data_5334 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5334 _Entry.Title ; Backbone 1H, 13C, and 15N resonance assignments and secondary structure of the D54A mutant of HTLV-I capsid protein ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2002-03-26 _Entry.Accession_date 2002-03-26 _Entry.Last_release_date 2003-06-10 _Entry.Original_release_date 2003-06-10 _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 Claudia Cornilescu . C. . 5334 2 Fadila Bouamr . . . 5334 3 Carol Carter . . . 5334 4 Nico Tjandra . . . 5334 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5334 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 436 5334 '13C chemical shifts' 361 5334 '15N chemical shifts' 115 5334 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 . . 2003-06-10 2002-03-26 original author . 5334 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5334 _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 ; Backbone 1H, 13C, and 15N resonance assignments and secondary structure of the D54A mutant of HTLV-I capsid protein ; _Citation.Status 'in preparation' _Citation.Type journal _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 . 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 Claudia Cornilescu . C. . 5334 1 2 Fadila Bouamr . . . 5334 1 3 Carol Carter . . . 5334 1 4 Nico Tjandra . . . 5334 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID HTLV-I 5334 1 mutant 5334 1 retrovirus 5334 1 'capsid protein' 5334 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 5334 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 11243788 _Citation.Full_citation ; Cornilescu, C. C., Bouamr, F., Yao, X., Carter, C. & Tjandra, N. (2001) J. Mol. Biol., 306, 783-797. ; _Citation.Title 'Structural analysis of the N-terminal domain of the human T-cell leukemia virus capsid protein.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 306 _Citation.Journal_issue 4 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0022-2836 _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 783 _Citation.Page_last 797 _Citation.Year 2001 _Citation.Details ; The N-terminal domain of the retroviral capsid (CA) protein is one of the least conserved regions encoded in the genome. Surprisingly, the three-dimensional structures of the CA from different genera exhibit alpha-helical structural features that are highly conserved. The N-terminal residues of the human immunodeficiency virus type 1 (HIV-1) and Rous sarcoma virus (RSV) capsid proteins form a beta-hairpin. To determine if this feature is conserved in the retroviral family, we cloned, expressed, purified, and solved the structure of a N-terminal 134 amino acid fragment (CA(134)) from the human T-cell leukemia virus type 1 (HTLV-I) using high resolution nuclear magnetic resonance (NMR) spectroscopy. The CA(134) fragment contains an N-terminal beta-hairpin and a central coiled-coil-like structure composed of six alpha-helices. The N-terminal Pro1 residue contacts Asp54 in the helical cluster through a salt bridge. Thus, the beta-hairpin is conserved and the helical cluster is structurally similar to other retroviral CA domains. However, although the same Asp residue defines the orientation of the hairpin in both the HTLV-1 and HIV-1 CA proteins, the HTLV-I hairpin is oriented away, rather than towards, the helical core. Significant differences were also detected in the spatial orientation and helical content of the long centrally located loop connecting the helices in the core. It has been proposed that the salt bridge allows the formation of a CA-CA interface that is important for the assembly of the conical cores that are characteristic of HIV-1. As HTLV-I forms spherical cores, the salt-bridge feature is apparently not conserved for this function although its role in determining the orientation of the beta-hairpin may be critical, along with the central loop. Comparison of three-dimensional structures is expected to elucidate the relationships between the retroviral capsid protein structure and its function. ; 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 'C. C.' Cornilescu C. C. . 5334 2 2 F. Bouamr F. . . 5334 2 3 X. Yao X. . . 5334 2 4 C. Carter C. . . 5334 2 5 N. Tjandra N. . . 5334 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 5334 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8520220 _Citation.Full_citation ; Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J. & Bax, A. (1995) J. Biomol. NMR, 6, 277-293. ; _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. . . 5334 3 2 S. Grzesiek S. . . 5334 3 3 'G. W.' Vuister G. W. . 5334 3 4 G. Zhu G. . . 5334 3 5 J. Pfeifer J. . . 5334 3 6 A. Bax A. . . 5334 3 stop_ save_ save_ref_3 _Citation.Sf_category citations _Citation.Sf_framecode ref_3 _Citation.Entry_ID 5334 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10212987 _Citation.Full_citation ; Cornilescu, G., Delaglio, F. & Bax, A. (1999) J. Biomol. NMR, 13, 289-302. ; _Citation.Title 'Protein backbone angle restraints from searching a database for chemical shift and sequence homology.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full 'Journal of biomolecular NMR' _Citation.Journal_volume 13 _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 289 _Citation.Page_last 302 _Citation.Year 1999 _Citation.Details ; Chemical shifts of backbone atoms in proteins are exquisitely sensitive to local conformation, and homologous proteins show quite similar patterns of secondary chemical shifts. The inverse of this relation is used to search a database for triplets of adjacent residues with secondary chemical shifts and sequence similarity which provide the best match to the query triplet of interest. The database contains 13C alpha, 13C beta, 13C', 1H alpha and 15N chemical shifts for 20 proteins for which a high resolution X-ray structure is available. The computer program TALOS was developed to search this database for strings of residues with chemical shift and residue type homology. The relative importance of the weighting factors attached to the secondary chemical shifts of the five types of resonances relative to that of sequence similarity was optimized empirically. TALOS yields the 10 triplets which have the closest similarity in secondary chemical shift and amino acid sequence to those of the query sequence. If the central residues in these 10 triplets exhibit similar phi and psi backbone angles, their averages can reliably be used as angular restraints for the protein whose structure is being studied. Tests carried out for proteins of known structure indicate that the root-mean-square difference (rmsd) between the output of TALOS and the X-ray derived backbone angles is about 15 degrees. Approximately 3% of the predictions made by TALOS are found to be in error. ; 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 G Cornilescu G. . . 5334 4 2 F Delaglio F. . . 5334 4 3 A Bax A. . . 5334 4 stop_ save_ save_ref_4 _Citation.Sf_category citations _Citation.Sf_framecode ref_4 _Citation.Entry_ID 5334 _Citation.ID 5 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Garrett, D. S., Powers, R., Gronenborn, A. M. & Clore, G. M. (1991) J. Magn. Reson, 95, 214-220. ; _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_system_NTD_HTLV-I_CA _Assembly.Sf_category assembly _Assembly.Sf_framecode system_NTD_HTLV-I_CA _Assembly.Entry_ID 5334 _Assembly.ID 1 _Assembly.Name 'NTD HTLV-I capsid protein' _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 'all free' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details 'Residue Asp 54 has been replaced by an Ala.' _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 5334 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 HTLV-I 1 $HTLV-I . . . native . . . . . 5334 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 1G03 . . . . . . 5334 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'NTD HTLV-I capsid protein' system 5334 1 'NTD HTLV-I CA' abbreviation 5334 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_HTLV-I _Entity.Sf_category entity _Entity.Sf_framecode HTLV-I _Entity.Entry_ID 5334 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Human T-cell Leukemia Virus type I' _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 ; PVMHPHGAPPNHRPWQMKDL QAIKQEVSQAAPGSPQFMQT IRLAVQQFDPTAKALQDLLQ YLCSSLVASLHHQQLDSLIS EAETRGITSYNPLAGPLRVQ ANNPQQQGLRREYQQLWLAA FAALPGSAKDPSWA ; _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 134 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all free' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 14841.8 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 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 BMRB 4649 . HTLV-I . . . . . 100.00 134 99.25 99.25 5.21e-90 . . . . 5334 1 2 no PDB 1G03 . "Nmr Structure Of N-Terminal Domain Of Htlv-I Ca1-134" . . . . . 99.25 134 99.25 99.25 2.77e-89 . . . . 5334 1 3 no DBJ BAA02929 . "gag polyprotein precursor [Human T-lymphotropic virus 1]" . . . . . 100.00 429 98.51 98.51 3.47e-85 . . . . 5334 1 4 no DBJ BAF31288 . "gag protein [eukaryotic synthetic construct]" . . . . . 100.00 429 97.76 99.25 1.57e-84 . . . . 5334 1 5 no DBJ BAH85785 . "Gag protein [Human T-lymphotropic virus 1]" . . . . . 100.00 429 98.51 98.51 3.83e-85 . . . . 5334 1 6 no DBJ BAP28584 . "Gag protein [Human T-lymphotropic virus 1]" . . . . . 100.00 429 98.51 98.51 3.70e-85 . . . . 5334 1 7 no EMBL CAA34075 . "unnamed protein product [Human T-lymphotropic virus 1]" . . . . . 100.00 429 99.25 99.25 9.01e-86 . . . . 5334 1 8 no EMBL CAA62992 . "p24 protein [Human T-lymphotropic virus 1]" . . . . . 99.25 213 98.50 98.50 5.30e-88 . . . . 5334 1 9 no GB AAA85325 . "gag protein [Human T-lymphotropic virus 1]" . . . . . 100.00 429 98.51 98.51 3.83e-85 . . . . 5334 1 10 no GB AAA85841 . "gag [Human T-lymphotropic virus 1]" . . . . . 100.00 429 98.51 98.51 3.83e-85 . . . . 5334 1 11 no GB AAA96672 . "gag [Human T-lymphotropic virus 1]" . . . . . 100.00 429 98.51 98.51 2.86e-85 . . . . 5334 1 12 no GB AAB20767 . "Gag [Human T-lymphotropic virus 1]" . . . . . 100.00 429 97.76 98.51 2.24e-84 . . . . 5334 1 13 no GB AAC00185 . "gag protein [Human T-lymphotropic virus 1]" . . . . . 100.00 429 98.51 98.51 3.83e-85 . . . . 5334 1 14 no REF NP_049558 . "gag polyprotein [Simian T-lymphotropic virus 1]" . . . . . 100.00 428 97.76 98.51 3.33e-84 . . . . 5334 1 15 no REF NP_057860 . "Pr gag-pro-pol [Human T-lymphotropic virus 1]" . . . . . 100.00 1462 98.51 98.51 4.60e-80 . . . . 5334 1 16 no REF NP_057861 . "Pr gag-pro [Human T-lymphotropic virus 1]" . . . . . 100.00 651 98.51 98.51 2.87e-83 . . . . 5334 1 17 no REF NP_057862 . "Pr55 [Human T-lymphotropic virus 1]" . . . . . 100.00 429 98.51 98.51 3.47e-85 . . . . 5334 1 18 no REF NP_955618 . "p24 CA [Human T-lymphotropic virus 1]" . . . . . 100.00 215 98.51 98.51 7.96e-89 . . . . 5334 1 19 no SP P03345 . "RecName: Full=Gag polyprotein; AltName: Full=Pr53Gag; Contains: RecName: Full=Matrix protein p19; Short=MA; Contains: RecName: " . . . . . 100.00 429 98.51 98.51 2.86e-85 . . . . 5334 1 20 no SP P03362 . "RecName: Full=Gag-Pro-Pol polyprotein; AltName: Full=Pr160Gag-Pro-Pol; Contains: RecName: Full=Matrix protein p19; Short=MA; Co" . . . . . 100.00 1462 98.51 98.51 4.16e-80 . . . . 5334 1 21 no SP P10274 . "RecName: Full=Gag-Pro polyprotein; AltName: Full=Pr76Gag-Pro; Contains: RecName: Full=Matrix protein p19; Short=MA; Contains: R" . . . . . 100.00 651 98.51 98.51 2.50e-83 . . . . 5334 1 22 no SP P14074 . "RecName: Full=Gag-Pro polyprotein; AltName: Full=Pr76Gag-Pro; Contains: RecName: Full=Matrix protein p19; Short=MA; Contains: R" . . . . . 100.00 651 98.51 98.51 2.87e-83 . . . . 5334 1 23 no SP P14076 . "RecName: Full=Gag polyprotein; AltName: Full=Pr53Gag; Contains: RecName: Full=Matrix protein p19; Short=MA; Contains: RecName: " . . . . . 100.00 429 98.51 98.51 3.47e-85 . . . . 5334 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Human T-cell Leukemia Virus type I' common 5334 1 D54A variant 5334 1 HTLV-I abbreviation 5334 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 . PRO . 5334 1 2 . VAL . 5334 1 3 . MET . 5334 1 4 . HIS . 5334 1 5 . PRO . 5334 1 6 . HIS . 5334 1 7 . GLY . 5334 1 8 . ALA . 5334 1 9 . PRO . 5334 1 10 . PRO . 5334 1 11 . ASN . 5334 1 12 . HIS . 5334 1 13 . ARG . 5334 1 14 . PRO . 5334 1 15 . TRP . 5334 1 16 . GLN . 5334 1 17 . MET . 5334 1 18 . LYS . 5334 1 19 . ASP . 5334 1 20 . LEU . 5334 1 21 . GLN . 5334 1 22 . ALA . 5334 1 23 . ILE . 5334 1 24 . LYS . 5334 1 25 . GLN . 5334 1 26 . GLU . 5334 1 27 . VAL . 5334 1 28 . SER . 5334 1 29 . GLN . 5334 1 30 . ALA . 5334 1 31 . ALA . 5334 1 32 . PRO . 5334 1 33 . GLY . 5334 1 34 . SER . 5334 1 35 . PRO . 5334 1 36 . GLN . 5334 1 37 . PHE . 5334 1 38 . MET . 5334 1 39 . GLN . 5334 1 40 . THR . 5334 1 41 . ILE . 5334 1 42 . ARG . 5334 1 43 . LEU . 5334 1 44 . ALA . 5334 1 45 . VAL . 5334 1 46 . GLN . 5334 1 47 . GLN . 5334 1 48 . PHE . 5334 1 49 . ASP . 5334 1 50 . PRO . 5334 1 51 . THR . 5334 1 52 . ALA . 5334 1 53 . LYS . 5334 1 54 . ALA . 5334 1 55 . LEU . 5334 1 56 . GLN . 5334 1 57 . ASP . 5334 1 58 . LEU . 5334 1 59 . LEU . 5334 1 60 . GLN . 5334 1 61 . TYR . 5334 1 62 . LEU . 5334 1 63 . CYS . 5334 1 64 . SER . 5334 1 65 . SER . 5334 1 66 . LEU . 5334 1 67 . VAL . 5334 1 68 . ALA . 5334 1 69 . SER . 5334 1 70 . LEU . 5334 1 71 . HIS . 5334 1 72 . HIS . 5334 1 73 . GLN . 5334 1 74 . GLN . 5334 1 75 . LEU . 5334 1 76 . ASP . 5334 1 77 . SER . 5334 1 78 . LEU . 5334 1 79 . ILE . 5334 1 80 . SER . 5334 1 81 . GLU . 5334 1 82 . ALA . 5334 1 83 . GLU . 5334 1 84 . THR . 5334 1 85 . ARG . 5334 1 86 . GLY . 5334 1 87 . ILE . 5334 1 88 . THR . 5334 1 89 . SER . 5334 1 90 . TYR . 5334 1 91 . ASN . 5334 1 92 . PRO . 5334 1 93 . LEU . 5334 1 94 . ALA . 5334 1 95 . GLY . 5334 1 96 . PRO . 5334 1 97 . LEU . 5334 1 98 . ARG . 5334 1 99 . VAL . 5334 1 100 . GLN . 5334 1 101 . ALA . 5334 1 102 . ASN . 5334 1 103 . ASN . 5334 1 104 . PRO . 5334 1 105 . GLN . 5334 1 106 . GLN . 5334 1 107 . GLN . 5334 1 108 . GLY . 5334 1 109 . LEU . 5334 1 110 . ARG . 5334 1 111 . ARG . 5334 1 112 . GLU . 5334 1 113 . TYR . 5334 1 114 . GLN . 5334 1 115 . GLN . 5334 1 116 . LEU . 5334 1 117 . TRP . 5334 1 118 . LEU . 5334 1 119 . ALA . 5334 1 120 . ALA . 5334 1 121 . PHE . 5334 1 122 . ALA . 5334 1 123 . ALA . 5334 1 124 . LEU . 5334 1 125 . PRO . 5334 1 126 . GLY . 5334 1 127 . SER . 5334 1 128 . ALA . 5334 1 129 . LYS . 5334 1 130 . ASP . 5334 1 131 . PRO . 5334 1 132 . SER . 5334 1 133 . TRP . 5334 1 134 . ALA . 5334 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 . PRO 1 1 5334 1 . VAL 2 2 5334 1 . MET 3 3 5334 1 . HIS 4 4 5334 1 . PRO 5 5 5334 1 . HIS 6 6 5334 1 . GLY 7 7 5334 1 . ALA 8 8 5334 1 . PRO 9 9 5334 1 . PRO 10 10 5334 1 . ASN 11 11 5334 1 . HIS 12 12 5334 1 . ARG 13 13 5334 1 . PRO 14 14 5334 1 . TRP 15 15 5334 1 . GLN 16 16 5334 1 . MET 17 17 5334 1 . LYS 18 18 5334 1 . ASP 19 19 5334 1 . LEU 20 20 5334 1 . GLN 21 21 5334 1 . ALA 22 22 5334 1 . ILE 23 23 5334 1 . LYS 24 24 5334 1 . GLN 25 25 5334 1 . GLU 26 26 5334 1 . VAL 27 27 5334 1 . SER 28 28 5334 1 . GLN 29 29 5334 1 . ALA 30 30 5334 1 . ALA 31 31 5334 1 . PRO 32 32 5334 1 . GLY 33 33 5334 1 . SER 34 34 5334 1 . PRO 35 35 5334 1 . GLN 36 36 5334 1 . PHE 37 37 5334 1 . MET 38 38 5334 1 . GLN 39 39 5334 1 . THR 40 40 5334 1 . ILE 41 41 5334 1 . ARG 42 42 5334 1 . LEU 43 43 5334 1 . ALA 44 44 5334 1 . VAL 45 45 5334 1 . GLN 46 46 5334 1 . GLN 47 47 5334 1 . PHE 48 48 5334 1 . ASP 49 49 5334 1 . PRO 50 50 5334 1 . THR 51 51 5334 1 . ALA 52 52 5334 1 . LYS 53 53 5334 1 . ALA 54 54 5334 1 . LEU 55 55 5334 1 . GLN 56 56 5334 1 . ASP 57 57 5334 1 . LEU 58 58 5334 1 . LEU 59 59 5334 1 . GLN 60 60 5334 1 . TYR 61 61 5334 1 . LEU 62 62 5334 1 . CYS 63 63 5334 1 . SER 64 64 5334 1 . SER 65 65 5334 1 . LEU 66 66 5334 1 . VAL 67 67 5334 1 . ALA 68 68 5334 1 . SER 69 69 5334 1 . LEU 70 70 5334 1 . HIS 71 71 5334 1 . HIS 72 72 5334 1 . GLN 73 73 5334 1 . GLN 74 74 5334 1 . LEU 75 75 5334 1 . ASP 76 76 5334 1 . SER 77 77 5334 1 . LEU 78 78 5334 1 . ILE 79 79 5334 1 . SER 80 80 5334 1 . GLU 81 81 5334 1 . ALA 82 82 5334 1 . GLU 83 83 5334 1 . THR 84 84 5334 1 . ARG 85 85 5334 1 . GLY 86 86 5334 1 . ILE 87 87 5334 1 . THR 88 88 5334 1 . SER 89 89 5334 1 . TYR 90 90 5334 1 . ASN 91 91 5334 1 . PRO 92 92 5334 1 . LEU 93 93 5334 1 . ALA 94 94 5334 1 . GLY 95 95 5334 1 . PRO 96 96 5334 1 . LEU 97 97 5334 1 . ARG 98 98 5334 1 . VAL 99 99 5334 1 . GLN 100 100 5334 1 . ALA 101 101 5334 1 . ASN 102 102 5334 1 . ASN 103 103 5334 1 . PRO 104 104 5334 1 . GLN 105 105 5334 1 . GLN 106 106 5334 1 . GLN 107 107 5334 1 . GLY 108 108 5334 1 . LEU 109 109 5334 1 . ARG 110 110 5334 1 . ARG 111 111 5334 1 . GLU 112 112 5334 1 . TYR 113 113 5334 1 . GLN 114 114 5334 1 . GLN 115 115 5334 1 . LEU 116 116 5334 1 . TRP 117 117 5334 1 . LEU 118 118 5334 1 . ALA 119 119 5334 1 . ALA 120 120 5334 1 . PHE 121 121 5334 1 . ALA 122 122 5334 1 . ALA 123 123 5334 1 . LEU 124 124 5334 1 . PRO 125 125 5334 1 . GLY 126 126 5334 1 . SER 127 127 5334 1 . ALA 128 128 5334 1 . LYS 129 129 5334 1 . ASP 130 130 5334 1 . PRO 131 131 5334 1 . SER 132 132 5334 1 . TRP 133 133 5334 1 . ALA 134 134 5334 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 5334 _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 $HTLV-I . 11908 organism . 'Deltaretrovirus HTLV-I' 'Human T-cell lymphotropic virus type 1' . . Viruses . Deltaretrovirus HTLV-I . . . . . . . . . . . . . . . . . . . . . 5334 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 5334 _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 $HTLV-I . 'recombinant technology' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5334 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_N15_sample _Sample.Sf_category sample _Sample.Sf_framecode N15_sample _Sample.Entry_ID 5334 _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 'Human T-cell Leukemia Virus type I' [U-15N] . . 1 $HTLV-I . . . 0.8 1.0 mM . . . . 5334 1 stop_ save_ save_C13-N15_sample _Sample.Sf_category sample _Sample.Sf_framecode C13-N15_sample _Sample.Entry_ID 5334 _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 'Human T-cell Leukemia Virus type I' '[U-13C; U-15N]' . . 1 $HTLV-I . . . 0.8 1.0 mM . . . . 5334 2 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 5334 _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 6.0 0.05 n/a 5334 1 temperature 300 0.2 K 5334 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 5334 _Software.ID 1 _Software.Name NMRPipe _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'processed data' 5334 1 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 3 $ref_2 5334 1 stop_ save_ save_TALOS _Software.Sf_category software _Software.Sf_framecode TALOS _Software.Entry_ID 5334 _Software.ID 2 _Software.Name TALOS _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'predicted torsion angles' 5334 2 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 4 $ref_3 5334 2 stop_ save_ save_PIPP_STAPP _Software.Sf_category software _Software.Sf_framecode PIPP_STAPP _Software.Entry_ID 5334 _Software.ID 3 _Software.Name PIPP_STAPP _Software.Version . _Software.Details . loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'peak assignments' 5334 3 stop_ loop_ _Software_citation.Citation_ID _Software_citation.Citation_label _Software_citation.Entry_ID _Software_citation.Software_ID 5 $ref_4 5334 3 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 5334 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AVANCE _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 5334 _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 spectrometer_1 Bruker AVANCE . 600 . . . 5334 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 5334 _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 '1H-15N HSQC' . . . . . . . . . . . . . . . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 5334 1 2 CBCACONH . . . . . . . . . . . . . . . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 5334 1 3 HNCACB . . . . . . . . . . . . . . . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 5334 1 4 HBHACONH . . . . . . . . . . . . . . . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 5334 1 5 '3D HNCO' . . . . . . . . . . . . . . . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 5334 1 6 '3D 1H-15N NOESY' . . . . . . . . . . . . . . . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 5334 1 7 '1H-13C CT-HSQC' . . . . . . . . . . . . . . . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 5334 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 5334 _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 H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.000000000 . . . . . . . . . 5334 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 5334 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 5334 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_chemical_shifts _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chemical_shifts _Assigned_chem_shift_list.Entry_ID 5334 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_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 $N15_sample . 5334 1 . . 2 $C13-N15_sample . 5334 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 2 2 VAL HA H 1 3.952 . . 1 . . . . . . . . 5334 1 2 . 1 1 2 2 VAL HB H 1 1.882 . . 1 . . . . . . . . 5334 1 3 . 1 1 2 2 VAL C C 13 175.661 . . 1 . . . . . . . . 5334 1 4 . 1 1 2 2 VAL CA C 13 62.744 . . 1 . . . . . . . . 5334 1 5 . 1 1 2 2 VAL CB C 13 32.603 . . 1 . . . . . . . . 5334 1 6 . 1 1 3 3 MET H H 1 8.427 . . 1 . . . . . . . . 5334 1 7 . 1 1 3 3 MET HA H 1 4.337 . . 1 . . . . . . . . 5334 1 8 . 1 1 3 3 MET HB2 H 1 1.828 . . 1 . . . . . . . . 5334 1 9 . 1 1 3 3 MET HB3 H 1 1.828 . . 1 . . . . . . . . 5334 1 10 . 1 1 3 3 MET C C 13 175.457 . . 1 . . . . . . . . 5334 1 11 . 1 1 3 3 MET CA C 13 55.123 . . 1 . . . . . . . . 5334 1 12 . 1 1 3 3 MET CB C 13 33.082 . . 1 . . . . . . . . 5334 1 13 . 1 1 3 3 MET N N 15 124.513 . . 1 . . . . . . . . 5334 1 14 . 1 1 4 4 HIS H H 1 8.385 . . 1 . . . . . . . . 5334 1 15 . 1 1 4 4 HIS CA C 13 53.867 . . 1 . . . . . . . . 5334 1 16 . 1 1 4 4 HIS CB C 13 29.913 . . 1 . . . . . . . . 5334 1 17 . 1 1 4 4 HIS N N 15 121.194 . . 1 . . . . . . . . 5334 1 18 . 1 1 5 5 PRO HA H 1 4.652 . . 1 . . . . . . . . 5334 1 19 . 1 1 5 5 PRO HB2 H 1 1.430 . . 2 . . . . . . . . 5334 1 20 . 1 1 5 5 PRO HB3 H 1 1.953 . . 2 . . . . . . . . 5334 1 21 . 1 1 5 5 PRO C C 13 176.537 . . 1 . . . . . . . . 5334 1 22 . 1 1 5 5 PRO CA C 13 64.121 . . 1 . . . . . . . . 5334 1 23 . 1 1 5 5 PRO CB C 13 32.179 . . 1 . . . . . . . . 5334 1 24 . 1 1 6 6 HIS H H 1 8.408 . . 1 . . . . . . . . 5334 1 25 . 1 1 6 6 HIS HA H 1 4.579 . . 1 . . . . . . . . 5334 1 26 . 1 1 6 6 HIS HB2 H 1 3.088 . . 1 . . . . . . . . 5334 1 27 . 1 1 6 6 HIS HB3 H 1 3.088 . . 1 . . . . . . . . 5334 1 28 . 1 1 6 6 HIS C C 13 175.387 . . 1 . . . . . . . . 5334 1 29 . 1 1 6 6 HIS CA C 13 55.782 . . 1 . . . . . . . . 5334 1 30 . 1 1 6 6 HIS CB C 13 29.931 . . 1 . . . . . . . . 5334 1 31 . 1 1 6 6 HIS N N 15 115.135 . . 1 . . . . . . . . 5334 1 32 . 1 1 7 7 GLY H H 1 8.249 . . 1 . . . . . . . . 5334 1 33 . 1 1 7 7 GLY HA2 H 1 3.825 . . 1 . . . . . . . . 5334 1 34 . 1 1 7 7 GLY HA3 H 1 3.825 . . 1 . . . . . . . . 5334 1 35 . 1 1 7 7 GLY C C 13 173.171 . . 1 . . . . . . . . 5334 1 36 . 1 1 7 7 GLY CA C 13 45.046 . . 1 . . . . . . . . 5334 1 37 . 1 1 7 7 GLY N N 15 109.859 . . 1 . . . . . . . . 5334 1 38 . 1 1 8 8 ALA H H 1 8.107 . . 1 . . . . . . . . 5334 1 39 . 1 1 8 8 ALA CA C 13 50.498 . . 1 . . . . . . . . 5334 1 40 . 1 1 8 8 ALA CB C 13 18.481 . . 1 . . . . . . . . 5334 1 41 . 1 1 8 8 ALA N N 15 124.625 . . 1 . . . . . . . . 5334 1 42 . 1 1 10 10 PRO HA H 1 4.256 . . 1 . . . . . . . . 5334 1 43 . 1 1 10 10 PRO HB2 H 1 1.652 . . 2 . . . . . . . . 5334 1 44 . 1 1 10 10 PRO HB3 H 1 2.093 . . 2 . . . . . . . . 5334 1 45 . 1 1 10 10 PRO C C 13 176.522 . . 1 . . . . . . . . 5334 1 46 . 1 1 10 10 PRO CA C 13 63.105 . . 1 . . . . . . . . 5334 1 47 . 1 1 10 10 PRO CB C 13 32.111 . . 1 . . . . . . . . 5334 1 48 . 1 1 11 11 ASN H H 1 8.287 . . 1 . . . . . . . . 5334 1 49 . 1 1 11 11 ASN HB2 H 1 2.191 . . 1 . . . . . . . . 5334 1 50 . 1 1 11 11 ASN HB3 H 1 2.191 . . 1 . . . . . . . . 5334 1 51 . 1 1 11 11 ASN C C 13 174.758 . . 1 . . . . . . . . 5334 1 52 . 1 1 11 11 ASN CA C 13 53.107 . . 1 . . . . . . . . 5334 1 53 . 1 1 11 11 ASN CB C 13 39.096 . . 1 . . . . . . . . 5334 1 54 . 1 1 11 11 ASN N N 15 117.976 . . 1 . . . . . . . . 5334 1 55 . 1 1 12 12 HIS H H 1 8.273 . . 1 . . . . . . . . 5334 1 56 . 1 1 12 12 HIS HA H 1 4.487 . . 1 . . . . . . . . 5334 1 57 . 1 1 12 12 HIS HB2 H 1 2.962 . . 1 . . . . . . . . 5334 1 58 . 1 1 12 12 HIS HB3 H 1 2.962 . . 1 . . . . . . . . 5334 1 59 . 1 1 12 12 HIS CA C 13 55.950 . . 1 . . . . . . . . 5334 1 60 . 1 1 12 12 HIS CB C 13 29.984 . . 1 . . . . . . . . 5334 1 61 . 1 1 12 12 HIS N N 15 118.996 . . 1 . . . . . . . . 5334 1 62 . 1 1 13 13 ARG H H 1 8.113 . . 1 . . . . . . . . 5334 1 63 . 1 1 13 13 ARG CA C 13 54.023 . . 1 . . . . . . . . 5334 1 64 . 1 1 13 13 ARG CB C 13 30.244 . . 1 . . . . . . . . 5334 1 65 . 1 1 13 13 ARG N N 15 122.952 . . 1 . . . . . . . . 5334 1 66 . 1 1 14 14 PRO HA H 1 4.331 . . 1 . . . . . . . . 5334 1 67 . 1 1 14 14 PRO HB2 H 1 1.711 . . 2 . . . . . . . . 5334 1 68 . 1 1 14 14 PRO HB3 H 1 2.026 . . 2 . . . . . . . . 5334 1 69 . 1 1 14 14 PRO C C 13 176.804 . . 1 . . . . . . . . 5334 1 70 . 1 1 14 14 PRO CA C 13 62.499 . . 1 . . . . . . . . 5334 1 71 . 1 1 14 14 PRO CB C 13 32.248 . . 1 . . . . . . . . 5334 1 72 . 1 1 15 15 TRP H H 1 7.276 . . 1 . . . . . . . . 5334 1 73 . 1 1 15 15 TRP HA H 1 4.249 . . 1 . . . . . . . . 5334 1 74 . 1 1 15 15 TRP HB2 H 1 2.070 . . 2 . . . . . . . . 5334 1 75 . 1 1 15 15 TRP HB3 H 1 2.605 . . 2 . . . . . . . . 5334 1 76 . 1 1 15 15 TRP C C 13 177.530 . . 1 . . . . . . . . 5334 1 77 . 1 1 15 15 TRP CA C 13 55.009 . . 1 . . . . . . . . 5334 1 78 . 1 1 15 15 TRP CB C 13 28.092 . . 1 . . . . . . . . 5334 1 79 . 1 1 15 15 TRP N N 15 117.022 . . 1 . . . . . . . . 5334 1 80 . 1 1 16 16 GLN H H 1 9.328 . . 1 . . . . . . . . 5334 1 81 . 1 1 16 16 GLN HA H 1 4.586 . . 1 . . . . . . . . 5334 1 82 . 1 1 16 16 GLN HB2 H 1 1.855 . . 2 . . . . . . . . 5334 1 83 . 1 1 16 16 GLN HB3 H 1 2.328 . . 2 . . . . . . . . 5334 1 84 . 1 1 16 16 GLN C C 13 177.662 . . 1 . . . . . . . . 5334 1 85 . 1 1 16 16 GLN CA C 13 53.828 . . 1 . . . . . . . . 5334 1 86 . 1 1 16 16 GLN CB C 13 31.232 . . 1 . . . . . . . . 5334 1 87 . 1 1 16 16 GLN N N 15 118.636 . . 1 . . . . . . . . 5334 1 88 . 1 1 17 17 MET H H 1 8.915 . . 1 . . . . . . . . 5334 1 89 . 1 1 17 17 MET HA H 1 3.998 . . 1 . . . . . . . . 5334 1 90 . 1 1 17 17 MET HB2 H 1 1.948 . . 1 . . . . . . . . 5334 1 91 . 1 1 17 17 MET HB3 H 1 1.948 . . 1 . . . . . . . . 5334 1 92 . 1 1 17 17 MET CA C 13 58.736 . . 1 . . . . . . . . 5334 1 93 . 1 1 17 17 MET CB C 13 30.743 . . 1 . . . . . . . . 5334 1 94 . 1 1 17 17 MET N N 15 123.118 . . 1 . . . . . . . . 5334 1 95 . 1 1 18 18 LYS H H 1 8.571 . . 1 . . . . . . . . 5334 1 96 . 1 1 18 18 LYS HA H 1 4.013 . . 1 . . . . . . . . 5334 1 97 . 1 1 18 18 LYS HB2 H 1 1.702 . . 1 . . . . . . . . 5334 1 98 . 1 1 18 18 LYS HB3 H 1 1.702 . . 1 . . . . . . . . 5334 1 99 . 1 1 18 18 LYS C C 13 178.989 . . 1 . . . . . . . . 5334 1 100 . 1 1 18 18 LYS CA C 13 59.221 . . 1 . . . . . . . . 5334 1 101 . 1 1 18 18 LYS CB C 13 31.852 . . 1 . . . . . . . . 5334 1 102 . 1 1 18 18 LYS N N 15 115.584 . . 1 . . . . . . . . 5334 1 103 . 1 1 19 19 ASP H H 1 7.159 . . 1 . . . . . . . . 5334 1 104 . 1 1 19 19 ASP HA H 1 4.414 . . 1 . . . . . . . . 5334 1 105 . 1 1 19 19 ASP HB2 H 1 2.508 . . 2 . . . . . . . . 5334 1 106 . 1 1 19 19 ASP HB3 H 1 2.741 . . 2 . . . . . . . . 5334 1 107 . 1 1 19 19 ASP C C 13 178.064 . . 1 . . . . . . . . 5334 1 108 . 1 1 19 19 ASP CA C 13 57.105 . . 1 . . . . . . . . 5334 1 109 . 1 1 19 19 ASP CB C 13 42.034 . . 1 . . . . . . . . 5334 1 110 . 1 1 19 19 ASP N N 15 118.465 . . 1 . . . . . . . . 5334 1 111 . 1 1 20 20 LEU H H 1 7.261 . . 1 . . . . . . . . 5334 1 112 . 1 1 20 20 LEU HA H 1 3.313 . . 1 . . . . . . . . 5334 1 113 . 1 1 20 20 LEU HB2 H 1 1.216 . . 1 . . . . . . . . 5334 1 114 . 1 1 20 20 LEU HB3 H 1 1.216 . . 1 . . . . . . . . 5334 1 115 . 1 1 20 20 LEU C C 13 178.679 . . 1 . . . . . . . . 5334 1 116 . 1 1 20 20 LEU CA C 13 57.953 . . 1 . . . . . . . . 5334 1 117 . 1 1 20 20 LEU CB C 13 39.943 . . 1 . . . . . . . . 5334 1 118 . 1 1 20 20 LEU N N 15 119.466 . . 1 . . . . . . . . 5334 1 119 . 1 1 21 21 GLN H H 1 8.332 . . 1 . . . . . . . . 5334 1 120 . 1 1 21 21 GLN HA H 1 4.019 . . 1 . . . . . . . . 5334 1 121 . 1 1 21 21 GLN HB2 H 1 1.989 . . 1 . . . . . . . . 5334 1 122 . 1 1 21 21 GLN HB3 H 1 1.989 . . 1 . . . . . . . . 5334 1 123 . 1 1 21 21 GLN C C 13 178.654 . . 1 . . . . . . . . 5334 1 124 . 1 1 21 21 GLN CA C 13 58.973 . . 1 . . . . . . . . 5334 1 125 . 1 1 21 21 GLN CB C 13 28.324 . . 1 . . . . . . . . 5334 1 126 . 1 1 21 21 GLN N N 15 117.214 . . 1 . . . . . . . . 5334 1 127 . 1 1 22 22 ALA H H 1 7.409 . . 1 . . . . . . . . 5334 1 128 . 1 1 22 22 ALA HA H 1 4.085 . . 1 . . . . . . . . 5334 1 129 . 1 1 22 22 ALA HB1 H 1 1.510 . . 1 . . . . . . . . 5334 1 130 . 1 1 22 22 ALA HB2 H 1 1.510 . . 1 . . . . . . . . 5334 1 131 . 1 1 22 22 ALA HB3 H 1 1.510 . . 1 . . . . . . . . 5334 1 132 . 1 1 22 22 ALA C C 13 180.507 . . 1 . . . . . . . . 5334 1 133 . 1 1 22 22 ALA CA C 13 55.369 . . 1 . . . . . . . . 5334 1 134 . 1 1 22 22 ALA CB C 13 18.139 . . 1 . . . . . . . . 5334 1 135 . 1 1 22 22 ALA N N 15 121.958 . . 1 . . . . . . . . 5334 1 136 . 1 1 23 23 ILE H H 1 7.735 . . 1 . . . . . . . . 5334 1 137 . 1 1 23 23 ILE HA H 1 3.484 . . 1 . . . . . . . . 5334 1 138 . 1 1 23 23 ILE HB H 1 1.579 . . 1 . . . . . . . . 5334 1 139 . 1 1 23 23 ILE C C 13 177.359 . . 1 . . . . . . . . 5334 1 140 . 1 1 23 23 ILE CA C 13 65.473 . . 1 . . . . . . . . 5334 1 141 . 1 1 23 23 ILE CB C 13 38.545 . . 1 . . . . . . . . 5334 1 142 . 1 1 23 23 ILE N N 15 120.026 . . 1 . . . . . . . . 5334 1 143 . 1 1 24 24 LYS H H 1 8.209 . . 1 . . . . . . . . 5334 1 144 . 1 1 24 24 LYS HA H 1 3.643 . . 1 . . . . . . . . 5334 1 145 . 1 1 24 24 LYS HB2 H 1 1.666 . . 2 . . . . . . . . 5334 1 146 . 1 1 24 24 LYS HB3 H 1 2.012 . . 2 . . . . . . . . 5334 1 147 . 1 1 24 24 LYS C C 13 178.982 . . 1 . . . . . . . . 5334 1 148 . 1 1 24 24 LYS CA C 13 59.950 . . 1 . . . . . . . . 5334 1 149 . 1 1 24 24 LYS CB C 13 32.965 . . 1 . . . . . . . . 5334 1 150 . 1 1 24 24 LYS N N 15 118.622 . . 1 . . . . . . . . 5334 1 151 . 1 1 25 25 GLN H H 1 8.131 . . 1 . . . . . . . . 5334 1 152 . 1 1 25 25 GLN HA H 1 3.954 . . 1 . . . . . . . . 5334 1 153 . 1 1 25 25 GLN HB2 H 1 2.108 . . 1 . . . . . . . . 5334 1 154 . 1 1 25 25 GLN HB3 H 1 2.108 . . 1 . . . . . . . . 5334 1 155 . 1 1 25 25 GLN C C 13 178.910 . . 1 . . . . . . . . 5334 1 156 . 1 1 25 25 GLN CA C 13 58.861 . . 1 . . . . . . . . 5334 1 157 . 1 1 25 25 GLN CB C 13 28.471 . . 1 . . . . . . . . 5334 1 158 . 1 1 25 25 GLN N N 15 117.586 . . 1 . . . . . . . . 5334 1 159 . 1 1 26 26 GLU H H 1 7.835 . . 1 . . . . . . . . 5334 1 160 . 1 1 26 26 GLU HA H 1 4.022 . . 1 . . . . . . . . 5334 1 161 . 1 1 26 26 GLU HB2 H 1 2.067 . . 1 . . . . . . . . 5334 1 162 . 1 1 26 26 GLU HB3 H 1 2.067 . . 1 . . . . . . . . 5334 1 163 . 1 1 26 26 GLU C C 13 179.111 . . 1 . . . . . . . . 5334 1 164 . 1 1 26 26 GLU CA C 13 59.222 . . 1 . . . . . . . . 5334 1 165 . 1 1 26 26 GLU CB C 13 30.130 . . 1 . . . . . . . . 5334 1 166 . 1 1 26 26 GLU N N 15 119.623 . . 1 . . . . . . . . 5334 1 167 . 1 1 27 27 VAL H H 1 7.897 . . 1 . . . . . . . . 5334 1 168 . 1 1 27 27 VAL HA H 1 4.098 . . 1 . . . . . . . . 5334 1 169 . 1 1 27 27 VAL HB H 1 2.414 . . 1 . . . . . . . . 5334 1 170 . 1 1 27 27 VAL C C 13 176.935 . . 1 . . . . . . . . 5334 1 171 . 1 1 27 27 VAL CA C 13 62.905 . . 1 . . . . . . . . 5334 1 172 . 1 1 27 27 VAL CB C 13 31.755 . . 1 . . . . . . . . 5334 1 173 . 1 1 27 27 VAL N N 15 112.113 . . 1 . . . . . . . . 5334 1 174 . 1 1 28 28 SER H H 1 7.586 . . 1 . . . . . . . . 5334 1 175 . 1 1 28 28 SER HA H 1 4.037 . . 1 . . . . . . . . 5334 1 176 . 1 1 28 28 SER HB2 H 1 3.836 . . 1 . . . . . . . . 5334 1 177 . 1 1 28 28 SER HB3 H 1 3.836 . . 1 . . . . . . . . 5334 1 178 . 1 1 28 28 SER C C 13 175.591 . . 1 . . . . . . . . 5334 1 179 . 1 1 28 28 SER CA C 13 60.740 . . 1 . . . . . . . . 5334 1 180 . 1 1 28 28 SER CB C 13 62.682 . . 1 . . . . . . . . 5334 1 181 . 1 1 28 28 SER N N 15 115.068 . . 1 . . . . . . . . 5334 1 182 . 1 1 29 29 GLN H H 1 8.367 . . 1 . . . . . . . . 5334 1 183 . 1 1 29 29 GLN HA H 1 4.332 . . 1 . . . . . . . . 5334 1 184 . 1 1 29 29 GLN HB2 H 1 1.855 . . 2 . . . . . . . . 5334 1 185 . 1 1 29 29 GLN HB3 H 1 2.291 . . 2 . . . . . . . . 5334 1 186 . 1 1 29 29 GLN C C 13 174.870 . . 1 . . . . . . . . 5334 1 187 . 1 1 29 29 GLN CA C 13 55.313 . . 1 . . . . . . . . 5334 1 188 . 1 1 29 29 GLN CB C 13 28.694 . . 1 . . . . . . . . 5334 1 189 . 1 1 29 29 GLN N N 15 118.063 . . 1 . . . . . . . . 5334 1 190 . 1 1 30 30 ALA H H 1 7.856 . . 1 . . . . . . . . 5334 1 191 . 1 1 30 30 ALA HA H 1 4.406 . . 1 . . . . . . . . 5334 1 192 . 1 1 30 30 ALA HB1 H 1 1.328 . . 1 . . . . . . . . 5334 1 193 . 1 1 30 30 ALA HB2 H 1 1.328 . . 1 . . . . . . . . 5334 1 194 . 1 1 30 30 ALA HB3 H 1 1.328 . . 1 . . . . . . . . 5334 1 195 . 1 1 30 30 ALA C C 13 175.953 . . 1 . . . . . . . . 5334 1 196 . 1 1 30 30 ALA CA C 13 51.352 . . 1 . . . . . . . . 5334 1 197 . 1 1 30 30 ALA CB C 13 20.630 . . 1 . . . . . . . . 5334 1 198 . 1 1 30 30 ALA N N 15 124.199 . . 1 . . . . . . . . 5334 1 199 . 1 1 31 31 ALA H H 1 8.617 . . 1 . . . . . . . . 5334 1 200 . 1 1 31 31 ALA CA C 13 50.505 . . 1 . . . . . . . . 5334 1 201 . 1 1 31 31 ALA CB C 13 17.915 . . 1 . . . . . . . . 5334 1 202 . 1 1 31 31 ALA N N 15 124.587 . . 1 . . . . . . . . 5334 1 203 . 1 1 32 32 PRO HB2 H 1 1.519 . . 2 . . . . . . . . 5334 1 204 . 1 1 32 32 PRO C C 13 176.199 . . 1 . . . . . . . . 5334 1 205 . 1 1 32 32 PRO CA C 13 63.027 . . 1 . . . . . . . . 5334 1 206 . 1 1 32 32 PRO CB C 13 31.620 . . 1 . . . . . . . . 5334 1 207 . 1 1 33 33 GLY H H 1 5.460 . . 1 . . . . . . . . 5334 1 208 . 1 1 33 33 GLY HA2 H 1 3.463 . . 2 . . . . . . . . 5334 1 209 . 1 1 33 33 GLY HA3 H 1 4.231 . . 2 . . . . . . . . 5334 1 210 . 1 1 33 33 GLY C C 13 172.772 . . 1 . . . . . . . . 5334 1 211 . 1 1 33 33 GLY CA C 13 45.427 . . 1 . . . . . . . . 5334 1 212 . 1 1 33 33 GLY N N 15 107.707 . . 1 . . . . . . . . 5334 1 213 . 1 1 34 34 SER H H 1 7.978 . . 1 . . . . . . . . 5334 1 214 . 1 1 34 34 SER CA C 13 58.243 . . 1 . . . . . . . . 5334 1 215 . 1 1 34 34 SER CB C 13 62.799 . . 1 . . . . . . . . 5334 1 216 . 1 1 34 34 SER N N 15 117.124 . . 1 . . . . . . . . 5334 1 217 . 1 1 35 35 PRO HA H 1 4.176 . . 1 . . . . . . . . 5334 1 218 . 1 1 35 35 PRO HB2 H 1 1.884 . . 2 . . . . . . . . 5334 1 219 . 1 1 35 35 PRO HB3 H 1 2.323 . . 2 . . . . . . . . 5334 1 220 . 1 1 35 35 PRO C C 13 179.513 . . 1 . . . . . . . . 5334 1 221 . 1 1 35 35 PRO CA C 13 66.905 . . 1 . . . . . . . . 5334 1 222 . 1 1 35 35 PRO CB C 13 31.986 . . 1 . . . . . . . . 5334 1 223 . 1 1 36 36 GLN H H 1 8.920 . . 1 . . . . . . . . 5334 1 224 . 1 1 36 36 GLN HA H 1 3.974 . . 1 . . . . . . . . 5334 1 225 . 1 1 36 36 GLN HB2 H 1 1.830 . . 2 . . . . . . . . 5334 1 226 . 1 1 36 36 GLN HB3 H 1 2.059 . . 2 . . . . . . . . 5334 1 227 . 1 1 36 36 GLN C C 13 178.289 . . 1 . . . . . . . . 5334 1 228 . 1 1 36 36 GLN CA C 13 59.314 . . 1 . . . . . . . . 5334 1 229 . 1 1 36 36 GLN CB C 13 28.317 . . 1 . . . . . . . . 5334 1 230 . 1 1 36 36 GLN N N 15 116.642 . . 1 . . . . . . . . 5334 1 231 . 1 1 37 37 PHE H H 1 7.155 . . 1 . . . . . . . . 5334 1 232 . 1 1 37 37 PHE HA H 1 3.791 . . 1 . . . . . . . . 5334 1 233 . 1 1 37 37 PHE HB2 H 1 2.579 . . 2 . . . . . . . . 5334 1 234 . 1 1 37 37 PHE HB3 H 1 3.194 . . 2 . . . . . . . . 5334 1 235 . 1 1 37 37 PHE C C 13 176.695 . . 1 . . . . . . . . 5334 1 236 . 1 1 37 37 PHE CA C 13 61.063 . . 1 . . . . . . . . 5334 1 237 . 1 1 37 37 PHE CB C 13 40.643 . . 1 . . . . . . . . 5334 1 238 . 1 1 37 37 PHE N N 15 120.421 . . 1 . . . . . . . . 5334 1 239 . 1 1 38 38 MET H H 1 8.762 . . 1 . . . . . . . . 5334 1 240 . 1 1 38 38 MET HA H 1 4.253 . . 1 . . . . . . . . 5334 1 241 . 1 1 38 38 MET HB2 H 1 1.895 . . 2 . . . . . . . . 5334 1 242 . 1 1 38 38 MET HB3 H 1 2.079 . . 2 . . . . . . . . 5334 1 243 . 1 1 38 38 MET C C 13 178.846 . . 1 . . . . . . . . 5334 1 244 . 1 1 38 38 MET CA C 13 55.397 . . 1 . . . . . . . . 5334 1 245 . 1 1 38 38 MET CB C 13 28.955 . . 1 . . . . . . . . 5334 1 246 . 1 1 38 38 MET N N 15 113.948 . . 1 . . . . . . . . 5334 1 247 . 1 1 39 39 GLN H H 1 8.280 . . 1 . . . . . . . . 5334 1 248 . 1 1 39 39 GLN HA H 1 3.974 . . 1 . . . . . . . . 5334 1 249 . 1 1 39 39 GLN HB2 H 1 2.071 . . 1 . . . . . . . . 5334 1 250 . 1 1 39 39 GLN HB3 H 1 2.071 . . 1 . . . . . . . . 5334 1 251 . 1 1 39 39 GLN C C 13 178.420 . . 1 . . . . . . . . 5334 1 252 . 1 1 39 39 GLN CA C 13 59.415 . . 1 . . . . . . . . 5334 1 253 . 1 1 39 39 GLN CB C 13 28.469 . . 1 . . . . . . . . 5334 1 254 . 1 1 39 39 GLN N N 15 119.316 . . 1 . . . . . . . . 5334 1 255 . 1 1 40 40 THR H H 1 7.293 . . 1 . . . . . . . . 5334 1 256 . 1 1 40 40 THR HA H 1 3.768 . . 4 . . . . . . . . 5334 1 257 . 1 1 40 40 THR HB H 1 3.768 . . 4 . . . . . . . . 5334 1 258 . 1 1 40 40 THR CA C 13 67.113 . . 1 . . . . . . . . 5334 1 259 . 1 1 40 40 THR CB C 13 68.745 . . 1 . . . . . . . . 5334 1 260 . 1 1 40 40 THR N N 15 115.054 . . 1 . . . . . . . . 5334 1 261 . 1 1 41 41 ILE H H 1 8.008 . . 1 . . . . . . . . 5334 1 262 . 1 1 41 41 ILE HA H 1 3.766 . . 1 . . . . . . . . 5334 1 263 . 1 1 41 41 ILE HB H 1 1.580 . . 1 . . . . . . . . 5334 1 264 . 1 1 41 41 ILE C C 13 177.668 . . 1 . . . . . . . . 5334 1 265 . 1 1 41 41 ILE CA C 13 64.067 . . 1 . . . . . . . . 5334 1 266 . 1 1 41 41 ILE CB C 13 36.831 . . 1 . . . . . . . . 5334 1 267 . 1 1 41 41 ILE N N 15 118.994 . . 1 . . . . . . . . 5334 1 268 . 1 1 42 42 ARG H H 1 8.904 . . 1 . . . . . . . . 5334 1 269 . 1 1 42 42 ARG HB2 H 1 1.805 . . 1 . . . . . . . . 5334 1 270 . 1 1 42 42 ARG HB3 H 1 1.805 . . 1 . . . . . . . . 5334 1 271 . 1 1 42 42 ARG C C 13 179.580 . . 1 . . . . . . . . 5334 1 272 . 1 1 42 42 ARG CA C 13 61.025 . . 1 . . . . . . . . 5334 1 273 . 1 1 42 42 ARG CB C 13 30.100 . . 1 . . . . . . . . 5334 1 274 . 1 1 42 42 ARG N N 15 121.799 . . 1 . . . . . . . . 5334 1 275 . 1 1 43 43 LEU H H 1 7.401 . . 1 . . . . . . . . 5334 1 276 . 1 1 43 43 LEU HA H 1 4.082 . . 1 . . . . . . . . 5334 1 277 . 1 1 43 43 LEU HB2 H 1 1.692 . . 1 . . . . . . . . 5334 1 278 . 1 1 43 43 LEU HB3 H 1 1.692 . . 1 . . . . . . . . 5334 1 279 . 1 1 43 43 LEU C C 13 178.949 . . 1 . . . . . . . . 5334 1 280 . 1 1 43 43 LEU CA C 13 58.092 . . 1 . . . . . . . . 5334 1 281 . 1 1 43 43 LEU CB C 13 41.306 . . 1 . . . . . . . . 5334 1 282 . 1 1 43 43 LEU N N 15 119.594 . . 1 . . . . . . . . 5334 1 283 . 1 1 44 44 ALA H H 1 7.767 . . 1 . . . . . . . . 5334 1 284 . 1 1 44 44 ALA HA H 1 4.403 . . 1 . . . . . . . . 5334 1 285 . 1 1 44 44 ALA HB1 H 1 1.526 . . 1 . . . . . . . . 5334 1 286 . 1 1 44 44 ALA HB2 H 1 1.526 . . 1 . . . . . . . . 5334 1 287 . 1 1 44 44 ALA HB3 H 1 1.526 . . 1 . . . . . . . . 5334 1 288 . 1 1 44 44 ALA C C 13 180.130 . . 1 . . . . . . . . 5334 1 289 . 1 1 44 44 ALA CA C 13 55.424 . . 1 . . . . . . . . 5334 1 290 . 1 1 44 44 ALA CB C 13 17.727 . . 1 . . . . . . . . 5334 1 291 . 1 1 44 44 ALA N N 15 121.685 . . 1 . . . . . . . . 5334 1 292 . 1 1 45 45 VAL H H 1 8.464 . . 1 . . . . . . . . 5334 1 293 . 1 1 45 45 VAL HA H 1 3.372 . . 1 . . . . . . . . 5334 1 294 . 1 1 45 45 VAL HB H 1 2.272 . . 1 . . . . . . . . 5334 1 295 . 1 1 45 45 VAL C C 13 178.681 . . 1 . . . . . . . . 5334 1 296 . 1 1 45 45 VAL CA C 13 66.981 . . 1 . . . . . . . . 5334 1 297 . 1 1 45 45 VAL CB C 13 31.614 . . 1 . . . . . . . . 5334 1 298 . 1 1 45 45 VAL N N 15 117.886 . . 1 . . . . . . . . 5334 1 299 . 1 1 46 46 GLN H H 1 8.013 . . 1 . . . . . . . . 5334 1 300 . 1 1 46 46 GLN HA H 1 3.913 . . 1 . . . . . . . . 5334 1 301 . 1 1 46 46 GLN HB2 H 1 2.137 . . 1 . . . . . . . . 5334 1 302 . 1 1 46 46 GLN HB3 H 1 2.137 . . 1 . . . . . . . . 5334 1 303 . 1 1 46 46 GLN C C 13 177.873 . . 1 . . . . . . . . 5334 1 304 . 1 1 46 46 GLN CA C 13 59.059 . . 1 . . . . . . . . 5334 1 305 . 1 1 46 46 GLN CB C 13 29.000 . . 1 . . . . . . . . 5334 1 306 . 1 1 46 46 GLN N N 15 120.242 . . 1 . . . . . . . . 5334 1 307 . 1 1 47 47 GLN H H 1 8.385 . . 1 . . . . . . . . 5334 1 308 . 1 1 47 47 GLN HA H 1 3.776 . . 1 . . . . . . . . 5334 1 309 . 1 1 47 47 GLN HB2 H 1 1.443 . . 2 . . . . . . . . 5334 1 310 . 1 1 47 47 GLN HB3 H 1 1.902 . . 2 . . . . . . . . 5334 1 311 . 1 1 47 47 GLN C C 13 177.943 . . 1 . . . . . . . . 5334 1 312 . 1 1 47 47 GLN CA C 13 58.719 . . 1 . . . . . . . . 5334 1 313 . 1 1 47 47 GLN CB C 13 29.154 . . 1 . . . . . . . . 5334 1 314 . 1 1 47 47 GLN N N 15 116.576 . . 1 . . . . . . . . 5334 1 315 . 1 1 48 48 PHE H H 1 8.135 . . 1 . . . . . . . . 5334 1 316 . 1 1 48 48 PHE HA H 1 4.350 . . 1 . . . . . . . . 5334 1 317 . 1 1 48 48 PHE HB2 H 1 2.643 . . 2 . . . . . . . . 5334 1 318 . 1 1 48 48 PHE HB3 H 1 2.822 . . 2 . . . . . . . . 5334 1 319 . 1 1 48 48 PHE C C 13 174.801 . . 1 . . . . . . . . 5334 1 320 . 1 1 48 48 PHE CA C 13 59.381 . . 1 . . . . . . . . 5334 1 321 . 1 1 48 48 PHE CB C 13 40.327 . . 1 . . . . . . . . 5334 1 322 . 1 1 48 48 PHE N N 15 112.747 . . 1 . . . . . . . . 5334 1 323 . 1 1 49 49 ASP H H 1 7.813 . . 1 . . . . . . . . 5334 1 324 . 1 1 49 49 ASP CA C 13 54.264 . . 1 . . . . . . . . 5334 1 325 . 1 1 49 49 ASP CB C 13 40.380 . . 1 . . . . . . . . 5334 1 326 . 1 1 49 49 ASP N N 15 117.704 . . 1 . . . . . . . . 5334 1 327 . 1 1 50 50 PRO HA H 1 4.195 . . 1 . . . . . . . . 5334 1 328 . 1 1 50 50 PRO HB2 H 1 1.273 . . 2 . . . . . . . . 5334 1 329 . 1 1 50 50 PRO HB3 H 1 1.813 . . 2 . . . . . . . . 5334 1 330 . 1 1 50 50 PRO C C 13 177.984 . . 1 . . . . . . . . 5334 1 331 . 1 1 50 50 PRO CA C 13 61.794 . . 1 . . . . . . . . 5334 1 332 . 1 1 50 50 PRO CB C 13 33.562 . . 1 . . . . . . . . 5334 1 333 . 1 1 51 51 THR H H 1 7.466 . . 1 . . . . . . . . 5334 1 334 . 1 1 51 51 THR HA H 1 5.160 . . 1 . . . . . . . . 5334 1 335 . 1 1 51 51 THR HB H 1 3.793 . . 1 . . . . . . . . 5334 1 336 . 1 1 51 51 THR C C 13 174.057 . . 1 . . . . . . . . 5334 1 337 . 1 1 51 51 THR CA C 13 60.870 . . 1 . . . . . . . . 5334 1 338 . 1 1 51 51 THR CB C 13 70.366 . . 1 . . . . . . . . 5334 1 339 . 1 1 51 51 THR N N 15 108.023 . . 1 . . . . . . . . 5334 1 340 . 1 1 52 52 ALA H H 1 6.285 . . 1 . . . . . . . . 5334 1 341 . 1 1 52 52 ALA HA H 1 3.757 . . 1 . . . . . . . . 5334 1 342 . 1 1 52 52 ALA HB1 H 1 0.583 . . 1 . . . . . . . . 5334 1 343 . 1 1 52 52 ALA HB2 H 1 0.583 . . 1 . . . . . . . . 5334 1 344 . 1 1 52 52 ALA HB3 H 1 0.583 . . 1 . . . . . . . . 5334 1 345 . 1 1 52 52 ALA C C 13 180.995 . . 1 . . . . . . . . 5334 1 346 . 1 1 52 52 ALA CA C 13 56.159 . . 1 . . . . . . . . 5334 1 347 . 1 1 52 52 ALA CB C 13 18.441 . . 1 . . . . . . . . 5334 1 348 . 1 1 52 52 ALA N N 15 120.282 . . 1 . . . . . . . . 5334 1 349 . 1 1 53 53 LYS H H 1 8.952 . . 1 . . . . . . . . 5334 1 350 . 1 1 53 53 LYS HA H 1 3.902 . . 1 . . . . . . . . 5334 1 351 . 1 1 53 53 LYS HB2 H 1 1.512 . . 2 . . . . . . . . 5334 1 352 . 1 1 53 53 LYS HB3 H 1 1.726 . . 2 . . . . . . . . 5334 1 353 . 1 1 53 53 LYS C C 13 178.372 . . 1 . . . . . . . . 5334 1 354 . 1 1 53 53 LYS CA C 13 59.526 . . 1 . . . . . . . . 5334 1 355 . 1 1 53 53 LYS CB C 13 32.280 . . 1 . . . . . . . . 5334 1 356 . 1 1 53 53 LYS N N 15 122.038 . . 1 . . . . . . . . 5334 1 357 . 1 1 54 54 ALA H H 1 7.366 . . 1 . . . . . . . . 5334 1 358 . 1 1 54 54 ALA C C 13 180.922 . . 1 . . . . . . . . 5334 1 359 . 1 1 54 54 ALA CA C 13 55.172 . . 1 . . . . . . . . 5334 1 360 . 1 1 54 54 ALA CB C 13 18.454 . . 1 . . . . . . . . 5334 1 361 . 1 1 54 54 ALA N N 15 122.120 . . 1 . . . . . . . . 5334 1 362 . 1 1 55 55 LEU H H 1 8.252 . . 1 . . . . . . . . 5334 1 363 . 1 1 55 55 LEU N N 15 119.202 . . 1 . . . . . . . . 5334 1 364 . 1 1 57 57 ASP HA H 1 4.333 . . 1 . . . . . . . . 5334 1 365 . 1 1 57 57 ASP HB2 H 1 2.563 . . 2 . . . . . . . . 5334 1 366 . 1 1 57 57 ASP HB3 H 1 3.153 . . 2 . . . . . . . . 5334 1 367 . 1 1 57 57 ASP C C 13 179.548 . . 1 . . . . . . . . 5334 1 368 . 1 1 57 57 ASP CA C 13 57.539 . . 1 . . . . . . . . 5334 1 369 . 1 1 57 57 ASP CB C 13 39.966 . . 1 . . . . . . . . 5334 1 370 . 1 1 58 58 LEU H H 1 8.194 . . 1 . . . . . . . . 5334 1 371 . 1 1 58 58 LEU HA H 1 3.730 . . 1 . . . . . . . . 5334 1 372 . 1 1 58 58 LEU HB2 H 1 1.327 . . 2 . . . . . . . . 5334 1 373 . 1 1 58 58 LEU HB3 H 1 2.042 . . 2 . . . . . . . . 5334 1 374 . 1 1 58 58 LEU C C 13 177.852 . . 1 . . . . . . . . 5334 1 375 . 1 1 58 58 LEU CA C 13 58.262 . . 1 . . . . . . . . 5334 1 376 . 1 1 58 58 LEU CB C 13 41.45 . . 1 . . . . . . . . 5334 1 377 . 1 1 58 58 LEU N N 15 120.767 . . 1 . . . . . . . . 5334 1 378 . 1 1 59 59 LEU H H 1 8.608 . . 1 . . . . . . . . 5334 1 379 . 1 1 59 59 LEU HA H 1 3.970 . . 1 . . . . . . . . 5334 1 380 . 1 1 59 59 LEU HB2 H 1 1.862 . . 2 . . . . . . . . 5334 1 381 . 1 1 59 59 LEU HB3 H 1 2.265 . . 2 . . . . . . . . 5334 1 382 . 1 1 59 59 LEU C C 13 178.215 . . 1 . . . . . . . . 5334 1 383 . 1 1 59 59 LEU CA C 13 59.167 . . 1 . . . . . . . . 5334 1 384 . 1 1 59 59 LEU CB C 13 43.288 . . 1 . . . . . . . . 5334 1 385 . 1 1 59 59 LEU N N 15 119.777 . . 1 . . . . . . . . 5334 1 386 . 1 1 60 60 GLN H H 1 8.131 . . 1 . . . . . . . . 5334 1 387 . 1 1 60 60 GLN HA H 1 4.073 . . 1 . . . . . . . . 5334 1 388 . 1 1 60 60 GLN HB2 H 1 2.099 . . 1 . . . . . . . . 5334 1 389 . 1 1 60 60 GLN HB3 H 1 2.099 . . 1 . . . . . . . . 5334 1 390 . 1 1 60 60 GLN C C 13 176.944 . . 1 . . . . . . . . 5334 1 391 . 1 1 60 60 GLN CA C 13 57.835 . . 1 . . . . . . . . 5334 1 392 . 1 1 60 60 GLN CB C 13 28.913 . . 1 . . . . . . . . 5334 1 393 . 1 1 60 60 GLN N N 15 113.194 . . 1 . . . . . . . . 5334 1 394 . 1 1 61 61 TYR H H 1 7.753 . . 1 . . . . . . . . 5334 1 395 . 1 1 61 61 TYR HA H 1 4.192 . . 1 . . . . . . . . 5334 1 396 . 1 1 61 61 TYR HB2 H 1 2.784 . . 2 . . . . . . . . 5334 1 397 . 1 1 61 61 TYR HB3 H 1 3.083 . . 2 . . . . . . . . 5334 1 398 . 1 1 61 61 TYR C C 13 177.112 . . 1 . . . . . . . . 5334 1 399 . 1 1 61 61 TYR CA C 13 60.463 . . 1 . . . . . . . . 5334 1 400 . 1 1 61 61 TYR CB C 13 39.912 . . 1 . . . . . . . . 5334 1 401 . 1 1 61 61 TYR N N 15 118.467 . . 1 . . . . . . . . 5334 1 402 . 1 1 62 62 LEU H H 1 8.018 . . 1 . . . . . . . . 5334 1 403 . 1 1 62 62 LEU HA H 1 4.036 . . 1 . . . . . . . . 5334 1 404 . 1 1 62 62 LEU HB2 H 1 1.640 . . 2 . . . . . . . . 5334 1 405 . 1 1 62 62 LEU HB3 H 1 1.983 . . 2 . . . . . . . . 5334 1 406 . 1 1 62 62 LEU C C 13 178.408 . . 1 . . . . . . . . 5334 1 407 . 1 1 62 62 LEU CA C 13 56.558 . . 1 . . . . . . . . 5334 1 408 . 1 1 62 62 LEU CB C 13 46.096 . . 1 . . . . . . . . 5334 1 409 . 1 1 62 62 LEU N N 15 113.915 . . 1 . . . . . . . . 5334 1 410 . 1 1 63 63 CYS H H 1 8.054 . . 1 . . . . . . . . 5334 1 411 . 1 1 63 63 CYS HA H 1 4.729 . . 1 . . . . . . . . 5334 1 412 . 1 1 63 63 CYS HB2 H 1 2.749 . . 2 . . . . . . . . 5334 1 413 . 1 1 63 63 CYS HB3 H 1 2.988 . . 2 . . . . . . . . 5334 1 414 . 1 1 63 63 CYS C C 13 173.697 . . 1 . . . . . . . . 5334 1 415 . 1 1 63 63 CYS CA C 13 58.300 . . 1 . . . . . . . . 5334 1 416 . 1 1 63 63 CYS CB C 13 31.953 . . 1 . . . . . . . . 5334 1 417 . 1 1 63 63 CYS N N 15 114.666 . . 1 . . . . . . . . 5334 1 418 . 1 1 64 64 SER H H 1 8.848 . . 1 . . . . . . . . 5334 1 419 . 1 1 64 64 SER HA H 1 3.970 . . 1 . . . . . . . . 5334 1 420 . 1 1 64 64 SER HB2 H 1 4.329 . . 1 . . . . . . . . 5334 1 421 . 1 1 64 64 SER HB3 H 1 4.329 . . 1 . . . . . . . . 5334 1 422 . 1 1 64 64 SER C C 13 174.454 . . 1 . . . . . . . . 5334 1 423 . 1 1 64 64 SER CA C 13 57.251 . . 1 . . . . . . . . 5334 1 424 . 1 1 64 64 SER CB C 13 64.957 . . 1 . . . . . . . . 5334 1 425 . 1 1 64 64 SER N N 15 117.713 . . 1 . . . . . . . . 5334 1 426 . 1 1 65 65 SER H H 1 8.954 . . 1 . . . . . . . . 5334 1 427 . 1 1 65 65 SER HA H 1 4.082 . . 1 . . . . . . . . 5334 1 428 . 1 1 65 65 SER HB2 H 1 3.866 . . 1 . . . . . . . . 5334 1 429 . 1 1 65 65 SER HB3 H 1 3.866 . . 1 . . . . . . . . 5334 1 430 . 1 1 65 65 SER C C 13 177.392 . . 1 . . . . . . . . 5334 1 431 . 1 1 65 65 SER CB C 13 62.452 . . 1 . . . . . . . . 5334 1 432 . 1 1 65 65 SER N N 15 116.271 . . 1 . . . . . . . . 5334 1 433 . 1 1 66 66 LEU H H 1 8.029 . . 1 . . . . . . . . 5334 1 434 . 1 1 66 66 LEU HA H 1 4.099 . . 1 . . . . . . . . 5334 1 435 . 1 1 66 66 LEU HB2 H 1 1.575 . . 1 . . . . . . . . 5334 1 436 . 1 1 66 66 LEU HB3 H 1 1.575 . . 1 . . . . . . . . 5334 1 437 . 1 1 66 66 LEU C C 13 179.066 . . 1 . . . . . . . . 5334 1 438 . 1 1 66 66 LEU CA C 13 58.348 . . 1 . . . . . . . . 5334 1 439 . 1 1 66 66 LEU CB C 13 42.205 . . 1 . . . . . . . . 5334 1 440 . 1 1 66 66 LEU N N 15 122.685 . . 1 . . . . . . . . 5334 1 441 . 1 1 67 67 VAL H H 1 7.476 . . 1 . . . . . . . . 5334 1 442 . 1 1 67 67 VAL HA H 1 3.376 . . 1 . . . . . . . . 5334 1 443 . 1 1 67 67 VAL HB H 1 2.030 . . 1 . . . . . . . . 5334 1 444 . 1 1 67 67 VAL C C 13 177.664 . . 1 . . . . . . . . 5334 1 445 . 1 1 67 67 VAL CA C 13 67.108 . . 1 . . . . . . . . 5334 1 446 . 1 1 67 67 VAL CB C 13 31.794 . . 1 . . . . . . . . 5334 1 447 . 1 1 67 67 VAL N N 15 120.315 . . 1 . . . . . . . . 5334 1 448 . 1 1 68 68 ALA H H 1 8.760 . . 1 . . . . . . . . 5334 1 449 . 1 1 68 68 ALA HA H 1 3.852 . . 1 . . . . . . . . 5334 1 450 . 1 1 68 68 ALA HB1 H 1 1.322 . . 1 . . . . . . . . 5334 1 451 . 1 1 68 68 ALA HB2 H 1 1.322 . . 1 . . . . . . . . 5334 1 452 . 1 1 68 68 ALA HB3 H 1 1.322 . . 1 . . . . . . . . 5334 1 453 . 1 1 68 68 ALA C C 13 179.905 . . 1 . . . . . . . . 5334 1 454 . 1 1 68 68 ALA CA C 13 55.730 . . 1 . . . . . . . . 5334 1 455 . 1 1 68 68 ALA CB C 13 17.712 . . 1 . . . . . . . . 5334 1 456 . 1 1 68 68 ALA N N 15 120.716 . . 1 . . . . . . . . 5334 1 457 . 1 1 69 69 SER H H 1 7.977 . . 1 . . . . . . . . 5334 1 458 . 1 1 69 69 SER HA H 1 4.215 . . 1 . . . . . . . . 5334 1 459 . 1 1 69 69 SER HB2 H 1 3.983 . . 1 . . . . . . . . 5334 1 460 . 1 1 69 69 SER HB3 H 1 3.983 . . 1 . . . . . . . . 5334 1 461 . 1 1 69 69 SER C C 13 177.230 . . 1 . . . . . . . . 5334 1 462 . 1 1 69 69 SER CA C 13 61.851 . . 1 . . . . . . . . 5334 1 463 . 1 1 69 69 SER CB C 13 62.865 . . 1 . . . . . . . . 5334 1 464 . 1 1 69 69 SER N N 15 113.968 . . 1 . . . . . . . . 5334 1 465 . 1 1 70 70 LEU H H 1 7.940 . . 1 . . . . . . . . 5334 1 466 . 1 1 70 70 LEU HA H 1 4.011 . . 1 . . . . . . . . 5334 1 467 . 1 1 70 70 LEU HB2 H 1 1.308 . . 2 . . . . . . . . 5334 1 468 . 1 1 70 70 LEU HB3 H 1 1.818 . . 2 . . . . . . . . 5334 1 469 . 1 1 70 70 LEU C C 13 179.836 . . 1 . . . . . . . . 5334 1 470 . 1 1 70 70 LEU CA C 13 57.954 . . 1 . . . . . . . . 5334 1 471 . 1 1 70 70 LEU CB C 13 42.178 . . 1 . . . . . . . . 5334 1 472 . 1 1 70 70 LEU N N 15 123.623 . . 1 . . . . . . . . 5334 1 473 . 1 1 71 71 HIS H H 1 8.782 . . 1 . . . . . . . . 5334 1 474 . 1 1 71 71 HIS HA H 1 3.326 . . 1 . . . . . . . . 5334 1 475 . 1 1 71 71 HIS HB2 H 1 2.306 . . 2 . . . . . . . . 5334 1 476 . 1 1 71 71 HIS HB3 H 1 2.940 . . 2 . . . . . . . . 5334 1 477 . 1 1 71 71 HIS C C 13 176.562 . . 1 . . . . . . . . 5334 1 478 . 1 1 71 71 HIS CA C 13 62.212 . . 1 . . . . . . . . 5334 1 479 . 1 1 71 71 HIS CB C 13 31.298 . . 1 . . . . . . . . 5334 1 480 . 1 1 71 71 HIS N N 15 120.990 . . 1 . . . . . . . . 5334 1 481 . 1 1 72 72 HIS H H 1 8.281 . . 1 . . . . . . . . 5334 1 482 . 1 1 72 72 HIS HA H 1 4.085 . . 1 . . . . . . . . 5334 1 483 . 1 1 72 72 HIS HB2 H 1 3.341 . . 2 . . . . . . . . 5334 1 484 . 1 1 72 72 HIS HB3 H 1 3.434 . . 2 . . . . . . . . 5334 1 485 . 1 1 72 72 HIS C C 13 176.970 . . 1 . . . . . . . . 5334 1 486 . 1 1 72 72 HIS CA C 13 59.340 . . 1 . . . . . . . . 5334 1 487 . 1 1 72 72 HIS CB C 13 29.011 . . 1 . . . . . . . . 5334 1 488 . 1 1 72 72 HIS N N 15 116.404 . . 1 . . . . . . . . 5334 1 489 . 1 1 73 73 GLN H H 1 7.694 . . 1 . . . . . . . . 5334 1 490 . 1 1 73 73 GLN HA H 1 3.955 . . 1 . . . . . . . . 5334 1 491 . 1 1 73 73 GLN HB2 H 1 2.081 . . 2 . . . . . . . . 5334 1 492 . 1 1 73 73 GLN C C 13 178.906 . . 1 . . . . . . . . 5334 1 493 . 1 1 73 73 GLN CA C 13 58.926 . . 1 . . . . . . . . 5334 1 494 . 1 1 73 73 GLN CB C 13 29.012 . . 1 . . . . . . . . 5334 1 495 . 1 1 73 73 GLN N N 15 116.707 . . 1 . . . . . . . . 5334 1 496 . 1 1 74 74 GLN H H 1 7.742 . . 1 . . . . . . . . 5334 1 497 . 1 1 74 74 GLN HA H 1 4.014 . . 1 . . . . . . . . 5334 1 498 . 1 1 74 74 GLN HB2 H 1 1.705 . . 2 . . . . . . . . 5334 1 499 . 1 1 74 74 GLN C C 13 178.213 . . 1 . . . . . . . . 5334 1 500 . 1 1 74 74 GLN CA C 13 57.69 . . 1 . . . . . . . . 5334 1 501 . 1 1 74 74 GLN CB C 13 27.585 . . 1 . . . . . . . . 5334 1 502 . 1 1 74 74 GLN N N 15 118.888 . . 1 . . . . . . . . 5334 1 503 . 1 1 75 75 LEU H H 1 8.970 . . 1 . . . . . . . . 5334 1 504 . 1 1 75 75 LEU C C 13 177.836 . . 1 . . . . . . . . 5334 1 505 . 1 1 75 75 LEU CA C 13 57.918 . . 1 . . . . . . . . 5334 1 506 . 1 1 75 75 LEU CB C 13 40.678 . . 1 . . . . . . . . 5334 1 507 . 1 1 75 75 LEU N N 15 121.828 . . 1 . . . . . . . . 5334 1 508 . 1 1 76 76 ASP H H 1 8.229 . . 1 . . . . . . . . 5334 1 509 . 1 1 76 76 ASP HA H 1 4.275 . . 1 . . . . . . . . 5334 1 510 . 1 1 76 76 ASP HB2 H 1 2.533 . . 1 . . . . . . . . 5334 1 511 . 1 1 76 76 ASP HB3 H 1 2.533 . . 1 . . . . . . . . 5334 1 512 . 1 1 76 76 ASP C C 13 179.837 . . 1 . . . . . . . . 5334 1 513 . 1 1 76 76 ASP CA C 13 57.940 . . 1 . . . . . . . . 5334 1 514 . 1 1 76 76 ASP CB C 13 39.644 . . 1 . . . . . . . . 5334 1 515 . 1 1 76 76 ASP N N 15 118.717 . . 1 . . . . . . . . 5334 1 516 . 1 1 77 77 SER H H 1 7.299 . . 1 . . . . . . . . 5334 1 517 . 1 1 77 77 SER HA H 1 4.192 . . 1 . . . . . . . . 5334 1 518 . 1 1 77 77 SER HB2 H 1 3.881 . . 1 . . . . . . . . 5334 1 519 . 1 1 77 77 SER HB3 H 1 3.881 . . 1 . . . . . . . . 5334 1 520 . 1 1 77 77 SER C C 13 176.880 . . 1 . . . . . . . . 5334 1 521 . 1 1 77 77 SER CA C 13 61.838 . . 1 . . . . . . . . 5334 1 522 . 1 1 77 77 SER CB C 13 62.772 . . 1 . . . . . . . . 5334 1 523 . 1 1 77 77 SER N N 15 115.448 . . 1 . . . . . . . . 5334 1 524 . 1 1 78 78 LEU H H 1 8.215 . . 1 . . . . . . . . 5334 1 525 . 1 1 78 78 LEU HA H 1 3.967 . . 1 . . . . . . . . 5334 1 526 . 1 1 78 78 LEU HB2 H 1 1.319 . . 2 . . . . . . . . 5334 1 527 . 1 1 78 78 LEU HB3 H 1 1.860 . . 2 . . . . . . . . 5334 1 528 . 1 1 78 78 LEU C C 13 180.820 . . 1 . . . . . . . . 5334 1 529 . 1 1 78 78 LEU CA C 13 57.962 . . 1 . . . . . . . . 5334 1 530 . 1 1 78 78 LEU CB C 13 42.427 . . 1 . . . . . . . . 5334 1 531 . 1 1 78 78 LEU N N 15 122.517 . . 1 . . . . . . . . 5334 1 532 . 1 1 79 79 ILE H H 1 8.980 . . 1 . . . . . . . . 5334 1 533 . 1 1 79 79 ILE HA H 1 3.451 . . 1 . . . . . . . . 5334 1 534 . 1 1 79 79 ILE HB H 1 1.836 . . 1 . . . . . . . . 5334 1 535 . 1 1 79 79 ILE C C 13 177.316 . . 1 . . . . . . . . 5334 1 536 . 1 1 79 79 ILE CA C 13 66.310 . . 1 . . . . . . . . 5334 1 537 . 1 1 79 79 ILE CB C 13 38.156 . . 1 . . . . . . . . 5334 1 538 . 1 1 79 79 ILE N N 15 121.026 . . 1 . . . . . . . . 5334 1 539 . 1 1 80 80 SER H H 1 7.853 . . 1 . . . . . . . . 5334 1 540 . 1 1 80 80 SER CA C 13 61.797 . . 1 . . . . . . . . 5334 1 541 . 1 1 80 80 SER N N 15 114.555 . . 1 . . . . . . . . 5334 1 542 . 1 1 81 81 GLU H H 1 7.852 . . 1 . . . . . . . . 5334 1 543 . 1 1 81 81 GLU HA H 1 3.964 . . 1 . . . . . . . . 5334 1 544 . 1 1 81 81 GLU HB2 H 1 1.990 . . 1 . . . . . . . . 5334 1 545 . 1 1 81 81 GLU HB3 H 1 1.990 . . 1 . . . . . . . . 5334 1 546 . 1 1 81 81 GLU C C 13 178.681 . . 1 . . . . . . . . 5334 1 547 . 1 1 81 81 GLU CA C 13 59.597 . . 1 . . . . . . . . 5334 1 548 . 1 1 81 81 GLU CB C 13 29.738 . . 1 . . . . . . . . 5334 1 549 . 1 1 81 81 GLU N N 15 120.611 . . 1 . . . . . . . . 5334 1 550 . 1 1 82 82 ALA H H 1 8.146 . . 1 . . . . . . . . 5334 1 551 . 1 1 82 82 ALA HA H 1 3.948 . . 1 . . . . . . . . 5334 1 552 . 1 1 82 82 ALA HB1 H 1 1.362 . . 1 . . . . . . . . 5334 1 553 . 1 1 82 82 ALA HB2 H 1 1.362 . . 1 . . . . . . . . 5334 1 554 . 1 1 82 82 ALA HB3 H 1 1.362 . . 1 . . . . . . . . 5334 1 555 . 1 1 82 82 ALA C C 13 180.040 . . 1 . . . . . . . . 5334 1 556 . 1 1 82 82 ALA CA C 13 55.348 . . 1 . . . . . . . . 5334 1 557 . 1 1 82 82 ALA CB C 13 18.212 . . 1 . . . . . . . . 5334 1 558 . 1 1 82 82 ALA N N 15 123.179 . . 1 . . . . . . . . 5334 1 559 . 1 1 83 83 GLU H H 1 8.755 . . 1 . . . . . . . . 5334 1 560 . 1 1 83 83 GLU HA H 1 3.786 . . 1 . . . . . . . . 5334 1 561 . 1 1 83 83 GLU HB2 H 1 2.019 . . 2 . . . . . . . . 5334 1 562 . 1 1 83 83 GLU HB3 H 1 2.239 . . 2 . . . . . . . . 5334 1 563 . 1 1 83 83 GLU C C 13 179.664 . . 1 . . . . . . . . 5334 1 564 . 1 1 83 83 GLU CA C 13 59.608 . . 1 . . . . . . . . 5334 1 565 . 1 1 83 83 GLU CB C 13 30.030 . . 1 . . . . . . . . 5334 1 566 . 1 1 83 83 GLU N N 15 116.698 . . 1 . . . . . . . . 5334 1 567 . 1 1 84 84 THR H H 1 7.776 . . 1 . . . . . . . . 5334 1 568 . 1 1 84 84 THR HA H 1 3.959 . . 1 . . . . . . . . 5334 1 569 . 1 1 84 84 THR HB H 1 4.214 . . 1 . . . . . . . . 5334 1 570 . 1 1 84 84 THR C C 13 175.857 . . 1 . . . . . . . . 5334 1 571 . 1 1 84 84 THR CA C 13 65.862 . . 1 . . . . . . . . 5334 1 572 . 1 1 84 84 THR CB C 13 69.057 . . 1 . . . . . . . . 5334 1 573 . 1 1 84 84 THR N N 15 114.322 . . 1 . . . . . . . . 5334 1 574 . 1 1 85 85 ARG H H 1 7.694 . . 1 . . . . . . . . 5334 1 575 . 1 1 85 85 ARG HA H 1 4.121 . . 1 . . . . . . . . 5334 1 576 . 1 1 85 85 ARG HB2 H 1 1.838 . . 1 . . . . . . . . 5334 1 577 . 1 1 85 85 ARG HB3 H 1 1.838 . . 1 . . . . . . . . 5334 1 578 . 1 1 85 85 ARG C C 13 177.142 . . 1 . . . . . . . . 5334 1 579 . 1 1 85 85 ARG CA C 13 58.325 . . 1 . . . . . . . . 5334 1 580 . 1 1 85 85 ARG CB C 13 30.874 . . 1 . . . . . . . . 5334 1 581 . 1 1 85 85 ARG N N 15 120.449 . . 1 . . . . . . . . 5334 1 582 . 1 1 86 86 GLY H H 1 7.897 . . 1 . . . . . . . . 5334 1 583 . 1 1 86 86 GLY HA2 H 1 3.625 . . 2 . . . . . . . . 5334 1 584 . 1 1 86 86 GLY HA3 H 1 4.271 . . 2 . . . . . . . . 5334 1 585 . 1 1 86 86 GLY C C 13 173.269 . . 1 . . . . . . . . 5334 1 586 . 1 1 86 86 GLY CA C 13 45.258 . . 1 . . . . . . . . 5334 1 587 . 1 1 86 86 GLY N N 15 108.881 . . 1 . . . . . . . . 5334 1 588 . 1 1 87 87 ILE H H 1 8.610 . . 1 . . . . . . . . 5334 1 589 . 1 1 87 87 ILE HA H 1 4.169 . . 1 . . . . . . . . 5334 1 590 . 1 1 87 87 ILE HB H 1 1.565 . . 1 . . . . . . . . 5334 1 591 . 1 1 87 87 ILE C C 13 176.360 . . 1 . . . . . . . . 5334 1 592 . 1 1 87 87 ILE CA C 13 60.556 . . 1 . . . . . . . . 5334 1 593 . 1 1 87 87 ILE CB C 13 40.165 . . 1 . . . . . . . . 5334 1 594 . 1 1 87 87 ILE N N 15 124.963 . . 1 . . . . . . . . 5334 1 595 . 1 1 88 88 THR HA H 1 3.910 . . 4 . . . . . . . . 5334 1 596 . 1 1 88 88 THR HB H 1 3.910 . . 4 . . . . . . . . 5334 1 597 . 1 1 88 88 THR C C 13 175.115 . . 1 . . . . . . . . 5334 1 598 . 1 1 88 88 THR CA C 13 64.779 . . 1 . . . . . . . . 5334 1 599 . 1 1 88 88 THR CB C 13 69.256 . . 1 . . . . . . . . 5334 1 600 . 1 1 89 89 SER H H 1 8.877 . . 1 . . . . . . . . 5334 1 601 . 1 1 89 89 SER HB2 H 1 4.037 . . 1 . . . . . . . . 5334 1 602 . 1 1 89 89 SER HB3 H 1 4.037 . . 1 . . . . . . . . 5334 1 603 . 1 1 89 89 SER C C 13 173.349 . . 1 . . . . . . . . 5334 1 604 . 1 1 89 89 SER CA C 13 60.157 . . 1 . . . . . . . . 5334 1 605 . 1 1 89 89 SER CB C 13 63.161 . . 1 . . . . . . . . 5334 1 606 . 1 1 89 89 SER N N 15 117.528 . . 1 . . . . . . . . 5334 1 607 . 1 1 90 90 TYR H H 1 7.851 . . 1 . . . . . . . . 5334 1 608 . 1 1 90 90 TYR HA H 1 4.543 . . 1 . . . . . . . . 5334 1 609 . 1 1 90 90 TYR HB2 H 1 2.589 . . 2 . . . . . . . . 5334 1 610 . 1 1 90 90 TYR HB3 H 1 3.055 . . 2 . . . . . . . . 5334 1 611 . 1 1 90 90 TYR C C 13 173.329 . . 1 . . . . . . . . 5334 1 612 . 1 1 90 90 TYR CA C 13 56.561 . . 1 . . . . . . . . 5334 1 613 . 1 1 90 90 TYR CB C 13 39.308 . . 1 . . . . . . . . 5334 1 614 . 1 1 90 90 TYR N N 15 120.920 . . 1 . . . . . . . . 5334 1 615 . 1 1 91 91 ASN H H 1 8.948 . . 1 . . . . . . . . 5334 1 616 . 1 1 91 91 ASN CA C 13 48.734 . . 1 . . . . . . . . 5334 1 617 . 1 1 91 91 ASN CB C 13 39.382 . . 1 . . . . . . . . 5334 1 618 . 1 1 91 91 ASN N N 15 127.153 . . 1 . . . . . . . . 5334 1 619 . 1 1 92 92 PRO HA H 1 3.871 . . 1 . . . . . . . . 5334 1 620 . 1 1 92 92 PRO HB2 H 1 1.821 . . 2 . . . . . . . . 5334 1 621 . 1 1 92 92 PRO HB3 H 1 2.196 . . 2 . . . . . . . . 5334 1 622 . 1 1 92 92 PRO C C 13 178.533 . . 1 . . . . . . . . 5334 1 623 . 1 1 92 92 PRO CA C 13 63.605 . . 1 . . . . . . . . 5334 1 624 . 1 1 92 92 PRO CB C 13 32.132 . . 1 . . . . . . . . 5334 1 625 . 1 1 93 93 LEU H H 1 7.585 . . 1 . . . . . . . . 5334 1 626 . 1 1 93 93 LEU HA H 1 4.003 . . 1 . . . . . . . . 5334 1 627 . 1 1 93 93 LEU HB2 H 1 1.388 . . 2 . . . . . . . . 5334 1 628 . 1 1 93 93 LEU HB3 H 1 1.572 . . 2 . . . . . . . . 5334 1 629 . 1 1 93 93 LEU C C 13 178.373 . . 1 . . . . . . . . 5334 1 630 . 1 1 93 93 LEU CA C 13 56.627 . . 1 . . . . . . . . 5334 1 631 . 1 1 93 93 LEU CB C 13 40.861 . . 1 . . . . . . . . 5334 1 632 . 1 1 93 93 LEU N N 15 117.668 . . 1 . . . . . . . . 5334 1 633 . 1 1 94 94 ALA H H 1 7.406 . . 1 . . . . . . . . 5334 1 634 . 1 1 94 94 ALA HA H 1 4.331 . . 1 . . . . . . . . 5334 1 635 . 1 1 94 94 ALA HB1 H 1 1.282 . . 1 . . . . . . . . 5334 1 636 . 1 1 94 94 ALA HB2 H 1 1.282 . . 1 . . . . . . . . 5334 1 637 . 1 1 94 94 ALA HB3 H 1 1.282 . . 1 . . . . . . . . 5334 1 638 . 1 1 94 94 ALA C C 13 176.451 . . 1 . . . . . . . . 5334 1 639 . 1 1 94 94 ALA CA C 13 51.937 . . 1 . . . . . . . . 5334 1 640 . 1 1 94 94 ALA CB C 13 18.111 . . 1 . . . . . . . . 5334 1 641 . 1 1 94 94 ALA N N 15 119.448 . . 1 . . . . . . . . 5334 1 642 . 1 1 95 95 GLY H H 1 7.215 . . 1 . . . . . . . . 5334 1 643 . 1 1 95 95 GLY CA C 13 43.991 . . 1 . . . . . . . . 5334 1 644 . 1 1 95 95 GLY N N 15 106.935 . . 1 . . . . . . . . 5334 1 645 . 1 1 96 96 PRO HA H 1 4.715 . . 1 . . . . . . . . 5334 1 646 . 1 1 96 96 PRO HB2 H 1 1.844 . . 2 . . . . . . . . 5334 1 647 . 1 1 96 96 PRO HB3 H 1 2.572 . . 2 . . . . . . . . 5334 1 648 . 1 1 96 96 PRO C C 13 177.917 . . 1 . . . . . . . . 5334 1 649 . 1 1 96 96 PRO CA C 13 63.141 . . 1 . . . . . . . . 5334 1 650 . 1 1 96 96 PRO CB C 13 32.950 . . 1 . . . . . . . . 5334 1 651 . 1 1 97 97 LEU H H 1 8.838 . . 1 . . . . . . . . 5334 1 652 . 1 1 97 97 LEU HA H 1 3.697 . . 1 . . . . . . . . 5334 1 653 . 1 1 97 97 LEU HB2 H 1 1.079 . . 2 . . . . . . . . 5334 1 654 . 1 1 97 97 LEU HB3 H 1 1.646 . . 2 . . . . . . . . 5334 1 655 . 1 1 97 97 LEU C C 13 177.422 . . 1 . . . . . . . . 5334 1 656 . 1 1 97 97 LEU CA C 13 59.618 . . 1 . . . . . . . . 5334 1 657 . 1 1 97 97 LEU CB C 13 40.922 . . 1 . . . . . . . . 5334 1 658 . 1 1 97 97 LEU N N 15 126.874 . . 1 . . . . . . . . 5334 1 659 . 1 1 98 98 ARG H H 1 9.000 . . 1 . . . . . . . . 5334 1 660 . 1 1 98 98 ARG HA H 1 3.263 . . 1 . . . . . . . . 5334 1 661 . 1 1 98 98 ARG HB2 H 1 1.592 . . 1 . . . . . . . . 5334 1 662 . 1 1 98 98 ARG HB3 H 1 1.592 . . 1 . . . . . . . . 5334 1 663 . 1 1 98 98 ARG C C 13 175.662 . . 1 . . . . . . . . 5334 1 664 . 1 1 98 98 ARG CA C 13 59.208 . . 1 . . . . . . . . 5334 1 665 . 1 1 98 98 ARG CB C 13 30.285 . . 1 . . . . . . . . 5334 1 666 . 1 1 98 98 ARG N N 15 113.359 . . 1 . . . . . . . . 5334 1 667 . 1 1 99 99 VAL H H 1 6.789 . . 1 . . . . . . . . 5334 1 668 . 1 1 99 99 VAL HA H 1 3.747 . . 1 . . . . . . . . 5334 1 669 . 1 1 99 99 VAL HB H 1 1.967 . . 1 . . . . . . . . 5334 1 670 . 1 1 99 99 VAL C C 13 180.022 . . 1 . . . . . . . . 5334 1 671 . 1 1 99 99 VAL CA C 13 64.845 . . 1 . . . . . . . . 5334 1 672 . 1 1 99 99 VAL CB C 13 32.741 . . 1 . . . . . . . . 5334 1 673 . 1 1 99 99 VAL N N 15 115.252 . . 1 . . . . . . . . 5334 1 674 . 1 1 100 100 GLN H H 1 8.156 . . 1 . . . . . . . . 5334 1 675 . 1 1 100 100 GLN HA H 1 4.011 . . 1 . . . . . . . . 5334 1 676 . 1 1 100 100 GLN HB2 H 1 1.637 . . 2 . . . . . . . . 5334 1 677 . 1 1 100 100 GLN HB3 H 1 2.273 . . 2 . . . . . . . . 5334 1 678 . 1 1 100 100 GLN C C 13 177.790 . . 1 . . . . . . . . 5334 1 679 . 1 1 100 100 GLN CA C 13 60.943 . . 1 . . . . . . . . 5334 1 680 . 1 1 100 100 GLN CB C 13 29.714 . . 1 . . . . . . . . 5334 1 681 . 1 1 100 100 GLN N N 15 121.205 . . 1 . . . . . . . . 5334 1 682 . 1 1 101 101 ALA H H 1 8.232 . . 1 . . . . . . . . 5334 1 683 . 1 1 101 101 ALA HA H 1 3.764 . . 1 . . . . . . . . 5334 1 684 . 1 1 101 101 ALA HB1 H 1 0.980 . . 1 . . . . . . . . 5334 1 685 . 1 1 101 101 ALA HB2 H 1 0.980 . . 1 . . . . . . . . 5334 1 686 . 1 1 101 101 ALA HB3 H 1 0.980 . . 1 . . . . . . . . 5334 1 687 . 1 1 101 101 ALA C C 13 177.720 . . 1 . . . . . . . . 5334 1 688 . 1 1 101 101 ALA CA C 13 53.740 . . 1 . . . . . . . . 5334 1 689 . 1 1 101 101 ALA CB C 13 18.776 . . 1 . . . . . . . . 5334 1 690 . 1 1 101 101 ALA N N 15 116.368 . . 1 . . . . . . . . 5334 1 691 . 1 1 102 102 ASN H H 1 7.415 . . 1 . . . . . . . . 5334 1 692 . 1 1 102 102 ASN CA C 13 53.075 . . 1 . . . . . . . . 5334 1 693 . 1 1 102 102 ASN CB C 13 39.235 . . 1 . . . . . . . . 5334 1 694 . 1 1 102 102 ASN N N 15 115.653 . . 1 . . . . . . . . 5334 1 695 . 1 1 104 104 PRO HA H 1 4.099 . . 1 . . . . . . . . 5334 1 696 . 1 1 104 104 PRO HB2 H 1 1.895 . . 2 . . . . . . . . 5334 1 697 . 1 1 104 104 PRO HB3 H 1 2.259 . . 2 . . . . . . . . 5334 1 698 . 1 1 104 104 PRO C C 13 177.334 . . 1 . . . . . . . . 5334 1 699 . 1 1 104 104 PRO CA C 13 64.902 . . 1 . . . . . . . . 5334 1 700 . 1 1 104 104 PRO CB C 13 32.480 . . 1 . . . . . . . . 5334 1 701 . 1 1 105 105 GLN H H 1 8.135 . . 1 . . . . . . . . 5334 1 702 . 1 1 105 105 GLN HA H 1 4.284 . . 1 . . . . . . . . 5334 1 703 . 1 1 105 105 GLN HB2 H 1 1.890 . . 2 . . . . . . . . 5334 1 704 . 1 1 105 105 GLN HB3 H 1 2.203 . . 2 . . . . . . . . 5334 1 705 . 1 1 105 105 GLN C C 13 177.133 . . 1 . . . . . . . . 5334 1 706 . 1 1 105 105 GLN CA C 13 56.592 . . 1 . . . . . . . . 5334 1 707 . 1 1 105 105 GLN CB C 13 29.079 . . 1 . . . . . . . . 5334 1 708 . 1 1 105 105 GLN N N 15 113.896 . . 1 . . . . . . . . 5334 1 709 . 1 1 106 106 GLN H H 1 7.637 . . 1 . . . . . . . . 5334 1 710 . 1 1 106 106 GLN HA H 1 4.700 . . 1 . . . . . . . . 5334 1 711 . 1 1 106 106 GLN HB2 H 1 2.086 . . 1 . . . . . . . . 5334 1 712 . 1 1 106 106 GLN HB3 H 1 2.086 . . 1 . . . . . . . . 5334 1 713 . 1 1 106 106 GLN C C 13 175.230 . . 1 . . . . . . . . 5334 1 714 . 1 1 106 106 GLN CA C 13 53.493 . . 1 . . . . . . . . 5334 1 715 . 1 1 106 106 GLN CB C 13 26.707 . . 1 . . . . . . . . 5334 1 716 . 1 1 106 106 GLN N N 15 119.742 . . 1 . . . . . . . . 5334 1 717 . 1 1 107 107 GLN H H 1 7.756 . . 1 . . . . . . . . 5334 1 718 . 1 1 107 107 GLN HA H 1 3.686 . . 1 . . . . . . . . 5334 1 719 . 1 1 107 107 GLN HB2 H 1 1.891 . . 2 . . . . . . . . 5334 1 720 . 1 1 107 107 GLN HB3 H 1 2.123 . . 2 . . . . . . . . 5334 1 721 . 1 1 107 107 GLN C C 13 177.501 . . 1 . . . . . . . . 5334 1 722 . 1 1 107 107 GLN CA C 13 60.016 . . 1 . . . . . . . . 5334 1 723 . 1 1 107 107 GLN CB C 13 29.496 . . 1 . . . . . . . . 5334 1 724 . 1 1 107 107 GLN N N 15 120.794 . . 1 . . . . . . . . 5334 1 725 . 1 1 108 108 GLY H H 1 8.481 . . 1 . . . . . . . . 5334 1 726 . 1 1 108 108 GLY HA2 H 1 3.689 . . 1 . . . . . . . . 5334 1 727 . 1 1 108 108 GLY HA3 H 1 3.689 . . 1 . . . . . . . . 5334 1 728 . 1 1 108 108 GLY C C 13 177.200 . . 1 . . . . . . . . 5334 1 729 . 1 1 108 108 GLY CA C 13 47.378 . . 1 . . . . . . . . 5334 1 730 . 1 1 108 108 GLY N N 15 105.892 . . 1 . . . . . . . . 5334 1 731 . 1 1 109 109 LEU H H 1 7.873 . . 1 . . . . . . . . 5334 1 732 . 1 1 109 109 LEU HA H 1 4.015 . . 1 . . . . . . . . 5334 1 733 . 1 1 109 109 LEU HB2 H 1 1.152 . . 2 . . . . . . . . 5334 1 734 . 1 1 109 109 LEU HB3 H 1 1.675 . . 2 . . . . . . . . 5334 1 735 . 1 1 109 109 LEU C C 13 178.904 . . 1 . . . . . . . . 5334 1 736 . 1 1 109 109 LEU CA C 13 49.031 . . 1 . . . . . . . . 5334 1 737 . 1 1 109 109 LEU CB C 13 40.510 . . 1 . . . . . . . . 5334 1 738 . 1 1 109 109 LEU N N 15 120.688 . . 1 . . . . . . . . 5334 1 739 . 1 1 110 110 ARG H H 1 8.255 . . 1 . . . . . . . . 5334 1 740 . 1 1 110 110 ARG HA H 1 3.899 . . 1 . . . . . . . . 5334 1 741 . 1 1 110 110 ARG HB2 H 1 2.001 . . 1 . . . . . . . . 5334 1 742 . 1 1 110 110 ARG HB3 H 1 2.001 . . 1 . . . . . . . . 5334 1 743 . 1 1 110 110 ARG C C 13 178.994 . . 1 . . . . . . . . 5334 1 744 . 1 1 110 110 ARG CA C 13 60.770 . . 1 . . . . . . . . 5334 1 745 . 1 1 110 110 ARG CB C 13 29.211 . . 1 . . . . . . . . 5334 1 746 . 1 1 110 110 ARG N N 15 120.343 . . 1 . . . . . . . . 5334 1 747 . 1 1 111 111 ARG H H 1 8.157 . . 1 . . . . . . . . 5334 1 748 . 1 1 111 111 ARG HA H 1 3.951 . . 1 . . . . . . . . 5334 1 749 . 1 1 111 111 ARG HB2 H 1 1.851 . . 2 . . . . . . . . 5334 1 750 . 1 1 111 111 ARG HB3 H 1 1.931 . . 2 . . . . . . . . 5334 1 751 . 1 1 111 111 ARG C C 13 179.221 . . 1 . . . . . . . . 5334 1 752 . 1 1 111 111 ARG CA C 13 58.421 . . 1 . . . . . . . . 5334 1 753 . 1 1 111 111 ARG CB C 13 28.969 . . 1 . . . . . . . . 5334 1 754 . 1 1 111 111 ARG N N 15 118.576 . . 1 . . . . . . . . 5334 1 755 . 1 1 112 112 GLU H H 1 8.062 . . 1 . . . . . . . . 5334 1 756 . 1 1 112 112 GLU HA H 1 4.265 . . 1 . . . . . . . . 5334 1 757 . 1 1 112 112 GLU HB2 H 1 1.712 . . 2 . . . . . . . . 5334 1 758 . 1 1 112 112 GLU HB3 H 1 2.126 . . 2 . . . . . . . . 5334 1 759 . 1 1 112 112 GLU C C 13 179.182 . . 1 . . . . . . . . 5334 1 760 . 1 1 112 112 GLU CA C 13 59.252 . . 1 . . . . . . . . 5334 1 761 . 1 1 112 112 GLU CB C 13 28.880 . . 1 . . . . . . . . 5334 1 762 . 1 1 112 112 GLU N N 15 120.105 . . 1 . . . . . . . . 5334 1 763 . 1 1 113 113 TYR H H 1 8.596 . . 1 . . . . . . . . 5334 1 764 . 1 1 113 113 TYR CB C 13 38.723 . . 1 . . . . . . . . 5334 1 765 . 1 1 113 113 TYR N N 15 119.166 . . 1 . . . . . . . . 5334 1 766 . 1 1 114 114 GLN HA H 1 3.716 . . 1 . . . . . . . . 5334 1 767 . 1 1 114 114 GLN HB2 H 1 1.738 . . 2 . . . . . . . . 5334 1 768 . 1 1 114 114 GLN HB3 H 1 2.702 . . 2 . . . . . . . . 5334 1 769 . 1 1 114 114 GLN C C 13 178.308 . . 1 . . . . . . . . 5334 1 770 . 1 1 114 114 GLN CA C 13 59.243 . . 1 . . . . . . . . 5334 1 771 . 1 1 114 114 GLN CB C 13 28.144 . . 1 . . . . . . . . 5334 1 772 . 1 1 115 115 GLN H H 1 7.680 . . 1 . . . . . . . . 5334 1 773 . 1 1 115 115 GLN C C 13 175.129 . . 1 . . . . . . . . 5334 1 774 . 1 1 115 115 GLN CA C 13 59.115 . . 1 . . . . . . . . 5334 1 775 . 1 1 115 115 GLN CB C 13 28.295 . . 1 . . . . . . . . 5334 1 776 . 1 1 115 115 GLN N N 15 114.472 . . 1 . . . . . . . . 5334 1 777 . 1 1 116 116 LEU H H 1 7.777 . . 1 . . . . . . . . 5334 1 778 . 1 1 116 116 LEU HA H 1 3.927 . . 1 . . . . . . . . 5334 1 779 . 1 1 116 116 LEU HB2 H 1 0.953 . . 2 . . . . . . . . 5334 1 780 . 1 1 116 116 LEU HB3 H 1 1.554 . . 2 . . . . . . . . 5334 1 781 . 1 1 116 116 LEU C C 13 176.990 . . 1 . . . . . . . . 5334 1 782 . 1 1 116 116 LEU CA C 13 58.264 . . 1 . . . . . . . . 5334 1 783 . 1 1 116 116 LEU CB C 13 41.790 . . 1 . . . . . . . . 5334 1 784 . 1 1 116 116 LEU N N 15 121.771 . . 1 . . . . . . . . 5334 1 785 . 1 1 117 117 TRP H H 1 8.875 . . 1 . . . . . . . . 5334 1 786 . 1 1 117 117 TRP HA H 1 3.728 . . 1 . . . . . . . . 5334 1 787 . 1 1 117 117 TRP HB2 H 1 2.702 . . 2 . . . . . . . . 5334 1 788 . 1 1 117 117 TRP HB3 H 1 3.518 . . 2 . . . . . . . . 5334 1 789 . 1 1 117 117 TRP C C 13 179.401 . . 1 . . . . . . . . 5334 1 790 . 1 1 117 117 TRP CA C 13 62.662 . . 1 . . . . . . . . 5334 1 791 . 1 1 117 117 TRP CB C 13 29.605 . . 1 . . . . . . . . 5334 1 792 . 1 1 117 117 TRP N N 15 120.988 . . 1 . . . . . . . . 5334 1 793 . 1 1 118 118 LEU H H 1 8.606 . . 1 . . . . . . . . 5334 1 794 . 1 1 118 118 LEU HA H 1 4.263 . . 1 . . . . . . . . 5334 1 795 . 1 1 118 118 LEU HB2 H 1 1.417 . . 2 . . . . . . . . 5334 1 796 . 1 1 118 118 LEU HB3 H 1 2.157 . . 2 . . . . . . . . 5334 1 797 . 1 1 118 118 LEU C C 13 179.397 . . 1 . . . . . . . . 5334 1 798 . 1 1 118 118 LEU CA C 13 58.366 . . 1 . . . . . . . . 5334 1 799 . 1 1 118 118 LEU CB C 13 43.035 . . 1 . . . . . . . . 5334 1 800 . 1 1 118 118 LEU N N 15 118.621 . . 1 . . . . . . . . 5334 1 801 . 1 1 119 119 ALA H H 1 8.054 . . 1 . . . . . . . . 5334 1 802 . 1 1 119 119 ALA HA H 1 4.044 . . 1 . . . . . . . . 5334 1 803 . 1 1 119 119 ALA HB1 H 1 1.437 . . 1 . . . . . . . . 5334 1 804 . 1 1 119 119 ALA HB2 H 1 1.437 . . 1 . . . . . . . . 5334 1 805 . 1 1 119 119 ALA HB3 H 1 1.437 . . 1 . . . . . . . . 5334 1 806 . 1 1 119 119 ALA C C 13 180.680 . . 1 . . . . . . . . 5334 1 807 . 1 1 119 119 ALA CA C 13 54.800 . . 1 . . . . . . . . 5334 1 808 . 1 1 119 119 ALA CB C 13 18.160 . . 1 . . . . . . . . 5334 1 809 . 1 1 119 119 ALA N N 15 122.392 . . 1 . . . . . . . . 5334 1 810 . 1 1 120 120 ALA H H 1 7.917 . . 1 . . . . . . . . 5334 1 811 . 1 1 120 120 ALA HA H 1 3.589 . . 1 . . . . . . . . 5334 1 812 . 1 1 120 120 ALA HB1 H 1 0.452 . . 1 . . . . . . . . 5334 1 813 . 1 1 120 120 ALA HB2 H 1 0.452 . . 1 . . . . . . . . 5334 1 814 . 1 1 120 120 ALA HB3 H 1 0.452 . . 1 . . . . . . . . 5334 1 815 . 1 1 120 120 ALA C C 13 177.752 . . 1 . . . . . . . . 5334 1 816 . 1 1 120 120 ALA CA C 13 54.413 . . 1 . . . . . . . . 5334 1 817 . 1 1 120 120 ALA CB C 13 16.727 . . 1 . . . . . . . . 5334 1 818 . 1 1 120 120 ALA N N 15 120.335 . . 1 . . . . . . . . 5334 1 819 . 1 1 121 121 PHE H H 1 7.136 . . 1 . . . . . . . . 5334 1 820 . 1 1 121 121 PHE HA H 1 3.904 . . 1 . . . . . . . . 5334 1 821 . 1 1 121 121 PHE HB2 H 1 3.013 . . 1 . . . . . . . . 5334 1 822 . 1 1 121 121 PHE HB3 H 1 3.013 . . 1 . . . . . . . . 5334 1 823 . 1 1 121 121 PHE C C 13 177.147 . . 1 . . . . . . . . 5334 1 824 . 1 1 121 121 PHE CA C 13 62.263 . . 1 . . . . . . . . 5334 1 825 . 1 1 121 121 PHE CB C 13 40.299 . . 1 . . . . . . . . 5334 1 826 . 1 1 121 121 PHE N N 15 111.355 . . 1 . . . . . . . . 5334 1 827 . 1 1 122 122 ALA H H 1 7.576 . . 1 . . . . . . . . 5334 1 828 . 1 1 122 122 ALA HA H 1 4.198 . . 1 . . . . . . . . 5334 1 829 . 1 1 122 122 ALA HB1 H 1 1.395 . . 1 . . . . . . . . 5334 1 830 . 1 1 122 122 ALA HB2 H 1 1.395 . . 1 . . . . . . . . 5334 1 831 . 1 1 122 122 ALA HB3 H 1 1.395 . . 1 . . . . . . . . 5334 1 832 . 1 1 122 122 ALA C C 13 177.711 . . 1 . . . . . . . . 5334 1 833 . 1 1 122 122 ALA CA C 13 54.075 . . 1 . . . . . . . . 5334 1 834 . 1 1 122 122 ALA CB C 13 18.531 . . 1 . . . . . . . . 5334 1 835 . 1 1 122 122 ALA N N 15 119.705 . . 1 . . . . . . . . 5334 1 836 . 1 1 123 123 ALA H H 1 7.198 . . 1 . . . . . . . . 5334 1 837 . 1 1 123 123 ALA HA H 1 4.237 . . 1 . . . . . . . . 5334 1 838 . 1 1 123 123 ALA HB1 H 1 1.189 . . 1 . . . . . . . . 5334 1 839 . 1 1 123 123 ALA HB2 H 1 1.189 . . 1 . . . . . . . . 5334 1 840 . 1 1 123 123 ALA HB3 H 1 1.189 . . 1 . . . . . . . . 5334 1 841 . 1 1 123 123 ALA C C 13 177.491 . . 1 . . . . . . . . 5334 1 842 . 1 1 123 123 ALA CA C 13 51.790 . . 1 . . . . . . . . 5334 1 843 . 1 1 123 123 ALA CB C 13 19.239 . . 1 . . . . . . . . 5334 1 844 . 1 1 123 123 ALA N N 15 117.577 . . 1 . . . . . . . . 5334 1 845 . 1 1 124 124 LEU H H 1 7.332 . . 1 . . . . . . . . 5334 1 846 . 1 1 124 124 LEU CA C 13 54.568 . . 1 . . . . . . . . 5334 1 847 . 1 1 124 124 LEU CB C 13 40.174 . . 1 . . . . . . . . 5334 1 848 . 1 1 124 124 LEU N N 15 119.394 . . 1 . . . . . . . . 5334 1 849 . 1 1 125 125 PRO HA H 1 4.274 . . 1 . . . . . . . . 5334 1 850 . 1 1 125 125 PRO HB2 H 1 1.774 . . 2 . . . . . . . . 5334 1 851 . 1 1 125 125 PRO HB3 H 1 2.166 . . 2 . . . . . . . . 5334 1 852 . 1 1 125 125 PRO C C 13 177.695 . . 1 . . . . . . . . 5334 1 853 . 1 1 125 125 PRO CA C 13 64.119 . . 1 . . . . . . . . 5334 1 854 . 1 1 125 125 PRO CB C 13 31.696 . . 1 . . . . . . . . 5334 1 855 . 1 1 126 126 GLY H H 1 8.409 . . 1 . . . . . . . . 5334 1 856 . 1 1 126 126 GLY HA2 H 1 3.766 . . 1 . . . . . . . . 5334 1 857 . 1 1 126 126 GLY HA3 H 1 3.766 . . 1 . . . . . . . . 5334 1 858 . 1 1 126 126 GLY C C 13 174.500 . . 1 . . . . . . . . 5334 1 859 . 1 1 126 126 GLY CA C 13 45.683 . . 1 . . . . . . . . 5334 1 860 . 1 1 126 126 GLY N N 15 107.943 . . 1 . . . . . . . . 5334 1 861 . 1 1 127 127 SER H H 1 7.820 . . 1 . . . . . . . . 5334 1 862 . 1 1 127 127 SER HA H 1 3.970 . . 1 . . . . . . . . 5334 1 863 . 1 1 127 127 SER C C 13 174.369 . . 1 . . . . . . . . 5334 1 864 . 1 1 127 127 SER CA C 13 58.710 . . 1 . . . . . . . . 5334 1 865 . 1 1 127 127 SER CB C 13 64.034 . . 1 . . . . . . . . 5334 1 866 . 1 1 127 127 SER N N 15 114.623 . . 1 . . . . . . . . 5334 1 867 . 1 1 128 128 ALA H H 1 8.013 . . 1 . . . . . . . . 5334 1 868 . 1 1 128 128 ALA HA H 1 4.229 . . 1 . . . . . . . . 5334 1 869 . 1 1 128 128 ALA HB1 H 1 1.182 . . 1 . . . . . . . . 5334 1 870 . 1 1 128 128 ALA HB2 H 1 1.182 . . 1 . . . . . . . . 5334 1 871 . 1 1 128 128 ALA HB3 H 1 1.182 . . 1 . . . . . . . . 5334 1 872 . 1 1 128 128 ALA C C 13 177.197 . . 1 . . . . . . . . 5334 1 873 . 1 1 128 128 ALA CA C 13 52.585 . . 1 . . . . . . . . 5334 1 874 . 1 1 128 128 ALA CB C 13 19.531 . . 1 . . . . . . . . 5334 1 875 . 1 1 128 128 ALA N N 15 124.520 . . 1 . . . . . . . . 5334 1 876 . 1 1 129 129 LYS H H 1 8.059 . . 1 . . . . . . . . 5334 1 877 . 1 1 129 129 LYS HA H 1 4.099 . . 1 . . . . . . . . 5334 1 878 . 1 1 129 129 LYS HB2 H 1 1.626 . . 1 . . . . . . . . 5334 1 879 . 1 1 129 129 LYS HB3 H 1 1.626 . . 1 . . . . . . . . 5334 1 880 . 1 1 129 129 LYS C C 13 175.873 . . 1 . . . . . . . . 5334 1 881 . 1 1 129 129 LYS CA C 13 56.152 . . 1 . . . . . . . . 5334 1 882 . 1 1 129 129 LYS CB C 13 33.263 . . 1 . . . . . . . . 5334 1 883 . 1 1 129 129 LYS N N 15 119.320 . . 1 . . . . . . . . 5334 1 884 . 1 1 130 130 ASP H H 1 7.773 . . 1 . . . . . . . . 5334 1 885 . 1 1 130 130 ASP CA C 13 52.332 . . 1 . . . . . . . . 5334 1 886 . 1 1 130 130 ASP CB C 13 41.697 . . 1 . . . . . . . . 5334 1 887 . 1 1 130 130 ASP N N 15 122.443 . . 1 . . . . . . . . 5334 1 888 . 1 1 131 131 PRO HA H 1 4.269 . . 1 . . . . . . . . 5334 1 889 . 1 1 131 131 PRO HB2 H 1 1.689 . . 2 . . . . . . . . 5334 1 890 . 1 1 131 131 PRO HB3 H 1 2.079 . . 2 . . . . . . . . 5334 1 891 . 1 1 131 131 PRO C C 13 177.083 . . 1 . . . . . . . . 5334 1 892 . 1 1 131 131 PRO CA C 13 63.754 . . 1 . . . . . . . . 5334 1 893 . 1 1 131 131 PRO CB C 13 32.134 . . 1 . . . . . . . . 5334 1 894 . 1 1 132 132 SER H H 1 8.419 . . 1 . . . . . . . . 5334 1 895 . 1 1 132 132 SER HA H 1 4.220 . . 1 . . . . . . . . 5334 1 896 . 1 1 132 132 SER HB2 H 1 3.705 . . 2 . . . . . . . . 5334 1 897 . 1 1 132 132 SER C C 13 174.372 . . 1 . . . . . . . . 5334 1 898 . 1 1 132 132 SER CA C 13 59.203 . . 1 . . . . . . . . 5334 1 899 . 1 1 132 132 SER CB C 13 63.695 . . 1 . . . . . . . . 5334 1 900 . 1 1 132 132 SER N N 15 114.659 . . 1 . . . . . . . . 5334 1 901 . 1 1 133 133 TRP H H 1 7.790 . . 1 . . . . . . . . 5334 1 902 . 1 1 133 133 TRP HA H 1 4.585 . . 1 . . . . . . . . 5334 1 903 . 1 1 133 133 TRP HB2 H 1 3.167 . . 1 . . . . . . . . 5334 1 904 . 1 1 133 133 TRP HB3 H 1 3.167 . . 1 . . . . . . . . 5334 1 905 . 1 1 133 133 TRP C C 13 174.773 . . 1 . . . . . . . . 5334 1 906 . 1 1 133 133 TRP CA C 13 56.975 . . 1 . . . . . . . . 5334 1 907 . 1 1 133 133 TRP CB C 13 29.692 . . 1 . . . . . . . . 5334 1 908 . 1 1 133 133 TRP N N 15 122.387 . . 1 . . . . . . . . 5334 1 909 . 1 1 134 134 ALA H H 1 7.543 . . 1 . . . . . . . . 5334 1 910 . 1 1 134 134 ALA CA C 13 54.031 . . 1 . . . . . . . . 5334 1 911 . 1 1 134 134 ALA CB C 13 20.575 . . 1 . . . . . . . . 5334 1 912 . 1 1 134 134 ALA N N 15 130.152 . . 1 . . . . . . . . 5334 1 stop_ loop_ _Ambiguous_atom_chem_shift.Ambiguous_shift_set_ID _Ambiguous_atom_chem_shift.Atom_chem_shift_ID _Ambiguous_atom_chem_shift.Entry_ID _Ambiguous_atom_chem_shift.Assigned_chem_shift_list_ID 1 257 5334 1 1 256 5334 1 2 596 5334 1 2 595 5334 1 stop_ save_