data_19931 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; DC-SIGN ; _BMRB_accession_number 19931 _BMRB_flat_file_name bmr19931.str _Entry_type original _Submission_date 2014-04-23 _Accession_date 2014-04-23 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; The Dendritic Cell-Specific Intracellular adhesion molecule-3-Grabbing Nonintegrin (DC-SIGN) is a C-type lectin expressed on the surface of antigen presenting dendritic cells. DC-SIGN binds both fucosylated and mannose oligosaccharides. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Pederson Kari . . 2 Prestegard James H. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 122 "13C chemical shifts" 364 "15N chemical shifts" 122 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2014-05-27 original author . stop_ _Original_release_date 2014-05-27 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structural Characterization of the DC-SIGN-LewisX Complex' _Citation_status 'in preparation' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Pederson Kari . . 2 Mitchell Daniel H. . 3 Prestegard James A. . stop_ _Journal_abbreviation Biochemistry _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name DC-SIGN _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label DC-SIGN $DC-SIGN CA_1 $entity_CA CA_2 $entity_CA CA_3 $entity_CA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_DC-SIGN _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common DC-SIGN _Molecular_mass 20097.2 _Mol_thiol_state 'all disulfide bound' loop_ _Biological_function 'Pathogen-recognition receptor expressed on the surface of immature dendritic cells (DCs) and involved in initiation of primary immune response. Thought to mediate the endocytosis of pathogens which are subsequently degraded in lysosomal compartments. The receptor returns to the cell membrane surface and the pathogen-derived antigens are presented to resting T-cells via MHC class II proteins to initiate the adaptive immune response. Probably recognizes in a calcium-dependent manner high mannose N-linked oligosaccharides in a variety of pathogen antigens, including HIV-1 gp120, HIV-2 gp120, SIV gp120, ebolavirus glycoproteins, cytomegalovirus gB, HCV E2, dengue virus gE, Leishmania pifanoi LPG, Lewis-x antigen in Helicobacter pylori LPS, mannose in Klebsiella pneumonae LPS, di-mannose and tri-mannose in Mycobacterium tuberculosis ManLAM and Lewis-x antigen in Schistosoma mansoni SEA.' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 177 _Mol_residue_sequence ; MGSSHHHHHHSSGLVPRGSH MAERLCHPCPWEWTFFQGNC YFMSNSQRNWHDSITACKEV GAQLVVIKSAEEQNFLQLQS SRSNRFTWMGLSDLNQEGTW QWVDGSPLLPSFKQYWNRGE PNNVGEEDCAEFSGNGWNDD KCNLAKFWICKKSAASCSRD EEQFLSPAPATPNPPPA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 228 MET 2 229 GLY 3 230 SER 4 231 SER 5 232 HIS 6 233 HIS 7 234 HIS 8 235 HIS 9 236 HIS 10 237 HIS 11 238 SER 12 239 SER 13 240 GLY 14 241 LEU 15 242 VAL 16 243 PRO 17 244 ARG 18 245 GLY 19 246 SER 20 247 HIS 21 248 MET 22 249 ALA 23 250 GLU 24 251 ARG 25 252 LEU 26 253 CYS 27 254 HIS 28 255 PRO 29 256 CYS 30 257 PRO 31 258 TRP 32 259 GLU 33 260 TRP 34 261 THR 35 262 PHE 36 263 PHE 37 264 GLN 38 265 GLY 39 266 ASN 40 267 CYS 41 268 TYR 42 269 PHE 43 270 MET 44 271 SER 45 272 ASN 46 273 SER 47 274 GLN 48 275 ARG 49 276 ASN 50 277 TRP 51 278 HIS 52 279 ASP 53 280 SER 54 281 ILE 55 282 THR 56 283 ALA 57 284 CYS 58 285 LYS 59 286 GLU 60 287 VAL 61 288 GLY 62 289 ALA 63 290 GLN 64 291 LEU 65 292 VAL 66 293 VAL 67 294 ILE 68 295 LYS 69 296 SER 70 297 ALA 71 298 GLU 72 299 GLU 73 300 GLN 74 301 ASN 75 302 PHE 76 303 LEU 77 304 GLN 78 305 LEU 79 306 GLN 80 307 SER 81 308 SER 82 309 ARG 83 310 SER 84 311 ASN 85 312 ARG 86 313 PHE 87 314 THR 88 315 TRP 89 316 MET 90 317 GLY 91 318 LEU 92 319 SER 93 320 ASP 94 321 LEU 95 322 ASN 96 323 GLN 97 324 GLU 98 325 GLY 99 326 THR 100 327 TRP 101 328 GLN 102 329 TRP 103 330 VAL 104 331 ASP 105 332 GLY 106 333 SER 107 334 PRO 108 335 LEU 109 336 LEU 110 337 PRO 111 338 SER 112 339 PHE 113 340 LYS 114 341 GLN 115 342 TYR 116 343 TRP 117 344 ASN 118 345 ARG 119 346 GLY 120 347 GLU 121 348 PRO 122 349 ASN 123 350 ASN 124 351 VAL 125 352 GLY 126 353 GLU 127 354 GLU 128 355 ASP 129 356 CYS 130 357 ALA 131 358 GLU 132 359 PHE 133 360 SER 134 361 GLY 135 362 ASN 136 363 GLY 137 364 TRP 138 365 ASN 139 366 ASP 140 367 ASP 141 368 LYS 142 369 CYS 143 370 ASN 144 371 LEU 145 372 ALA 146 373 LYS 147 374 PHE 148 375 TRP 149 376 ILE 150 377 CYS 151 378 LYS 152 379 LYS 153 380 SER 154 381 ALA 155 382 ALA 156 383 SER 157 384 CYS 158 385 SER 159 386 ARG 160 387 ASP 161 388 GLU 162 389 GLU 163 390 GLN 164 391 PHE 165 392 LEU 166 393 SER 167 394 PRO 168 395 ALA 169 396 PRO 170 397 ALA 171 398 THR 172 399 PRO 173 400 ASN 174 401 PRO 175 402 PRO 176 403 PRO 177 404 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-29 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1K9I "Complex Of Dc-Sign And Glcnac2man3" 88.14 156 100.00 100.00 4.41e-111 PDB 1SL4 "Crystal Structure Of Dc-Sign Carbohydrate Recognition Domain Complexed With Man4" 87.57 155 100.00 100.00 3.25e-110 PDB 1SL5 "Crystal Structure Of Dc-Sign Carbohydrate Recognition Domain Complexed With Lnfp Iii (Dextra L504)." 78.53 139 100.00 100.00 7.14e-98 PDB 2B6B "Cryo Em Structure Of Dengue Complexed With Crd Of Dc-Sign" 100.00 175 98.87 98.87 9.57e-125 PDB 2IT5 "Crystal Structure Of Dcsign-crd With Man6" 78.53 139 100.00 100.00 7.14e-98 PDB 2IT6 "Crystal Structure Of Dcsign-Crd With Man2" 87.57 155 100.00 100.00 3.25e-110 PDB 2XR5 "Crystal Structure Of The Complex Of The Carbohydrate Recognition Domain Of Human Dc-sign With Pseudo Dimannoside Mimic" 85.31 166 100.00 100.00 5.31e-107 PDB 2XR6 "Crystal Structure Of The Complex Of The Carbohydrate Recognition Domain Of Human Dc-sign With Pseudo Trimannoside Mimic" 87.57 170 98.71 98.71 4.06e-108 DBJ BAF85778 "unnamed protein product [Homo sapiens]" 88.14 404 99.36 99.36 3.76e-114 DBJ BAG36354 "unnamed protein product [Homo sapiens]" 88.14 404 99.36 99.36 3.97e-114 DBJ BAG65070 "unnamed protein product [Homo sapiens]" 76.27 135 100.00 100.00 1.00e-92 DBJ BAI45727 "CD209 antigen [synthetic construct]" 88.14 404 99.36 99.36 3.76e-114 GB AAF77072 "membrane-associated lectin type-C [Homo sapiens]" 88.14 404 99.36 99.36 3.76e-114 GB AAG13814 "probable mannose-binding C-type lectin DC-SIGN [Homo sapiens]" 88.14 404 99.36 99.36 3.76e-114 GB AAI10616 "CD209 protein [Homo sapiens]" 88.14 380 99.36 99.36 3.49e-114 GB AAK20997 "DC-SIGN [Homo sapiens]" 88.14 404 99.36 99.36 3.76e-114 GB AAK91846 "mDC-SIGN1A type I isoform [Homo sapiens]" 88.14 404 99.36 99.36 3.76e-114 REF NP_001138365 "CD209 antigen isoform 5 [Homo sapiens]" 88.14 268 99.36 99.36 3.01e-113 REF NP_001138366 "CD209 antigen isoform 6 [Homo sapiens]" 88.14 360 99.36 99.36 1.59e-114 REF NP_001138367 "CD209 antigen isoform 7 [Homo sapiens]" 88.14 312 99.36 99.36 6.04e-113 REF NP_001138368 "CD209 antigen isoform 3 [Homo sapiens]" 88.14 380 99.36 99.36 1.49e-114 REF NP_001138371 "CD209 antigen isoform 8 [Homo sapiens]" 88.14 243 99.36 99.36 7.63e-112 SP Q8HY00 "RecName: Full=CD209 antigen; AltName: Full=Dendritic cell-specific ICAM-3-grabbing non-integrin 1; Short=DC-SIGN1; AltName: CD_" 88.14 404 98.08 99.36 2.34e-113 SP Q9NNX6 "RecName: Full=CD209 antigen; AltName: Full=C-type lectin domain family 4 member L; AltName: Full=Dendritic cell-specific ICAM-3" 88.14 404 99.36 99.36 3.76e-114 stop_ save_ ############# # Ligands # ############# save_CA _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common 'CALCIUM ION' _BMRB_code CA _PDB_code CA _Molecular_mass 40.078 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $DC-SIGN Human 9606 Eukaryota Metazoa Homo sapiens 'CD209, CLEC4L' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $DC-SIGN 'recombinant technology' . Escherichia coli BL21(DE3) peT28a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_NC_sample _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $DC-SIGN . uM 100 400 '[U-100% 13C; U-100% 15N]' D2O 10 % . . 'natural abundance' H2O 90 % . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version 3.113 loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $NC_sample save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $NC_sample save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $NC_sample save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $NC_sample save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $NC_sample save_ ####################### # Sample conditions # ####################### save_high_temperature _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 100 . mM pH 7.5 . pH pressure 1 . atm temperature 310 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.00000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $SPARKY stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCA' '3D HNCACB' '3D HNCO' stop_ loop_ _Sample_label $NC_sample stop_ _Sample_conditions_label $high_temperature _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name DC-SIGN _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 240 13 GLY CA C 45.416 0.035 1 2 241 14 LEU H H 7.837 0.003 1 3 241 14 LEU C C 176.529 0.000 1 4 241 14 LEU CA C 54.849 0.052 1 5 241 14 LEU CB C 40.671 0.000 1 6 241 14 LEU N N 123.805 0.016 1 7 242 15 VAL H H 7.123 0.003 1 8 242 15 VAL CA C 65.475 0.000 1 9 242 15 VAL N N 121.211 0.023 1 10 259 32 GLU C C 176.181 0.000 1 11 259 32 GLU CA C 59.112 0.000 1 12 259 32 GLU CB C 27.823 0.386 1 13 260 33 TRP H H 8.445 0.015 1 14 260 33 TRP C C 175.993 0.000 1 15 260 33 TRP CA C 57.205 0.097 1 16 260 33 TRP CB C 29.542 0.144 1 17 260 33 TRP N N 120.659 0.104 1 18 261 34 THR H H 9.737 0.011 1 19 261 34 THR C C 173.870 0.000 1 20 261 34 THR CA C 62.713 0.007 1 21 261 34 THR CB C 71.447 0.027 1 22 261 34 THR N N 119.197 0.060 1 23 262 35 PHE H H 9.050 0.011 1 24 262 35 PHE C C 174.964 0.000 1 25 262 35 PHE CA C 57.470 0.049 1 26 262 35 PHE CB C 40.780 0.150 1 27 262 35 PHE N N 129.158 0.063 1 28 263 36 PHE H H 8.744 0.003 1 29 263 36 PHE CA C 58.793 0.019 1 30 263 36 PHE CB C 40.833 0.000 1 31 263 36 PHE N N 127.138 0.025 1 32 264 37 GLN H H 8.715 0.002 1 33 264 37 GLN C C 174.569 0.000 1 34 264 37 GLN CA C 56.370 0.063 1 35 264 37 GLN CB C 27.430 0.122 1 36 264 37 GLN N N 127.239 0.075 1 37 265 38 GLY H H 5.872 0.003 1 38 265 38 GLY C C 172.793 0.000 1 39 265 38 GLY CA C 45.668 0.078 1 40 265 38 GLY N N 101.645 0.019 1 41 266 39 ASN H H 7.593 0.004 1 42 266 39 ASN C C 171.491 0.000 1 43 266 39 ASN CA C 52.186 0.071 1 44 266 39 ASN CB C 43.824 0.024 1 45 266 39 ASN N N 117.870 0.017 1 46 267 40 CYS H H 9.353 0.004 1 47 267 40 CYS C C 174.041 0.000 1 48 267 40 CYS CA C 53.325 0.015 1 49 267 40 CYS CB C 43.276 0.111 1 50 267 40 CYS N N 116.726 0.026 1 51 268 41 TYR H H 9.884 0.008 1 52 268 41 TYR C C 174.376 0.000 1 53 268 41 TYR CA C 56.998 0.059 1 54 268 41 TYR CB C 41.796 0.131 1 55 268 41 TYR N N 121.050 0.055 1 56 269 42 PHE H H 8.521 0.010 1 57 269 42 PHE C C 172.697 0.000 1 58 269 42 PHE CA C 55.290 0.011 1 59 269 42 PHE CB C 39.950 0.000 1 60 269 42 PHE N N 124.947 0.066 1 61 270 43 MET H H 7.748 0.005 1 62 270 43 MET C C 174.073 0.000 1 63 270 43 MET CA C 53.576 0.129 1 64 270 43 MET CB C 32.627 0.015 1 65 270 43 MET N N 127.966 0.019 1 66 271 44 SER H H 7.785 0.016 1 67 271 44 SER CA C 58.935 0.000 1 68 271 44 SER CB C 62.052 0.000 1 69 271 44 SER N N 120.509 0.039 1 70 272 45 ASN C C 174.586 0.000 1 71 272 45 ASN CA C 52.289 0.007 1 72 272 45 ASN CB C 39.707 0.000 1 73 273 46 SER H H 7.277 0.011 1 74 273 46 SER C C 170.959 0.000 1 75 273 46 SER CA C 56.586 0.183 1 76 273 46 SER CB C 64.963 0.055 1 77 273 46 SER N N 113.848 0.107 1 78 274 47 GLN H H 8.231 0.006 1 79 274 47 GLN C C 176.044 0.000 1 80 274 47 GLN CA C 54.908 0.062 1 81 274 47 GLN CB C 31.879 0.042 1 82 274 47 GLN N N 116.355 0.061 1 83 275 48 ARG H H 9.672 0.005 1 84 275 48 ARG C C 176.812 0.000 1 85 275 48 ARG CA C 55.208 0.036 1 86 275 48 ARG CB C 36.925 0.110 1 87 275 48 ARG N N 123.025 0.031 1 88 276 49 ASN H H 9.525 0.005 1 89 276 49 ASN C C 175.821 0.000 1 90 276 49 ASN CA C 52.705 0.033 1 91 276 49 ASN CB C 37.305 0.083 1 92 276 49 ASN N N 120.275 0.018 1 93 277 50 TRP H H 8.029 0.004 1 94 277 50 TRP C C 177.149 0.000 1 95 277 50 TRP CA C 64.147 0.050 1 96 277 50 TRP CB C 30.830 0.000 1 97 277 50 TRP N N 121.464 0.029 1 98 278 51 HIS H H 7.403 0.009 1 99 278 51 HIS C C 178.999 0.000 1 100 278 51 HIS CA C 60.290 0.048 1 101 278 51 HIS CB C 29.959 0.105 1 102 278 51 HIS N N 114.639 0.018 1 103 279 52 ASP H H 8.958 0.005 1 104 279 52 ASP C C 179.289 0.000 1 105 279 52 ASP CA C 56.057 0.037 1 106 279 52 ASP CB C 39.294 0.025 1 107 279 52 ASP N N 118.974 0.024 1 108 280 53 SER H H 8.053 0.008 1 109 280 53 SER C C 174.705 0.000 1 110 280 53 SER CA C 63.014 0.140 1 111 280 53 SER CB C 61.998 0.158 1 112 280 53 SER N N 123.928 0.066 1 113 281 54 ILE H H 7.048 0.009 1 114 281 54 ILE CA C 65.134 0.012 1 115 281 54 ILE CB C 36.999 0.026 1 116 281 54 ILE N N 121.963 0.028 1 117 282 55 THR H H 7.309 0.004 1 118 282 55 THR C C 175.321 0.000 1 119 282 55 THR CA C 66.194 0.052 1 120 282 55 THR CB C 68.227 0.099 1 121 282 55 THR N N 116.044 0.035 1 122 283 56 ALA H H 7.766 0.004 1 123 283 56 ALA C C 181.420 0.000 1 124 283 56 ALA CA C 54.965 0.011 1 125 283 56 ALA CB C 17.742 0.058 1 126 283 56 ALA N N 123.585 0.029 1 127 284 57 CYS H H 7.747 0.006 1 128 284 57 CYS C C 177.214 0.000 1 129 284 57 CYS CA C 54.996 0.063 1 130 284 57 CYS CB C 35.872 0.049 1 131 284 57 CYS N N 113.162 0.077 1 132 285 58 LYS H H 8.270 0.010 1 133 285 58 LYS CA C 60.193 0.029 1 134 285 58 LYS CB C 32.428 0.377 1 135 285 58 LYS N N 124.242 0.076 1 136 286 59 GLU H H 8.192 0.007 1 137 286 59 GLU C C 177.955 0.000 1 138 286 59 GLU CA C 59.055 0.060 1 139 286 59 GLU CB C 29.962 0.055 1 140 286 59 GLU N N 118.925 0.090 1 141 287 60 VAL H H 7.162 0.004 1 142 287 60 VAL C C 175.625 0.000 1 143 287 60 VAL CA C 59.677 0.074 1 144 287 60 VAL CB C 31.138 0.638 1 145 287 60 VAL N N 108.867 0.018 1 146 288 61 GLY H H 7.818 0.004 1 147 288 61 GLY C C 173.996 0.000 1 148 288 61 GLY CA C 46.838 0.019 1 149 288 61 GLY N N 108.974 0.021 1 150 289 62 ALA H H 8.265 0.003 1 151 289 62 ALA C C 174.157 0.000 1 152 289 62 ALA CA C 49.824 0.019 1 153 289 62 ALA CB C 24.731 0.078 1 154 289 62 ALA N N 121.941 0.016 1 155 290 63 GLN H H 8.034 0.006 1 156 290 63 GLN C C 175.565 0.000 1 157 290 63 GLN CA C 53.794 0.026 1 158 290 63 GLN CB C 33.473 0.298 1 159 290 63 GLN N N 117.261 0.050 1 160 291 64 LEU H H 8.866 0.003 1 161 291 64 LEU C C 178.923 0.000 1 162 291 64 LEU CA C 57.508 0.043 1 163 291 64 LEU CB C 43.012 0.085 1 164 291 64 LEU N N 131.924 0.045 1 165 292 65 VAL H H 7.844 0.008 1 166 292 65 VAL C C 172.591 0.000 1 167 292 65 VAL CA C 65.036 0.009 1 168 292 65 VAL CB C 33.462 0.026 1 169 292 65 VAL N N 122.647 0.063 1 170 293 66 VAL H H 6.956 0.004 1 171 293 66 VAL CA C 60.111 0.000 1 172 293 66 VAL CB C 33.276 0.000 1 173 293 66 VAL N N 126.957 0.016 1 174 296 69 SER C C 176.472 0.000 1 175 296 69 SER CA C 57.575 0.052 1 176 296 69 SER CB C 64.200 0.024 1 177 297 70 ALA H H 7.955 0.019 1 178 297 70 ALA C C 179.598 0.000 1 179 297 70 ALA CA C 55.035 0.135 1 180 297 70 ALA CB C 18.585 0.026 1 181 297 70 ALA N N 123.191 0.143 1 182 298 71 GLU H H 8.963 0.004 1 183 298 71 GLU C C 179.242 0.000 1 184 298 71 GLU CA C 60.361 0.034 1 185 298 71 GLU CB C 29.338 0.282 1 186 298 71 GLU N N 117.632 0.016 1 187 299 72 GLU H H 7.964 0.009 1 188 299 72 GLU C C 177.173 0.000 1 189 299 72 GLU CA C 59.536 0.084 1 190 299 72 GLU CB C 29.654 0.027 1 191 299 72 GLU N N 122.517 0.131 1 192 300 73 GLN H H 7.780 0.005 1 193 300 73 GLN C C 176.474 0.000 1 194 300 73 GLN CA C 58.328 0.041 1 195 300 73 GLN CB C 25.956 0.059 1 196 300 73 GLN N N 121.514 0.231 1 197 301 74 ASN H H 8.160 0.006 1 198 301 74 ASN C C 177.104 0.000 1 199 301 74 ASN CA C 56.413 0.022 1 200 301 74 ASN CB C 38.236 0.006 1 201 301 74 ASN N N 116.961 0.045 1 202 302 75 PHE H H 7.505 0.003 1 203 302 75 PHE C C 176.918 0.000 1 204 302 75 PHE CA C 60.244 0.031 1 205 302 75 PHE CB C 39.123 0.000 1 206 302 75 PHE N N 119.718 0.019 1 207 303 76 LEU H H 8.005 0.007 1 208 303 76 LEU C C 178.918 0.000 1 209 303 76 LEU CA C 56.848 0.060 1 210 303 76 LEU CB C 42.646 0.046 1 211 303 76 LEU N N 119.776 0.039 1 212 304 77 GLN H H 8.857 0.004 1 213 304 77 GLN C C 178.975 0.000 1 214 304 77 GLN CA C 58.709 0.014 1 215 304 77 GLN CB C 29.194 0.072 1 216 304 77 GLN N N 121.955 0.045 1 217 305 78 LEU H H 7.329 0.017 1 218 305 78 LEU C C 178.962 0.000 1 219 305 78 LEU CA C 57.293 0.009 1 220 305 78 LEU CB C 41.548 0.015 1 221 305 78 LEU N N 118.118 0.051 1 222 306 79 GLN H H 7.219 0.006 1 223 306 79 GLN C C 178.811 0.000 1 224 306 79 GLN CA C 57.791 0.073 1 225 306 79 GLN CB C 27.058 0.078 1 226 306 79 GLN N N 115.893 0.013 1 227 307 80 SER H H 7.399 0.008 1 228 307 80 SER C C 176.012 0.000 1 229 307 80 SER CA C 61.524 0.000 1 230 307 80 SER CB C 63.018 0.000 1 231 307 80 SER N N 113.796 0.027 1 232 308 81 SER H H 8.497 0.005 1 233 308 81 SER C C 178.234 0.000 1 234 308 81 SER CA C 61.006 0.075 1 235 308 81 SER CB C 62.979 0.151 1 236 308 81 SER N N 117.458 0.021 1 237 309 82 ARG H H 8.157 0.007 1 238 309 82 ARG C C 177.312 0.000 1 239 309 82 ARG CA C 58.438 0.005 1 240 309 82 ARG CB C 29.933 0.000 1 241 309 82 ARG N N 121.223 0.014 1 242 310 83 SER H H 7.137 0.005 1 243 310 83 SER C C 173.601 0.000 1 244 310 83 SER CA C 58.111 0.021 1 245 310 83 SER CB C 63.887 0.129 1 246 310 83 SER N N 111.011 0.017 1 247 311 84 ASN H H 7.795 0.007 1 248 311 84 ASN C C 173.687 0.000 1 249 311 84 ASN CA C 54.046 0.049 1 250 311 84 ASN CB C 37.341 0.005 1 251 311 84 ASN N N 118.351 0.062 1 252 312 85 ARG H H 7.500 0.003 1 253 312 85 ARG C C 176.481 0.000 1 254 312 85 ARG CA C 55.425 0.013 1 255 312 85 ARG CB C 32.237 0.145 1 256 312 85 ARG N N 116.498 0.025 1 257 313 86 PHE H H 8.411 0.006 1 258 313 86 PHE C C 176.808 0.000 1 259 313 86 PHE CA C 57.240 0.018 1 260 313 86 PHE CB C 37.153 0.145 1 261 313 86 PHE N N 127.404 0.031 1 262 314 87 THR H H 7.769 0.006 1 263 314 87 THR C C 173.473 0.000 1 264 314 87 THR CA C 61.264 0.040 1 265 314 87 THR CB C 73.061 0.111 1 266 314 87 THR N N 120.016 0.036 1 267 315 88 TRP H H 9.979 0.008 1 268 315 88 TRP C C 175.117 0.000 1 269 315 88 TRP CA C 57.883 0.024 1 270 315 88 TRP CB C 34.075 0.225 1 271 315 88 TRP N N 127.030 0.056 1 272 316 89 MET H H 8.450 0.005 1 273 316 89 MET C C 176.576 0.000 1 274 316 89 MET CA C 53.052 0.008 1 275 316 89 MET CB C 38.028 0.115 1 276 316 89 MET N N 113.175 0.056 1 277 317 90 GLY H H 9.689 0.006 1 278 317 90 GLY C C 172.899 0.000 1 279 317 90 GLY CA C 48.696 0.075 1 280 317 90 GLY N N 111.203 0.042 1 281 318 91 LEU H H 8.266 0.006 1 282 318 91 LEU C C 173.709 0.000 1 283 318 91 LEU CA C 54.839 0.035 1 284 318 91 LEU CB C 46.502 0.018 1 285 318 91 LEU N N 128.166 0.013 1 286 319 92 SER H H 8.462 0.006 1 287 319 92 SER C C 173.032 0.000 1 288 319 92 SER CA C 58.609 0.086 1 289 319 92 SER CB C 67.956 0.052 1 290 319 92 SER N N 120.132 0.084 1 291 320 93 ASP H H 7.851 0.006 1 292 320 93 ASP CA C 51.580 0.035 1 293 320 93 ASP CB C 37.566 0.110 1 294 320 93 ASP N N 123.648 0.060 1 295 321 94 LEU H H 6.706 0.010 1 296 321 94 LEU C C 178.552 0.000 1 297 321 94 LEU CA C 57.202 0.035 1 298 321 94 LEU CB C 44.422 0.103 1 299 321 94 LEU N N 119.547 0.077 1 300 322 95 ASN H H 7.886 0.006 1 301 322 95 ASN C C 175.315 0.000 1 302 322 95 ASN CA C 55.958 0.036 1 303 322 95 ASN CB C 38.278 0.033 1 304 322 95 ASN N N 115.386 0.024 1 305 323 96 GLN H H 7.651 0.003 1 306 323 96 GLN C C 172.238 0.000 1 307 323 96 GLN CA C 55.393 0.187 1 308 323 96 GLN CB C 30.405 0.000 1 309 323 96 GLN N N 120.474 0.014 1 310 324 97 GLU H H 8.004 0.006 1 311 324 97 GLU CA C 56.846 0.000 1 312 324 97 GLU N N 128.191 0.045 1 313 325 98 GLY C C 174.245 0.000 1 314 325 98 GLY CA C 45.048 0.010 1 315 326 99 THR H H 8.514 0.009 1 316 326 99 THR C C 172.259 0.000 1 317 326 99 THR CA C 61.585 0.072 1 318 326 99 THR CB C 68.897 0.401 1 319 326 99 THR N N 121.171 0.134 1 320 327 100 TRP H H 8.691 0.005 1 321 327 100 TRP C C 175.691 0.000 1 322 327 100 TRP CA C 57.668 0.047 1 323 327 100 TRP CB C 29.299 0.040 1 324 327 100 TRP N N 128.749 0.028 1 325 328 101 GLN H H 9.039 0.006 1 326 328 101 GLN C C 175.772 0.000 1 327 328 101 GLN CA C 54.465 0.020 1 328 328 101 GLN CB C 33.914 0.107 1 329 328 101 GLN N N 123.076 0.090 1 330 329 102 TRP H H 9.426 0.006 1 331 329 102 TRP C C 181.202 0.000 1 332 329 102 TRP CA C 56.770 0.043 1 333 329 102 TRP CB C 31.866 0.042 1 334 329 102 TRP N N 128.525 0.056 1 335 330 103 VAL H H 8.873 0.004 1 336 330 103 VAL C C 176.120 0.000 1 337 330 103 VAL CA C 64.361 0.050 1 338 330 103 VAL CB C 31.967 0.068 1 339 330 103 VAL N N 115.037 0.022 1 340 331 104 ASP H H 7.393 0.003 1 341 331 104 ASP C C 176.758 0.000 1 342 331 104 ASP CA C 53.379 0.032 1 343 331 104 ASP CB C 40.332 0.015 1 344 331 104 ASP N N 117.868 0.029 1 345 332 105 GLY H H 8.551 0.004 1 346 332 105 GLY C C 174.145 0.000 1 347 332 105 GLY CA C 44.957 0.022 1 348 332 105 GLY N N 109.099 0.045 1 349 333 106 SER H H 8.277 0.004 1 350 333 106 SER CA C 57.133 0.000 1 351 333 106 SER CB C 62.949 0.000 1 352 333 106 SER N N 119.364 0.019 1 353 334 107 PRO C C 177.164 0.000 1 354 334 107 PRO CA C 62.669 0.014 1 355 335 108 LEU H H 7.811 0.004 1 356 335 108 LEU C C 176.756 0.000 1 357 335 108 LEU CA C 55.002 0.009 1 358 335 108 LEU CB C 42.571 0.051 1 359 335 108 LEU N N 120.527 0.020 1 360 336 109 LEU H H 8.685 0.005 1 361 336 109 LEU CA C 53.893 0.000 1 362 336 109 LEU CB C 41.544 0.000 1 363 336 109 LEU N N 131.894 0.029 1 364 338 111 SER C C 175.213 0.000 1 365 338 111 SER CA C 60.151 0.065 1 366 338 111 SER CB C 62.428 0.083 1 367 339 112 PHE H H 8.280 0.030 1 368 339 112 PHE C C 175.317 0.000 1 369 339 112 PHE CA C 57.747 0.042 1 370 339 112 PHE CB C 39.093 0.041 1 371 339 112 PHE N N 120.446 0.023 1 372 340 113 LYS H H 7.478 0.004 1 373 340 113 LYS C C 177.605 0.000 1 374 340 113 LYS CA C 59.201 0.022 1 375 340 113 LYS CB C 31.917 0.014 1 376 340 113 LYS N N 118.703 0.021 1 377 341 114 GLN H H 7.266 0.007 1 378 341 114 GLN C C 175.081 0.000 1 379 341 114 GLN CA C 56.265 0.050 1 380 341 114 GLN CB C 28.410 0.059 1 381 341 114 GLN N N 113.684 0.023 1 382 342 115 TYR H H 6.682 0.004 1 383 342 115 TYR C C 175.951 0.000 1 384 342 115 TYR CA C 58.109 0.047 1 385 342 115 TYR CB C 34.773 0.256 1 386 342 115 TYR N N 118.431 0.018 1 387 343 116 TRP H H 6.459 0.005 1 388 343 116 TRP C C 177.603 0.000 1 389 343 116 TRP CA C 57.857 0.068 1 390 343 116 TRP CB C 30.319 0.048 1 391 343 116 TRP N N 117.676 0.018 1 392 344 117 ASN H H 9.987 0.008 1 393 344 117 ASN C C 175.591 0.000 1 394 344 117 ASN CA C 53.085 0.147 1 395 344 117 ASN CB C 39.117 0.189 1 396 344 117 ASN N N 123.366 0.052 1 397 345 118 ARG H H 8.039 0.011 1 398 345 118 ARG CA C 57.346 0.117 1 399 345 118 ARG CB C 29.555 0.154 1 400 345 118 ARG N N 120.309 0.073 1 401 346 119 GLY H H 7.927 0.021 1 402 346 119 GLY CA C 45.318 0.074 1 403 346 119 GLY N N 121.498 0.054 1 404 347 120 GLU H H 8.203 0.005 1 405 347 120 GLU CA C 52.382 0.000 1 406 347 120 GLU N N 118.777 0.021 1 407 350 123 ASN C C 175.039 0.000 1 408 350 123 ASN CA C 53.246 0.017 1 409 350 123 ASN CB C 39.039 0.000 1 410 351 124 VAL H H 7.996 0.006 1 411 351 124 VAL C C 176.477 0.000 1 412 351 124 VAL CA C 62.582 0.035 1 413 351 124 VAL CB C 32.565 0.049 1 414 351 124 VAL N N 119.646 0.073 1 415 352 125 GLY H H 8.412 0.007 1 416 352 125 GLY C C 174.144 0.000 1 417 352 125 GLY CA C 45.269 0.029 1 418 352 125 GLY N N 112.184 0.033 1 419 353 126 GLU H H 8.141 0.004 1 420 353 126 GLU CA C 56.696 0.000 1 421 353 126 GLU CB C 30.353 0.000 1 422 353 126 GLU N N 120.389 0.034 1 423 355 128 ASP C C 173.859 0.000 1 424 355 128 ASP CA C 51.528 0.135 1 425 355 128 ASP CB C 41.234 0.000 1 426 356 129 CYS H H 8.063 0.004 1 427 356 129 CYS C C 172.067 0.000 1 428 356 129 CYS CA C 58.963 0.034 1 429 356 129 CYS CB C 49.118 0.045 1 430 356 129 CYS N N 116.577 0.099 1 431 357 130 ALA H H 7.970 0.007 1 432 357 130 ALA C C 174.383 0.000 1 433 357 130 ALA CA C 51.521 0.054 1 434 357 130 ALA CB C 21.690 0.034 1 435 357 130 ALA N N 125.667 0.041 1 436 358 131 GLU H H 9.043 0.007 1 437 358 131 GLU C C 176.066 0.000 1 438 358 131 GLU CA C 52.579 0.037 1 439 358 131 GLU CB C 33.336 0.193 1 440 358 131 GLU N N 116.676 0.037 1 441 359 132 PHE H H 9.453 0.009 1 442 359 132 PHE C C 175.684 0.000 1 443 359 132 PHE CA C 58.391 0.035 1 444 359 132 PHE CB C 39.895 0.095 1 445 359 132 PHE N N 119.838 0.055 1 446 360 133 SER H H 8.894 0.009 1 447 360 133 SER C C 174.475 0.000 1 448 360 133 SER CA C 56.212 0.067 1 449 360 133 SER CB C 63.870 0.023 1 450 360 133 SER N N 116.686 0.046 1 451 361 134 GLY H H 8.930 0.002 1 452 361 134 GLY CA C 47.175 0.065 1 453 361 134 GLY N N 117.032 0.021 1 454 362 135 ASN C C 174.514 0.000 1 455 362 135 ASN CA C 53.224 0.069 1 456 362 135 ASN CB C 39.624 0.058 1 457 363 136 GLY H H 7.551 0.004 1 458 363 136 GLY C C 172.601 0.000 1 459 363 136 GLY CA C 46.803 0.043 1 460 363 136 GLY N N 112.691 0.039 1 461 364 137 TRP H H 8.457 0.007 1 462 364 137 TRP C C 177.205 0.000 1 463 364 137 TRP CA C 52.684 0.018 1 464 364 137 TRP CB C 32.812 0.128 1 465 364 137 TRP N N 122.280 0.072 1 466 365 138 ASN H H 9.097 0.004 1 467 365 138 ASN C C 174.588 0.000 1 468 365 138 ASN CA C 51.841 0.069 1 469 365 138 ASN CB C 42.229 0.085 1 470 365 138 ASN N N 117.916 0.036 1 471 366 139 ASP H H 9.119 0.004 1 472 366 139 ASP C C 173.792 0.000 1 473 366 139 ASP CA C 52.093 0.031 1 474 366 139 ASP CB C 41.904 0.107 1 475 366 139 ASP N N 121.036 0.042 1 476 367 140 ASP H H 9.891 0.003 1 477 367 140 ASP C C 174.924 0.000 1 478 367 140 ASP CA C 51.371 0.055 1 479 367 140 ASP CB C 45.858 0.061 1 480 367 140 ASP N N 125.577 0.041 1 481 368 141 LYS H H 9.619 0.005 1 482 368 141 LYS C C 175.297 0.000 1 483 368 141 LYS CA C 58.181 0.120 1 484 368 141 LYS CB C 32.342 0.349 1 485 368 141 LYS N N 120.573 0.020 1 486 369 142 CYS H H 8.470 0.007 1 487 369 142 CYS C C 174.467 0.000 1 488 369 142 CYS CA C 58.215 0.087 1 489 369 142 CYS CB C 46.324 0.033 1 490 369 142 CYS N N 120.502 0.175 1 491 370 143 ASN H H 8.301 0.004 1 492 370 143 ASN C C 175.125 0.000 1 493 370 143 ASN CA C 54.041 0.018 1 494 370 143 ASN CB C 37.909 0.110 1 495 370 143 ASN N N 112.518 0.019 1 496 371 144 LEU H H 7.995 0.003 1 497 371 144 LEU C C 175.099 0.000 1 498 371 144 LEU CA C 54.978 0.019 1 499 371 144 LEU CB C 42.962 0.000 1 500 371 144 LEU N N 123.409 0.035 1 501 372 145 ALA H H 8.139 0.004 1 502 372 145 ALA C C 176.490 0.000 1 503 372 145 ALA CA C 51.205 0.032 1 504 372 145 ALA CB C 18.222 0.034 1 505 372 145 ALA N N 122.014 0.041 1 506 373 146 LYS H H 8.532 0.009 1 507 373 146 LYS CA C 54.998 0.015 1 508 373 146 LYS CB C 36.525 0.282 1 509 373 146 LYS N N 123.455 0.064 1 510 374 147 PHE H H 7.296 0.004 1 511 374 147 PHE C C 172.950 0.000 1 512 374 147 PHE CA C 59.763 0.034 1 513 374 147 PHE CB C 38.959 0.097 1 514 374 147 PHE N N 117.252 0.026 1 515 375 148 TRP H H 8.848 0.006 1 516 375 148 TRP C C 173.311 0.000 1 517 375 148 TRP CA C 58.779 0.048 1 518 375 148 TRP CB C 32.294 0.108 1 519 375 148 TRP N N 117.021 0.044 1 520 376 149 ILE H H 6.571 0.006 1 521 376 149 ILE C C 176.545 0.000 1 522 376 149 ILE CA C 59.043 0.080 1 523 376 149 ILE CB C 43.505 0.017 1 524 376 149 ILE N N 116.872 0.031 1 525 377 150 CYS H H 9.009 0.005 1 526 377 150 CYS C C 173.447 0.000 1 527 377 150 CYS CA C 51.400 0.057 1 528 377 150 CYS CB C 40.397 0.089 1 529 377 150 CYS N N 121.456 0.050 1 530 378 151 LYS H H 9.283 0.007 1 531 378 151 LYS C C 175.399 0.000 1 532 378 151 LYS CA C 54.833 0.039 1 533 378 151 LYS CB C 38.556 0.039 1 534 378 151 LYS N N 123.596 0.028 1 535 379 152 LYS H H 9.068 0.007 1 536 379 152 LYS CA C 55.019 0.059 1 537 379 152 LYS CB C 36.626 0.028 1 538 379 152 LYS N N 125.320 0.017 1 539 380 153 SER H H 8.691 0.009 1 540 380 153 SER CA C 59.619 0.059 1 541 380 153 SER CB C 63.767 0.100 1 542 380 153 SER N N 117.683 0.043 1 543 381 154 ALA H H 7.666 0.005 1 544 381 154 ALA C C 177.476 0.000 1 545 381 154 ALA CA C 52.036 0.045 1 546 381 154 ALA CB C 20.407 0.011 1 547 381 154 ALA N N 123.735 0.030 1 548 382 155 ALA H H 8.961 0.006 1 549 382 155 ALA C C 175.714 0.000 1 550 382 155 ALA CA C 52.169 0.209 1 551 382 155 ALA CB C 19.490 0.157 1 552 382 155 ALA N N 124.533 0.018 1 553 383 156 SER H H 7.759 0.012 1 554 383 156 SER CA C 58.672 0.000 1 555 383 156 SER CB C 70.481 0.000 1 556 383 156 SER N N 112.981 0.129 1 557 385 158 SER C C 175.989 0.000 1 558 385 158 SER CA C 63.067 0.065 1 559 386 159 ARG H H 8.352 0.017 1 560 386 159 ARG C C 176.787 0.000 1 561 386 159 ARG CA C 56.882 0.025 1 562 386 159 ARG CB C 30.300 0.099 1 563 386 159 ARG N N 121.640 0.058 1 564 387 160 ASP H H 8.213 0.006 1 565 387 160 ASP C C 176.420 0.000 1 566 387 160 ASP CA C 54.894 0.022 1 567 387 160 ASP CB C 41.167 0.031 1 568 387 160 ASP N N 120.975 0.029 1 569 388 161 GLU H H 8.249 0.005 1 570 388 161 GLU C C 176.101 0.000 1 571 388 161 GLU CA C 56.970 0.000 1 572 388 161 GLU CB C 30.228 0.000 1 573 388 161 GLU N N 120.351 0.061 1 574 389 162 GLU H H 8.214 0.004 1 575 389 162 GLU C C 176.607 0.000 1 576 389 162 GLU CA C 57.108 0.051 1 577 389 162 GLU CB C 30.160 0.028 1 578 389 162 GLU N N 120.994 0.021 1 579 390 163 GLN H H 8.091 0.004 1 580 390 163 GLN C C 174.486 0.000 1 581 390 163 GLN CA C 56.019 0.030 1 582 390 163 GLN CB C 29.447 0.055 1 583 390 163 GLN N N 119.798 0.026 1 584 391 164 PHE H H 8.041 0.006 1 585 391 164 PHE C C 175.360 0.000 1 586 391 164 PHE CB C 39.388 0.001 1 587 391 164 PHE N N 120.366 0.029 1 588 392 165 LEU H H 7.949 0.007 1 589 392 165 LEU C C 176.697 0.000 1 590 392 165 LEU CA C 54.835 0.034 1 591 392 165 LEU CB C 42.658 0.037 1 592 392 165 LEU N N 123.290 0.049 1 593 393 166 SER H H 8.107 0.004 1 594 393 166 SER CA C 56.238 0.000 1 595 393 166 SER CB C 63.434 0.000 1 596 393 166 SER N N 117.781 0.012 1 597 396 169 PRO C C 176.542 0.000 1 598 396 169 PRO CA C 62.885 0.035 1 599 396 169 PRO CB C 32.042 0.000 1 600 397 170 ALA H H 8.282 0.002 1 601 397 170 ALA C C 177.594 0.000 1 602 397 170 ALA CA C 52.329 0.038 1 603 397 170 ALA CB C 19.281 0.014 1 604 397 170 ALA N N 124.302 0.014 1 605 398 171 THR H H 8.018 0.004 1 606 398 171 THR CA C 59.377 0.000 1 607 398 171 THR CB C 69.789 0.000 1 608 398 171 THR N N 115.411 0.018 1 stop_ save_