET r   22  PHE r   41  1                                  20    
HELIX  304 BH7 LEU r   61  GLN r   81  1                                  21    
HELIX  305 BH8 ARG r   82  LEU r   84  5                                   3    
HELIX  306 BH9 PRO r   88  PHE r  110  1                                  23    
HELIX  307 BI1 GLU r  114  THR r  125  1                                  12    
HELIX  308 BI2 THR r  125  GLY r  137  1                                  13    
HELIX  309 BI3 GLU r  141  LEU r  171  1                                  31    
HELIX  310 BI4 ASN r  175  THR r  182  1                                   8    
HELIX  311 BI5 ASN r  188  MET r  207  1                                  20    
HELIX  312 BI6 LEU r  209  HIS r  213  5                                   5    
HELIX  313 BI7 LEU r  214  ALA r  223  1                                  10    
HELIX  314 BI8 PRO r  224  THR r  247  1                                  24    
HELIX  315 BI9 PRO r  252  ALA r  258  1                                   7    
HELIX  316 BJ1 ALA r  258  LEU r  277  1                                  20    
HELIX  317 BJ2 ASP r  281  GLN r  304  1                                  24    
HELIX  318 BJ3 THR r  305  HIS r  338  1                                  34    
HELIX  319 BJ4 ILE r  341  SER r  345  5                                   5    
HELIX  320 BJ5 GLY r  347  LEU r  351  5                                   5    
HELIX  321 BJ6 LEU r  352  LEU r  367  1                                  16    
HELIX  322 BJ7 THR r  372  SER r  389  1                                  18    
HELIX  323 BJ8 THR r  392  THR r  413  1                                  22    
HELIX  324 BJ9 ILE r  423  LYS r  427  5                                   5    
HELIX  325 BK1 PHE r  430  SER r  448  1                                  19    
HELIX  326 BK2 PRO s    2  GLN s   32  1                                  31    
HELIX  327 BK3 LEU s   46  LYS s   58  1                                  13    
HELIX  328 BK4 THR s   67  LEU s   85  1                                  19    
HELIX  329 BK5 LEU s  100  ALA s  112  1                                  13    
HELIX  330 BK6 ALA s  112  ASN s  124  1                                  13    
HELIX  331 BK7 SER s  125  GLY s  158  1                                  34    
HELIX  332 BK8 ASN s  161  THR s  168  1                                   8    
HELIX  333 BK9 SER s  178  ASN s  194  1                                  17    
HELIX  334 BL1 ARG s  195  ASP s  199  5                                   5    
HELIX  335 BL2 SER s  209  ILE s  213  5                                   5    
HELIX  336 BL3 ALA s  217  LEU s  243  1                                  27    
HELIX  337 BL4 SER s  251  TYR s  277  1                                  27    
HELIX  338 BL5 ARG s  281  TRP s  290  1                                  10    
HELIX  339 BL6 PHE s  293  SER s  312  1                                  20    
HELIX  340 BL7 SER u   21  CYS u   36  1                                  16    
HELIX  341 BL8 CYS u   36  GLU u   49  1                                  14    
HELIX  342 BL9 PRO u   53  ARG u   55  5                                   3    
HELIX  343 BM1 CYS u   56  ARG u   76  1                                  21    
HELIX  344 BM2 ALA u   79  TYR u   91  1                                  13    
HELIX  345 BM3 LEU u   96  CYS u  100  5                                   5    
HELIX  346 BM4 ARG u  101  ASP u  113  1                                  13    
HELIX  347 BM5 HIS v    4  ASP v   12  1                                   9    
HELIX  348 BM6 GLN v   43  GLN v   50  1                                   8    
HELIX  349 BM7 ASP v   57  CYS v   59  5                                   3    
HELIX  350 BM8 ALA v   60  SER v   73  1                                  14    
HELIX  351 BM9 CYS v   80  ALA v  123  1                                  44    
HELIX  352 BN1 GLY w   39  GLY w   46  1                                   8    
HELIX  353 BN2 ALA w   49  LEU w   53  5                                   5    
HELIX  354 BN3 GLY w   71  LEU w   81  1                                  11    
HELIX  355 BN4 HIS w   92  THR w   98  1                                   7    
HELIX  356 BN5 ALA w  105  GLY w  110  1                                   6    
HELIX  357 BN6 SER w  113  ASP w  119  1                                   7    
HELIX  358 BN7 SER w  128  SER w  137  1                                  10    
HELIX  359 BN8 ARG w  139  GLY w  154  1                                  16    
HELIX  360 BN9 SER w  162  SER w  165  5                                   4    
HELIX  361 BO1 ASP w  166  GLN w  176  1                                  11    
HELIX  362 BO2 ARG w  180  ILE w  195  1                                  16    
HELIX  363 BO3 CYS w  196  TYR w  198  5                                   3    
HELIX  364 BO4 PRO w  210  GLY w  222  1                                  13    
HELIX  365 BO5 HIS w  225  ILE w  229  5                                   5    
HELIX  366 BO6 THR w  230  LYS w  252  1                                  23    
HELIX  367 BO7 GLU w  262  VAL w  270  1                                   9    
HELIX  368 BO8 ILE w  273  LYS w  277  5                                   5    
HELIX  369 BO9 ASP w  287  GLN w  299  1                                  13    
HELIX  370 BP1 ASP w  300  ASN w  306  1                                   7    
HELIX  371 BP2 HIS w  322  LEU w  334  1                                  13    
HELIX  372 BP3 LYS w  350  LYS w  355  5                                   6    
SHEET    1 AA1 4 ASP A 194  ARG A 199  0                                        
SHEET    2 AA1 4 ALA A 153  ILE A 158  1  N  ILE A 156   O  VAL A 198           
SHEET    3 AA1 4 VAL A 114  ASN A 116  1  N  VAL A 115   O  TYR A 155           
SHEET    4 AA1 4 VAL A 242  ASN A 244  1  O  ALA A 243   N  ASN A 116           
SHEET    1 AA2 5 CYS A 286  GLU A 291  0                                        
SHEET    2 AA2 5 THR A 273  GLY A 280 -1  N  LYS A 274   O  GLU A 290           
SHEET    3 AA2 5 ALA A 353  ASP A 358  1  O  VAL A 356   N  SER A 279           
SHEET    4 AA2 5 LEU A 314  PRO A 319 -1  N  ILE A 318   O  ILE A 355           
SHEET    5 AA2 5 ILE A 327  PRO A 328 -1  O  ILE A 327   N  VAL A 317           
SHEET    1 AA3 2 TYR B  36  TYR B  38  0                                        
SHEET    2 AA3 2 VAL Q 318  VAL Q 320  1  O  VAL Q 318   N  LYS B  37           
SHEET    1 AA4 2 HIS B  99  LEU B 101  0                                        
SHEET    2 AA4 2 ILE B 165  GLU B 167 -1  O  VAL B 166   N  ALA B 100           
SHEET    1 AA5 2 ALA B 130  PRO B 132  0                                        
SHEET    2 AA5 2 ARG B 138  THR B 140 -1  O  ARG B 139   N  GLU B 131           
SHEET    1 AA6 2 ASP B 144  ASP B 146  0                                        
SHEET    2 AA6 2 LEU B 182  ASN B 184 -1  O  TYR B 183   N  ILE B 145           
SHEET    1 AA7 2 MET C 120  ILE C 121  0                                        
SHEET    2 AA7 2 VAL C 147  VAL C 148  1  O  VAL C 148   N  MET C 120           
SHEET    1 AA8 4 ILE F  53  ARG F  56  0                                        
SHEET    2 AA8 4 ILE F  19  HIS F  22  1  N  ILE F  21   O  LEU F  54           
SHEET    3 AA8 4 LYS F  64  ARG F  68 -1  O  TRP F  66   N  ARG F  20           
SHEET    4 AA8 4 GLU F  74  ASN F  76 -1  O  THR F  75   N  ALA F  67           
SHEET    1 AA9 3 VAL J  55  THR J  57  0                                        
SHEET    2 AA9 3 GLN J  79  TYR J  84  1  O  ILE J  81   N  ALA J  56           
SHEET    3 AA9 3 LEU J 103  GLU J 107  1  O  LEU J 106   N  TYR J  84           
SHEET    1 AB1 3 VAL J 125  VAL J 126  0                                        
SHEET    2 AB1 3 LYS J 163  VAL J 167  1  O  ILE J 165   N  VAL J 126           
SHEET    3 AB1 3 ILE J 199  VAL J 201  1  O  VAL J 201   N  HIS J 166           
SHEET    1 AB2 2 ILE J 226  GLY J 229  0                                        
SHEET    2 AB2 2 PRO J 290  LEU J 293  1  O  PHE J 291   N  ILE J 226           
SHEET    1 AB3 3 VAL L  77  PHE L  80  0                                        
SHEET    2 AB3 3 TRP L  97  PHE L 101 -1  O  LYS L  98   N  PHE L  80           
SHEET    3 AB3 3 VAL L 125  PHE L 128 -1  O  PHE L 128   N  TRP L  97           
SHEET    1 AB4 2 ARG L 106  GLU L 108  0                                        
SHEET    2 AB4 2 ALA L 115  THR L 117 -1  O  SER L 116   N  TRP L 107           
SHEET    1 AB5 3 SER M  40  VAL M  43  0                                        
SHEET    2 AB5 3 ILE M  32  VAL M  36 -1  N  VAL M  34   O  VAL M  41           
SHEET    3 AB5 3 ASN M 101  ILE M 102  1  O  ILE M 102   N  PHE M  35           
SHEET    1 AB6 2 LEU M  79  VAL M  80  0                                        
SHEET    2 AB6 2 VAL M  89  ALA M  90 -1  O  VAL M  89   N  VAL M  80           
SHEET    1 AB7 3 ARG M 246  ILE M 251  0                                        
SHEET    2 AB7 3 ASN M 260  ARG M 266 -1  O  ILE M 261   N  SER M 250           
SHEET    3 AB7 3 GLU M 269  PRO M 275 -1  O  GLU M 269   N  ARG M 266           
SHEET    1 AB8 2 MET M 306  ARG M 308  0                                        
SHEET    2 AB8 2 LEU M 314  TYR M 316 -1  O  THR M 315   N  VAL M 307           
SHEET    1 AB9 3 ALA M 340  ILE M 341  0                                        
SHEET    2 AB9 3 LEU M 545  PHE M 546  1  O  LEU M 545   N  ILE M 341           
SHEET    3 AB9 3 ILE M 567  TYR M 568  1  O  ILE M 567   N  PHE M 546           
SHEET    1 AC1 2 THR M 595  VAL M 597  0                                        
SHEET    2 AC1 2 ALA M 603  GLN M 605 -1  O  GLN M 604   N  TYR M 596           
SHEET    1 AC2 5 VAL P  76  VAL P  78  0                                        
SHEET    2 AC2 5 LEU P  84  CYS P  87 -1  O  GLU P  85   N  GLN P  77           
SHEET    3 AC2 5 SER P 139  LYS P 144  1  O  ARG P 142   N  VAL P  86           
SHEET    4 AC2 5 VAL P 129  SER P 134 -1  N  TYR P 130   O  VAL P 143           
SHEET    5 AC2 5 ASP P 113  THR P 115 -1  N  THR P 115   O  VAL P 129           
SHEET    1 AC3 2 VAL P 208  ASP P 213  0                                        
SHEET    2 AC3 2 ARG P 218  PRO P 223 -1  O  VAL P 220   N  ARG P 211           
SHEET    1 AC4 2 ARG Q  96  GLU Q 100  0                                        
SHEET    2 AC4 2 LYS Q 108  HIS Q 112 -1  O  HIS Q 112   N  ARG Q  96           
SHEET    1 AC5 2 ILE Q 227  ARG Q 228  0                                        
SHEET    2 AC5 2 GLY Q 231  VAL Q 232 -1  O  GLY Q 231   N  ARG Q 228           
SHEET    1 AC6 3 GLY Q 394  ALA Q 402  0                                        
SHEET    2 AC6 3 GLY Q 405  SER Q 413 -1  O  SER Q 413   N  GLY Q 394           
SHEET    3 AC6 3 PRO Q 419  LYS Q 423 -1  O  TYR Q 420   N  VAL Q 412           
SHEET    1 AC7 2 SER T  78  GLU T  79  0                                        
SHEET    2 AC7 2 PHE T 119  ARG T 120  1  O  ARG T 120   N  SER T  78           
SHEET    1 AC8 2 ILE T  85  CYS T  87  0                                        
SHEET    2 AC8 2 VAL T  99  ILE T 101 -1  O  VAL T  99   N  CYS T  87           
SHEET    1 AC9 2 VAL U  57  ARG U  58  0                                        
SHEET    2 AC9 2 LYS u 130  VAL u 131  1  O  VAL u 131   N  VAL U  57           
SHEET    1 AD1 3 ILE b  97  GLU b  99  0                                        
SHEET    2 AD1 3 VAL l  61  ILE l  63 -1  O  ILE l  62   N  VAL b  98           
SHEET    3 AD1 3 PHE l  80  LYS l  81 -1  O  PHE l  80   N  ILE l  63           
SHEET    1 AD2 2 MET i 307  SER i 308  0                                        
SHEET    2 AD2 2 THR w 318  ILE w 319 -1  O  ILE w 319   N  MET i 307           
SHEET    1 AD3 4 LYS w  84  HIS w  85  0                                        
SHEET    2 AD3 4 VAL w 157  LEU w 159  1  O  VAL w 158   N  LYS w  84           
SHEET    3 AD3 4 ILE w  60  ASP w  63  1  N  ILE w  60   O  LEU w 159           
SHEET    4 AD3 4 VAL w 204  TYR w 206  1  O  ILE w 205   N  ASP w  63           
SSBOND   1 CYS V   95    CYS V  115                          1555   1555  2.03  
SSBOND   2 CYS c  144    CYS l  279                          1555   1555  2.05  
SSBOND   3 CYS d  149    CYS e  141                          1555   1555  2.04  
SSBOND   4 CYS h   33    CYS h   66                          1555   1555  2.02  
SSBOND   5 CYS h   43    CYS h   56                          1555   1555  2.03  
SSBOND   6 CYS u   78    CYS u  110                          1555   1555  2.02  
SSBOND   7 CYS v   69    CYS v   80                          1555   1555  1.94  
LINK         NE2 GLN A 381                FE1  SF4 A 501     1555   1555  2.52  
LINK         N   CYS B 114                FE2  SF4 B 301     1555   1555  2.67  
LINK         N   GLY B 154                FE4  SF4 B 302     1555   1555  2.79  
LINK         SG  CYS C  89                FE2  SF4 C 301     1555   1555  2.59  
LINK         NE2 HIS M 124                FE3  SF4 M 801     1555   1555  2.14  
LINK         SG  CYS M 137                FE4  SF4 M 801     1555   1555  2.56  
LINK         SG  CYS M 176                 S3  SF4 M 802     1555   1555  2.15  
LINK         SG  CYS M 176                FE1  SF4 M 802     1555   1555  2.24  
LINK         O   ILE M 177                 N   CYS M 179     1555   1555  1.48  
LINK         O   CYS M 179                FE1  SF4 M 802     1555   1555  2.57  
LINK         SG  CYS O 176                FE2  FES O 301     1555   1555  2.52  
LINK         SG  CYS O 180                FE2  FES O 301     1555   1555  2.61  
LINK         OD2 ASP b 108                 CB  VAL d  19     1555   1555  1.46  
LINK         CE  MET k   1                 ND2 ASN k  50     1555   1555  1.34  
LINK         O   LEU l 186                 CD1 ILE l 190     1555   1555  1.37  
LINK         SG  CYS u  78                 CB  CYS u 110     1555   1555  2.00  
CISPEP   1 TYR B   84    PRO B   85          0        -3.86                     
CISPEP   2 GLU C  143    PRO C  144          0        -0.84                     
CISPEP   3 CYS C  183    PRO C  184          0       -17.99                     
CISPEP   4 TRP H  114    PRO H  115          0         0.63                     
CISPEP   5 SER M  650    PRO M  651          0       -18.82                     
CISPEP   6 ASP M  682    PRO M  683          0        -7.63                     
CISPEP   7 HIS U   69    PRO U   70          0        18.92                     
CISPEP   8 LYS V   83    PRO V   84          0       -12.92                     
CISPEP   9 GLU Y   41    PRO Y   42          0       -14.59                     
CISPEP  10 TYR Y   86    PRO Y   87          0         4.91                     
CISPEP  11 LEU e  134    PRO e  135          0       -14.28                     
CISPEP  12 ALA i  109    PRO i  110          0         3.23                     
CISPEP  13 THR i  323    PRO i  324          0        -1.31                     
CISPEP  14 ASN r  251    PRO r  252          0         3.70                     
CISPEP  15 PRO r  370    PRO r  371          0        -2.91                     
CISPEP  16 GLY s   41    PRO s   42          0       -12.87                     
CISPEP  17 MET s   91    PRO s   92          0       -12.43                     
SITE     1 AC1 10 ILE A 205  PRO A 223  SER A 378  CYS A 379                    
SITE     2 AC1 10 GLN A 381  CYS A 382  CYS A 385  THR A 423                    
SITE     3 AC1 10 ILE A 424  CYS A 425                                          
SITE     1 AC2 11 GLY A  87  ARG A  88  GLY A  89  ASN A 116                    
SITE     2 AC2 11 GLU A 119  GLY A 207  GLU A 208  GLU A 209                    
SITE     3 AC2 11 ALA A 243  ASN A 244  ALA A 426                               
SITE     1 AC3  8 CYS B 111  ALA B 113  CYS B 114  LYS B 115                    
SITE     2 AC3  8 CYS B 117  CYS B 160  ALA B 164  ILE B 165                    
SITE     1 AC4 11 HIS B  99  CYS B 121  PRO B 122  CYS B 150                    
SITE     2 AC4 11 ILE B 151  TYR B 152  CYS B 153  GLY B 154                    
SITE     3 AC4 11 PHE B 155  CYS B 156  GLU B 167                               
SITE     1 AC5 12 THR B  58  TRP B  61  PHE B  65  ARG Q 266                    
SITE     2 AC5 12 ASN Q 270  MET s 183  MET s 184  ILE s 273                    
SITE     3 AC5 12 TYR s 277  PHE s 280  LEU s 288  ASN s 292                    
SITE     1 AC6  9 ALA C  87  CYS C  88  CYS C  89  GLY C 151                    
SITE     2 AC6  9 SER C 152  CYS C 153  CYS C 183  PRO C 184                    
SITE     3 AC6  9 HIS Q 223                                                     
SITE     1 AC7  9 MET E  25  TRP E  39  MET E  66  PHE E  67                    
SITE     2 AC7  9 ASN E  70  VAL E  79  LEU E  82  VAL E  83                    
SITE     3 AC7  9 SER G 112                                                     
SITE     1 AC8 18 GLY J  60  THR J  62  GLY J  63  PHE J  64                    
SITE     2 AC8 18 LEU J  65  ALA J 110  LEU J 129  ILE J 130                    
SITE     3 AC8 18 GLY J 131  ARG J 132  PHE J 145  SER J 168                    
SITE     4 AC8 18 HIS J 169  TYR J 180  LYS J 184  PRO J 203                    
SITE     5 AC8 18 ILE J 206  ARG J 212                                          
SITE     1 AC9  9 HIS M 124  ASP M 127  CYS M 128  CYS M 131                    
SITE     2 AC9  9 GLY M 134  CYS M 137  GLN M 140  VAL M 228                    
SITE     3 AC9  9 GLY M 229                                                     
SITE     1 AD1  9 CYS M 176  ILE M 177  CYS M 179  CYS M 182                    
SITE     2 AD1  9 CYS M 226  PRO M 227  VAL M 228  ALA M 230                    
SITE     3 AD1  9 LEU M 231                                                     
SITE     1 AD2  9 ARG M  62  CYS M  64  TYR M  65  ALA M  72                    
SITE     2 AD2  9 ASN M  74  CYS M  75  MET M  77  CYS M  78                    
SITE     3 AD2  9 CYS M  92                                                     
SITE     1 AD3  9 CYS O 135  THR O 137  PRO O 139  CYS O 140                    
SITE     2 AD3  9 CYS O 176  LEU O 177  GLY O 178  ALA O 179                    
SITE     3 AD3  9 CYS O 180                                                     
SITE     1 AD4  8 ALA U  12  GLU U  16  PHE U  23  GLY U  26                    
SITE     2 AD4  8 TRP j 106  LEU j 107  ASP j 112  PRO s 295                    
SITE     1 AD5 11 THR V  35  TYR V  39  ARG V  40  ASN V  44                    
SITE     2 AD5 11 TYR V  59  THR V  62  PRO i 110  HIS i 112                    
SITE     3 AD5 11 LEU i 160  ILE l 576  THR l 577                               
SITE     1 AD6  5 TRP V 133  LEU i 276  ILE i 277  THR i 284                    
SITE     2 AD6  5 PEE l 701                                                     
SITE     1 AD7  7 TYR V 108  GLY V 109  ALA V 112  LEU l 553                    
SITE     2 AD7  7 PRO o  82  ALA o  91  PHE o  95                               
SITE     1 AD8 12 HIS S  40  PHE W 140  MET W 141  TYR W 143                    
SITE     2 AD8 12 THR W 144  LEU j   7  VAL m  37  LEU m  44                    
SITE     3 AD8 12 PHE m  56  LEU s  77  LEU s  98  PHE s 104                    
SITE     1 AD9  9 THR a  87  ASN a  90  GLN a  95  TYR b  84                    
SITE     2 AD9  9 TYR b  88  GLU b  92  ARG d  43  TYR e 108                    
SITE     3 AD9  9 PLX r 502                                                     
SITE     1 AE1 10 PRO g   9  LEU g  10  PHE g  12  ARG g  77                    
SITE     2 AE1 10 PRO h   2  PHE h   3  THR i 132  TRP i 133                    
SITE     3 AE1 10 TYR i 143  ILE i 346                                          
SITE     1 AE2  4 HIS f  62  LEU g  25  PHE g  35  PHE g  68                    
SITE     1 AE3 10 LYS f  43  THR f  47  ARG g  48  ARG g  50                    
SITE     2 AE3 10 ARG g  59  LEU g  62  TYR g  63  PHE g  67                    
SITE     3 AE3 10 PRO i 324  PHE i 325                                          
SITE     1 AE4  9 LEU g  46  THR i 238  TRP i 239  THR i 241                    
SITE     2 AE4  9 PRO i 242  LEU i 243  TRP r  16  SER r  90                    
SITE     3 AE4  9 LYS r  93                                                     
SITE     1 AE5 11 GLN Q  46  TYR Q  53  PEE V 202  ILE i 285                    
SITE     2 AE5 11 LEU i 288  TYR i 291  ARG i 295  SER l 567                    
SITE     3 AE5 11 GLN l 570  ILE l 571  VAL r 155                               
SITE     1 AE6 11 ARG c 116  THR l 166  GLN l 170  LEU l 173                    
SITE     2 AE6 11 TYR l 174  MET l 533  HIS l 534  ILE l 537                    
SITE     3 AE6 11 PRO l 538  GLY l 541  THR l 544                               
SITE     1 AE7 13 LEU a  68  LEU a  71  ARG a  72  THR l  22                    
SITE     2 AE7 13 LEU l  23  PRO l  26  LYS l  28  GLN l 116                    
SITE     3 AE7 13 LYS l 119  TYR l 120  LEU r 354  PHE r 357                    
SITE     4 AE7 13 LEU r 360                                                     
SITE     1 AE8  6 ASP c 148  SER l 209  THR l 211  LEU l 214                    
SITE     2 AE8  6 LEU l 272  ASN r 390                                          
SITE     1 AE9 11 THR g  26  LEU g  31  TYR g  32  PRO i 338                    
SITE     2 AE9 11 TYR n  26  LYS n  30  ARG n  34  THR r  55                    
SITE     3 AE9 11 PHE r 121  PHE u 169  TRP u 170                               
SITE     1 AF1 15 ASP X 111  SER X 112  LEU X 113  GLN p  13                    
SITE     2 AF1 15 ALA p  23  HIS p  26  LEU p  27  MET p  44                    
SITE     3 AF1 15 ARG p  47  PHE p  48  HIS p  51  LYS p  52                    
SITE     4 AF1 15 GLU p  54  ALA p  60  ARG p  74                               
SITE     1 AF2  7 TYR o 102  ASN r 188  TRP r 190  ASN r 193                    
SITE     2 AF2  7 HIS r 256  MET r 257  PRO r 260                               
SITE     1 AF3  8 PLX b 201  ALA e 107  TYR e 108  ILE l  16                    
SITE     2 AF3  8 LEU r  68  TRP r  71  LEU r 447  ASN r 450                    
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 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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