data_4381 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4381 _Entry.Title ; Letter to the Editor:Sequence-specific 1H, 13C, and 15N assignments for the third EH domain of Eps15 (EH3) ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 1999-08-19 _Entry.Accession_date 1999-08-19 _Entry.Last_release_date 2000-03-20 _Entry.Original_release_date 2000-03-20 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 Jennifer Enmon . L. . 4381 2 Tonny 'de Beer' . . . 4381 3 Michael Overduin . . . 4381 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4381 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 445 4381 '15N chemical shifts' 92 4381 '1H chemical shifts' 713 4381 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2000-03-20 1999-08-19 original author . 4381 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4381 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title ; Letter to the Editor: Sequence-specific 1H, 13C, and 15N assignments for the third EH domain of Eps15 (EH3) ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full . _Citation.Journal_volume 16 _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 81 _Citation.Page_last 82 _Citation.Year 2000 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Jennifer Enmon . L. . 4381 1 2 Tonny 'de Beer' . . . 4381 1 3 Michael Overduin . . . 4381 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID calcium-binding 4381 1 'EH domain' 4381 1 Eps15 4381 1 'peptide bindin' 4381 1 stop_ save_ save_citation_1 _Citation.Sf_category citations _Citation.Sf_framecode citation_1 _Citation.Entry_ID 4381 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8520220 _Citation.Full_citation 'Delaglio et al., J. Biomol NMR 6, 277-293 (1995)' _Citation.Title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of biomolecular NMR' _Citation.Journal_volume 6 _Citation.Journal_issue 3 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0925-2738 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 277 _Citation.Page_last 293 _Citation.Year 1995 _Citation.Details ; The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 F Delaglio F. . . 4381 2 2 S Grzesiek S. . . 4381 2 3 'G W' Vuister G. W. . 4381 2 4 G Zhu G. . . 4381 2 5 J Pfeifer J. . . 4381 2 6 A Bax A. . . 4381 2 stop_ save_ save_citation_2 _Citation.Sf_category citations _Citation.Sf_framecode citation_2 _Citation.Entry_ID 4381 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation 'Garret et al., J. Magn. Reson. 95, 214-220.(1995)' _Citation.Title . _Citation.Status . _Citation.Type . _Citation.Journal_abbrev . _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _Citation.Details . save_ ############################################# # Molecular system (assembly) description # ############################################# save_Eps15-EH3 _Assembly.Sf_category assembly _Assembly.Sf_framecode Eps15-EH3 _Assembly.Entry_ID 4381 _Assembly.ID 1 _Assembly.Name 'Third EH domain of human Eps15' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'not reported' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 4381 1 stop_ loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 EH3 1 $EH3 . . . native . . . . . 4381 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID . PDB 1C07A . 'Chain A, Structure Of The Third Eps15 Homology Domain Of Human Eps15' . . . . 4381 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID Eps15-EH3 abbreviation 4381 1 'Third EH domain of human Eps15' system 4381 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_EH3 _Entity.Sf_category entity _Entity.Sf_framecode EH3 _Entity.Entry_ID 4381 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'third EH domain of Eps15' _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; KRKTWVVSPAEKAKYDEIFL KTDKDMDGFVSGLEVREIFL KTGLPSTLLAHIWSLCDTKD CGKLSKDQFALAFHLISQKL IKGIDPPHVLTPEMIPPSDR ASLQ ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 104 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-24 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no PDB 1C07 . "Structure Of The Third Eps15 Homology Domain Of Human Eps15" . . . . . 90.38 95 100.00 100.00 1.38e-60 . . . . 4381 1 2 no REF XP_006710509 . "PREDICTED: epidermal growth factor receptor substrate 15 isoform X3 [Homo sapiens]" . . . . . 75.96 658 100.00 100.00 6.13e-47 . . . . 4381 1 3 no REF XP_007976962 . "PREDICTED: epidermal growth factor receptor substrate 15 isoform X5 [Chlorocebus sabaeus]" . . . . . 98.08 756 98.04 99.02 2.70e-62 . . . . 4381 1 4 no REF XP_009455980 . "PREDICTED: epidermal growth factor receptor substrate 15 isoform X7 [Pan troglodytes]" . . . . . 98.08 772 98.04 99.02 4.34e-62 . . . . 4381 1 5 no REF XP_011539293 . "PREDICTED: epidermal growth factor receptor substrate 15 isoform X2 [Homo sapiens]" . . . . . 100.00 708 100.00 100.00 4.84e-65 . . . . 4381 1 6 no REF XP_011781647 . "PREDICTED: epidermal growth factor receptor substrate 15 isoform X1 [Colobus angolensis palliatus]" . . . . . 100.00 726 99.04 100.00 2.38e-64 . . . . 4381 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID EH3 abbreviation 4381 1 'third EH domain of Eps15' common 4381 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 214 LYS . 4381 1 2 215 ARG . 4381 1 3 216 LYS . 4381 1 4 217 THR . 4381 1 5 218 TRP . 4381 1 6 219 VAL . 4381 1 7 220 VAL . 4381 1 8 221 SER . 4381 1 9 222 PRO . 4381 1 10 223 ALA . 4381 1 11 224 GLU . 4381 1 12 225 LYS . 4381 1 13 226 ALA . 4381 1 14 227 LYS . 4381 1 15 228 TYR . 4381 1 16 229 ASP . 4381 1 17 230 GLU . 4381 1 18 231 ILE . 4381 1 19 232 PHE . 4381 1 20 233 LEU . 4381 1 21 234 LYS . 4381 1 22 235 THR . 4381 1 23 236 ASP . 4381 1 24 237 LYS . 4381 1 25 238 ASP . 4381 1 26 239 MET . 4381 1 27 240 ASP . 4381 1 28 241 GLY . 4381 1 29 242 PHE . 4381 1 30 243 VAL . 4381 1 31 244 SER . 4381 1 32 245 GLY . 4381 1 33 246 LEU . 4381 1 34 247 GLU . 4381 1 35 248 VAL . 4381 1 36 249 ARG . 4381 1 37 250 GLU . 4381 1 38 251 ILE . 4381 1 39 252 PHE . 4381 1 40 253 LEU . 4381 1 41 254 LYS . 4381 1 42 255 THR . 4381 1 43 256 GLY . 4381 1 44 257 LEU . 4381 1 45 258 PRO . 4381 1 46 259 SER . 4381 1 47 260 THR . 4381 1 48 261 LEU . 4381 1 49 262 LEU . 4381 1 50 263 ALA . 4381 1 51 264 HIS . 4381 1 52 265 ILE . 4381 1 53 266 TRP . 4381 1 54 267 SER . 4381 1 55 268 LEU . 4381 1 56 269 CYS . 4381 1 57 270 ASP . 4381 1 58 271 THR . 4381 1 59 272 LYS . 4381 1 60 273 ASP . 4381 1 61 274 CYS . 4381 1 62 275 GLY . 4381 1 63 276 LYS . 4381 1 64 277 LEU . 4381 1 65 278 SER . 4381 1 66 279 LYS . 4381 1 67 280 ASP . 4381 1 68 281 GLN . 4381 1 69 282 PHE . 4381 1 70 283 ALA . 4381 1 71 284 LEU . 4381 1 72 285 ALA . 4381 1 73 286 PHE . 4381 1 74 287 HIS . 4381 1 75 288 LEU . 4381 1 76 289 ILE . 4381 1 77 290 SER . 4381 1 78 291 GLN . 4381 1 79 292 LYS . 4381 1 80 293 LEU . 4381 1 81 294 ILE . 4381 1 82 295 LYS . 4381 1 83 296 GLY . 4381 1 84 297 ILE . 4381 1 85 298 ASP . 4381 1 86 299 PRO . 4381 1 87 300 PRO . 4381 1 88 301 HIS . 4381 1 89 302 VAL . 4381 1 90 303 LEU . 4381 1 91 304 THR . 4381 1 92 305 PRO . 4381 1 93 306 GLU . 4381 1 94 307 MET . 4381 1 95 308 ILE . 4381 1 96 309 PRO . 4381 1 97 310 PRO . 4381 1 98 311 SER . 4381 1 99 312 ASP . 4381 1 100 313 ARG . 4381 1 101 314 ALA . 4381 1 102 315 SER . 4381 1 103 316 LEU . 4381 1 104 317 GLN . 4381 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . LYS 1 1 4381 1 . ARG 2 2 4381 1 . LYS 3 3 4381 1 . THR 4 4 4381 1 . TRP 5 5 4381 1 . VAL 6 6 4381 1 . VAL 7 7 4381 1 . SER 8 8 4381 1 . PRO 9 9 4381 1 . ALA 10 10 4381 1 . GLU 11 11 4381 1 . LYS 12 12 4381 1 . ALA 13 13 4381 1 . LYS 14 14 4381 1 . TYR 15 15 4381 1 . ASP 16 16 4381 1 . GLU 17 17 4381 1 . ILE 18 18 4381 1 . PHE 19 19 4381 1 . LEU 20 20 4381 1 . LYS 21 21 4381 1 . THR 22 22 4381 1 . ASP 23 23 4381 1 . LYS 24 24 4381 1 . ASP 25 25 4381 1 . MET 26 26 4381 1 . ASP 27 27 4381 1 . GLY 28 28 4381 1 . PHE 29 29 4381 1 . VAL 30 30 4381 1 . SER 31 31 4381 1 . GLY 32 32 4381 1 . LEU 33 33 4381 1 . GLU 34 34 4381 1 . VAL 35 35 4381 1 . ARG 36 36 4381 1 . GLU 37 37 4381 1 . ILE 38 38 4381 1 . PHE 39 39 4381 1 . LEU 40 40 4381 1 . LYS 41 41 4381 1 . THR 42 42 4381 1 . GLY 43 43 4381 1 . LEU 44 44 4381 1 . PRO 45 45 4381 1 . SER 46 46 4381 1 . THR 47 47 4381 1 . LEU 48 48 4381 1 . LEU 49 49 4381 1 . ALA 50 50 4381 1 . HIS 51 51 4381 1 . ILE 52 52 4381 1 . TRP 53 53 4381 1 . SER 54 54 4381 1 . LEU 55 55 4381 1 . CYS 56 56 4381 1 . ASP 57 57 4381 1 . THR 58 58 4381 1 . LYS 59 59 4381 1 . ASP 60 60 4381 1 . CYS 61 61 4381 1 . GLY 62 62 4381 1 . LYS 63 63 4381 1 . LEU 64 64 4381 1 . SER 65 65 4381 1 . LYS 66 66 4381 1 . ASP 67 67 4381 1 . GLN 68 68 4381 1 . PHE 69 69 4381 1 . ALA 70 70 4381 1 . LEU 71 71 4381 1 . ALA 72 72 4381 1 . PHE 73 73 4381 1 . HIS 74 74 4381 1 . LEU 75 75 4381 1 . ILE 76 76 4381 1 . SER 77 77 4381 1 . GLN 78 78 4381 1 . LYS 79 79 4381 1 . LEU 80 80 4381 1 . ILE 81 81 4381 1 . LYS 82 82 4381 1 . GLY 83 83 4381 1 . ILE 84 84 4381 1 . ASP 85 85 4381 1 . PRO 86 86 4381 1 . PRO 87 87 4381 1 . HIS 88 88 4381 1 . VAL 89 89 4381 1 . LEU 90 90 4381 1 . THR 91 91 4381 1 . PRO 92 92 4381 1 . GLU 93 93 4381 1 . MET 94 94 4381 1 . ILE 95 95 4381 1 . PRO 96 96 4381 1 . PRO 97 97 4381 1 . SER 98 98 4381 1 . ASP 99 99 4381 1 . ARG 100 100 4381 1 . ALA 101 101 4381 1 . SER 102 102 4381 1 . LEU 103 103 4381 1 . GLN 104 104 4381 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 4381 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $EH3 . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . . . . 'human Eps15' . . . . 4381 1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Entity_experimental_src_list.Sf_category experimental_source _Entity_experimental_src_list.Sf_framecode experimental_source _Entity_experimental_src_list.Entry_ID 4381 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $EH3 . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli 'B834 pLys S' . . . . . . . . . . . . plasmid . . pRSETA . . . . . . 4381 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 4381 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'third EH domain of Eps15' '[U-13C; U-15N]' . . 1 $EH3 . . 1.0 0.5 1.0 mM . . . . 4381 1 2 d-tris . . . . . . . 10 . . mM . . . . 4381 1 3 KCl . . . . . . . 100 . . mM . . . . 4381 1 4 NaN3 . . . . . . . 2 . . mM . . . . 4381 1 5 APMSF . . . . . . . 0.010 . . mM . . . . 4381 1 6 d-DTT . . . . . . . . 0.1 40 mM . . . . 4381 1 7 D2O . . . . . . . 10 . . % . . . . 4381 1 8 H2O . . . . . . . 90 . . % . . . . 4381 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 4381 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'third EH domain of Eps15' '[U-13C; U-15N]' . . 1 $EH3 . . 1.0 0.5 1.0 mM . . . . 4381 2 2 d-tris . . . . . . . 10 . . mM . . . . 4381 2 3 KCl . . . . . . . 100 . . mM . . . . 4381 2 4 NaN3 . . . . . . . 2 . . mM . . . . 4381 2 5 APMSF . . . . . . . 0.010 . . mM . . . . 4381 2 6 d-DTT . . . . . . . . 0.1 40 mM . . . . 4381 2 7 D2O . . . . . . . 99.9 . . % . . . . 4381 2 stop_ save_ ####################### # Sample conditions # ####################### save_condition_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode condition_1 _Sample_condition_list.Entry_ID 4381 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 7.8 . n/a 4381 1 temperature 298 . K 4381 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 4381 _Software.ID 1 _Software.Name NMRPipe _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 4381 1 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 2 $citation_1 4381 1 stop_ save_ save_PIPP _Software.Sf_category software _Software.Sf_framecode PIPP _Software.Entry_ID 4381 _Software.ID 2 _Software.Name PIPP _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID analysis 4381 2 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 3 $citation_2 4381 2 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 4381 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model Inova _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 4381 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model Inova _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4381 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 NMR_spectrometer1 Varian Inova . 500 . . . 4381 1 2 NMR_spectrometer2 Varian Inova . 600 . . . 4381 1 stop_ save_ ############################# # NMR applied experiments # ############################# save_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list _Experiment_list.Entry_ID 4381 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 CBCA(CO)NH . . . . . . . . . . . . . . . . 1 $condition_1 . . . . . . . . . . . . . . . . . . . . . 4381 1 2 HNCACB . . . . . . . . . . . . . . . . 1 $condition_1 . . . . . . . . . . . . . . . . . . . . . 4381 1 3 HCC-TOCSY . . . . . . . . . . . . . . . . 1 $condition_1 . . . . . . . . . . . . . . . . . . . . . 4381 1 4 CCC-TOCSY . . . . . . . . . . . . . . . . 1 $condition_1 . . . . . . . . . . . . . . . . . . . . . 4381 1 5 HCCH_TOCSY . . . . . . . . . . . . . . . . 1 $condition_1 . . . . . . . . . . . . . . . . . . . . . 4381 1 6 3D-15N-NOESY . . . . . . . . . . . . . . . . 1 $condition_1 . . . . . . . . . . . . . . . . . . . . . 4381 1 7 HNCO . . . . . . . . . . . . . . . . 1 $condition_1 . . . . . . . . . . . . . . . . . . . . . 4381 1 8 '2D CB corelation with HD and HE' . . . . . . . . . . . . . . . . 1 $condition_1 . . . . . . . . . . . . . . . . . . . . . 4381 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 4381 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 4381 1 H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . . . . . 4381 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 4381 1 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_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_1 _Assigned_chem_shift_list.Entry_ID 4381 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $condition_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_1 . 4381 1 . . 2 $sample_2 . 4381 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 4 4 THR HA H 1 4.316 0.05 . 1 . . . . . . . . 4381 1 2 . 1 1 4 4 THR HB H 1 4.176 0.05 . 1 . . . . . . . . 4381 1 3 . 1 1 4 4 THR HG21 H 1 1.216 0.05 . 1 . . . . . . . . 4381 1 4 . 1 1 4 4 THR HG22 H 1 1.216 0.05 . 1 . . . . . . . . 4381 1 5 . 1 1 4 4 THR HG23 H 1 1.216 0.05 . 1 . . . . . . . . 4381 1 6 . 1 1 4 4 THR C C 13 173.52 0.1 . 1 . . . . . . . . 4381 1 7 . 1 1 4 4 THR CA C 13 62.216 0.1 . 1 . . . . . . . . 4381 1 8 . 1 1 4 4 THR CB C 13 69.776 0.1 . 1 . . . . . . . . 4381 1 9 . 1 1 4 4 THR CG2 C 13 21.616 0.1 . 1 . . . . . . . . 4381 1 10 . 1 1 5 5 TRP H H 1 8.486 0.05 . 1 . . . . . . . . 4381 1 11 . 1 1 5 5 TRP HA H 1 5.586 0.05 . 1 . . . . . . . . 4381 1 12 . 1 1 5 5 TRP HB2 H 1 3.366 0.05 . 2 . . . . . . . . 4381 1 13 . 1 1 5 5 TRP HB3 H 1 3.006 0.05 . 2 . . . . . . . . 4381 1 14 . 1 1 5 5 TRP HD1 H 1 7.906 0.05 . 1 . . . . . . . . 4381 1 15 . 1 1 5 5 TRP HE1 H 1 9.166 0.05 . 1 . . . . . . . . 4381 1 16 . 1 1 5 5 TRP HE3 H 1 7.636 0.05 . 1 . . . . . . . . 4381 1 17 . 1 1 5 5 TRP HH2 H 1 7.346 0.05 . 1 . . . . . . . . 4381 1 18 . 1 1 5 5 TRP HZ2 H 1 7.446 0.05 . 1 . . . . . . . . 4381 1 19 . 1 1 5 5 TRP HZ3 H 1 6.946 0.05 . 1 . . . . . . . . 4381 1 20 . 1 1 5 5 TRP C C 13 176.65 0.1 . 1 . . . . . . . . 4381 1 21 . 1 1 5 5 TRP CA C 13 54.286 0.1 . 1 . . . . . . . . 4381 1 22 . 1 1 5 5 TRP CB C 13 31.136 0.1 . 1 . . . . . . . . 4381 1 23 . 1 1 5 5 TRP CD1 C 13 126.08 0.1 . 1 . . . . . . . . 4381 1 24 . 1 1 5 5 TRP CE3 C 13 122.74 0.1 . 1 . . . . . . . . 4381 1 25 . 1 1 5 5 TRP CH2 C 13 125.38 0.1 . 1 . . . . . . . . 4381 1 26 . 1 1 5 5 TRP CZ2 C 13 113.43 0.1 . 1 . . . . . . . . 4381 1 27 . 1 1 5 5 TRP CZ3 C 13 121.29 0.1 . 1 . . . . . . . . 4381 1 28 . 1 1 5 5 TRP N N 15 124.47 0.1 . 1 . . . . . . . . 4381 1 29 . 1 1 5 5 TRP NE1 N 15 127.37 0.1 . 1 . . . . . . . . 4381 1 30 . 1 1 6 6 VAL H H 1 7.006 0.05 . 1 . . . . . . . . 4381 1 31 . 1 1 6 6 VAL HA H 1 3.776 0.05 . 1 . . . . . . . . 4381 1 32 . 1 1 6 6 VAL HB H 1 1.976 0.05 . 1 . . . . . . . . 4381 1 33 . 1 1 6 6 VAL HG11 H 1 0.756 0.05 . 2 . . . . . . . . 4381 1 34 . 1 1 6 6 VAL HG12 H 1 0.756 0.05 . 2 . . . . . . . . 4381 1 35 . 1 1 6 6 VAL HG13 H 1 0.756 0.05 . 2 . . . . . . . . 4381 1 36 . 1 1 6 6 VAL HG21 H 1 0.376 0.05 . 2 . . . . . . . . 4381 1 37 . 1 1 6 6 VAL HG22 H 1 0.376 0.05 . 2 . . . . . . . . 4381 1 38 . 1 1 6 6 VAL HG23 H 1 0.376 0.05 . 2 . . . . . . . . 4381 1 39 . 1 1 6 6 VAL CA C 13 63.056 0.1 . 1 . . . . . . . . 4381 1 40 . 1 1 6 6 VAL CB C 13 31.586 0.1 . 1 . . . . . . . . 4381 1 41 . 1 1 6 6 VAL CG1 C 13 21.766 0.1 . 2 . . . . . . . . 4381 1 42 . 1 1 6 6 VAL CG2 C 13 19.796 0.1 . 2 . . . . . . . . 4381 1 43 . 1 1 6 6 VAL N N 15 118.59 0.1 . 1 . . . . . . . . 4381 1 44 . 1 1 7 7 VAL HA H 1 3.256 0.05 . 1 . . . . . . . . 4381 1 45 . 1 1 7 7 VAL HB H 1 -0.254 0.05 . 1 . . . . . . . . 4381 1 46 . 1 1 7 7 VAL HG11 H 1 0.546 0.05 . 2 . . . . . . . . 4381 1 47 . 1 1 7 7 VAL HG12 H 1 0.546 0.05 . 2 . . . . . . . . 4381 1 48 . 1 1 7 7 VAL HG13 H 1 0.546 0.05 . 2 . . . . . . . . 4381 1 49 . 1 1 7 7 VAL HG21 H 1 -0.284 0.05 . 2 . . . . . . . . 4381 1 50 . 1 1 7 7 VAL HG22 H 1 -0.284 0.05 . 2 . . . . . . . . 4381 1 51 . 1 1 7 7 VAL HG23 H 1 -0.284 0.05 . 2 . . . . . . . . 4381 1 52 . 1 1 7 7 VAL C C 13 175.11 0.1 . 1 . . . . . . . . 4381 1 53 . 1 1 7 7 VAL CA C 13 61.266 0.1 . 1 . . . . . . . . 4381 1 54 . 1 1 7 7 VAL CB C 13 30.326 0.1 . 1 . . . . . . . . 4381 1 55 . 1 1 7 7 VAL CG1 C 13 22.006 0.1 . 2 . . . . . . . . 4381 1 56 . 1 1 7 7 VAL CG2 C 13 21.076 0.1 . 2 . . . . . . . . 4381 1 57 . 1 1 8 8 SER H H 1 8.356 0.05 . 1 . . . . . . . . 4381 1 58 . 1 1 8 8 SER HA H 1 4.656 0.05 . 1 . . . . . . . . 4381 1 59 . 1 1 8 8 SER HB2 H 1 4.286 0.05 . 2 . . . . . . . . 4381 1 60 . 1 1 8 8 SER HB3 H 1 4.006 0.05 . 2 . . . . . . . . 4381 1 61 . 1 1 8 8 SER CA C 13 57.006 0.1 . 1 . . . . . . . . 4381 1 62 . 1 1 8 8 SER CB C 13 63.036 0.1 . 1 . . . . . . . . 4381 1 63 . 1 1 8 8 SER N N 15 125.77 0.1 . 1 . . . . . . . . 4381 1 64 . 1 1 9 9 PRO HA H 1 4.266 0.05 . 1 . . . . . . . . 4381 1 65 . 1 1 9 9 PRO HB2 H 1 2.376 0.05 . 2 . . . . . . . . 4381 1 66 . 1 1 9 9 PRO HB3 H 1 1.946 0.05 . 2 . . . . . . . . 4381 1 67 . 1 1 9 9 PRO HD2 H 1 3.956 0.05 . 2 . . . . . . . . 4381 1 68 . 1 1 9 9 PRO HD3 H 1 3.886 0.05 . 2 . . . . . . . . 4381 1 69 . 1 1 9 9 PRO HG2 H 1 2.206 0.05 . 2 . . . . . . . . 4381 1 70 . 1 1 9 9 PRO HG3 H 1 2.056 0.05 . 2 . . . . . . . . 4381 1 71 . 1 1 9 9 PRO CA C 13 65.896 0.1 . 1 . . . . . . . . 4381 1 72 . 1 1 9 9 PRO CB C 13 31.846 0.1 . 1 . . . . . . . . 4381 1 73 . 1 1 9 9 PRO CD C 13 50.176 0.1 . 1 . . . . . . . . 4381 1 74 . 1 1 9 9 PRO CG C 13 28.116 0.1 . 1 . . . . . . . . 4381 1 75 . 1 1 10 10 ALA H H 1 8.186 0.05 . 1 . . . . . . . . 4381 1 76 . 1 1 10 10 ALA HA H 1 4.096 0.05 . 1 . . . . . . . . 4381 1 77 . 1 1 10 10 ALA HB1 H 1 1.346 0.05 . 1 . . . . . . . . 4381 1 78 . 1 1 10 10 ALA HB2 H 1 1.346 0.05 . 1 . . . . . . . . 4381 1 79 . 1 1 10 10 ALA HB3 H 1 1.346 0.05 . 1 . . . . . . . . 4381 1 80 . 1 1 10 10 ALA C C 13 180.7 0.1 . 1 . . . . . . . . 4381 1 81 . 1 1 10 10 ALA CA C 13 54.836 0.1 . 1 . . . . . . . . 4381 1 82 . 1 1 10 10 ALA CB C 13 18.376 0.1 . 1 . . . . . . . . 4381 1 83 . 1 1 10 10 ALA N N 15 119.64 0.1 . 1 . . . . . . . . 4381 1 84 . 1 1 11 11 GLU H H 1 7.476 0.05 . 1 . . . . . . . . 4381 1 85 . 1 1 11 11 GLU HA H 1 3.576 0.05 . 1 . . . . . . . . 4381 1 86 . 1 1 11 11 GLU HB2 H 1 2.026 0.05 . 2 . . . . . . . . 4381 1 87 . 1 1 11 11 GLU HB3 H 1 1.836 0.05 . 2 . . . . . . . . 4381 1 88 . 1 1 11 11 GLU HG2 H 1 2.196 0.05 . 1 . . . . . . . . 4381 1 89 . 1 1 11 11 GLU HG3 H 1 2.196 0.05 . 1 . . . . . . . . 4381 1 90 . 1 1 11 11 GLU C C 13 176.88 0.1 . 1 . . . . . . . . 4381 1 91 . 1 1 11 11 GLU CA C 13 58.716 0.1 . 1 . . . . . . . . 4381 1 92 . 1 1 11 11 GLU CB C 13 29.786 0.1 . 1 . . . . . . . . 4381 1 93 . 1 1 11 11 GLU CG C 13 37.446 0.1 . 1 . . . . . . . . 4381 1 94 . 1 1 11 11 GLU N N 15 119.76 0.1 . 1 . . . . . . . . 4381 1 95 . 1 1 12 12 LYS H H 1 8.516 0.05 . 1 . . . . . . . . 4381 1 96 . 1 1 12 12 LYS HA H 1 3.676 0.05 . 1 . . . . . . . . 4381 1 97 . 1 1 12 12 LYS HB2 H 1 2.056 0.05 . 2 . . . . . . . . 4381 1 98 . 1 1 12 12 LYS HB3 H 1 1.676 0.05 . 2 . . . . . . . . 4381 1 99 . 1 1 12 12 LYS HD2 H 1 2.186 0.05 . 2 . . . . . . . . 4381 1 100 . 1 1 12 12 LYS HD3 H 1 1.586 0.05 . 2 . . . . . . . . 4381 1 101 . 1 1 12 12 LYS HE2 H 1 3.366 0.05 . 2 . . . . . . . . 4381 1 102 . 1 1 12 12 LYS HE3 H 1 3.136 0.05 . 2 . . . . . . . . 4381 1 103 . 1 1 12 12 LYS HG2 H 1 1.666 0.05 . 2 . . . . . . . . 4381 1 104 . 1 1 12 12 LYS HG3 H 1 1.566 0.05 . 2 . . . . . . . . 4381 1 105 . 1 1 12 12 LYS C C 13 176.94 0.1 . 1 . . . . . . . . 4381 1 106 . 1 1 12 12 LYS CA C 13 58.776 0.1 . 1 . . . . . . . . 4381 1 107 . 1 1 12 12 LYS CB C 13 32.516 0.1 . 1 . . . . . . . . 4381 1 108 . 1 1 12 12 LYS CD C 13 28.866 0.1 . 1 . . . . . . . . 4381 1 109 . 1 1 12 12 LYS CE C 13 42.416 0.1 . 1 . . . . . . . . 4381 1 110 . 1 1 12 12 LYS CG C 13 24.866 0.1 . 1 . . . . . . . . 4381 1 111 . 1 1 12 12 LYS N N 15 119.2 0.1 . 1 . . . . . . . . 4381 1 112 . 1 1 13 13 ALA H H 1 7.636 0.05 . 1 . . . . . . . . 4381 1 113 . 1 1 13 13 ALA HA H 1 4.156 0.05 . 1 . . . . . . . . 4381 1 114 . 1 1 13 13 ALA HB1 H 1 1.436 0.05 . 1 . . . . . . . . 4381 1 115 . 1 1 13 13 ALA HB2 H 1 1.436 0.05 . 1 . . . . . . . . 4381 1 116 . 1 1 13 13 ALA HB3 H 1 1.436 0.05 . 1 . . . . . . . . 4381 1 117 . 1 1 13 13 ALA C C 13 180.76 0.1 . 1 . . . . . . . . 4381 1 118 . 1 1 13 13 ALA CA C 13 54.996 0.1 . 1 . . . . . . . . 4381 1 119 . 1 1 13 13 ALA CB C 13 17.746 0.1 . 1 . . . . . . . . 4381 1 120 . 1 1 13 13 ALA N N 15 118.26 0.1 . 1 . . . . . . . . 4381 1 121 . 1 1 14 14 LYS H H 1 7.016 0.05 . 1 . . . . . . . . 4381 1 122 . 1 1 14 14 LYS HA H 1 4.116 0.05 . 1 . . . . . . . . 4381 1 123 . 1 1 14 14 LYS HB2 H 1 1.766 0.05 . 1 . . . . . . . . 4381 1 124 . 1 1 14 14 LYS HB3 H 1 1.766 0.05 . 1 . . . . . . . . 4381 1 125 . 1 1 14 14 LYS HD2 H 1 1.626 0.05 . 1 . . . . . . . . 4381 1 126 . 1 1 14 14 LYS HD3 H 1 1.626 0.05 . 1 . . . . . . . . 4381 1 127 . 1 1 14 14 LYS HE2 H 1 2.896 0.05 . 1 . . . . . . . . 4381 1 128 . 1 1 14 14 LYS HE3 H 1 2.896 0.05 . 1 . . . . . . . . 4381 1 129 . 1 1 14 14 LYS HG2 H 1 1.506 0.05 . 2 . . . . . . . . 4381 1 130 . 1 1 14 14 LYS HG3 H 1 1.276 0.05 . 2 . . . . . . . . 4381 1 131 . 1 1 14 14 LYS C C 13 179.89 0.1 . 1 . . . . . . . . 4381 1 132 . 1 1 14 14 LYS CA C 13 58.656 0.1 . 1 . . . . . . . . 4381 1 133 . 1 1 14 14 LYS CB C 13 31.746 0.1 . 1 . . . . . . . . 4381 1 134 . 1 1 14 14 LYS CD C 13 29.046 0.1 . 1 . . . . . . . . 4381 1 135 . 1 1 14 14 LYS CE C 13 41.876 0.1 . 1 . . . . . . . . 4381 1 136 . 1 1 14 14 LYS CG C 13 24.826 0.1 . 1 . . . . . . . . 4381 1 137 . 1 1 14 14 LYS N N 15 118.18 0.1 . 1 . . . . . . . . 4381 1 138 . 1 1 15 15 TYR H H 1 8.276 0.05 . 1 . . . . . . . . 4381 1 139 . 1 1 15 15 TYR HA H 1 4.626 0.05 . 1 . . . . . . . . 4381 1 140 . 1 1 15 15 TYR HB2 H 1 3.456 0.05 . 2 . . . . . . . . 4381 1 141 . 1 1 15 15 TYR HB3 H 1 3.136 0.05 . 2 . . . . . . . . 4381 1 142 . 1 1 15 15 TYR HD1 H 1 6.826 0.05 . 1 . . . . . . . . 4381 1 143 . 1 1 15 15 TYR HD2 H 1 6.826 0.05 . 1 . . . . . . . . 4381 1 144 . 1 1 15 15 TYR HE1 H 1 6.746 0.05 . 1 . . . . . . . . 4381 1 145 . 1 1 15 15 TYR HE2 H 1 6.746 0.05 . 1 . . . . . . . . 4381 1 146 . 1 1 15 15 TYR C C 13 178.31 0.1 . 1 . . . . . . . . 4381 1 147 . 1 1 15 15 TYR CA C 13 58.436 0.1 . 1 . . . . . . . . 4381 1 148 . 1 1 15 15 TYR CB C 13 35.696 0.1 . 1 . . . . . . . . 4381 1 149 . 1 1 15 15 TYR CD1 C 13 131.81 0.1 . 1 . . . . . . . . 4381 1 150 . 1 1 15 15 TYR CD2 C 13 131.81 0.1 . 1 . . . . . . . . 4381 1 151 . 1 1 15 15 TYR CE1 C 13 118.48 0.1 . 1 . . . . . . . . 4381 1 152 . 1 1 15 15 TYR CE2 C 13 118.48 0.1 . 1 . . . . . . . . 4381 1 153 . 1 1 15 15 TYR N N 15 121.57 0.1 . 1 . . . . . . . . 4381 1 154 . 1 1 16 16 ASP H H 1 9.296 0.05 . 1 . . . . . . . . 4381 1 155 . 1 1 16 16 ASP HA H 1 4.466 0.05 . 1 . . . . . . . . 4381 1 156 . 1 1 16 16 ASP HB2 H 1 2.856 0.05 . 2 . . . . . . . . 4381 1 157 . 1 1 16 16 ASP HB3 H 1 2.606 0.05 . 2 . . . . . . . . 4381 1 158 . 1 1 16 16 ASP C C 13 178.95 0.1 . 1 . . . . . . . . 4381 1 159 . 1 1 16 16 ASP CA C 13 57.156 0.1 . 1 . . . . . . . . 4381 1 160 . 1 1 16 16 ASP CB C 13 39.906 0.1 . 1 . . . . . . . . 4381 1 161 . 1 1 16 16 ASP N N 15 121.49 0.1 . 1 . . . . . . . . 4381 1 162 . 1 1 17 17 GLU H H 1 7.266 0.05 . 1 . . . . . . . . 4381 1 163 . 1 1 17 17 GLU HA H 1 4.136 0.05 . 1 . . . . . . . . 4381 1 164 . 1 1 17 17 GLU HB2 H 1 2.226 0.05 . 1 . . . . . . . . 4381 1 165 . 1 1 17 17 GLU HB3 H 1 2.226 0.05 . 1 . . . . . . . . 4381 1 166 . 1 1 17 17 GLU HG2 H 1 2.516 0.05 . 2 . . . . . . . . 4381 1 167 . 1 1 17 17 GLU HG3 H 1 2.256 0.05 . 2 . . . . . . . . 4381 1 168 . 1 1 17 17 GLU C C 13 179.48 0.1 . 1 . . . . . . . . 4381 1 169 . 1 1 17 17 GLU CA C 13 59.536 0.1 . 1 . . . . . . . . 4381 1 170 . 1 1 17 17 GLU CB C 13 29.546 0.1 . 1 . . . . . . . . 4381 1 171 . 1 1 17 17 GLU CG C 13 36.226 0.1 . 1 . . . . . . . . 4381 1 172 . 1 1 17 17 GLU N N 15 119.09 0.1 . 1 . . . . . . . . 4381 1 173 . 1 1 18 18 ILE H H 1 7.436 0.05 . 1 . . . . . . . . 4381 1 174 . 1 1 18 18 ILE HA H 1 3.726 0.05 . 1 . . . . . . . . 4381 1 175 . 1 1 18 18 ILE HB H 1 2.216 0.05 . 1 . . . . . . . . 4381 1 176 . 1 1 18 18 ILE HD11 H 1 0.796 0.05 . 1 . . . . . . . . 4381 1 177 . 1 1 18 18 ILE HD12 H 1 0.796 0.05 . 1 . . . . . . . . 4381 1 178 . 1 1 18 18 ILE HD13 H 1 0.796 0.05 . 1 . . . . . . . . 4381 1 179 . 1 1 18 18 ILE HG12 H 1 1.946 0.05 . 2 . . . . . . . . 4381 1 180 . 1 1 18 18 ILE HG13 H 1 1.156 0.05 . 2 . . . . . . . . 4381 1 181 . 1 1 18 18 ILE HG21 H 1 0.996 0.05 . 1 . . . . . . . . 4381 1 182 . 1 1 18 18 ILE HG22 H 1 0.996 0.05 . 1 . . . . . . . . 4381 1 183 . 1 1 18 18 ILE HG23 H 1 0.996 0.05 . 1 . . . . . . . . 4381 1 184 . 1 1 18 18 ILE C C 13 179.88 0.1 . 1 . . . . . . . . 4381 1 185 . 1 1 18 18 ILE CA C 13 64.896 0.1 . 1 . . . . . . . . 4381 1 186 . 1 1 18 18 ILE CB C 13 38.486 0.1 . 1 . . . . . . . . 4381 1 187 . 1 1 18 18 ILE CD1 C 13 13.466 0.1 . 1 . . . . . . . . 4381 1 188 . 1 1 18 18 ILE CG1 C 13 28.406 0.1 . 1 . . . . . . . . 4381 1 189 . 1 1 18 18 ILE CG2 C 13 18.126 0.1 . 1 . . . . . . . . 4381 1 190 . 1 1 18 18 ILE N N 15 120.22 0.1 . 1 . . . . . . . . 4381 1 191 . 1 1 19 19 PHE H H 1 9.586 0.05 . 1 . . . . . . . . 4381 1 192 . 1 1 19 19 PHE HA H 1 2.896 0.05 . 1 . . . . . . . . 4381 1 193 . 1 1 19 19 PHE HB2 H 1 3.386 0.05 . 2 . . . . . . . . 4381 1 194 . 1 1 19 19 PHE HB3 H 1 3.146 0.05 . 2 . . . . . . . . 4381 1 195 . 1 1 19 19 PHE HD1 H 1 6.616 0.05 . 1 . . . . . . . . 4381 1 196 . 1 1 19 19 PHE HD2 H 1 6.616 0.05 . 1 . . . . . . . . 4381 1 197 . 1 1 19 19 PHE HE1 H 1 7.016 0.05 . 1 . . . . . . . . 4381 1 198 . 1 1 19 19 PHE HE2 H 1 7.016 0.05 . 1 . . . . . . . . 4381 1 199 . 1 1 19 19 PHE C C 13 177.19 0.1 . 1 . . . . . . . . 4381 1 200 . 1 1 19 19 PHE CA C 13 62.286 0.1 . 1 . . . . . . . . 4381 1 201 . 1 1 19 19 PHE CB C 13 38.446 0.1 . 1 . . . . . . . . 4381 1 202 . 1 1 19 19 PHE CD1 C 13 131.92 0.1 . 1 . . . . . . . . 4381 1 203 . 1 1 19 19 PHE CD2 C 13 131.92 0.1 . 1 . . . . . . . . 4381 1 204 . 1 1 19 19 PHE CE1 C 13 131.25 0.1 . 1 . . . . . . . . 4381 1 205 . 1 1 19 19 PHE CE2 C 13 131.25 0.1 . 1 . . . . . . . . 4381 1 206 . 1 1 19 19 PHE N N 15 127.07 0.1 . 1 . . . . . . . . 4381 1 207 . 1 1 20 20 LEU H H 1 7.976 0.05 . 1 . . . . . . . . 4381 1 208 . 1 1 20 20 LEU HA H 1 4.016 0.05 . 1 . . . . . . . . 4381 1 209 . 1 1 20 20 LEU HB2 H 1 1.936 0.05 . 2 . . . . . . . . 4381 1 210 . 1 1 20 20 LEU HB3 H 1 1.696 0.05 . 2 . . . . . . . . 4381 1 211 . 1 1 20 20 LEU HD11 H 1 1.006 0.05 . 2 . . . . . . . . 4381 1 212 . 1 1 20 20 LEU HD12 H 1 1.006 0.05 . 2 . . . . . . . . 4381 1 213 . 1 1 20 20 LEU HD13 H 1 1.006 0.05 . 2 . . . . . . . . 4381 1 214 . 1 1 20 20 LEU HD21 H 1 0.996 0.05 . 2 . . . . . . . . 4381 1 215 . 1 1 20 20 LEU HD22 H 1 0.996 0.05 . 2 . . . . . . . . 4381 1 216 . 1 1 20 20 LEU HD23 H 1 0.996 0.05 . 2 . . . . . . . . 4381 1 217 . 1 1 20 20 LEU HG H 1 1.946 0.05 . 1 . . . . . . . . 4381 1 218 . 1 1 20 20 LEU C C 13 179.5 0.1 . 1 . . . . . . . . 4381 1 219 . 1 1 20 20 LEU CA C 13 57.736 0.1 . 1 . . . . . . . . 4381 1 220 . 1 1 20 20 LEU CB C 13 42.036 0.1 . 1 . . . . . . . . 4381 1 221 . 1 1 20 20 LEU CD1 C 13 24.996 0.1 . 2 . . . . . . . . 4381 1 222 . 1 1 20 20 LEU CD2 C 13 23.566 0.1 . 2 . . . . . . . . 4381 1 223 . 1 1 20 20 LEU CG C 13 27.146 0.1 . 1 . . . . . . . . 4381 1 224 . 1 1 20 20 LEU N N 15 117.44 0.1 . 1 . . . . . . . . 4381 1 225 . 1 1 21 21 LYS H H 1 7.106 0.05 . 1 . . . . . . . . 4381 1 226 . 1 1 21 21 LYS HA H 1 4.126 0.05 . 1 . . . . . . . . 4381 1 227 . 1 1 21 21 LYS HB2 H 1 1.926 0.05 . 1 . . . . . . . . 4381 1 228 . 1 1 21 21 LYS HB3 H 1 1.926 0.05 . 1 . . . . . . . . 4381 1 229 . 1 1 21 21 LYS HD2 H 1 1.656 0.05 . 1 . . . . . . . . 4381 1 230 . 1 1 21 21 LYS HD3 H 1 1.656 0.05 . 1 . . . . . . . . 4381 1 231 . 1 1 21 21 LYS HE2 H 1 3.086 0.05 . 2 . . . . . . . . 4381 1 232 . 1 1 21 21 LYS HE3 H 1 2.976 0.05 . 2 . . . . . . . . 4381 1 233 . 1 1 21 21 LYS HG2 H 1 1.616 0.05 . 2 . . . . . . . . 4381 1 234 . 1 1 21 21 LYS HG3 H 1 1.516 0.05 . 2 . . . . . . . . 4381 1 235 . 1 1 21 21 LYS C C 13 176.91 0.1 . 1 . . . . . . . . 4381 1 236 . 1 1 21 21 LYS CA C 13 57.596 0.1 . 1 . . . . . . . . 4381 1 237 . 1 1 21 21 LYS CB C 13 32.906 0.1 . 1 . . . . . . . . 4381 1 238 . 1 1 21 21 LYS CD C 13 29.286 0.1 . 1 . . . . . . . . 4381 1 239 . 1 1 21 21 LYS CE C 13 42.046 0.1 . 1 . . . . . . . . 4381 1 240 . 1 1 21 21 LYS CG C 13 25.776 0.1 . 1 . . . . . . . . 4381 1 241 . 1 1 21 21 LYS N N 15 115.59 0.1 . 1 . . . . . . . . 4381 1 242 . 1 1 22 22 THR H H 1 7.616 0.05 . 1 . . . . . . . . 4381 1 243 . 1 1 22 22 THR HA H 1 3.956 0.05 . 1 . . . . . . . . 4381 1 244 . 1 1 22 22 THR HB H 1 3.596 0.05 . 1 . . . . . . . . 4381 1 245 . 1 1 22 22 THR HG21 H 1 1.116 0.05 . 1 . . . . . . . . 4381 1 246 . 1 1 22 22 THR HG22 H 1 1.116 0.05 . 1 . . . . . . . . 4381 1 247 . 1 1 22 22 THR HG23 H 1 1.116 0.05 . 1 . . . . . . . . 4381 1 248 . 1 1 22 22 THR C C 13 174.75 0.1 . 1 . . . . . . . . 4381 1 249 . 1 1 22 22 THR CA C 13 64.496 0.1 . 1 . . . . . . . . 4381 1 250 . 1 1 22 22 THR CB C 13 68.586 0.1 . 1 . . . . . . . . 4381 1 251 . 1 1 22 22 THR CG2 C 13 22.796 0.1 . 1 . . . . . . . . 4381 1 252 . 1 1 22 22 THR N N 15 116.27 0.1 . 1 . . . . . . . . 4381 1 253 . 1 1 23 23 ASP H H 1 7.626 0.05 . 1 . . . . . . . . 4381 1 254 . 1 1 23 23 ASP HA H 1 4.406 0.05 . 1 . . . . . . . . 4381 1 255 . 1 1 23 23 ASP HB2 H 1 2.446 0.05 . 2 . . . . . . . . 4381 1 256 . 1 1 23 23 ASP HB3 H 1 1.516 0.05 . 2 . . . . . . . . 4381 1 257 . 1 1 23 23 ASP C C 13 176.71 0.1 . 1 . . . . . . . . 4381 1 258 . 1 1 23 23 ASP CA C 13 53.136 0.1 . 1 . . . . . . . . 4381 1 259 . 1 1 23 23 ASP CB C 13 38.206 0.1 . 1 . . . . . . . . 4381 1 260 . 1 1 23 23 ASP N N 15 121.33 0.1 . 1 . . . . . . . . 4381 1 261 . 1 1 24 24 LYS H H 1 7.736 0.05 . 1 . . . . . . . . 4381 1 262 . 1 1 24 24 LYS HA H 1 4.046 0.05 . 1 . . . . . . . . 4381 1 263 . 1 1 24 24 LYS HB2 H 1 1.886 0.05 . 1 . . . . . . . . 4381 1 264 . 1 1 24 24 LYS HB3 H 1 1.886 0.05 . 1 . . . . . . . . 4381 1 265 . 1 1 24 24 LYS HD2 H 1 1.726 0.05 . 1 . . . . . . . . 4381 1 266 . 1 1 24 24 LYS HD3 H 1 1.726 0.05 . 1 . . . . . . . . 4381 1 267 . 1 1 24 24 LYS HE2 H 1 3.096 0.05 . 1 . . . . . . . . 4381 1 268 . 1 1 24 24 LYS HE3 H 1 3.096 0.05 . 1 . . . . . . . . 4381 1 269 . 1 1 24 24 LYS HG2 H 1 1.596 0.05 . 2 . . . . . . . . 4381 1 270 . 1 1 24 24 LYS HG3 H 1 1.486 0.05 . 2 . . . . . . . . 4381 1 271 . 1 1 24 24 LYS C C 13 178.03 0.1 . 1 . . . . . . . . 4381 1 272 . 1 1 24 24 LYS CA C 13 58.076 0.1 . 1 . . . . . . . . 4381 1 273 . 1 1 24 24 LYS CB C 13 33.066 0.1 . 1 . . . . . . . . 4381 1 274 . 1 1 24 24 LYS CD C 13 28.506 0.1 . 1 . . . . . . . . 4381 1 275 . 1 1 24 24 LYS CE C 13 42.436 0.1 . 1 . . . . . . . . 4381 1 276 . 1 1 24 24 LYS CG C 13 25.016 0.1 . 1 . . . . . . . . 4381 1 277 . 1 1 24 24 LYS N N 15 127.45 0.1 . 1 . . . . . . . . 4381 1 278 . 1 1 25 25 ASP H H 1 8.006 0.05 . 1 . . . . . . . . 4381 1 279 . 1 1 25 25 ASP HA H 1 4.576 0.05 . 1 . . . . . . . . 4381 1 280 . 1 1 25 25 ASP HB2 H 1 3.056 0.05 . 2 . . . . . . . . 4381 1 281 . 1 1 25 25 ASP HB3 H 1 2.596 0.05 . 2 . . . . . . . . 4381 1 282 . 1 1 25 25 ASP C C 13 175.93 0.1 . 1 . . . . . . . . 4381 1 283 . 1 1 25 25 ASP CA C 13 52.916 0.1 . 1 . . . . . . . . 4381 1 284 . 1 1 25 25 ASP CB C 13 39.056 0.1 . 1 . . . . . . . . 4381 1 285 . 1 1 25 25 ASP N N 15 114.38 0.1 . 1 . . . . . . . . 4381 1 286 . 1 1 26 26 MET H H 1 7.606 0.05 . 1 . . . . . . . . 4381 1 287 . 1 1 26 26 MET HA H 1 3.976 0.05 . 1 . . . . . . . . 4381 1 288 . 1 1 26 26 MET HB2 H 1 2.256 0.05 . 2 . . . . . . . . 4381 1 289 . 1 1 26 26 MET HB3 H 1 2.186 0.05 . 2 . . . . . . . . 4381 1 290 . 1 1 26 26 MET HE1 H 1 2.096 0.05 . 1 . . . . . . . . 4381 1 291 . 1 1 26 26 MET HE2 H 1 2.096 0.05 . 1 . . . . . . . . 4381 1 292 . 1 1 26 26 MET HE3 H 1 2.096 0.05 . 1 . . . . . . . . 4381 1 293 . 1 1 26 26 MET HG2 H 1 2.476 0.05 . 1 . . . . . . . . 4381 1 294 . 1 1 26 26 MET HG3 H 1 2.476 0.05 . 1 . . . . . . . . 4381 1 295 . 1 1 26 26 MET C C 13 175.73 0.1 . 1 . . . . . . . . 4381 1 296 . 1 1 26 26 MET CA C 13 56.976 0.1 . 1 . . . . . . . . 4381 1 297 . 1 1 26 26 MET CB C 13 29.436 0.1 . 1 . . . . . . . . 4381 1 298 . 1 1 26 26 MET CE C 13 16.836 0.1 . 1 . . . . . . . . 4381 1 299 . 1 1 26 26 MET CG C 13 32.536 0.1 . 1 . . . . . . . . 4381 1 300 . 1 1 26 26 MET N N 15 114.84 0.1 . 1 . . . . . . . . 4381 1 301 . 1 1 27 27 ASP H H 1 8.686 0.05 . 1 . . . . . . . . 4381 1 302 . 1 1 27 27 ASP HA H 1 4.616 0.05 . 1 . . . . . . . . 4381 1 303 . 1 1 27 27 ASP HB2 H 1 3.126 0.05 . 2 . . . . . . . . 4381 1 304 . 1 1 27 27 ASP HB3 H 1 2.576 0.05 . 2 . . . . . . . . 4381 1 305 . 1 1 27 27 ASP C C 13 177.42 0.1 . 1 . . . . . . . . 4381 1 306 . 1 1 27 27 ASP CA C 13 53.516 0.1 . 1 . . . . . . . . 4381 1 307 . 1 1 27 27 ASP CB C 13 40.556 0.1 . 1 . . . . . . . . 4381 1 308 . 1 1 27 27 ASP N N 15 118.82 0.1 . 1 . . . . . . . . 4381 1 309 . 1 1 28 28 GLY H H 1 9.976 0.05 . 1 . . . . . . . . 4381 1 310 . 1 1 28 28 GLY HA2 H 1 3.976 0.05 . 2 . . . . . . . . 4381 1 311 . 1 1 28 28 GLY HA3 H 1 3.416 0.05 . 2 . . . . . . . . 4381 1 312 . 1 1 28 28 GLY C C 13 172.35 0.1 . 1 . . . . . . . . 4381 1 313 . 1 1 28 28 GLY CA C 13 45.226 0.1 . 1 . . . . . . . . 4381 1 314 . 1 1 28 28 GLY N N 15 111.84 0.1 . 1 . . . . . . . . 4381 1 315 . 1 1 29 29 PHE H H 1 8.116 0.05 . 1 . . . . . . . . 4381 1 316 . 1 1 29 29 PHE HA H 1 5.426 0.05 . 1 . . . . . . . . 4381 1 317 . 1 1 29 29 PHE HB2 H 1 2.766 0.05 . 2 . . . . . . . . 4381 1 318 . 1 1 29 29 PHE HB3 H 1 2.686 0.05 . 2 . . . . . . . . 4381 1 319 . 1 1 29 29 PHE HD1 H 1 6.886 0.05 . 1 . . . . . . . . 4381 1 320 . 1 1 29 29 PHE HD2 H 1 6.886 0.05 . 1 . . . . . . . . 4381 1 321 . 1 1 29 29 PHE HE1 H 1 7.326 0.05 . 1 . . . . . . . . 4381 1 322 . 1 1 29 29 PHE HE2 H 1 7.326 0.05 . 1 . . . . . . . . 4381 1 323 . 1 1 29 29 PHE C C 13 175.73 0.1 . 1 . . . . . . . . 4381 1 324 . 1 1 29 29 PHE CA C 13 56.236 0.1 . 1 . . . . . . . . 4381 1 325 . 1 1 29 29 PHE CB C 13 44.476 0.1 . 1 . . . . . . . . 4381 1 326 . 1 1 29 29 PHE CD1 C 13 132.35 0.1 . 1 . . . . . . . . 4381 1 327 . 1 1 29 29 PHE CD2 C 13 132.35 0.1 . 1 . . . . . . . . 4381 1 328 . 1 1 29 29 PHE CE1 C 13 131.17 0.1 . 1 . . . . . . . . 4381 1 329 . 1 1 29 29 PHE CE2 C 13 131.17 0.1 . 1 . . . . . . . . 4381 1 330 . 1 1 29 29 PHE N N 15 116.79 0.1 . 1 . . . . . . . . 4381 1 331 . 1 1 30 30 VAL H H 1 9.556 0.05 . 1 . . . . . . . . 4381 1 332 . 1 1 30 30 VAL HA H 1 5.166 0.05 . 1 . . . . . . . . 4381 1 333 . 1 1 30 30 VAL HB H 1 1.776 0.05 . 1 . . . . . . . . 4381 1 334 . 1 1 30 30 VAL HG11 H 1 0.546 0.05 . 2 . . . . . . . . 4381 1 335 . 1 1 30 30 VAL HG12 H 1 0.546 0.05 . 2 . . . . . . . . 4381 1 336 . 1 1 30 30 VAL HG13 H 1 0.546 0.05 . 2 . . . . . . . . 4381 1 337 . 1 1 30 30 VAL HG21 H 1 0.316 0.05 . 2 . . . . . . . . 4381 1 338 . 1 1 30 30 VAL HG22 H 1 0.316 0.05 . 2 . . . . . . . . 4381 1 339 . 1 1 30 30 VAL HG23 H 1 0.316 0.05 . 2 . . . . . . . . 4381 1 340 . 1 1 30 30 VAL C C 13 175.36 0.1 . 1 . . . . . . . . 4381 1 341 . 1 1 30 30 VAL CA C 13 59.556 0.1 . 1 . . . . . . . . 4381 1 342 . 1 1 30 30 VAL CB C 13 33.636 0.1 . 1 . . . . . . . . 4381 1 343 . 1 1 30 30 VAL CG1 C 13 22.636 0.1 . 2 . . . . . . . . 4381 1 344 . 1 1 30 30 VAL CG2 C 13 21.766 0.1 . 2 . . . . . . . . 4381 1 345 . 1 1 30 30 VAL N N 15 120.94 0.1 . 1 . . . . . . . . 4381 1 346 . 1 1 31 31 SER H H 1 9.526 0.05 . 1 . . . . . . . . 4381 1 347 . 1 1 31 31 SER HA H 1 5.126 0.05 . 1 . . . . . . . . 4381 1 348 . 1 1 31 31 SER HB2 H 1 4.506 0.05 . 2 . . . . . . . . 4381 1 349 . 1 1 31 31 SER HB3 H 1 4.046 0.05 . 2 . . . . . . . . 4381 1 350 . 1 1 31 31 SER C C 13 174.84 0.1 . 1 . . . . . . . . 4381 1 351 . 1 1 31 31 SER CA C 13 56.386 0.1 . 1 . . . . . . . . 4381 1 352 . 1 1 31 31 SER CB C 13 65.996 0.1 . 1 . . . . . . . . 4381 1 353 . 1 1 31 31 SER N N 15 124.04 0.1 . 1 . . . . . . . . 4381 1 354 . 1 1 32 32 GLY H H 1 8.266 0.05 . 1 . . . . . . . . 4381 1 355 . 1 1 32 32 GLY HA2 H 1 3.376 0.05 . 2 . . . . . . . . 4381 1 356 . 1 1 32 32 GLY HA3 H 1 2.986 0.05 . 2 . . . . . . . . 4381 1 357 . 1 1 32 32 GLY C C 13 176.01 0.1 . 1 . . . . . . . . 4381 1 358 . 1 1 32 32 GLY CA C 13 46.836 0.1 . 1 . . . . . . . . 4381 1 359 . 1 1 32 32 GLY N N 15 107.1 0.1 . 1 . . . . . . . . 4381 1 360 . 1 1 33 33 LEU H H 1 7.786 0.05 . 1 . . . . . . . . 4381 1 361 . 1 1 33 33 LEU HA H 1 4.076 0.05 . 1 . . . . . . . . 4381 1 362 . 1 1 33 33 LEU HB2 H 1 1.616 0.05 . 2 . . . . . . . . 4381 1 363 . 1 1 33 33 LEU HB3 H 1 1.546 0.05 . 2 . . . . . . . . 4381 1 364 . 1 1 33 33 LEU HD11 H 1 0.906 0.05 . 2 . . . . . . . . 4381 1 365 . 1 1 33 33 LEU HD12 H 1 0.906 0.05 . 2 . . . . . . . . 4381 1 366 . 1 1 33 33 LEU HD13 H 1 0.906 0.05 . 2 . . . . . . . . 4381 1 367 . 1 1 33 33 LEU HD21 H 1 0.846 0.05 . 2 . . . . . . . . 4381 1 368 . 1 1 33 33 LEU HD22 H 1 0.846 0.05 . 2 . . . . . . . . 4381 1 369 . 1 1 33 33 LEU HD23 H 1 0.846 0.05 . 2 . . . . . . . . 4381 1 370 . 1 1 33 33 LEU HG H 1 1.626 0.05 . 1 . . . . . . . . 4381 1 371 . 1 1 33 33 LEU C C 13 179.96 0.1 . 1 . . . . . . . . 4381 1 372 . 1 1 33 33 LEU CA C 13 57.386 0.1 . 1 . . . . . . . . 4381 1 373 . 1 1 33 33 LEU CB C 13 42.156 0.1 . 1 . . . . . . . . 4381 1 374 . 1 1 33 33 LEU CD1 C 13 24.306 0.1 . 2 . . . . . . . . 4381 1 375 . 1 1 33 33 LEU CD2 C 13 23.976 0.1 . 2 . . . . . . . . 4381 1 376 . 1 1 33 33 LEU CG C 13 27.126 0.1 . 1 . . . . . . . . 4381 1 377 . 1 1 33 33 LEU N N 15 120.12 0.1 . 1 . . . . . . . . 4381 1 378 . 1 1 34 34 GLU H H 1 7.716 0.05 . 1 . . . . . . . . 4381 1 379 . 1 1 34 34 GLU HA H 1 4.026 0.05 . 1 . . . . . . . . 4381 1 380 . 1 1 34 34 GLU HB2 H 1 2.466 0.05 . 1 . . . . . . . . 4381 1 381 . 1 1 34 34 GLU HB3 H 1 2.466 0.05 . 1 . . . . . . . . 4381 1 382 . 1 1 34 34 GLU HG2 H 1 2.576 0.05 . 2 . . . . . . . . 4381 1 383 . 1 1 34 34 GLU HG3 H 1 2.356 0.05 . 2 . . . . . . . . 4381 1 384 . 1 1 34 34 GLU C C 13 178.96 0.1 . 1 . . . . . . . . 4381 1 385 . 1 1 34 34 GLU CA C 13 58.656 0.1 . 1 . . . . . . . . 4381 1 386 . 1 1 34 34 GLU CB C 13 29.356 0.1 . 1 . . . . . . . . 4381 1 387 . 1 1 34 34 GLU CG C 13 38.066 0.1 . 1 . . . . . . . . 4381 1 388 . 1 1 34 34 GLU N N 15 119.04 0.1 . 1 . . . . . . . . 4381 1 389 . 1 1 35 35 VAL H H 1 7.696 0.05 . 1 . . . . . . . . 4381 1 390 . 1 1 35 35 VAL HA H 1 4.056 0.05 . 1 . . . . . . . . 4381 1 391 . 1 1 35 35 VAL HB H 1 1.836 0.05 . 1 . . . . . . . . 4381 1 392 . 1 1 35 35 VAL HG11 H 1 0.656 0.05 . 2 . . . . . . . . 4381 1 393 . 1 1 35 35 VAL HG12 H 1 0.656 0.05 . 2 . . . . . . . . 4381 1 394 . 1 1 35 35 VAL HG13 H 1 0.656 0.05 . 2 . . . . . . . . 4381 1 395 . 1 1 35 35 VAL HG21 H 1 0.576 0.05 . 2 . . . . . . . . 4381 1 396 . 1 1 35 35 VAL HG22 H 1 0.576 0.05 . 2 . . . . . . . . 4381 1 397 . 1 1 35 35 VAL HG23 H 1 0.576 0.05 . 2 . . . . . . . . 4381 1 398 . 1 1 35 35 VAL C C 13 175.05 0.1 . 1 . . . . . . . . 4381 1 399 . 1 1 35 35 VAL CA C 13 61.816 0.1 . 1 . . . . . . . . 4381 1 400 . 1 1 35 35 VAL CB C 13 32.816 0.1 . 1 . . . . . . . . 4381 1 401 . 1 1 35 35 VAL CG1 C 13 22.616 0.1 . 2 . . . . . . . . 4381 1 402 . 1 1 35 35 VAL CG2 C 13 19.706 0.1 . 2 . . . . . . . . 4381 1 403 . 1 1 35 35 VAL N N 15 113.89 0.1 . 1 . . . . . . . . 4381 1 404 . 1 1 36 36 ARG H H 1 6.976 0.05 . 1 . . . . . . . . 4381 1 405 . 1 1 36 36 ARG HA H 1 3.756 0.05 . 1 . . . . . . . . 4381 1 406 . 1 1 36 36 ARG HB2 H 1 1.956 0.05 . 2 . . . . . . . . 4381 1 407 . 1 1 36 36 ARG HB3 H 1 1.856 0.05 . 2 . . . . . . . . 4381 1 408 . 1 1 36 36 ARG HD2 H 1 3.186 0.05 . 1 . . . . . . . . 4381 1 409 . 1 1 36 36 ARG HD3 H 1 3.186 0.05 . 1 . . . . . . . . 4381 1 410 . 1 1 36 36 ARG HG2 H 1 1.716 0.05 . 2 . . . . . . . . 4381 1 411 . 1 1 36 36 ARG HG3 H 1 1.586 0.05 . 2 . . . . . . . . 4381 1 412 . 1 1 36 36 ARG C C 13 177.49 0.1 . 1 . . . . . . . . 4381 1 413 . 1 1 36 36 ARG CA C 13 60.526 0.1 . 1 . . . . . . . . 4381 1 414 . 1 1 36 36 ARG CB C 13 30.476 0.1 . 1 . . . . . . . . 4381 1 415 . 1 1 36 36 ARG CD C 13 43.416 0.1 . 1 . . . . . . . . 4381 1 416 . 1 1 36 36 ARG CG C 13 26.906 0.1 . 1 . . . . . . . . 4381 1 417 . 1 1 36 36 ARG N N 15 121.03 0.1 . 1 . . . . . . . . 4381 1 418 . 1 1 37 37 GLU H H 1 8.396 0.05 . 1 . . . . . . . . 4381 1 419 . 1 1 37 37 GLU HA H 1 4.066 0.05 . 1 . . . . . . . . 4381 1 420 . 1 1 37 37 GLU HB2 H 1 2.146 0.05 . 1 . . . . . . . . 4381 1 421 . 1 1 37 37 GLU HB3 H 1 2.146 0.05 . 1 . . . . . . . . 4381 1 422 . 1 1 37 37 GLU HG2 H 1 2.336 0.05 . 2 . . . . . . . . 4381 1 423 . 1 1 37 37 GLU HG3 H 1 2.256 0.05 . 2 . . . . . . . . 4381 1 424 . 1 1 37 37 GLU C C 13 179.15 0.1 . 1 . . . . . . . . 4381 1 425 . 1 1 37 37 GLU CA C 13 60.326 0.1 . 1 . . . . . . . . 4381 1 426 . 1 1 37 37 GLU CB C 13 29.116 0.1 . 1 . . . . . . . . 4381 1 427 . 1 1 37 37 GLU CG C 13 36.756 0.1 . 1 . . . . . . . . 4381 1 428 . 1 1 37 37 GLU N N 15 117.29 0.1 . 1 . . . . . . . . 4381 1 429 . 1 1 38 38 ILE H H 1 8.366 0.05 . 1 . . . . . . . . 4381 1 430 . 1 1 38 38 ILE HA H 1 4.096 0.05 . 1 . . . . . . . . 4381 1 431 . 1 1 38 38 ILE HB H 1 2.146 0.05 . 1 . . . . . . . . 4381 1 432 . 1 1 38 38 ILE HD11 H 1 1.096 0.05 . 1 . . . . . . . . 4381 1 433 . 1 1 38 38 ILE HD12 H 1 1.096 0.05 . 1 . . . . . . . . 4381 1 434 . 1 1 38 38 ILE HD13 H 1 1.096 0.05 . 1 . . . . . . . . 4381 1 435 . 1 1 38 38 ILE HG12 H 1 1.826 0.05 . 2 . . . . . . . . 4381 1 436 . 1 1 38 38 ILE HG13 H 1 1.496 0.05 . 2 . . . . . . . . 4381 1 437 . 1 1 38 38 ILE HG21 H 1 1.206 0.05 . 1 . . . . . . . . 4381 1 438 . 1 1 38 38 ILE HG22 H 1 1.206 0.05 . 1 . . . . . . . . 4381 1 439 . 1 1 38 38 ILE HG23 H 1 1.206 0.05 . 1 . . . . . . . . 4381 1 440 . 1 1 38 38 ILE C C 13 178.94 0.1 . 1 . . . . . . . . 4381 1 441 . 1 1 38 38 ILE CA C 13 64.366 0.1 . 1 . . . . . . . . 4381 1 442 . 1 1 38 38 ILE CB C 13 38.156 0.1 . 1 . . . . . . . . 4381 1 443 . 1 1 38 38 ILE CD1 C 13 14.676 0.1 . 1 . . . . . . . . 4381 1 444 . 1 1 38 38 ILE CG1 C 13 28.746 0.1 . 1 . . . . . . . . 4381 1 445 . 1 1 38 38 ILE CG2 C 13 18.126 0.1 . 1 . . . . . . . . 4381 1 446 . 1 1 38 38 ILE N N 15 118.67 0.1 . 1 . . . . . . . . 4381 1 447 . 1 1 39 39 PHE H H 1 8.556 0.05 . 1 . . . . . . . . 4381 1 448 . 1 1 39 39 PHE HA H 1 4.556 0.05 . 1 . . . . . . . . 4381 1 449 . 1 1 39 39 PHE HB2 H 1 3.516 0.05 . 2 . . . . . . . . 4381 1 450 . 1 1 39 39 PHE HB3 H 1 3.146 0.05 . 2 . . . . . . . . 4381 1 451 . 1 1 39 39 PHE HD1 H 1 7.126 0.05 . 1 . . . . . . . . 4381 1 452 . 1 1 39 39 PHE HD2 H 1 7.126 0.05 . 1 . . . . . . . . 4381 1 453 . 1 1 39 39 PHE HE1 H 1 7.166 0.05 . 1 . . . . . . . . 4381 1 454 . 1 1 39 39 PHE HE2 H 1 7.166 0.05 . 1 . . . . . . . . 4381 1 455 . 1 1 39 39 PHE HZ H 1 7.026 0.05 . 1 . . . . . . . . 4381 1 456 . 1 1 39 39 PHE C C 13 179.74 0.1 . 1 . . . . . . . . 4381 1 457 . 1 1 39 39 PHE CA C 13 58.726 0.1 . 1 . . . . . . . . 4381 1 458 . 1 1 39 39 PHE CB C 13 36.666 0.1 . 1 . . . . . . . . 4381 1 459 . 1 1 39 39 PHE CD1 C 13 129.74 0.1 . 1 . . . . . . . . 4381 1 460 . 1 1 39 39 PHE CD2 C 13 129.74 0.1 . 1 . . . . . . . . 4381 1 461 . 1 1 39 39 PHE CE1 C 13 131.36 0.1 . 1 . . . . . . . . 4381 1 462 . 1 1 39 39 PHE CE2 C 13 131.36 0.1 . 1 . . . . . . . . 4381 1 463 . 1 1 39 39 PHE CZ C 13 127.67 0.1 . 1 . . . . . . . . 4381 1 464 . 1 1 39 39 PHE N N 15 121.27 0.1 . 1 . . . . . . . . 4381 1 465 . 1 1 40 40 LEU H H 1 8.786 0.05 . 1 . . . . . . . . 4381 1 466 . 1 1 40 40 LEU HA H 1 4.136 0.05 . 1 . . . . . . . . 4381 1 467 . 1 1 40 40 LEU HB2 H 1 1.976 0.05 . 2 . . . . . . . . 4381 1 468 . 1 1 40 40 LEU HB3 H 1 1.666 0.05 . 2 . . . . . . . . 4381 1 469 . 1 1 40 40 LEU HD11 H 1 0.906 0.05 . 1 . . . . . . . . 4381 1 470 . 1 1 40 40 LEU HD12 H 1 0.906 0.05 . 1 . . . . . . . . 4381 1 471 . 1 1 40 40 LEU HD13 H 1 0.906 0.05 . 1 . . . . . . . . 4381 1 472 . 1 1 40 40 LEU HD21 H 1 0.906 0.05 . 1 . . . . . . . . 4381 1 473 . 1 1 40 40 LEU HD22 H 1 0.906 0.05 . 1 . . . . . . . . 4381 1 474 . 1 1 40 40 LEU HD23 H 1 0.906 0.05 . 1 . . . . . . . . 4381 1 475 . 1 1 40 40 LEU HG H 1 1.846 0.05 . 1 . . . . . . . . 4381 1 476 . 1 1 40 40 LEU C C 13 180.49 0.1 . 1 . . . . . . . . 4381 1 477 . 1 1 40 40 LEU CA C 13 58.436 0.1 . 1 . . . . . . . . 4381 1 478 . 1 1 40 40 LEU CB C 13 41.516 0.1 . 1 . . . . . . . . 4381 1 479 . 1 1 40 40 LEU CD1 C 13 25.096 0.1 . 2 . . . . . . . . 4381 1 480 . 1 1 40 40 LEU CD2 C 13 23.306 0.1 . 2 . . . . . . . . 4381 1 481 . 1 1 40 40 LEU CG C 13 27.166 0.1 . 1 . . . . . . . . 4381 1 482 . 1 1 40 40 LEU N N 15 122.97 0.1 . 1 . . . . . . . . 4381 1 483 . 1 1 41 41 LYS H H 1 7.956 0.05 . 1 . . . . . . . . 4381 1 484 . 1 1 41 41 LYS HA H 1 4.126 0.05 . 1 . . . . . . . . 4381 1 485 . 1 1 41 41 LYS HB2 H 1 2.076 0.05 . 1 . . . . . . . . 4381 1 486 . 1 1 41 41 LYS HB3 H 1 2.076 0.05 . 1 . . . . . . . . 4381 1 487 . 1 1 41 41 LYS HD2 H 1 1.736 0.05 . 1 . . . . . . . . 4381 1 488 . 1 1 41 41 LYS HD3 H 1 1.736 0.05 . 1 . . . . . . . . 4381 1 489 . 1 1 41 41 LYS HE2 H 1 3.026 0.05 . 1 . . . . . . . . 4381 1 490 . 1 1 41 41 LYS HE3 H 1 3.026 0.05 . 1 . . . . . . . . 4381 1 491 . 1 1 41 41 LYS HG2 H 1 1.736 0.05 . 2 . . . . . . . . 4381 1 492 . 1 1 41 41 LYS HG3 H 1 1.606 0.05 . 2 . . . . . . . . 4381 1 493 . 1 1 41 41 LYS C C 13 177.91 0.1 . 1 . . . . . . . . 4381 1 494 . 1 1 41 41 LYS CA C 13 58.076 0.1 . 1 . . . . . . . . 4381 1 495 . 1 1 41 41 LYS CB C 13 32.506 0.1 . 1 . . . . . . . . 4381 1 496 . 1 1 41 41 LYS CD C 13 29.096 0.1 . 1 . . . . . . . . 4381 1 497 . 1 1 41 41 LYS CE C 13 41.966 0.1 . 1 . . . . . . . . 4381 1 498 . 1 1 41 41 LYS CG C 13 25.646 0.1 . 1 . . . . . . . . 4381 1 499 . 1 1 41 41 LYS N N 15 118.37 0.1 . 1 . . . . . . . . 4381 1 500 . 1 1 42 42 THR H H 1 7.536 0.05 . 1 . . . . . . . . 4381 1 501 . 1 1 42 42 THR HA H 1 4.116 0.05 . 1 . . . . . . . . 4381 1 502 . 1 1 42 42 THR HB H 1 4.096 0.05 . 1 . . . . . . . . 4381 1 503 . 1 1 42 42 THR HG21 H 1 1.536 0.05 . 1 . . . . . . . . 4381 1 504 . 1 1 42 42 THR HG22 H 1 1.536 0.05 . 1 . . . . . . . . 4381 1 505 . 1 1 42 42 THR HG23 H 1 1.536 0.05 . 1 . . . . . . . . 4381 1 506 . 1 1 42 42 THR C C 13 176.42 0.1 . 1 . . . . . . . . 4381 1 507 . 1 1 42 42 THR CA C 13 64.326 0.1 . 1 . . . . . . . . 4381 1 508 . 1 1 42 42 THR CB C 13 70.996 0.1 . 1 . . . . . . . . 4381 1 509 . 1 1 42 42 THR CG2 C 13 21.366 0.1 . 1 . . . . . . . . 4381 1 510 . 1 1 42 42 THR N N 15 108.5 0.1 . 1 . . . . . . . . 4381 1 511 . 1 1 43 43 GLY H H 1 7.546 0.05 . 1 . . . . . . . . 4381 1 512 . 1 1 43 43 GLY HA2 H 1 4.106 0.05 . 2 . . . . . . . . 4381 1 513 . 1 1 43 43 GLY HA3 H 1 3.806 0.05 . 2 . . . . . . . . 4381 1 514 . 1 1 43 43 GLY C C 13 174.28 0.1 . 1 . . . . . . . . 4381 1 515 . 1 1 43 43 GLY CA C 13 45.526 0.1 . 1 . . . . . . . . 4381 1 516 . 1 1 43 43 GLY N N 15 106.67 0.1 . 1 . . . . . . . . 4381 1 517 . 1 1 44 44 LEU H H 1 7.646 0.05 . 1 . . . . . . . . 4381 1 518 . 1 1 44 44 LEU HA H 1 4.496 0.05 . 1 . . . . . . . . 4381 1 519 . 1 1 44 44 LEU HB2 H 1 1.546 0.05 . 2 . . . . . . . . 4381 1 520 . 1 1 44 44 LEU HB3 H 1 1.166 0.05 . 2 . . . . . . . . 4381 1 521 . 1 1 44 44 LEU HD11 H 1 0.836 0.05 . 2 . . . . . . . . 4381 1 522 . 1 1 44 44 LEU HD12 H 1 0.836 0.05 . 2 . . . . . . . . 4381 1 523 . 1 1 44 44 LEU HD13 H 1 0.836 0.05 . 2 . . . . . . . . 4381 1 524 . 1 1 44 44 LEU HD21 H 1 0.746 0.05 . 2 . . . . . . . . 4381 1 525 . 1 1 44 44 LEU HD22 H 1 0.746 0.05 . 2 . . . . . . . . 4381 1 526 . 1 1 44 44 LEU HD23 H 1 0.746 0.05 . 2 . . . . . . . . 4381 1 527 . 1 1 44 44 LEU HG H 1 1.546 0.05 . 1 . . . . . . . . 4381 1 528 . 1 1 44 44 LEU CA C 13 53.016 0.1 . 1 . . . . . . . . 4381 1 529 . 1 1 44 44 LEU CB C 13 40.886 0.1 . 1 . . . . . . . . 4381 1 530 . 1 1 44 44 LEU CD1 C 13 23.626 0.1 . 2 . . . . . . . . 4381 1 531 . 1 1 44 44 LEU CD2 C 13 25.766 0.1 . 2 . . . . . . . . 4381 1 532 . 1 1 44 44 LEU CG C 13 27.596 0.1 . 1 . . . . . . . . 4381 1 533 . 1 1 44 44 LEU N N 15 120.7 0.1 . 1 . . . . . . . . 4381 1 534 . 1 1 45 45 PRO HA H 1 4.496 0.05 . 1 . . . . . . . . 4381 1 535 . 1 1 45 45 PRO HB2 H 1 2.496 0.05 . 2 . . . . . . . . 4381 1 536 . 1 1 45 45 PRO HB3 H 1 1.856 0.05 . 2 . . . . . . . . 4381 1 537 . 1 1 45 45 PRO HD2 H 1 3.956 0.05 . 2 . . . . . . . . 4381 1 538 . 1 1 45 45 PRO HD3 H 1 3.386 0.05 . 2 . . . . . . . . 4381 1 539 . 1 1 45 45 PRO HG2 H 1 2.106 0.05 . 1 . . . . . . . . 4381 1 540 . 1 1 45 45 PRO HG3 H 1 2.106 0.05 . 1 . . . . . . . . 4381 1 541 . 1 1 45 45 PRO CA C 13 62.676 0.1 . 1 . . . . . . . . 4381 1 542 . 1 1 45 45 PRO CB C 13 32.556 0.1 . 1 . . . . . . . . 4381 1 543 . 1 1 45 45 PRO CD C 13 50.506 0.1 . 1 . . . . . . . . 4381 1 544 . 1 1 45 45 PRO CG C 13 28.086 0.1 . 1 . . . . . . . . 4381 1 545 . 1 1 47 47 THR HA H 1 4.046 0.05 . 1 . . . . . . . . 4381 1 546 . 1 1 47 47 THR HB H 1 4.156 0.05 . 1 . . . . . . . . 4381 1 547 . 1 1 47 47 THR HG21 H 1 1.296 0.05 . 1 . . . . . . . . 4381 1 548 . 1 1 47 47 THR HG22 H 1 1.296 0.05 . 1 . . . . . . . . 4381 1 549 . 1 1 47 47 THR HG23 H 1 1.296 0.05 . 1 . . . . . . . . 4381 1 550 . 1 1 47 47 THR C C 13 176.77 0.1 . 1 . . . . . . . . 4381 1 551 . 1 1 47 47 THR CA C 13 64.586 0.1 . 1 . . . . . . . . 4381 1 552 . 1 1 47 47 THR CB C 13 67.906 0.1 . 1 . . . . . . . . 4381 1 553 . 1 1 47 47 THR CG2 C 13 22.376 0.1 . 1 . . . . . . . . 4381 1 554 . 1 1 48 48 LEU H H 1 6.866 0.05 . 1 . . . . . . . . 4381 1 555 . 1 1 48 48 LEU HA H 1 4.366 0.05 . 1 . . . . . . . . 4381 1 556 . 1 1 48 48 LEU HB2 H 1 1.776 0.05 . 2 . . . . . . . . 4381 1 557 . 1 1 48 48 LEU HB3 H 1 1.726 0.05 . 2 . . . . . . . . 4381 1 558 . 1 1 48 48 LEU HD11 H 1 0.956 0.05 . 2 . . . . . . . . 4381 1 559 . 1 1 48 48 LEU HD12 H 1 0.956 0.05 . 2 . . . . . . . . 4381 1 560 . 1 1 48 48 LEU HD13 H 1 0.956 0.05 . 2 . . . . . . . . 4381 1 561 . 1 1 48 48 LEU HD21 H 1 0.886 0.05 . 2 . . . . . . . . 4381 1 562 . 1 1 48 48 LEU HD22 H 1 0.886 0.05 . 2 . . . . . . . . 4381 1 563 . 1 1 48 48 LEU HD23 H 1 0.886 0.05 . 2 . . . . . . . . 4381 1 564 . 1 1 48 48 LEU HG H 1 1.636 0.05 . 1 . . . . . . . . 4381 1 565 . 1 1 48 48 LEU C C 13 179 0.1 . 1 . . . . . . . . 4381 1 566 . 1 1 48 48 LEU CA C 13 57.436 0.1 . 1 . . . . . . . . 4381 1 567 . 1 1 48 48 LEU CB C 13 42.466 0.1 . 1 . . . . . . . . 4381 1 568 . 1 1 48 48 LEU CD1 C 13 25.116 0.1 . 2 . . . . . . . . 4381 1 569 . 1 1 48 48 LEU CD2 C 13 26.426 0.1 . 2 . . . . . . . . 4381 1 570 . 1 1 48 48 LEU CG C 13 27.716 0.1 . 1 . . . . . . . . 4381 1 571 . 1 1 48 48 LEU N N 15 125.08 0.1 . 1 . . . . . . . . 4381 1 572 . 1 1 49 49 LEU H H 1 7.696 0.05 . 1 . . . . . . . . 4381 1 573 . 1 1 49 49 LEU HA H 1 3.686 0.05 . 1 . . . . . . . . 4381 1 574 . 1 1 49 49 LEU HB2 H 1 1.756 0.05 . 2 . . . . . . . . 4381 1 575 . 1 1 49 49 LEU HB3 H 1 1.256 0.05 . 2 . . . . . . . . 4381 1 576 . 1 1 49 49 LEU HD11 H 1 0.666 0.05 . 2 . . . . . . . . 4381 1 577 . 1 1 49 49 LEU HD12 H 1 0.666 0.05 . 2 . . . . . . . . 4381 1 578 . 1 1 49 49 LEU HD13 H 1 0.666 0.05 . 2 . . . . . . . . 4381 1 579 . 1 1 49 49 LEU HD21 H 1 0.246 0.05 . 2 . . . . . . . . 4381 1 580 . 1 1 49 49 LEU HD22 H 1 0.246 0.05 . 2 . . . . . . . . 4381 1 581 . 1 1 49 49 LEU HD23 H 1 0.246 0.05 . 2 . . . . . . . . 4381 1 582 . 1 1 49 49 LEU HG H 1 1.366 0.05 . 1 . . . . . . . . 4381 1 583 . 1 1 49 49 LEU C C 13 178.32 0.1 . 1 . . . . . . . . 4381 1 584 . 1 1 49 49 LEU CA C 13 57.926 0.1 . 1 . . . . . . . . 4381 1 585 . 1 1 49 49 LEU CB C 13 41.556 0.1 . 1 . . . . . . . . 4381 1 586 . 1 1 49 49 LEU CD1 C 13 26.536 0.1 . 2 . . . . . . . . 4381 1 587 . 1 1 49 49 LEU CD2 C 13 21.626 0.1 . 2 . . . . . . . . 4381 1 588 . 1 1 49 49 LEU CG C 13 26.386 0.1 . 1 . . . . . . . . 4381 1 589 . 1 1 49 49 LEU N N 15 119.83 0.1 . 1 . . . . . . . . 4381 1 590 . 1 1 50 50 ALA H H 1 8.326 0.05 . 1 . . . . . . . . 4381 1 591 . 1 1 50 50 ALA HA H 1 4.306 0.05 . 1 . . . . . . . . 4381 1 592 . 1 1 50 50 ALA HB1 H 1 1.536 0.05 . 1 . . . . . . . . 4381 1 593 . 1 1 50 50 ALA HB2 H 1 1.536 0.05 . 1 . . . . . . . . 4381 1 594 . 1 1 50 50 ALA HB3 H 1 1.536 0.05 . 1 . . . . . . . . 4381 1 595 . 1 1 50 50 ALA C C 13 180.48 0.1 . 1 . . . . . . . . 4381 1 596 . 1 1 50 50 ALA CA C 13 54.936 0.1 . 1 . . . . . . . . 4381 1 597 . 1 1 50 50 ALA CB C 13 17.956 0.1 . 1 . . . . . . . . 4381 1 598 . 1 1 50 50 ALA N N 15 120.39 0.1 . 1 . . . . . . . . 4381 1 599 . 1 1 51 51 HIS H H 1 7.676 0.05 . 1 . . . . . . . . 4381 1 600 . 1 1 51 51 HIS HA H 1 4.496 0.05 . 1 . . . . . . . . 4381 1 601 . 1 1 51 51 HIS HB2 H 1 3.426 0.05 . 2 . . . . . . . . 4381 1 602 . 1 1 51 51 HIS HB3 H 1 3.216 0.05 . 2 . . . . . . . . 4381 1 603 . 1 1 51 51 HIS HD2 H 1 6.466 0.05 . 1 . . . . . . . . 4381 1 604 . 1 1 51 51 HIS HE1 H 1 7.736 0.05 . 1 . . . . . . . . 4381 1 605 . 1 1 51 51 HIS C C 13 177.71 0.1 . 1 . . . . . . . . 4381 1 606 . 1 1 51 51 HIS CA C 13 59.716 0.1 . 1 . . . . . . . . 4381 1 607 . 1 1 51 51 HIS CB C 13 31.326 0.1 . 1 . . . . . . . . 4381 1 608 . 1 1 51 51 HIS CE1 C 13 115.91 0.1 . 1 . . . . . . . . 4381 1 609 . 1 1 51 51 HIS N N 15 120.25 0.1 . 1 . . . . . . . . 4381 1 610 . 1 1 52 52 ILE H H 1 8.276 0.05 . 1 . . . . . . . . 4381 1 611 . 1 1 52 52 ILE HA H 1 3.336 0.05 . 1 . . . . . . . . 4381 1 612 . 1 1 52 52 ILE HB H 1 1.946 0.05 . 1 . . . . . . . . 4381 1 613 . 1 1 52 52 ILE HD11 H 1 0.596 0.05 . 1 . . . . . . . . 4381 1 614 . 1 1 52 52 ILE HD12 H 1 0.596 0.05 . 1 . . . . . . . . 4381 1 615 . 1 1 52 52 ILE HD13 H 1 0.596 0.05 . 1 . . . . . . . . 4381 1 616 . 1 1 52 52 ILE HG12 H 1 1.946 0.05 . 2 . . . . . . . . 4381 1 617 . 1 1 52 52 ILE HG13 H 1 0.746 0.05 . 2 . . . . . . . . 4381 1 618 . 1 1 52 52 ILE HG21 H 1 0.906 0.05 . 1 . . . . . . . . 4381 1 619 . 1 1 52 52 ILE HG22 H 1 0.906 0.05 . 1 . . . . . . . . 4381 1 620 . 1 1 52 52 ILE HG23 H 1 0.906 0.05 . 1 . . . . . . . . 4381 1 621 . 1 1 52 52 ILE C C 13 177.19 0.1 . 1 . . . . . . . . 4381 1 622 . 1 1 52 52 ILE CA C 13 66.856 0.1 . 1 . . . . . . . . 4381 1 623 . 1 1 52 52 ILE CB C 13 38.206 0.1 . 1 . . . . . . . . 4381 1 624 . 1 1 52 52 ILE CD1 C 13 13.606 0.1 . 1 . . . . . . . . 4381 1 625 . 1 1 52 52 ILE CG1 C 13 30.546 0.1 . 1 . . . . . . . . 4381 1 626 . 1 1 52 52 ILE CG2 C 13 17.356 0.1 . 1 . . . . . . . . 4381 1 627 . 1 1 52 52 ILE N N 15 119.32 0.1 . 1 . . . . . . . . 4381 1 628 . 1 1 53 53 TRP H H 1 8.886 0.05 . 1 . . . . . . . . 4381 1 629 . 1 1 53 53 TRP HA H 1 3.856 0.05 . 1 . . . . . . . . 4381 1 630 . 1 1 53 53 TRP HB2 H 1 3.536 0.05 . 2 . . . . . . . . 4381 1 631 . 1 1 53 53 TRP HB3 H 1 3.466 0.05 . 2 . . . . . . . . 4381 1 632 . 1 1 53 53 TRP HD1 H 1 7.216 0.05 . 1 . . . . . . . . 4381 1 633 . 1 1 53 53 TRP HE1 H 1 10.066 0.05 . 1 . . . . . . . . 4381 1 634 . 1 1 53 53 TRP HE3 H 1 7.446 0.05 . 1 . . . . . . . . 4381 1 635 . 1 1 53 53 TRP HH2 H 1 7.156 0.05 . 1 . . . . . . . . 4381 1 636 . 1 1 53 53 TRP HZ2 H 1 7.056 0.05 . 1 . . . . . . . . 4381 1 637 . 1 1 53 53 TRP HZ3 H 1 6.446 0.05 . 1 . . . . . . . . 4381 1 638 . 1 1 53 53 TRP C C 13 176.83 0.1 . 1 . . . . . . . . 4381 1 639 . 1 1 53 53 TRP CA C 13 62.026 0.1 . 1 . . . . . . . . 4381 1 640 . 1 1 53 53 TRP CB C 13 29.036 0.1 . 1 . . . . . . . . 4381 1 641 . 1 1 53 53 TRP CD1 C 13 124.6 0.1 . 1 . . . . . . . . 4381 1 642 . 1 1 53 53 TRP CE3 C 13 118.71 0.1 . 1 . . . . . . . . 4381 1 643 . 1 1 53 53 TRP CH2 C 13 124.52 0.1 . 1 . . . . . . . . 4381 1 644 . 1 1 53 53 TRP CZ2 C 13 113.32 0.1 . 1 . . . . . . . . 4381 1 645 . 1 1 53 53 TRP CZ3 C 13 121.95 0.1 . 1 . . . . . . . . 4381 1 646 . 1 1 53 53 TRP N N 15 120.08 0.1 . 1 . . . . . . . . 4381 1 647 . 1 1 53 53 TRP NE1 N 15 129.22 0.1 . 1 . . . . . . . . 4381 1 648 . 1 1 54 54 SER H H 1 8.186 0.05 . 1 . . . . . . . . 4381 1 649 . 1 1 54 54 SER HA H 1 4.256 0.05 . 1 . . . . . . . . 4381 1 650 . 1 1 54 54 SER HB2 H 1 4.086 0.05 . 1 . . . . . . . . 4381 1 651 . 1 1 54 54 SER HB3 H 1 4.086 0.05 . 1 . . . . . . . . 4381 1 652 . 1 1 54 54 SER C C 13 176.6 0.1 . 1 . . . . . . . . 4381 1 653 . 1 1 54 54 SER CA C 13 61.626 0.1 . 1 . . . . . . . . 4381 1 654 . 1 1 54 54 SER CB C 13 63.056 0.1 . 1 . . . . . . . . 4381 1 655 . 1 1 54 54 SER N N 15 112.18 0.1 . 1 . . . . . . . . 4381 1 656 . 1 1 55 55 LEU H H 1 7.916 0.05 . 1 . . . . . . . . 4381 1 657 . 1 1 55 55 LEU HA H 1 3.916 0.05 . 1 . . . . . . . . 4381 1 658 . 1 1 55 55 LEU HB2 H 1 1.956 0.05 . 2 . . . . . . . . 4381 1 659 . 1 1 55 55 LEU HB3 H 1 1.196 0.05 . 2 . . . . . . . . 4381 1 660 . 1 1 55 55 LEU HD11 H 1 0.656 0.05 . 2 . . . . . . . . 4381 1 661 . 1 1 55 55 LEU HD12 H 1 0.656 0.05 . 2 . . . . . . . . 4381 1 662 . 1 1 55 55 LEU HD13 H 1 0.656 0.05 . 2 . . . . . . . . 4381 1 663 . 1 1 55 55 LEU HD21 H 1 0.636 0.05 . 2 . . . . . . . . 4381 1 664 . 1 1 55 55 LEU HD22 H 1 0.636 0.05 . 2 . . . . . . . . 4381 1 665 . 1 1 55 55 LEU HD23 H 1 0.636 0.05 . 2 . . . . . . . . 4381 1 666 . 1 1 55 55 LEU HG H 1 1.286 0.05 . 1 . . . . . . . . 4381 1 667 . 1 1 55 55 LEU C C 13 177.94 0.1 . 1 . . . . . . . . 4381 1 668 . 1 1 55 55 LEU CA C 13 56.796 0.1 . 1 . . . . . . . . 4381 1 669 . 1 1 55 55 LEU CB C 13 43.496 0.1 . 1 . . . . . . . . 4381 1 670 . 1 1 55 55 LEU CD1 C 13 22.586 0.1 . 2 . . . . . . . . 4381 1 671 . 1 1 55 55 LEU CD2 C 13 25.896 0.1 . 2 . . . . . . . . 4381 1 672 . 1 1 55 55 LEU CG C 13 25.736 0.1 . 1 . . . . . . . . 4381 1 673 . 1 1 55 55 LEU N N 15 119.93 0.1 . 1 . . . . . . . . 4381 1 674 . 1 1 56 56 CYS H H 1 7.216 0.05 . 1 . . . . . . . . 4381 1 675 . 1 1 56 56 CYS HA H 1 4.156 0.05 . 1 . . . . . . . . 4381 1 676 . 1 1 56 56 CYS HB2 H 1 2.696 0.05 . 2 . . . . . . . . 4381 1 677 . 1 1 56 56 CYS HB3 H 1 2.576 0.05 . 2 . . . . . . . . 4381 1 678 . 1 1 56 56 CYS C C 13 174.11 0.1 . 1 . . . . . . . . 4381 1 679 . 1 1 56 56 CYS CA C 13 62.926 0.1 . 1 . . . . . . . . 4381 1 680 . 1 1 56 56 CYS CB C 13 28.216 0.1 . 1 . . . . . . . . 4381 1 681 . 1 1 56 56 CYS N N 15 113.12 0.1 . 1 . . . . . . . . 4381 1 682 . 1 1 57 57 ASP H H 1 7.776 0.05 . 1 . . . . . . . . 4381 1 683 . 1 1 57 57 ASP HA H 1 4.516 0.05 . 1 . . . . . . . . 4381 1 684 . 1 1 57 57 ASP HB2 H 1 2.716 0.05 . 2 . . . . . . . . 4381 1 685 . 1 1 57 57 ASP HB3 H 1 1.726 0.05 . 2 . . . . . . . . 4381 1 686 . 1 1 57 57 ASP C C 13 178.49 0.1 . 1 . . . . . . . . 4381 1 687 . 1 1 57 57 ASP CA C 13 51.326 0.1 . 1 . . . . . . . . 4381 1 688 . 1 1 57 57 ASP CB C 13 37.616 0.1 . 1 . . . . . . . . 4381 1 689 . 1 1 57 57 ASP N N 15 119.31 0.1 . 1 . . . . . . . . 4381 1 690 . 1 1 58 58 THR H H 1 7.896 0.05 . 1 . . . . . . . . 4381 1 691 . 1 1 58 58 THR HA H 1 3.936 0.05 . 1 . . . . . . . . 4381 1 692 . 1 1 58 58 THR HB H 1 4.216 0.05 . 1 . . . . . . . . 4381 1 693 . 1 1 58 58 THR HG21 H 1 1.296 0.05 . 1 . . . . . . . . 4381 1 694 . 1 1 58 58 THR HG22 H 1 1.296 0.05 . 1 . . . . . . . . 4381 1 695 . 1 1 58 58 THR HG23 H 1 1.296 0.05 . 1 . . . . . . . . 4381 1 696 . 1 1 58 58 THR C C 13 176.88 0.1 . 1 . . . . . . . . 4381 1 697 . 1 1 58 58 THR CA C 13 64.936 0.1 . 1 . . . . . . . . 4381 1 698 . 1 1 58 58 THR CB C 13 68.216 0.1 . 1 . . . . . . . . 4381 1 699 . 1 1 58 58 THR CG2 C 13 22.376 0.1 . 1 . . . . . . . . 4381 1 700 . 1 1 58 58 THR N N 15 115.87 0.1 . 1 . . . . . . . . 4381 1 701 . 1 1 59 59 LYS H H 1 8.546 0.05 . 1 . . . . . . . . 4381 1 702 . 1 1 59 59 LYS HA H 1 4.426 0.05 . 1 . . . . . . . . 4381 1 703 . 1 1 59 59 LYS HB2 H 1 2.066 0.05 . 2 . . . . . . . . 4381 1 704 . 1 1 59 59 LYS HB3 H 1 1.906 0.05 . 2 . . . . . . . . 4381 1 705 . 1 1 59 59 LYS HD2 H 1 1.676 0.05 . 1 . . . . . . . . 4381 1 706 . 1 1 59 59 LYS HD3 H 1 1.676 0.05 . 1 . . . . . . . . 4381 1 707 . 1 1 59 59 LYS HE2 H 1 2.966 0.05 . 1 . . . . . . . . 4381 1 708 . 1 1 59 59 LYS HE3 H 1 2.966 0.05 . 1 . . . . . . . . 4381 1 709 . 1 1 59 59 LYS HG2 H 1 1.506 0.05 . 2 . . . . . . . . 4381 1 710 . 1 1 59 59 LYS HG3 H 1 1.396 0.05 . 2 . . . . . . . . 4381 1 711 . 1 1 59 59 LYS C C 13 175.67 0.1 . 1 . . . . . . . . 4381 1 712 . 1 1 59 59 LYS CA C 13 55.106 0.1 . 1 . . . . . . . . 4381 1 713 . 1 1 59 59 LYS CB C 13 31.706 0.1 . 1 . . . . . . . . 4381 1 714 . 1 1 59 59 LYS CD C 13 28.456 0.1 . 1 . . . . . . . . 4381 1 715 . 1 1 59 59 LYS CE C 13 41.976 0.1 . 1 . . . . . . . . 4381 1 716 . 1 1 59 59 LYS CG C 13 25.226 0.1 . 1 . . . . . . . . 4381 1 717 . 1 1 59 59 LYS N N 15 119.28 0.1 . 1 . . . . . . . . 4381 1 718 . 1 1 60 60 ASP H H 1 8.006 0.05 . 1 . . . . . . . . 4381 1 719 . 1 1 60 60 ASP HA H 1 4.176 0.05 . 1 . . . . . . . . 4381 1 720 . 1 1 60 60 ASP HB2 H 1 3.036 0.05 . 2 . . . . . . . . 4381 1 721 . 1 1 60 60 ASP HB3 H 1 2.436 0.05 . 2 . . . . . . . . 4381 1 722 . 1 1 60 60 ASP C C 13 175.35 0.1 . 1 . . . . . . . . 4381 1 723 . 1 1 60 60 ASP CA C 13 54.996 0.1 . 1 . . . . . . . . 4381 1 724 . 1 1 60 60 ASP CB C 13 39.266 0.1 . 1 . . . . . . . . 4381 1 725 . 1 1 60 60 ASP N N 15 121.01 0.1 . 1 . . . . . . . . 4381 1 726 . 1 1 61 61 CYS H H 1 9.866 0.05 . 1 . . . . . . . . 4381 1 727 . 1 1 61 61 CYS HA H 1 4.916 0.05 . 1 . . . . . . . . 4381 1 728 . 1 1 61 61 CYS HB2 H 1 2.956 0.05 . 2 . . . . . . . . 4381 1 729 . 1 1 61 61 CYS HB3 H 1 2.716 0.05 . 2 . . . . . . . . 4381 1 730 . 1 1 61 61 CYS C C 13 176.59 0.1 . 1 . . . . . . . . 4381 1 731 . 1 1 61 61 CYS CA C 13 58.046 0.1 . 1 . . . . . . . . 4381 1 732 . 1 1 61 61 CYS CB C 13 30.096 0.1 . 1 . . . . . . . . 4381 1 733 . 1 1 61 61 CYS N N 15 115.58 0.1 . 1 . . . . . . . . 4381 1 734 . 1 1 62 62 GLY H H 1 10.886 0.05 . 1 . . . . . . . . 4381 1 735 . 1 1 62 62 GLY HA2 H 1 4.266 0.05 . 2 . . . . . . . . 4381 1 736 . 1 1 62 62 GLY HA3 H 1 3.916 0.05 . 2 . . . . . . . . 4381 1 737 . 1 1 62 62 GLY C C 13 173.32 0.1 . 1 . . . . . . . . 4381 1 738 . 1 1 62 62 GLY CA C 13 46.166 0.1 . 1 . . . . . . . . 4381 1 739 . 1 1 62 62 GLY N N 15 116.49 0.1 . 1 . . . . . . . . 4381 1 740 . 1 1 63 63 LYS H H 1 7.666 0.05 . 1 . . . . . . . . 4381 1 741 . 1 1 63 63 LYS HA H 1 5.186 0.05 . 1 . . . . . . . . 4381 1 742 . 1 1 63 63 LYS HB2 H 1 1.686 0.05 . 2 . . . . . . . . 4381 1 743 . 1 1 63 63 LYS HB3 H 1 1.416 0.05 . 2 . . . . . . . . 4381 1 744 . 1 1 63 63 LYS HD2 H 1 1.306 0.05 . 2 . . . . . . . . 4381 1 745 . 1 1 63 63 LYS HD3 H 1 1.036 0.05 . 2 . . . . . . . . 4381 1 746 . 1 1 63 63 LYS HE2 H 1 2.396 0.05 . 2 . . . . . . . . 4381 1 747 . 1 1 63 63 LYS HE3 H 1 1.746 0.05 . 2 . . . . . . . . 4381 1 748 . 1 1 63 63 LYS HG2 H 1 1.136 0.05 . 2 . . . . . . . . 4381 1 749 . 1 1 63 63 LYS HG3 H 1 0.886 0.05 . 2 . . . . . . . . 4381 1 750 . 1 1 63 63 LYS C C 13 173 0.1 . 1 . . . . . . . . 4381 1 751 . 1 1 63 63 LYS CA C 13 55.036 0.1 . 1 . . . . . . . . 4381 1 752 . 1 1 63 63 LYS CB C 13 35.326 0.1 . 1 . . . . . . . . 4381 1 753 . 1 1 63 63 LYS CD C 13 29.386 0.1 . 1 . . . . . . . . 4381 1 754 . 1 1 63 63 LYS CE C 13 41.466 0.1 . 1 . . . . . . . . 4381 1 755 . 1 1 63 63 LYS CG C 13 23.896 0.1 . 1 . . . . . . . . 4381 1 756 . 1 1 63 63 LYS N N 15 117.83 0.1 . 1 . . . . . . . . 4381 1 757 . 1 1 64 64 LEU H H 1 9.016 0.05 . 1 . . . . . . . . 4381 1 758 . 1 1 64 64 LEU HA H 1 5.206 0.05 . 1 . . . . . . . . 4381 1 759 . 1 1 64 64 LEU HB2 H 1 1.926 0.05 . 2 . . . . . . . . 4381 1 760 . 1 1 64 64 LEU HB3 H 1 1.696 0.05 . 2 . . . . . . . . 4381 1 761 . 1 1 64 64 LEU HD11 H 1 0.476 0.05 . 2 . . . . . . . . 4381 1 762 . 1 1 64 64 LEU HD12 H 1 0.476 0.05 . 2 . . . . . . . . 4381 1 763 . 1 1 64 64 LEU HD13 H 1 0.476 0.05 . 2 . . . . . . . . 4381 1 764 . 1 1 64 64 LEU HD21 H 1 -0.054 0.05 . 2 . . . . . . . . 4381 1 765 . 1 1 64 64 LEU HD22 H 1 -0.054 0.05 . 2 . . . . . . . . 4381 1 766 . 1 1 64 64 LEU HD23 H 1 -0.054 0.05 . 2 . . . . . . . . 4381 1 767 . 1 1 64 64 LEU HG H 1 1.136 0.05 . 1 . . . . . . . . 4381 1 768 . 1 1 64 64 LEU C C 13 177.98 0.1 . 1 . . . . . . . . 4381 1 769 . 1 1 64 64 LEU CA C 13 53.136 0.1 . 1 . . . . . . . . 4381 1 770 . 1 1 64 64 LEU CB C 13 43.776 0.1 . 1 . . . . . . . . 4381 1 771 . 1 1 64 64 LEU CD1 C 13 26.426 0.1 . 2 . . . . . . . . 4381 1 772 . 1 1 64 64 LEU CD2 C 13 20.836 0.1 . 2 . . . . . . . . 4381 1 773 . 1 1 64 64 LEU CG C 13 26.036 0.1 . 1 . . . . . . . . 4381 1 774 . 1 1 64 64 LEU N N 15 118.7 0.1 . 1 . . . . . . . . 4381 1 775 . 1 1 65 65 SER H H 1 9.206 0.05 . 1 . . . . . . . . 4381 1 776 . 1 1 65 65 SER HA H 1 4.636 0.05 . 1 . . . . . . . . 4381 1 777 . 1 1 65 65 SER HB2 H 1 4.336 0.05 . 2 . . . . . . . . 4381 1 778 . 1 1 65 65 SER HB3 H 1 3.986 0.05 . 2 . . . . . . . . 4381 1 779 . 1 1 65 65 SER C C 13 174.43 0.1 . 1 . . . . . . . . 4381 1 780 . 1 1 65 65 SER CA C 13 56.636 0.1 . 1 . . . . . . . . 4381 1 781 . 1 1 65 65 SER CB C 13 65.376 0.1 . 1 . . . . . . . . 4381 1 782 . 1 1 65 65 SER N N 15 118.54 0.1 . 1 . . . . . . . . 4381 1 783 . 1 1 66 66 LYS H H 1 8.576 0.05 . 1 . . . . . . . . 4381 1 784 . 1 1 66 66 LYS HA H 1 3.226 0.05 . 1 . . . . . . . . 4381 1 785 . 1 1 66 66 LYS HB2 H 1 1.116 0.05 . 2 . . . . . . . . 4381 1 786 . 1 1 66 66 LYS HB3 H 1 1.346 0.05 . 2 . . . . . . . . 4381 1 787 . 1 1 66 66 LYS HD2 H 1 1.276 0.05 . 1 . . . . . . . . 4381 1 788 . 1 1 66 66 LYS HD3 H 1 1.276 0.05 . 1 . . . . . . . . 4381 1 789 . 1 1 66 66 LYS HE2 H 1 2.616 0.05 . 2 . . . . . . . . 4381 1 790 . 1 1 66 66 LYS HE3 H 1 2.586 0.05 . 2 . . . . . . . . 4381 1 791 . 1 1 66 66 LYS HG2 H 1 0.426 0.05 . 2 . . . . . . . . 4381 1 792 . 1 1 66 66 LYS HG3 H 1 0.216 0.05 . 2 . . . . . . . . 4381 1 793 . 1 1 66 66 LYS C C 13 180 0.1 . 1 . . . . . . . . 4381 1 794 . 1 1 66 66 LYS CA C 13 61.046 0.1 . 1 . . . . . . . . 4381 1 795 . 1 1 66 66 LYS CB C 13 32.086 0.1 . 1 . . . . . . . . 4381 1 796 . 1 1 66 66 LYS CD C 13 29.276 0.1 . 1 . . . . . . . . 4381 1 797 . 1 1 66 66 LYS CE C 13 41.296 0.1 . 1 . . . . . . . . 4381 1 798 . 1 1 66 66 LYS CG C 13 24.706 0.1 . 1 . . . . . . . . 4381 1 799 . 1 1 66 66 LYS N N 15 120.92 0.1 . 1 . . . . . . . . 4381 1 800 . 1 1 67 67 ASP H H 1 8.616 0.05 . 1 . . . . . . . . 4381 1 801 . 1 1 67 67 ASP HA H 1 4.666 0.05 . 1 . . . . . . . . 4381 1 802 . 1 1 67 67 ASP HB2 H 1 2.486 0.05 . 2 . . . . . . . . 4381 1 803 . 1 1 67 67 ASP HB3 H 1 2.436 0.05 . 2 . . . . . . . . 4381 1 804 . 1 1 67 67 ASP C C 13 178.52 0.1 . 1 . . . . . . . . 4381 1 805 . 1 1 67 67 ASP CA C 13 57.656 0.1 . 1 . . . . . . . . 4381 1 806 . 1 1 67 67 ASP CB C 13 41.006 0.1 . 1 . . . . . . . . 4381 1 807 . 1 1 67 67 ASP N N 15 118.81 0.1 . 1 . . . . . . . . 4381 1 808 . 1 1 68 68 GLN H H 1 7.446 0.05 . 1 . . . . . . . . 4381 1 809 . 1 1 68 68 GLN HA H 1 4.046 0.05 . 1 . . . . . . . . 4381 1 810 . 1 1 68 68 GLN HB2 H 1 2.486 0.05 . 2 . . . . . . . . 4381 1 811 . 1 1 68 68 GLN HB3 H 1 2.156 0.05 . 2 . . . . . . . . 4381 1 812 . 1 1 68 68 GLN HE21 H 1 8.536 0.05 . 2 . . . . . . . . 4381 1 813 . 1 1 68 68 GLN HE22 H 1 6.736 0.05 . 2 . . . . . . . . 4381 1 814 . 1 1 68 68 GLN HG2 H 1 2.826 0.05 . 2 . . . . . . . . 4381 1 815 . 1 1 68 68 GLN HG3 H 1 2.476 0.05 . 2 . . . . . . . . 4381 1 816 . 1 1 68 68 GLN C C 13 178.12 0.1 . 1 . . . . . . . . 4381 1 817 . 1 1 68 68 GLN CA C 13 59.006 0.1 . 1 . . . . . . . . 4381 1 818 . 1 1 68 68 GLN CB C 13 29.336 0.1 . 1 . . . . . . . . 4381 1 819 . 1 1 68 68 GLN CD C 13 180.13 0.1 . 1 . . . . . . . . 4381 1 820 . 1 1 68 68 GLN CG C 13 34.586 0.1 . 1 . . . . . . . . 4381 1 821 . 1 1 68 68 GLN N N 15 119.57 0.1 . 1 . . . . . . . . 4381 1 822 . 1 1 68 68 GLN NE2 N 15 112.28 0.1 . 1 . . . . . . . . 4381 1 823 . 1 1 69 69 PHE H H 1 9.306 0.05 . 1 . . . . . . . . 4381 1 824 . 1 1 69 69 PHE HA H 1 4.216 0.05 . 1 . . . . . . . . 4381 1 825 . 1 1 69 69 PHE HB2 H 1 3.476 0.05 . 2 . . . . . . . . 4381 1 826 . 1 1 69 69 PHE HB3 H 1 3.206 0.05 . 2 . . . . . . . . 4381 1 827 . 1 1 69 69 PHE HD1 H 1 7.516 0.05 . 1 . . . . . . . . 4381 1 828 . 1 1 69 69 PHE HD2 H 1 7.516 0.05 . 1 . . . . . . . . 4381 1 829 . 1 1 69 69 PHE HE1 H 1 7.316 0.05 . 1 . . . . . . . . 4381 1 830 . 1 1 69 69 PHE HE2 H 1 7.316 0.05 . 1 . . . . . . . . 4381 1 831 . 1 1 69 69 PHE C C 13 176.07 0.1 . 1 . . . . . . . . 4381 1 832 . 1 1 69 69 PHE CA C 13 61.486 0.1 . 1 . . . . . . . . 4381 1 833 . 1 1 69 69 PHE CB C 13 40.266 0.1 . 1 . . . . . . . . 4381 1 834 . 1 1 69 69 PHE CD1 C 13 132.82 0.1 . 1 . . . . . . . . 4381 1 835 . 1 1 69 69 PHE CD2 C 13 132.82 0.1 . 1 . . . . . . . . 4381 1 836 . 1 1 69 69 PHE CE1 C 13 130.72 0.1 . 1 . . . . . . . . 4381 1 837 . 1 1 69 69 PHE CE2 C 13 130.72 0.1 . 1 . . . . . . . . 4381 1 838 . 1 1 69 69 PHE N N 15 120.58 0.1 . 1 . . . . . . . . 4381 1 839 . 1 1 70 70 ALA H H 1 8.246 0.05 . 1 . . . . . . . . 4381 1 840 . 1 1 70 70 ALA HA H 1 4.096 0.05 . 1 . . . . . . . . 4381 1 841 . 1 1 70 70 ALA HB1 H 1 2.016 0.05 . 1 . . . . . . . . 4381 1 842 . 1 1 70 70 ALA HB2 H 1 2.016 0.05 . 1 . . . . . . . . 4381 1 843 . 1 1 70 70 ALA HB3 H 1 2.016 0.05 . 1 . . . . . . . . 4381 1 844 . 1 1 70 70 ALA C C 13 179.01 0.1 . 1 . . . . . . . . 4381 1 845 . 1 1 70 70 ALA CA C 13 54.836 0.1 . 1 . . . . . . . . 4381 1 846 . 1 1 70 70 ALA CB C 13 18.876 0.1 . 1 . . . . . . . . 4381 1 847 . 1 1 70 70 ALA N N 15 120.56 0.1 . 1 . . . . . . . . 4381 1 848 . 1 1 71 71 LEU H H 1 7.766 0.05 . 1 . . . . . . . . 4381 1 849 . 1 1 71 71 LEU HA H 1 4.026 0.05 . 1 . . . . . . . . 4381 1 850 . 1 1 71 71 LEU HB2 H 1 2.476 0.05 . 2 . . . . . . . . 4381 1 851 . 1 1 71 71 LEU HB3 H 1 1.696 0.05 . 2 . . . . . . . . 4381 1 852 . 1 1 71 71 LEU HD11 H 1 1.236 0.05 . 2 . . . . . . . . 4381 1 853 . 1 1 71 71 LEU HD12 H 1 1.236 0.05 . 2 . . . . . . . . 4381 1 854 . 1 1 71 71 LEU HD13 H 1 1.236 0.05 . 2 . . . . . . . . 4381 1 855 . 1 1 71 71 LEU HD21 H 1 1.026 0.05 . 2 . . . . . . . . 4381 1 856 . 1 1 71 71 LEU HD22 H 1 1.026 0.05 . 2 . . . . . . . . 4381 1 857 . 1 1 71 71 LEU HD23 H 1 1.026 0.05 . 2 . . . . . . . . 4381 1 858 . 1 1 71 71 LEU HG H 1 1.786 0.05 . 1 . . . . . . . . 4381 1 859 . 1 1 71 71 LEU C C 13 177.36 0.1 . 1 . . . . . . . . 4381 1 860 . 1 1 71 71 LEU CA C 13 57.706 0.1 . 1 . . . . . . . . 4381 1 861 . 1 1 71 71 LEU CB C 13 41.526 0.1 . 1 . . . . . . . . 4381 1 862 . 1 1 71 71 LEU CD1 C 13 27.206 0.1 . 2 . . . . . . . . 4381 1 863 . 1 1 71 71 LEU CD2 C 13 22.236 0.1 . 2 . . . . . . . . 4381 1 864 . 1 1 71 71 LEU CG C 13 27.166 0.1 . 1 . . . . . . . . 4381 1 865 . 1 1 71 71 LEU N N 15 117.45 0.1 . 1 . . . . . . . . 4381 1 866 . 1 1 72 72 ALA H H 1 8.296 0.05 . 1 . . . . . . . . 4381 1 867 . 1 1 72 72 ALA HA H 1 3.716 0.05 . 1 . . . . . . . . 4381 1 868 . 1 1 72 72 ALA HB1 H 1 1.386 0.05 . 1 . . . . . . . . 4381 1 869 . 1 1 72 72 ALA HB2 H 1 1.386 0.05 . 1 . . . . . . . . 4381 1 870 . 1 1 72 72 ALA HB3 H 1 1.386 0.05 . 1 . . . . . . . . 4381 1 871 . 1 1 72 72 ALA C C 13 179.28 0.1 . 1 . . . . . . . . 4381 1 872 . 1 1 72 72 ALA CA C 13 55.896 0.1 . 1 . . . . . . . . 4381 1 873 . 1 1 72 72 ALA CB C 13 16.826 0.1 . 1 . . . . . . . . 4381 1 874 . 1 1 72 72 ALA N N 15 123.23 0.1 . 1 . . . . . . . . 4381 1 875 . 1 1 73 73 PHE H H 1 8.336 0.05 . 1 . . . . . . . . 4381 1 876 . 1 1 73 73 PHE HA H 1 3.616 0.05 . 1 . . . . . . . . 4381 1 877 . 1 1 73 73 PHE HB2 H 1 1.786 0.05 . 2 . . . . . . . . 4381 1 878 . 1 1 73 73 PHE HB3 H 1 1.556 0.05 . 2 . . . . . . . . 4381 1 879 . 1 1 73 73 PHE HD1 H 1 6.586 0.05 . 1 . . . . . . . . 4381 1 880 . 1 1 73 73 PHE HD2 H 1 6.586 0.05 . 1 . . . . . . . . 4381 1 881 . 1 1 73 73 PHE HE1 H 1 7.116 0.05 . 1 . . . . . . . . 4381 1 882 . 1 1 73 73 PHE HE2 H 1 7.116 0.05 . 1 . . . . . . . . 4381 1 883 . 1 1 73 73 PHE HZ H 1 7.176 0.05 . 1 . . . . . . . . 4381 1 884 . 1 1 73 73 PHE C C 13 178.97 0.1 . 1 . . . . . . . . 4381 1 885 . 1 1 73 73 PHE CA C 13 61.996 0.1 . 1 . . . . . . . . 4381 1 886 . 1 1 73 73 PHE CB C 13 36.756 0.1 . 1 . . . . . . . . 4381 1 887 . 1 1 73 73 PHE CD1 C 13 130.45 0.1 . 1 . . . . . . . . 4381 1 888 . 1 1 73 73 PHE CD2 C 13 130.45 0.1 . 1 . . . . . . . . 4381 1 889 . 1 1 73 73 PHE CE1 C 13 130.9 0.1 . 1 . . . . . . . . 4381 1 890 . 1 1 73 73 PHE CE2 C 13 130.9 0.1 . 1 . . . . . . . . 4381 1 891 . 1 1 73 73 PHE CZ C 13 128.4 0.1 . 1 . . . . . . . . 4381 1 892 . 1 1 73 73 PHE N N 15 117.48 0.1 . 1 . . . . . . . . 4381 1 893 . 1 1 74 74 HIS H H 1 8.516 0.05 . 1 . . . . . . . . 4381 1 894 . 1 1 74 74 HIS HA H 1 4.416 0.05 . 1 . . . . . . . . 4381 1 895 . 1 1 74 74 HIS HB2 H 1 3.586 0.05 . 2 . . . . . . . . 4381 1 896 . 1 1 74 74 HIS HB3 H 1 3.096 0.05 . 2 . . . . . . . . 4381 1 897 . 1 1 74 74 HIS HD2 H 1 6.356 0.05 . 1 . . . . . . . . 4381 1 898 . 1 1 74 74 HIS HE1 H 1 7.546 0.05 . 1 . . . . . . . . 4381 1 899 . 1 1 74 74 HIS C C 13 177.38 0.1 . 1 . . . . . . . . 4381 1 900 . 1 1 74 74 HIS CA C 13 60.406 0.1 . 1 . . . . . . . . 4381 1 901 . 1 1 74 74 HIS CB C 13 29.696 0.1 . 1 . . . . . . . . 4381 1 902 . 1 1 74 74 HIS CE1 C 13 115.68 0.1 . 1 . . . . . . . . 4381 1 903 . 1 1 74 74 HIS N N 15 123.99 0.1 . 1 . . . . . . . . 4381 1 904 . 1 1 75 75 LEU H H 1 8.466 0.05 . 1 . . . . . . . . 4381 1 905 . 1 1 75 75 LEU HA H 1 3.706 0.05 . 1 . . . . . . . . 4381 1 906 . 1 1 75 75 LEU HB2 H 1 2.116 0.05 . 2 . . . . . . . . 4381 1 907 . 1 1 75 75 LEU HB3 H 1 0.986 0.05 . 2 . . . . . . . . 4381 1 908 . 1 1 75 75 LEU HD11 H 1 0.906 0.05 . 2 . . . . . . . . 4381 1 909 . 1 1 75 75 LEU HD12 H 1 0.906 0.05 . 2 . . . . . . . . 4381 1 910 . 1 1 75 75 LEU HD13 H 1 0.906 0.05 . 2 . . . . . . . . 4381 1 911 . 1 1 75 75 LEU HD21 H 1 0.746 0.05 . 2 . . . . . . . . 4381 1 912 . 1 1 75 75 LEU HD22 H 1 0.746 0.05 . 2 . . . . . . . . 4381 1 913 . 1 1 75 75 LEU HD23 H 1 0.746 0.05 . 2 . . . . . . . . 4381 1 914 . 1 1 75 75 LEU HG H 1 2.056 0.05 . 1 . . . . . . . . 4381 1 915 . 1 1 75 75 LEU C C 13 180.6 0.1 . 1 . . . . . . . . 4381 1 916 . 1 1 75 75 LEU CA C 13 57.926 0.1 . 1 . . . . . . . . 4381 1 917 . 1 1 75 75 LEU CB C 13 42.076 0.1 . 1 . . . . . . . . 4381 1 918 . 1 1 75 75 LEU CD1 C 13 22.766 0.1 . 2 . . . . . . . . 4381 1 919 . 1 1 75 75 LEU CD2 C 13 27.046 0.1 . 2 . . . . . . . . 4381 1 920 . 1 1 75 75 LEU CG C 13 26.846 0.1 . 1 . . . . . . . . 4381 1 921 . 1 1 75 75 LEU N N 15 119.36 0.1 . 1 . . . . . . . . 4381 1 922 . 1 1 76 76 ILE H H 1 8.366 0.05 . 1 . . . . . . . . 4381 1 923 . 1 1 76 76 ILE HA H 1 3.126 0.05 . 1 . . . . . . . . 4381 1 924 . 1 1 76 76 ILE HB H 1 1.446 0.05 . 1 . . . . . . . . 4381 1 925 . 1 1 76 76 ILE HD11 H 1 -0.254 0.05 . 1 . . . . . . . . 4381 1 926 . 1 1 76 76 ILE HD12 H 1 -0.254 0.05 . 1 . . . . . . . . 4381 1 927 . 1 1 76 76 ILE HD13 H 1 -0.254 0.05 . 1 . . . . . . . . 4381 1 928 . 1 1 76 76 ILE HG12 H 1 1.536 0.05 . 2 . . . . . . . . 4381 1 929 . 1 1 76 76 ILE HG13 H 1 0.266 0.05 . 2 . . . . . . . . 4381 1 930 . 1 1 76 76 ILE HG21 H 1 0.596 0.05 . 1 . . . . . . . . 4381 1 931 . 1 1 76 76 ILE HG22 H 1 0.596 0.05 . 1 . . . . . . . . 4381 1 932 . 1 1 76 76 ILE HG23 H 1 0.596 0.05 . 1 . . . . . . . . 4381 1 933 . 1 1 76 76 ILE C C 13 177.1 0.1 . 1 . . . . . . . . 4381 1 934 . 1 1 76 76 ILE CA C 13 66.146 0.1 . 1 . . . . . . . . 4381 1 935 . 1 1 76 76 ILE CB C 13 38.186 0.1 . 1 . . . . . . . . 4381 1 936 . 1 1 76 76 ILE CD1 C 13 12.806 0.1 . 1 . . . . . . . . 4381 1 937 . 1 1 76 76 ILE CG1 C 13 30.566 0.1 . 1 . . . . . . . . 4381 1 938 . 1 1 76 76 ILE CG2 C 13 16.756 0.1 . 1 . . . . . . . . 4381 1 939 . 1 1 76 76 ILE N N 15 121.73 0.1 . 1 . . . . . . . . 4381 1 940 . 1 1 77 77 SER H H 1 8.526 0.05 . 1 . . . . . . . . 4381 1 941 . 1 1 77 77 SER HA H 1 4.086 0.05 . 1 . . . . . . . . 4381 1 942 . 1 1 77 77 SER HB2 H 1 3.976 0.05 . 1 . . . . . . . . 4381 1 943 . 1 1 77 77 SER HB3 H 1 3.976 0.05 . 1 . . . . . . . . 4381 1 944 . 1 1 77 77 SER C C 13 176.3 0.1 . 1 . . . . . . . . 4381 1 945 . 1 1 77 77 SER CA C 13 62.516 0.1 . 1 . . . . . . . . 4381 1 946 . 1 1 77 77 SER N N 15 116.6 0.1 . 1 . . . . . . . . 4381 1 947 . 1 1 78 78 GLN H H 1 8.466 0.05 . 1 . . . . . . . . 4381 1 948 . 1 1 78 78 GLN HA H 1 3.826 0.05 . 1 . . . . . . . . 4381 1 949 . 1 1 78 78 GLN HB2 H 1 1.986 0.05 . 2 . . . . . . . . 4381 1 950 . 1 1 78 78 GLN HB3 H 1 1.846 0.05 . 2 . . . . . . . . 4381 1 951 . 1 1 78 78 GLN HE21 H 1 7.516 0.05 . 2 . . . . . . . . 4381 1 952 . 1 1 78 78 GLN HE22 H 1 6.866 0.05 . 2 . . . . . . . . 4381 1 953 . 1 1 78 78 GLN HG2 H 1 1.896 0.05 . 2 . . . . . . . . 4381 1 954 . 1 1 78 78 GLN HG3 H 1 1.796 0.05 . 2 . . . . . . . . 4381 1 955 . 1 1 78 78 GLN C C 13 178.85 0.1 . 1 . . . . . . . . 4381 1 956 . 1 1 78 78 GLN CA C 13 58.826 0.1 . 1 . . . . . . . . 4381 1 957 . 1 1 78 78 GLN CB C 13 28.856 0.1 . 1 . . . . . . . . 4381 1 958 . 1 1 78 78 GLN CD C 13 179.97 0.1 . 1 . . . . . . . . 4381 1 959 . 1 1 78 78 GLN CG C 13 34.226 0.1 . 1 . . . . . . . . 4381 1 960 . 1 1 78 78 GLN N N 15 119.71 0.1 . 1 . . . . . . . . 4381 1 961 . 1 1 78 78 GLN NE2 N 15 112.58 0.1 . 1 . . . . . . . . 4381 1 962 . 1 1 79 79 LYS H H 1 7.296 0.05 . 1 . . . . . . . . 4381 1 963 . 1 1 79 79 LYS HA H 1 4.266 0.05 . 1 . . . . . . . . 4381 1 964 . 1 1 79 79 LYS HB2 H 1 2.126 0.05 . 2 . . . . . . . . 4381 1 965 . 1 1 79 79 LYS HB3 H 1 1.736 0.05 . 2 . . . . . . . . 4381 1 966 . 1 1 79 79 LYS HD2 H 1 1.456 0.05 . 1 . . . . . . . . 4381 1 967 . 1 1 79 79 LYS HD3 H 1 1.456 0.05 . 1 . . . . . . . . 4381 1 968 . 1 1 79 79 LYS HE2 H 1 2.756 0.05 . 2 . . . . . . . . 4381 1 969 . 1 1 79 79 LYS HE3 H 1 2.626 0.05 . 2 . . . . . . . . 4381 1 970 . 1 1 79 79 LYS HG2 H 1 1.316 0.05 . 2 . . . . . . . . 4381 1 971 . 1 1 79 79 LYS HG3 H 1 1.106 0.05 . 2 . . . . . . . . 4381 1 972 . 1 1 79 79 LYS C C 13 178.48 0.1 . 1 . . . . . . . . 4381 1 973 . 1 1 79 79 LYS CA C 13 57.936 0.1 . 1 . . . . . . . . 4381 1 974 . 1 1 79 79 LYS CB C 13 30.886 0.1 . 1 . . . . . . . . 4381 1 975 . 1 1 79 79 LYS CD C 13 28.026 0.1 . 1 . . . . . . . . 4381 1 976 . 1 1 79 79 LYS CE C 13 42.076 0.1 . 1 . . . . . . . . 4381 1 977 . 1 1 79 79 LYS CG C 13 25.836 0.1 . 1 . . . . . . . . 4381 1 978 . 1 1 79 79 LYS N N 15 120.55 0.1 . 1 . . . . . . . . 4381 1 979 . 1 1 80 80 LEU H H 1 8.636 0.05 . 1 . . . . . . . . 4381 1 980 . 1 1 80 80 LEU HA H 1 3.996 0.05 . 1 . . . . . . . . 4381 1 981 . 1 1 80 80 LEU HB2 H 1 1.856 0.05 . 2 . . . . . . . . 4381 1 982 . 1 1 80 80 LEU HB3 H 1 1.526 0.05 . 2 . . . . . . . . 4381 1 983 . 1 1 80 80 LEU HD11 H 1 0.906 0.05 . 2 . . . . . . . . 4381 1 984 . 1 1 80 80 LEU HD12 H 1 0.906 0.05 . 2 . . . . . . . . 4381 1 985 . 1 1 80 80 LEU HD13 H 1 0.906 0.05 . 2 . . . . . . . . 4381 1 986 . 1 1 80 80 LEU HD21 H 1 0.866 0.05 . 2 . . . . . . . . 4381 1 987 . 1 1 80 80 LEU HD22 H 1 0.866 0.05 . 2 . . . . . . . . 4381 1 988 . 1 1 80 80 LEU HD23 H 1 0.866 0.05 . 2 . . . . . . . . 4381 1 989 . 1 1 80 80 LEU HG H 1 1.726 0.05 . 1 . . . . . . . . 4381 1 990 . 1 1 80 80 LEU C C 13 178.73 0.1 . 1 . . . . . . . . 4381 1 991 . 1 1 80 80 LEU CA C 13 57.996 0.1 . 1 . . . . . . . . 4381 1 992 . 1 1 80 80 LEU CB C 13 43.206 0.1 . 1 . . . . . . . . 4381 1 993 . 1 1 80 80 LEU CD1 C 13 23.086 0.1 . 2 . . . . . . . . 4381 1 994 . 1 1 80 80 LEU CD2 C 13 25.966 0.1 . 2 . . . . . . . . 4381 1 995 . 1 1 80 80 LEU CG C 13 26.806 0.1 . 1 . . . . . . . . 4381 1 996 . 1 1 80 80 LEU N N 15 119.88 0.1 . 1 . . . . . . . . 4381 1 997 . 1 1 81 81 ILE H H 1 8.926 0.05 . 1 . . . . . . . . 4381 1 998 . 1 1 81 81 ILE HA H 1 4.056 0.05 . 1 . . . . . . . . 4381 1 999 . 1 1 81 81 ILE HB H 1 1.926 0.05 . 1 . . . . . . . . 4381 1 1000 . 1 1 81 81 ILE HD11 H 1 0.826 0.05 . 1 . . . . . . . . 4381 1 1001 . 1 1 81 81 ILE HD12 H 1 0.826 0.05 . 1 . . . . . . . . 4381 1 1002 . 1 1 81 81 ILE HD13 H 1 0.826 0.05 . 1 . . . . . . . . 4381 1 1003 . 1 1 81 81 ILE HG12 H 1 1.606 0.05 . 2 . . . . . . . . 4381 1 1004 . 1 1 81 81 ILE HG13 H 1 1.316 0.05 . 2 . . . . . . . . 4381 1 1005 . 1 1 81 81 ILE HG21 H 1 0.886 0.05 . 1 . . . . . . . . 4381 1 1006 . 1 1 81 81 ILE HG22 H 1 0.886 0.05 . 1 . . . . . . . . 4381 1 1007 . 1 1 81 81 ILE HG23 H 1 0.886 0.05 . 1 . . . . . . . . 4381 1 1008 . 1 1 81 81 ILE C C 13 177.82 0.1 . 1 . . . . . . . . 4381 1 1009 . 1 1 81 81 ILE CA C 13 62.536 0.1 . 1 . . . . . . . . 4381 1 1010 . 1 1 81 81 ILE CB C 13 37.926 0.1 . 1 . . . . . . . . 4381 1 1011 . 1 1 81 81 ILE CD1 C 13 11.846 0.1 . 1 . . . . . . . . 4381 1 1012 . 1 1 81 81 ILE CG1 C 13 28.096 0.1 . 1 . . . . . . . . 4381 1 1013 . 1 1 81 81 ILE CG2 C 13 17.466 0.1 . 1 . . . . . . . . 4381 1 1014 . 1 1 81 81 ILE N N 15 115.45 0.1 . 1 . . . . . . . . 4381 1 1015 . 1 1 82 82 LYS H H 1 6.846 0.05 . 1 . . . . . . . . 4381 1 1016 . 1 1 82 82 LYS HA H 1 4.576 0.05 . 1 . . . . . . . . 4381 1 1017 . 1 1 82 82 LYS HB2 H 1 2.026 0.05 . 1 . . . . . . . . 4381 1 1018 . 1 1 82 82 LYS HB3 H 1 2.026 0.05 . 1 . . . . . . . . 4381 1 1019 . 1 1 82 82 LYS HD2 H 1 1.666 0.05 . 1 . . . . . . . . 4381 1 1020 . 1 1 82 82 LYS HD3 H 1 1.666 0.05 . 1 . . . . . . . . 4381 1 1021 . 1 1 82 82 LYS HE2 H 1 2.966 0.05 . 1 . . . . . . . . 4381 1 1022 . 1 1 82 82 LYS HE3 H 1 2.966 0.05 . 1 . . . . . . . . 4381 1 1023 . 1 1 82 82 LYS HG2 H 1 1.466 0.05 . 2 . . . . . . . . 4381 1 1024 . 1 1 82 82 LYS HG3 H 1 1.376 0.05 . 2 . . . . . . . . 4381 1 1025 . 1 1 82 82 LYS C C 13 177.03 0.1 . 1 . . . . . . . . 4381 1 1026 . 1 1 82 82 LYS CA C 13 55.386 0.1 . 1 . . . . . . . . 4381 1 1027 . 1 1 82 82 LYS CB C 13 34.306 0.1 . 1 . . . . . . . . 4381 1 1028 . 1 1 82 82 LYS CD C 13 29.026 0.1 . 1 . . . . . . . . 4381 1 1029 . 1 1 82 82 LYS CE C 13 42.006 0.1 . 1 . . . . . . . . 4381 1 1030 . 1 1 82 82 LYS CG C 13 25.446 0.1 . 1 . . . . . . . . 4381 1 1031 . 1 1 82 82 LYS N N 15 114.84 0.1 . 1 . . . . . . . . 4381 1 1032 . 1 1 83 83 GLY H H 1 7.446 0.05 . 1 . . . . . . . . 4381 1 1033 . 1 1 83 83 GLY HA2 H 1 4.026 0.05 . 1 . . . . . . . . 4381 1 1034 . 1 1 83 83 GLY HA3 H 1 4.026 0.05 . 1 . . . . . . . . 4381 1 1035 . 1 1 83 83 GLY C C 13 174.4 0.1 . 1 . . . . . . . . 4381 1 1036 . 1 1 83 83 GLY CA C 13 46.486 0.1 . 1 . . . . . . . . 4381 1 1037 . 1 1 83 83 GLY N N 15 109.35 0.1 . 1 . . . . . . . . 4381 1 1038 . 1 1 84 84 ILE H H 1 7.376 0.05 . 1 . . . . . . . . 4381 1 1039 . 1 1 84 84 ILE HA H 1 3.956 0.05 . 1 . . . . . . . . 4381 1 1040 . 1 1 84 84 ILE HB H 1 1.286 0.05 . 1 . . . . . . . . 4381 1 1041 . 1 1 84 84 ILE HD11 H 1 0.776 0.05 . 1 . . . . . . . . 4381 1 1042 . 1 1 84 84 ILE HD12 H 1 0.776 0.05 . 1 . . . . . . . . 4381 1 1043 . 1 1 84 84 ILE HD13 H 1 0.776 0.05 . 1 . . . . . . . . 4381 1 1044 . 1 1 84 84 ILE HG12 H 1 1.356 0.05 . 2 . . . . . . . . 4381 1 1045 . 1 1 84 84 ILE HG13 H 1 0.916 0.05 . 2 . . . . . . . . 4381 1 1046 . 1 1 84 84 ILE HG21 H 1 0.846 0.05 . 1 . . . . . . . . 4381 1 1047 . 1 1 84 84 ILE HG22 H 1 0.846 0.05 . 1 . . . . . . . . 4381 1 1048 . 1 1 84 84 ILE HG23 H 1 0.846 0.05 . 1 . . . . . . . . 4381 1 1049 . 1 1 84 84 ILE C C 13 175.26 0.1 . 1 . . . . . . . . 4381 1 1050 . 1 1 84 84 ILE CA C 13 60.616 0.1 . 1 . . . . . . . . 4381 1 1051 . 1 1 84 84 ILE CB C 13 39.406 0.1 . 1 . . . . . . . . 4381 1 1052 . 1 1 84 84 ILE CD1 C 13 12.976 0.1 . 1 . . . . . . . . 4381 1 1053 . 1 1 84 84 ILE CG1 C 13 27.206 0.1 . 1 . . . . . . . . 4381 1 1054 . 1 1 84 84 ILE CG2 C 13 16.946 0.1 . 1 . . . . . . . . 4381 1 1055 . 1 1 84 84 ILE N N 15 122.75 0.1 . 1 . . . . . . . . 4381 1 1056 . 1 1 85 85 ASP H H 1 8.536 0.05 . 1 . . . . . . . . 4381 1 1057 . 1 1 85 85 ASP HA H 1 4.686 0.05 . 1 . . . . . . . . 4381 1 1058 . 1 1 85 85 ASP HB2 H 1 2.566 0.05 . 2 . . . . . . . . 4381 1 1059 . 1 1 85 85 ASP HB3 H 1 2.376 0.05 . 2 . . . . . . . . 4381 1 1060 . 1 1 85 85 ASP CA C 13 53.606 0.1 . 1 . . . . . . . . 4381 1 1061 . 1 1 85 85 ASP CB C 13 40.066 0.1 . 1 . . . . . . . . 4381 1 1062 . 1 1 85 85 ASP N N 15 128.63 0.1 . 1 . . . . . . . . 4381 1 1063 . 1 1 86 86 PRO HA H 1 4.656 0.05 . 1 . . . . . . . . 4381 1 1064 . 1 1 86 86 PRO HB2 H 1 2.066 0.05 . 2 . . . . . . . . 4381 1 1065 . 1 1 86 86 PRO HB3 H 1 1.876 0.05 . 2 . . . . . . . . 4381 1 1066 . 1 1 86 86 PRO HD2 H 1 3.756 0.05 . 2 . . . . . . . . 4381 1 1067 . 1 1 86 86 PRO HD3 H 1 3.556 0.05 . 2 . . . . . . . . 4381 1 1068 . 1 1 86 86 PRO HG2 H 1 1.976 0.05 . 2 . . . . . . . . 4381 1 1069 . 1 1 86 86 PRO HG3 H 1 1.826 0.05 . 2 . . . . . . . . 4381 1 1070 . 1 1 86 86 PRO CA C 13 53.626 0.1 . 1 . . . . . . . . 4381 1 1071 . 1 1 86 86 PRO CB C 13 30.646 0.1 . 1 . . . . . . . . 4381 1 1072 . 1 1 86 86 PRO CD C 13 49.786 0.1 . 1 . . . . . . . . 4381 1 1073 . 1 1 86 86 PRO CG C 13 27.586 0.1 . 1 . . . . . . . . 4381 1 1074 . 1 1 87 87 PRO HA H 1 4.626 0.05 . 1 . . . . . . . . 4381 1 1075 . 1 1 87 87 PRO HB2 H 1 2.396 0.05 . 2 . . . . . . . . 4381 1 1076 . 1 1 87 87 PRO HB3 H 1 2.296 0.05 . 2 . . . . . . . . 4381 1 1077 . 1 1 87 87 PRO HD2 H 1 3.816 0.05 . 2 . . . . . . . . 4381 1 1078 . 1 1 87 87 PRO HD3 H 1 3.256 0.05 . 2 . . . . . . . . 4381 1 1079 . 1 1 87 87 PRO HG2 H 1 2.026 0.05 . 2 . . . . . . . . 4381 1 1080 . 1 1 87 87 PRO HG3 H 1 1.696 0.05 . 2 . . . . . . . . 4381 1 1081 . 1 1 87 87 PRO CA C 13 61.856 0.1 . 1 . . . . . . . . 4381 1 1082 . 1 1 87 87 PRO CB C 13 32.446 0.1 . 1 . . . . . . . . 4381 1 1083 . 1 1 87 87 PRO CD C 13 49.386 0.1 . 1 . . . . . . . . 4381 1 1084 . 1 1 87 87 PRO CG C 13 26.946 0.1 . 1 . . . . . . . . 4381 1 1085 . 1 1 88 88 HIS HA H 1 4.446 0.05 . 1 . . . . . . . . 4381 1 1086 . 1 1 88 88 HIS HB2 H 1 3.156 0.05 . 2 . . . . . . . . 4381 1 1087 . 1 1 88 88 HIS HB3 H 1 3.136 0.05 . 2 . . . . . . . . 4381 1 1088 . 1 1 88 88 HIS HD2 H 1 6.956 0.05 . 1 . . . . . . . . 4381 1 1089 . 1 1 88 88 HIS HE1 H 1 7.676 0.05 . 1 . . . . . . . . 4381 1 1090 . 1 1 88 88 HIS C C 13 175.14 0.1 . 1 . . . . . . . . 4381 1 1091 . 1 1 88 88 HIS CA C 13 59.226 0.1 . 1 . . . . . . . . 4381 1 1092 . 1 1 88 88 HIS CB C 13 31.336 0.1 . 1 . . . . . . . . 4381 1 1093 . 1 1 88 88 HIS CE1 C 13 115.52 0.1 . 1 . . . . . . . . 4381 1 1094 . 1 1 89 89 VAL H H 1 7.166 0.05 . 1 . . . . . . . . 4381 1 1095 . 1 1 89 89 VAL HA H 1 4.246 0.05 . 1 . . . . . . . . 4381 1 1096 . 1 1 89 89 VAL HB H 1 1.966 0.05 . 1 . . . . . . . . 4381 1 1097 . 1 1 89 89 VAL HG11 H 1 0.856 0.05 . 2 . . . . . . . . 4381 1 1098 . 1 1 89 89 VAL HG12 H 1 0.856 0.05 . 2 . . . . . . . . 4381 1 1099 . 1 1 89 89 VAL HG13 H 1 0.856 0.05 . 2 . . . . . . . . 4381 1 1100 . 1 1 89 89 VAL HG21 H 1 0.786 0.05 . 2 . . . . . . . . 4381 1 1101 . 1 1 89 89 VAL HG22 H 1 0.786 0.05 . 2 . . . . . . . . 4381 1 1102 . 1 1 89 89 VAL HG23 H 1 0.786 0.05 . 2 . . . . . . . . 4381 1 1103 . 1 1 89 89 VAL C C 13 174.79 0.1 . 1 . . . . . . . . 4381 1 1104 . 1 1 89 89 VAL CA C 13 59.226 0.1 . 1 . . . . . . . . 4381 1 1105 . 1 1 89 89 VAL CB C 13 35.736 0.1 . 1 . . . . . . . . 4381 1 1106 . 1 1 89 89 VAL CG1 C 13 21.196 0.1 . 2 . . . . . . . . 4381 1 1107 . 1 1 89 89 VAL CG2 C 13 19.446 0.1 . 2 . . . . . . . . 4381 1 1108 . 1 1 89 89 VAL N N 15 110.74 0.1 . 1 . . . . . . . . 4381 1 1109 . 1 1 90 90 LEU H H 1 8.656 0.05 . 1 . . . . . . . . 4381 1 1110 . 1 1 90 90 LEU HA H 1 4.376 0.05 . 1 . . . . . . . . 4381 1 1111 . 1 1 90 90 LEU HB2 H 1 1.766 0.05 . 2 . . . . . . . . 4381 1 1112 . 1 1 90 90 LEU HB3 H 1 1.456 0.05 . 2 . . . . . . . . 4381 1 1113 . 1 1 90 90 LEU HD11 H 1 0.926 0.05 . 2 . . . . . . . . 4381 1 1114 . 1 1 90 90 LEU HD12 H 1 0.926 0.05 . 2 . . . . . . . . 4381 1 1115 . 1 1 90 90 LEU HD13 H 1 0.926 0.05 . 2 . . . . . . . . 4381 1 1116 . 1 1 90 90 LEU HD21 H 1 0.906 0.05 . 2 . . . . . . . . 4381 1 1117 . 1 1 90 90 LEU HD22 H 1 0.906 0.05 . 2 . . . . . . . . 4381 1 1118 . 1 1 90 90 LEU HD23 H 1 0.906 0.05 . 2 . . . . . . . . 4381 1 1119 . 1 1 90 90 LEU HG H 1 1.826 0.05 . 1 . . . . . . . . 4381 1 1120 . 1 1 90 90 LEU C C 13 177.96 0.1 . 1 . . . . . . . . 4381 1 1121 . 1 1 90 90 LEU CA C 13 55.286 0.1 . 1 . . . . . . . . 4381 1 1122 . 1 1 90 90 LEU CB C 13 41.936 0.1 . 1 . . . . . . . . 4381 1 1123 . 1 1 90 90 LEU CD1 C 13 26.746 0.1 . 2 . . . . . . . . 4381 1 1124 . 1 1 90 90 LEU CD2 C 13 24.566 0.1 . 2 . . . . . . . . 4381 1 1125 . 1 1 90 90 LEU CG C 13 26.646 0.1 . 1 . . . . . . . . 4381 1 1126 . 1 1 90 90 LEU N N 15 121.47 0.1 . 1 . . . . . . . . 4381 1 1127 . 1 1 91 91 THR H H 1 7.366 0.05 . 1 . . . . . . . . 4381 1 1128 . 1 1 91 91 THR HA H 1 4.686 0.05 . 1 . . . . . . . . 4381 1 1129 . 1 1 91 91 THR HB H 1 4.696 0.05 . 1 . . . . . . . . 4381 1 1130 . 1 1 91 91 THR HG21 H 1 1.356 0.05 . 1 . . . . . . . . 4381 1 1131 . 1 1 91 91 THR HG22 H 1 1.356 0.05 . 1 . . . . . . . . 4381 1 1132 . 1 1 91 91 THR HG23 H 1 1.356 0.05 . 1 . . . . . . . . 4381 1 1133 . 1 1 91 91 THR CA C 13 59.556 0.1 . 1 . . . . . . . . 4381 1 1134 . 1 1 91 91 THR CB C 13 67.146 0.1 . 1 . . . . . . . . 4381 1 1135 . 1 1 91 91 THR CG2 C 13 22.756 0.1 . 1 . . . . . . . . 4381 1 1136 . 1 1 91 91 THR N N 15 113.49 0.1 . 1 . . . . . . . . 4381 1 1137 . 1 1 92 92 PRO HA H 1 4.176 0.05 . 1 . . . . . . . . 4381 1 1138 . 1 1 92 92 PRO HB2 H 1 2.386 0.05 . 2 . . . . . . . . 4381 1 1139 . 1 1 92 92 PRO HB3 H 1 1.856 0.05 . 2 . . . . . . . . 4381 1 1140 . 1 1 92 92 PRO HD2 H 1 3.876 0.05 . 2 . . . . . . . . 4381 1 1141 . 1 1 92 92 PRO HD3 H 1 3.826 0.05 . 2 . . . . . . . . 4381 1 1142 . 1 1 92 92 PRO HG2 H 1 2.216 0.05 . 2 . . . . . . . . 4381 1 1143 . 1 1 92 92 PRO HG3 H 1 2.016 0.05 . 2 . . . . . . . . 4381 1 1144 . 1 1 92 92 PRO C C 13 178.92 0.1 . 1 . . . . . . . . 4381 1 1145 . 1 1 92 92 PRO CA C 13 66.416 0.1 . 1 . . . . . . . . 4381 1 1146 . 1 1 92 92 PRO CB C 13 32.076 0.1 . 1 . . . . . . . . 4381 1 1147 . 1 1 92 92 PRO CD C 13 50.356 0.1 . 1 . . . . . . . . 4381 1 1148 . 1 1 92 92 PRO CG C 13 28.256 0.1 . 1 . . . . . . . . 4381 1 1149 . 1 1 93 93 GLU H H 1 8.866 0.05 . 1 . . . . . . . . 4381 1 1150 . 1 1 93 93 GLU HA H 1 4.236 0.05 . 1 . . . . . . . . 4381 1 1151 . 1 1 93 93 GLU HB2 H 1 2.016 0.05 . 1 . . . . . . . . 4381 1 1152 . 1 1 93 93 GLU HB3 H 1 2.016 0.05 . 1 . . . . . . . . 4381 1 1153 . 1 1 93 93 GLU HG2 H 1 2.266 0.05 . 2 . . . . . . . . 4381 1 1154 . 1 1 93 93 GLU HG3 H 1 2.206 0.05 . 2 . . . . . . . . 4381 1 1155 . 1 1 93 93 GLU C C 13 176.82 0.1 . 1 . . . . . . . . 4381 1 1156 . 1 1 93 93 GLU CA C 13 58.246 0.1 . 1 . . . . . . . . 4381 1 1157 . 1 1 93 93 GLU CB C 13 28.206 0.1 . 1 . . . . . . . . 4381 1 1158 . 1 1 93 93 GLU CG C 13 36.646 0.1 . 1 . . . . . . . . 4381 1 1159 . 1 1 93 93 GLU N N 15 113.45 0.1 . 1 . . . . . . . . 4381 1 1160 . 1 1 94 94 MET H H 1 8.166 0.05 . 1 . . . . . . . . 4381 1 1161 . 1 1 94 94 MET HA H 1 4.396 0.05 . 1 . . . . . . . . 4381 1 1162 . 1 1 94 94 MET HB2 H 1 2.356 0.05 . 1 . . . . . . . . 4381 1 1163 . 1 1 94 94 MET HB3 H 1 2.356 0.05 . 1 . . . . . . . . 4381 1 1164 . 1 1 94 94 MET HE1 H 1 2.206 0.05 . 1 . . . . . . . . 4381 1 1165 . 1 1 94 94 MET HE2 H 1 2.206 0.05 . 1 . . . . . . . . 4381 1 1166 . 1 1 94 94 MET HE3 H 1 2.206 0.05 . 1 . . . . . . . . 4381 1 1167 . 1 1 94 94 MET HG2 H 1 2.916 0.05 . 2 . . . . . . . . 4381 1 1168 . 1 1 94 94 MET HG3 H 1 2.386 0.05 . 2 . . . . . . . . 4381 1 1169 . 1 1 94 94 MET C C 13 176.22 0.1 . 1 . . . . . . . . 4381 1 1170 . 1 1 94 94 MET CA C 13 57.756 0.1 . 1 . . . . . . . . 4381 1 1171 . 1 1 94 94 MET CB C 13 35.396 0.1 . 1 . . . . . . . . 4381 1 1172 . 1 1 94 94 MET CE C 13 18.516 0.1 . 1 . . . . . . . . 4381 1 1173 . 1 1 94 94 MET CG C 13 34.396 0.1 . 1 . . . . . . . . 4381 1 1174 . 1 1 94 94 MET N N 15 117.97 0.1 . 1 . . . . . . . . 4381 1 1175 . 1 1 95 95 ILE H H 1 7.146 0.05 . 1 . . . . . . . . 4381 1 1176 . 1 1 95 95 ILE HA H 1 3.886 0.05 . 1 . . . . . . . . 4381 1 1177 . 1 1 95 95 ILE HB H 1 1.796 0.05 . 1 . . . . . . . . 4381 1 1178 . 1 1 95 95 ILE HD11 H 1 0.826 0.05 . 1 . . . . . . . . 4381 1 1179 . 1 1 95 95 ILE HD12 H 1 0.826 0.05 . 1 . . . . . . . . 4381 1 1180 . 1 1 95 95 ILE HD13 H 1 0.826 0.05 . 1 . . . . . . . . 4381 1 1181 . 1 1 95 95 ILE HG12 H 1 1.756 0.05 . 2 . . . . . . . . 4381 1 1182 . 1 1 95 95 ILE HG13 H 1 1.316 0.05 . 2 . . . . . . . . 4381 1 1183 . 1 1 95 95 ILE HG21 H 1 0.916 0.05 . 1 . . . . . . . . 4381 1 1184 . 1 1 95 95 ILE HG22 H 1 0.916 0.05 . 1 . . . . . . . . 4381 1 1185 . 1 1 95 95 ILE HG23 H 1 0.916 0.05 . 1 . . . . . . . . 4381 1 1186 . 1 1 95 95 ILE CA C 13 59.696 0.1 . 1 . . . . . . . . 4381 1 1187 . 1 1 95 95 ILE CB C 13 38.336 0.1 . 1 . . . . . . . . 4381 1 1188 . 1 1 95 95 ILE CD1 C 13 12.196 0.1 . 1 . . . . . . . . 4381 1 1189 . 1 1 95 95 ILE CG1 C 13 28.096 0.1 . 1 . . . . . . . . 4381 1 1190 . 1 1 95 95 ILE CG2 C 13 16.436 0.1 . 1 . . . . . . . . 4381 1 1191 . 1 1 95 95 ILE N N 15 119.32 0.1 . 1 . . . . . . . . 4381 1 1192 . 1 1 96 96 PRO HA H 1 3.386 0.05 . 1 . . . . . . . . 4381 1 1193 . 1 1 96 96 PRO HB2 H 1 1.786 0.05 . 2 . . . . . . . . 4381 1 1194 . 1 1 96 96 PRO HB3 H 1 1.696 0.05 . 2 . . . . . . . . 4381 1 1195 . 1 1 96 96 PRO HD2 H 1 4.126 0.05 . 2 . . . . . . . . 4381 1 1196 . 1 1 96 96 PRO HD3 H 1 3.726 0.05 . 2 . . . . . . . . 4381 1 1197 . 1 1 96 96 PRO HG2 H 1 2.196 0.05 . 2 . . . . . . . . 4381 1 1198 . 1 1 96 96 PRO HG3 H 1 1.886 0.05 . 2 . . . . . . . . 4381 1 1199 . 1 1 96 96 PRO CA C 13 61.106 0.1 . 1 . . . . . . . . 4381 1 1200 . 1 1 96 96 PRO CB C 13 31.656 0.1 . 1 . . . . . . . . 4381 1 1201 . 1 1 96 96 PRO CD C 13 50.706 0.1 . 1 . . . . . . . . 4381 1 1202 . 1 1 96 96 PRO CG C 13 28.486 0.1 . 1 . . . . . . . . 4381 1 1203 . 1 1 97 97 PRO HA H 1 3.616 0.05 . 1 . . . . . . . . 4381 1 1204 . 1 1 97 97 PRO HB2 H 1 2.016 0.05 . 2 . . . . . . . . 4381 1 1205 . 1 1 97 97 PRO HB3 H 1 1.686 0.05 . 2 . . . . . . . . 4381 1 1206 . 1 1 97 97 PRO HD2 H 1 1.856 0.05 . 2 . . . . . . . . 4381 1 1207 . 1 1 97 97 PRO HD3 H 1 1.656 0.05 . 2 . . . . . . . . 4381 1 1208 . 1 1 97 97 PRO HG2 H 1 1.596 0.05 . 2 . . . . . . . . 4381 1 1209 . 1 1 97 97 PRO HG3 H 1 1.276 0.05 . 2 . . . . . . . . 4381 1 1210 . 1 1 97 97 PRO C C 13 177.99 0.1 . 1 . . . . . . . . 4381 1 1211 . 1 1 97 97 PRO CA C 13 65.826 0.1 . 1 . . . . . . . . 4381 1 1212 . 1 1 97 97 PRO CB C 13 31.696 0.1 . 1 . . . . . . . . 4381 1 1213 . 1 1 97 97 PRO CD C 13 48.856 0.1 . 1 . . . . . . . . 4381 1 1214 . 1 1 97 97 PRO CG C 13 27.666 0.1 . 1 . . . . . . . . 4381 1 1215 . 1 1 98 98 SER H H 1 7.926 0.05 . 1 . . . . . . . . 4381 1 1216 . 1 1 98 98 SER HA H 1 4.096 0.05 . 1 . . . . . . . . 4381 1 1217 . 1 1 98 98 SER HB2 H 1 3.926 0.05 . 2 . . . . . . . . 4381 1 1218 . 1 1 98 98 SER HB3 H 1 3.156 0.05 . 2 . . . . . . . . 4381 1 1219 . 1 1 98 98 SER C C 13 174.83 0.1 . 1 . . . . . . . . 4381 1 1220 . 1 1 98 98 SER CA C 13 59.456 0.1 . 1 . . . . . . . . 4381 1 1221 . 1 1 98 98 SER CB C 13 62.366 0.1 . 1 . . . . . . . . 4381 1 1222 . 1 1 98 98 SER N N 15 110.26 0.1 . 1 . . . . . . . . 4381 1 1223 . 1 1 99 99 ASP H H 1 7.926 0.05 . 1 . . . . . . . . 4381 1 1224 . 1 1 99 99 ASP HA H 1 4.726 0.05 . 1 . . . . . . . . 4381 1 1225 . 1 1 99 99 ASP HB2 H 1 2.706 0.05 . 2 . . . . . . . . 4381 1 1226 . 1 1 99 99 ASP HB3 H 1 2.556 0.05 . 2 . . . . . . . . 4381 1 1227 . 1 1 99 99 ASP C C 13 175.62 0.1 . 1 . . . . . . . . 4381 1 1228 . 1 1 99 99 ASP CA C 13 54.676 0.1 . 1 . . . . . . . . 4381 1 1229 . 1 1 99 99 ASP CB C 13 41.866 0.1 . 1 . . . . . . . . 4381 1 1230 . 1 1 99 99 ASP N N 15 121.8 0.1 . 1 . . . . . . . . 4381 1 1231 . 1 1 100 100 ARG H H 1 7.146 0.05 . 1 . . . . . . . . 4381 1 1232 . 1 1 100 100 ARG N N 15 125.35 0.1 . 1 . . . . . . . . 4381 1 1233 . 1 1 101 101 ALA HA H 1 4.246 0.05 . 1 . . . . . . . . 4381 1 1234 . 1 1 101 101 ALA HB1 H 1 1.366 0.05 . 1 . . . . . . . . 4381 1 1235 . 1 1 101 101 ALA HB2 H 1 1.366 0.05 . 1 . . . . . . . . 4381 1 1236 . 1 1 101 101 ALA HB3 H 1 1.366 0.05 . 1 . . . . . . . . 4381 1 1237 . 1 1 101 101 ALA CA C 13 52.786 0.1 . 1 . . . . . . . . 4381 1 1238 . 1 1 101 101 ALA CB C 13 19.006 0.1 . 1 . . . . . . . . 4381 1 1239 . 1 1 102 102 SER C C 13 174.37 0.1 . 1 . . . . . . . . 4381 1 1240 . 1 1 103 103 LEU H H 1 8.106 0.05 . 1 . . . . . . . . 4381 1 1241 . 1 1 103 103 LEU HA H 1 4.356 0.05 . 1 . . . . . . . . 4381 1 1242 . 1 1 103 103 LEU C C 13 176.34 0.1 . 1 . . . . . . . . 4381 1 1243 . 1 1 103 103 LEU CA C 13 55.196 0.1 . 1 . . . . . . . . 4381 1 1244 . 1 1 103 103 LEU N N 15 124.14 0.1 . 1 . . . . . . . . 4381 1 1245 . 1 1 104 104 GLN H H 1 7.806 0.05 . 1 . . . . . . . . 4381 1 1246 . 1 1 104 104 GLN HE21 H 1 6.756 0.05 . 2 . . . . . . . . 4381 1 1247 . 1 1 104 104 GLN HE22 H 1 7.456 0.05 . 2 . . . . . . . . 4381 1 1248 . 1 1 104 104 GLN CD C 13 181.25 0.1 . 1 . . . . . . . . 4381 1 1249 . 1 1 104 104 GLN N N 15 125.26 0.1 . 1 . . . . . . . . 4381 1 1250 . 1 1 104 104 GLN NE2 N 15 112.04 0.1 . 1 . . . . . . . . 4381 1 stop_ save_